accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
P26921 | TRPB2_METTM | Tryptophan synthase beta chain 2 | Methanothermobacter | MDGKFGKYGGIFVPELLIPALEELEAAFLHYSKDRRFNEDLEHYLREYAGRPTGLYHARNLSEKLGCRVYLKREDMLHTGAHKINNTIGQALLAGYMGKRRLIAETGAGQHGIATAAAGALFGMDVDVYMGTEDVERQKLNVFRMEISGARVIPVDSGSRTLKDAINQAMRDWISSVEDTHYLIGSTMGPHPYPTMVKHFQSVIGREAREQILEIEGELPDTIIACVGGGSNAIGIFSAFLDDDVELIGAEGGGEGIESGNHGATLSAGSEGVLHGSLSYVLQDDDGQINEAHSVSAGLDYPGVGPEHAYLMETGRAMYEPITDAEALRGFKLLSRCEGIMPALESAHAIACLEKYASKPENRGKTVIVNLSGRGDKDMFLAAGLLGVDL | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | P26921 |
Q9PN51 | UVRC_CAMJE | Excinuclease ABC subunit C | Campylobacter | MTKENLENELKTLPNSTGVYQYFNQEGKLLYVGKAKNLKNRVRSYFAFTPNLHANPRNSLRIQKMIEETVHLEFIATNSEADALILENSFIKQLHPKYNILLRDDKTYPYIYVDFEEEFPRFEITRKLVKKSKIKYFGPFFKGARELLDALYLYYPLKQKASCKSPCIFYQISRCLAPCDKLISREKYLEILDEAIHALLNPSVLLKNLEKQMLVLAQNENYEEAAKVRDQIAMIKDLEVKVEIDIAKLEDFEVFALAFKNSVLSTLRFVVQNGKIISANSKITPIKNDIQWDQNEIYKQLILENFSMDIPLLANVIYVYEEFEDRVLLEEILSQRFDKKISIKIPKIGEKRRICDLAFQNALLNIEKEQKNHDFTIQKELKSYFELENLPNDIEIFDNSHLQGVANVGAMVTYRINSWDKSKYRKFHLKHKNDYDQMREVLTRRALDFDKIPPPDLWLIDGGKALLDLAKEIIVSSGVNVDILAISKEKIDAKAHRAKGGAKDKIHSLKGEFSLSINDKKLQFLQKLRDEAHRFAISFHQNTKKKQDLKSSKLANLGLSSGVMQKLLAYYGNFESIYKADFKDLTMLVGRKAAQKIKEN | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q9PN51 |
Q59674 | XY11A_CELJA | Acetylxylan deacetylase | Cellvibrio | MKLPTLGKCVVRTLMGAVALGAISVNAQTLSSNSTGTNNGFYYTFWKDSGDASMTLLSGGRYQSSWGNSTNNWVGGKGWNPGNNSRVISYSGSYGVDSSQNSYLALYGWTRSPLIEYYVIESYGSYNPASCSGGTDYGSFQSDGATYNVRRCQRVNQPSIDGTQTFYQYFSVRNPKKGFGNISGTITFANHVNFWASKGLNLGNHNYQVLATEGYQSRGSSDITVSEGTSGGGTSSVGGASSSVNSSTGGGSSGGITVRARGANGSEHINLRVGGAVVANWTLGTSFQNYLYSGNASGDIQVQFDNDASGRDVVVDYIIVNGETRQAEDMEHNSAVYANGRCGGGSYSENMHCNGEIGFGYTYDCFSGNCSGGNGGSNSSAGNSSSGNTGGGGSNCSGYVGITFDDGPNSNTATLVNLLRQNNLTPVTWFNQGNNVASNAHLMSQQLSVGEVHNHSYTHPHMTSWTYQQVYDELNRTNQAIQNAGAPKPTLFRPPYGELNSTIQQAAQALGLRVVTWDVDSQDWNGASAAAIANAANQLQNGQVILMHDGSYTNTNSAIAQIATNLRAKGLCPGRIDPNTGRAVAPSSSGGSSSVALSSSSRSSSSAGGNTGGNCQCNWWGTFYPLCQTQTSGWGWENSRSCISTSTCNSQGTGGGGVVCN | Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and the arabinoxylans from wheat and rye, releasing xylobiose as the major product. Also likely catalyzes, via its C-terminal domain, the removal of acetyl groups from acetylated xylan. Thus, has the capability of hydrolyzing acetylated xylan. Does not attack mannan, galactan, arabinan or any cellulosic substrates. | Q59674 |
B6EGG3 | XNI_ALISL | Flap endonuclease Xni | Aliivibrio | MAIHLVIIDALNLIRRVHSAQPNQDDIQAVVTTTGRTINRILKETEPTHIIAVFDHHLQDRGWRAEVLPKYKEDRKPMPEALQKGMDAIQESWWKLGIDSLLSDGDEADDLVATLANKVASRNEQVTIVSTDKGYCQLLSPTLRIRDYFQHRWLDEPFIEKEFGLKPEQLADYWGLAGISSSKITGIPGIGPKAALEILTQFPTIEAANESDELPKKYRKKFDEYYNTAILCRKVAGLRTDIELGFNLQDIRYEKPE | Has flap endonuclease activity. During DNA replication, flap endonucleases cleave the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. | B6EGG3 |
P13726 | TF_HUMAN | Thromboplastin | Homo | METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS | Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. | P13726 |
Q925D8 | TS1R3_MOUSE | Sweet taste receptor T1R3 | Mus | MPALAIMGLSLAAFLELGMGASLCLSQQFKAQGDYILGGLFPLGSTEEATLNQRTQPNSIPCNRFSPLGLFLAMAMKMAVEEINNGSALLPGLRLGYDLFDTCSEPVVTMKSSLMFLAKVGSQSIAAYCNYTQYQPRVLAVIGPHSSELALITGKFFSFFLMPQVSYSASMDRLSDRETFPSFFRTVPSDRVQLQAVVTLLQNFSWNWVAALGSDDDYGREGLSIFSSLANARGICIAHEGLVPQHDTSGQQLGKVLDVLRQVNQSKVQVVVLFASARAVYSLFSYSIHHGLSPKVWVASESWLTSDLVMTLPNIARVGTVLGFLQRGALLPEFSHYVETHLALAADPAFCASLNAELDLEEHVMGQRCPRCDDIMLQNLSSGLLQNLSAGQLHHQIFATYAAVYSVAQALHNTLQCNVSHCHVSEHVLPWQLLENMYNMSFHARDLTLQFDAEGNVDMEYDLKMWVWQSPTPVLHTVGTFNGTLQLQQSKMYWPGNQVPVSQCSRQCKDGQVRRVKGFHSCCYDCVDCKAGSYRKHPDDFTCTPCNQDQWSPEKSTACLPRRPKFLAWGEPVVLSLLLLLCLVLGLALAALGLSVHHWDSPLVQASGGSQFCFGLICLGLFCLSVLLFPGRPSSASCLAQQPMAHLPLTGCLSTLFLQAAETFVESELPLSWANWLCSYLRGLWAWLVVLLATFVEAALCAWYLIAFPPEVVTDWSVLPTEVLEHCHVRSWVSLGLVHITNAMLAFLCFLGTFLVQSQPGRYNRARGLTFAMLAYFITWVSFVPLLANVQVAYQPAVQMGAILVCALGILVTFHLPKCYVLLWLPKLNTQEFFLGRNAKKAADENSGGGEAAQGHNE | Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate) and also to most of the 20 standard L-amino acids, but not to their D-enantiomers or other compounds. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose. Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses. | Q925D8 |
B8CLE4 | TOLB_SHEPW | Tol-Pal system protein TolB | Shewanella | MKILGKWLLASLLICSMPAKAALDIVITEGVDAARPIAVVPFVWQGTGPMPSQISDVVMSDLARSGTFSPSDELSLPQRNISTLAQFDAKAWMAQPAEAVVMGSIKPYGADKYLVSFQLIDLVKAQLQSGAGPQAANDLVIDSRETVISAAQFRQYGHRISDVVYEKLTGIRGAFLTRIAYVVVKHGEKSPYQLMISDYDGYNEQMLLRSPEPLMSPSWSPDGQQLAYVSFENRKAEVFVQNIYTQARKKVTSFNGINGAPVFSPDGKKLALTLSKDGQPDIYVVDIATSALKRVTNHYSIDTEPSWFPDGKSLLLTSERGGRPQLYRVFLDSGKISRLTFEGEWNLGGSIAPDGRSIVFVNRTNGKFNIARMDLETRFMQVLTSTRLDESPSLAPNGTMVIYGTTYQGKQVLAAVSMDGRFKARLPVGQGEVKSPSWSPFL | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | B8CLE4 |
Q6ZRF7 | ZN818_HUMAN | Putative zinc finger protein 818 | Homo | MLERNLTSMMSVEEPLPRPLTSLYIRLSILERNHMNMTYMAKSSVKIHISKVIIGFVLKRSLTNVCGKVLSQNSHLVNHQRIHTGEKSYRCHECGKAFTQGSRFINHQIVHTGENFPNVLNVARLLRMALNSGLTK | May be involved in transcriptional regulation. | Q6ZRF7 |
B2U928 | TSAD_RALPJ | tRNA threonylcarbamoyladenosine biosynthesis protein TsaD | Ralstonia | MLVLGIESSCDETGVALYDTHSGLRAHALYSQIAMHREYGGVVPELASRDHIRRVIPLLEEVLGKAGATRADIDAIAYTKGPGLAGALLVGASVANALAFALGKPLVAVHHLEGHLLSPLLEADRPEFPFLALLVSGGHTQLMRVDAVGQYTLLGETLDDAAGEAFDKTAKLLGLGYPGGPAVSRLAEFGNPGVFDLPRPMLHSGNFDFSFAGLKTAVLTQVRKLNLTDSETCYQPRADLARAFVDAIVEVLVKKTLRAAREHGLKRIVVAGGVGANRQLREGLNAEGKKRGLRVYYPDLQFCTDNGAMIAFAGAMRLQADPAQVQDGYGYGVTPRWDLEDIRIRHA | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. | B2U928 |
Q8IWB9 | TEX2_HUMAN | Transmembrane protein 96 | Homo | MTSLYGRHAEKTTDMPKPSAPKVHVQRSVSRDTIAIHFSASGEEEEEEEEEFREYFEEGLDDQSIVTGLEAKEDLYLEPQVGHDPAGPAASPVLADGLSVSQAPAILPVSKNTVKLLESPVPAAQVLSTVPLAVSPGSSSSGPLASSPSVSSLSEQKTSSSSPLSSPSKSPILSSSASTSTLSSAKPFMSLVKSLSTEVEPKESPHPARHRHLMKTLVKSLSTDTSRQESDTVSYKPPDSKLNLHLFKQFTQPRNTGGDSKTAPSSPLTSPSDTRSFFKVPEMEAKIEDTKRRLSEVIYEPFQLLSKIIGEESGSHRPKALSSSASELSNLSSLNGHLESNNNYSIKEEECDSEGDGYGSDSNIPRSDHPKSTGEPTREIELKSSQGSSLKDLGLKTSSLVLEKCSLSALVSKEDEEFCELYTEDFDLETEGESKVDKLSDIPLKPEVLAEDGVVLDSEDEVDSAVQHPELPVKTLGFFIMCVYVYLILPLPHYVSGLFLGIGLGFMTAVCVIWFFTPPSAHKYHKLHKNLRHWNTRSLDIKEPEILKGWMNEIYNYDPETYHATLTHSVFVRLEGGTLRLSKPNKNISRRASYNEPKPEVTYISQKIYDLSDSKIYLVPKTLARKRIWNKKYPICIELGQQDDFMSKAQTDKETSEEKPPAEGSEDPKKPPRPQEGTRSSQRDQILYLFGRTGREKEEWFRRFILASKLKSEIKKSSGVSGGKPGLLPAHSRHNSPSGHLTHSRSSSKGSVEEIMSQPKQKELAGSVRQKMLLDYSVYMGRCVPQESRSPQRSPLQSAESSPTAGKKLPEVPPSEEEEQEAWVNALLGRIFWDFLGEKYWSDLVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLGKEPLVEALKVGEIGKEGCRPRAFCLADSDEESSSAGSSEEDDAPEPSGGDKQLLPGAEGYVGGHRTSKIMRFVDKITKSKYFQKATETEFIKKKIEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRVWYGFRKPPHVELKARPKLGEREVTLVHVTDWIEKKLEQEFQKVFVMPNMDDVYITIMHSAMDPRSTSCLLKDPPVEAADQP | During endoplasmic reticulum (ER) stress or when cellular ceramide levels increase, may induce contacts between the ER and medial-Golgi complex to facilitate non-vesicular transport of ceramides from the ER to the Golgi complex where they are converted to complex sphingolipids, preventing toxic ceramide accumulation. | Q8IWB9 |
Q62HU9 | UBID_BURMA | Polyprenyl p-hydroxybenzoate decarboxylase | pseudomallei group | MKYRDLRDFIHGLEQRGELRRVTQPVSPVLEMTELCDRVLRAGGPALLFDAPAGHRFPVLGNLFGTPRRVALGMGVDADDEAALASLRDIGRLLSALKEPDPPKRLKDAGKLLSLAKAVWDMGPKTVSAPPCQEIVWEGDDVDLHKLPIQTCWPGDAGPLLTWGLTVTRGPNKTRQNLGIYRQQLIGRNKLIMRWLAHRGGALDFREFALKHPGQPYPVAVVLGADPATMLGAVTPVPDSLSEYQFAGLLRGARTELAKCVTPGVDALQVPARAEIVLEGFIHPQQGAPAPAPEGAPPRPAAGAAAGYEHALEGPYGDHTGYYNEQEWFPVFTVERITMRRDAIYHSTYTGKPPDEPAVLGVALNEVFVPLLQKQFAEITDFYLPPEGCSYRMAIVQMKKSYAGHAKRVMFGVWSFLRQFMYTKFIVVVDEDVNVRDWKEVIWAITTRVDPARDTVLVENTPIDYLDFASPVAGLGSKMGLDATNKWPGETQREWGRPIEMDAAVKARVDRLWTEIGLS | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q62HU9 |
B9E8X3 | Y1934_MACCJ | Nucleoid-associated protein MCCL_1934 | Macrococcus | MRGGGNMQQMMKQMQKMQKKMAEEQEKLKEERIEGTAGGGMVTVVVSGHKEVLDVIIKEEVVDPEDIEMLQDLVLAATNDALTKADDVTAQRLGQHTKGLNIPGMM | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | B9E8X3 |
O08712 | TR11B_MOUSE | Osteoprotegerin | Mus | MNKWLCCALLVLLDIIEWTTQETLPPKYLHYDPETGHQLLCDKCAPGTYLKQHCTVRRKTLCVPCPDHSYTDSWHTSDECVYCSPVCKELQSVKQECNRTHNRVCECEEGRYLEIEFCLKHRSCPPGSGVVQAGTPERNTVCKKCPDGFFSGETSSKAPCIKHTNCSTFGLLLIQKGNATHDNVCSGNREATQKCGIDVTLCEEAFFRFAVPTKIIPNWLSVLVDSLPGTKVNAESVERIKRRHSSQEQTFQLLKLWKHQNRDQEMVKKIIQDIDLCESSVQRHLGHSNLTTEQLLALMESLPGKKISPEEIERTRKTCKSSEQLLKLLSLWRIKNGDQDTLKGLMYALKHLKTSHFPKTVTHSLRKTMRFLHSFTMYRLYQKLFLEMIGNQVQSVKISCL | Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis. | O08712 |
A1S7I2 | TRPB_SHEAM | Tryptophan synthase beta chain | Shewanella | MSELKLDPYFGEYGGMYVPQILMPALKQLETAFVEAQQDPEFLTEFHDLLKNYAGRPTALTLTRNLSPNPKVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDVARQSPNVFRMRLMGAEVIPVTSGSATLKDACNEAMRDWSGSYDRAHYLLGTAAGPHPFPTIVREFQRMIGAETKAQMLEKEGRLPDAVIACVGGGSNAIGMFADFIDEPSVKLIGVEPAGKGIDTPMHGAPLKHGKTGIFFGMKAPLMQDAHGQIEESYSISAGLDFPSVGPQHAYLNATGRATYESATDDEALEAFQLLARSEGIIPALESAHALAYALRLAKDATEEQIIVVNLSGRGDKDIFTVSDILDGKASA | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A1S7I2 |
B8CKH5 | TRUB_SHEPW | tRNA-uridine isomerase | Shewanella | MARRSRGRHIDGVLLLDKDTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPICLGEATKFSQHLLDADKRYLVTAKLGQRTDTSDSDGEVVQTREIDFTQEQLDTALEYFRGKTMQVPSMYSALKYQGQPLYKYAREGIEVPREARPINVFELNFISLEGDELTLDIHCSKGTYIRTITDDLGEMLGCGAHVIMLRRTQVAGYPYDNMVSLAELEALVTKVEAESLTLAEVLDPLLLPMDTAVSDFKEINVSDDIAPFLMNGNPVQVANLPVDELVRITLGVERRFVGIGQMNDDGLLAPKRLIVLRDEAAQ | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | B8CKH5 |
Q8MKD1 | UBB_HORSE | Ubiquitin-related | Equus | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRFIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC | Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. | Q8MKD1 |
Q8KEJ1 | THIG_CHLTE | Thiazole synthase | Chlorobaculum | MDSLRLGTYTFSSRLILGTGKFSSTSAMIKAVRASGTQLVTVALRRFNREQAEDDLFGPLSEIEGLTLMPNTSGAATAKEAIKAAHIARELSGSPFIKVEIHPNPHHLMPDPIETWEACKILAAEGFIVMPYIPADPVLAKRLEEVGCSSVMPLGSAIGSGQGLSTAEMVKIIIRESSVPVIVDAGLRSPSEACAAMEMGCEAVLVNSAVAVARDPAAMALAFAKAVEAGFEARNAGLMPRSGSAVATSPLTSFLGATR | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | Q8KEJ1 |
A4Y845 | TRPB_SHEPC | Tryptophan synthase beta chain | Shewanella | MSTLKLNPYFGEYGGMYVPQILVPALKQLETAFVEAQEDEDFKAEFTDLLKNYAGRPTALTLTRNLSPNPMVKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKKEIIAETGAGQHGVATALACALLGLKCKVYMGAKDVARQSPNVFRMRLMGAEVIPVTSGSATLKDACNEAMRDWSGSYEKAHYLLGTAAGPHPFPTIVREFQRIIGEETKKQMLEREGRLPDAVIACVGGGSNAIGMFADFIDEPSVELIGVEPAGKGIDTPMHGAPLKHGKTGIFFGMKAPLMQDSEGQIEESYSISAGLDFPSVGPQHAHLNATGRARYESATDDEALEAFQQLARCEGIIPALESAHAIAYAVKMARECTKETILVVNLSGRGDKDIFTVSDILNGKEV | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A4Y845 |
B8EA59 | THIG_SHEB2 | Thiazole synthase | Shewanella | MLTIADVEFESRLFTGTGKFSNSQVMLEAITASKSQLVTVAMKRIDFKMGLDDLLTPLRQAGVRLLPNTSGARNAKEAVFAAELAREMLGTHWIKLEIHPDPKYLMPDAIETLEAARILCEKGFIVLPYVHADPVLCRRLEEVGCAAVMPLASPIGSNQGLVTESFLKIIIEQARVPVVIDAGIGAPSQAARAMELGADAVLVNTAIASSASPIVMAECFKEAVQCGRRAFEAGLGRVQTGAVHTSPLTGFLNQ | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | B8EA59 |
A0PJN4 | U2QL1_MOUSE | E2Q-like ubiquitin-conjugating enzyme 1 | Mus | MKELQDIARLSDRFISVELVNENLFDWNVKLHQVDKDSVLWQDMKETNTEFILLNLTFPDNFPFSPPFMRVLSPRLENGYVLDGGAICMELLTPRGWSSAYTVEAVMRQFAASLVKGQGRICRKAGKSKKSFSRKEAEATFKSLVKTHEKYGWVTPPVSDG | Probable E2 ubiquitin-protein ligase that catalyzes the covalent attachment of ubiquitin to target proteins. May facilitate the monoubiquitination and degradation of MTOR and CCNE1 through interaction with FBXW7. | A0PJN4 |
Q329B2 | YIDC_SHIDS | Membrane protein YidC | Shigella | MDSQRNLLVIALLFVSFMIWQAWEQDKNPQPQAQQTTQTTTTAAGSAADQGVPASGQGKLISVKTDVLDLTINTRGGDVEQALLPAYPKELNSTQPFQLLETSPQFIYQAQSGLTGRDGPDNPANGPRPLYNVEKDAYVLAEGQNELQVPMTYTDAAGNTFTKTFVLKRGDYAVNVNYNVQNAGEKPLEISSFGQLKQSITLPPHLDTGSSNFALHTFRGAAYSTPDEKYEKYKFDTIADNENLNISSKGGWVAMLQQYFATAWSPHNDGTNNFYTANLGNGIAAIGYKSQPVLVQPGQTGAMNSTLWVGPEIQDKMAAVAPHLDLTVDYGWLWFISQPLFKLLKWIHSFVGNWGFSIIIITFIVRGIMYPLTKAQYTSMAKMRMLQPKIQAMRERLGDDKQRISQEMMALYKAEKVNPLGGCFPLLIQMPIFLALYYMLMGSVELRQAPFALWIHDLSAQDPYYILPILMGVTMFFIQKMSPTTVTDPMQQKIMTFMPVIFTVFFLWFPSGLVLYYIVSNLVTIIQQQLIYRGLEKRGLHSREKKKS | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | Q329B2 |
P40200 | TACT_HUMAN | T cell-activated increased late expression protein | Homo | MEKKWKYCAVYYIIQIHFVKGVWEKTVNTEENVYATLGSDVNLTCQTQTVGFFVQMQWSKVTNKIDLIAVYHPQYGFYCAYGRPCESLVTFTETPENGSKWTLHLRNMSCSVSGRYECMLVLYPEGIQTKIYNLLIQTHVTADEWNSNHTIEIEINQTLEIPCFQNSSSKISSEFTYAWSVENSSTDSWVLLSKGIKEDNGTQETLISQNHLISNSTLLKDRVKLGTDYRLHLSPVQIFDDGRKFSCHIRVGPNKILRSSTTVKVFAKPEIPVIVENNSTDVLVERRFTCLLKNVFPKANITWFIDGSFLHDEKEGIYITNEERKGKDGFLELKSVLTRVHSNKPAQSDNLTIWCMALSPVPGNKVWNISSEKITFLLGSEISSTDPPLSVTESTLDTQPSPASSVSPARYPATSSVTLVDVSALRPNTTPQPSNSSMTTRGFNYPWTSSGTDTKKSVSRIPSETYSSSPSGAGSTLHDNVFTSTARAFSEVPTTANGSTKTNHVHITGIVVNKPKDGMSWPVIVAALLFCCMILFGLGVRKWCQYQKEIMERPPPFKPPPPPIKYTCIQEPNESDLPYHEMETL | May be involved in adhesive interactions of activated T and NK cells during the late phase of the immune response. Promotes NK cell-target adhesion by interacting with PVR present on target cells. May function at a time after T and NK cells have penetrated the endothelium using integrins and selectins, when they are actively engaging diseased cells and moving within areas of inflammation. | P40200 |
Q2KP58 | UQCC3_XENLA | Oocyte antigen VAP18 | Xenopus | METVRRIVKGTLLLGFCTGIGGDLWVLVAPGQERRLEMRMNYPEANPPMLAEAHKRNEMVLKVIEESAKTNENMARRSPWSS | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology. | Q2KP58 |
A4G8J0 | UPPP_HERAR | Undecaprenyl pyrophosphate phosphatase | Herminiimonas | MDTILALKVIIMGIVEGLTEFLPISSTGHLILAGSLLEFTGPKVKVFEIAIQTGAMLAVVWEYRVKIAAVLGGLFTERRAQKFAVNIVVAFLPAALLGLVFAGAIKEKLFAPVPVAIAFIVGGFVILWVERRNKQQVHAERVQSVDEMTLLDAFKVGCAQAFALIPGTSRSGASIIGGMMFGLSRKAATEFSFFLAIPTLMGATVYSVYKDRALLSMADIPLFGLGGLAAFFSAFLCVRWLLRYISTHDFTFFAYYRIGFGLFVLLSAHYGWVVWAE | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | A4G8J0 |
A7MMG1 | TRPB_CROS8 | Tryptophan synthase beta chain | Cronobacter | MSTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQSDAEFQAQFTDLLKNYAGRPTALTKCQNLTEGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMKLMGAEVIPVYSGSATLKDACNEALRDWSGSYDRAHYMLGTAAGPHPFPTIVREFQRMIGEETRAQIMEKEGRLPDAVIACVGGGSNAIGMFADFINETSVGLIGVEPAGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTDDGQIEESYSISAGLDFPSVGPQHAYLNSTGRAEYVSITDDEALEAFKTLCRQEGIIPALESSHALAHALKMMRAAPEKEQLLVVNLSGRGDKDIFTVHDIFKARGEM | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | A7MMG1 |
Q8CR47 | XYLB_STAES | Xylulose kinase | Staphylococcus | MVKEVVLGIDLGTSAIKIIAVDQLGNVIESVSETLKLYQEHPGYSEQDPNEWFEATKKGIKELIQSTEMSDKIVKGISFSGQMHGLVIVDDNGIPLRKAILWNDTRNSIQCRQIEDIYGERLNYNPILEGFTLPKMLWVQQHEPEIWNRVDVFMLPKDYLRYCLTQTIHMEYSDACSTLLFNPENYEWTKDVGDTFNIGDIYPPLVKSHSYVGNVTSSLAKELGLSSDVAVYAGGGDNACGAIGAGVIHDKSALCSIGTSGVVLNVEYQRVTSYDSNLHLFNHSVPDTYYAMGVTLAAGYSLNWLKQTFFENESFEEILNLAASSKIGANGLLFTPYLAGERTPHGDAQIRGSFIGISGQHTKADFARAVIEGITYSLYDSIKIMRRAGHEMNSITSIGGGAKSRFWLQLQADIFNVQIKRLKHEEGPSMGAAILAAYGLGWFKTIESCVEAFIKVDEVFEPNNENHDLYEQYYSVYEAIYKQTKQLTADLLTITN | Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-phosphate. | Q8CR47 |
B5YDB8 | UPP_DICT6 | UPRTase | Dictyoglomus | MVIVVDHPLVQHKLTKLRDKNTGPKEFRELLFEISSLMLYEVTKNLPTKEVEVETPLGIAKGKVLDNKDLAIVPILRAGLVMADGMLQILPSAKVGHIGLYRDPETLKPVQYYTKLPEDIDKREVIVVDPMLATGGSAVAAISILKAKGVKDIKFVCIISAPEGIETLRNSHPDVDIYTAAIDERLNDHGYIIPGLGDAGDRLFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | B5YDB8 |
O13489 | TRI5_PARRD | Sesquiterpene cyclase | Paramyrothecium | MDEFPTEYFLGTAVRLLENVKYRDSNYTREERIENLSYANNKAAAHFAQERQQRILKVNPKRLEASLRTIVGMVVYSWVKVSKELMADLSIHYTYTLILDDSEDDPHNNMLTFFDDLQAGREQKHPWWMLVNEHFPNVLRHFGPFCSLNLIRSTLDFFEGCWIEQYNFHGFPGSYDFPGFLRRMNGLGHCVGGSLWPKELFDEQKHFLEITSAVAQMENWMVWVNDLMSFYKEFDDPRDQTSLVKNYVVCDEISLTQALEKLTVDTLTSSEQMMEVFSDKDAKLMETIECFMHGYITWHLCDHRYRLKEVYEGTMHIETEDAIKFRKFYGQAAKVGAIEHEEWAFPTVAERIEVRLAEEKAAKDGQAVLTSAEPAVPQAAQEVLA | TS is a member of the terpene cyclase group of enzymes. It catalyzes the isomerization and cyclization of farnesyl pyro-phosphate to form trichodiene, the first cyclic intermediate in the biosynthetic pathway for trichothecenes. It serves to branch trichothecene biosynthesis from the isoprenoid pathway. | O13489 |
P42883 | THI12_YEAST | Thiamine pyrimidine synthase | Saccharomyces | MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDMAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPRLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA | Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. | P42883 |
Q9VYY3 | UBA5_DROME | UFM1-activating enzyme | Sophophora | MSHAIDELQAIIADLKTELETEPKSSGGVASNSRLARDRIDRMSAEVVDSNPYSRLMALQRMNIVKDYERIRYKAVAIVGVGGVGSVTADMLTRCGIGKLILFDYDKVELANMNRLFFTPDQAGLSKVAAAAATLSFINPDVEIETHNYNITTVENFDRFLDTISQGGRIAGQPVDLVLSCVDNFEARMAINAACNERNLNWFESGVSENAVSGHIQFIRPGDTACFACAPPLVVAENIDEKTLKREGVCAASLPTTMGITAGFLVQNALKYLLNFGEVSDYLGYNALSDFFPKMTLKPNPQCDDRNCLVRQKEFQARPKPVLIEEKAVSEEPLHATNEWGIELVAEDAPESNTTPAETPVMGEGLRLAYEAPEKSSETSEETVSAATADETSLEDLMAQMKSM | E1-like enzyme which activates UFM1. | Q9VYY3 |
Q491Y3 | TPIS_BLOPB | Triose-phosphate isomerase | Candidatus Blochmannia | MRRLLIIGNWKLNGNKNTITNLIITLVNTFYNISKCNVAIAPPVMYLDITKRYLLNSRIQLCAQNVDIHLSGSFTGDISAEMLQDLNVRYALIGHSERRIHHKENDAYIAKKFFILKKVGLIPILCVGENKREYDSGYTQSVCINQINTIITLLGIEAFKNSVIAYEPIWAIGSGASASPENAQLVHKSIRDYIASYDTSIADKITIQYGGSVTPENVTKFFDQKDIDGVLVGAASLNANSFSMIVQTAENHKKSYPA | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q491Y3 |
A1VYG9 | THIC_CAMJJ | Thiamine biosynthesis protein ThiC | Campylobacter | MKTQMNYAKEGIFTKEMQIVAQKENLSKDFLLENIACGKIIIPANINHKSLDPNGIGFGLRTKVNVNLGVSNDCVDYSEEMKKVELAHKFGIEAIMDLSNYGKTSRFRDELVNVSKAMIGTVPVYDAVGFLEKDLKQINAKDFLDVVYHHAKSGVDFMTIHAGINSRAAHIFKQSKRLTNIVSRGGSVLYAWMMMKDAENPFFEYYDDLLDICLKYDVTLSLGDALRPGSTHDASDGAQISELIELSLLTQRAWDVGIQVMIEGPGHMAINEIEANMQLEKRLCKGAPFYVLGPLVIDIGAGYDHISGAIGGAVAAASGADMLCYVTPAEHLRLPNLEDVREGIVATKIAAHAGDIAKLPKERARDDEMSKARQEIDWEKMFKLAIDGEKAKKMFNERRPDDLNSCSMCGKMCAMNTMNQILKGEDVSLA | Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. | A1VYG9 |
B2SIG7 | TTCA_XANOP | tRNA 2-thiocytidine biosynthesis protein TtcA | Xanthomonas | MTAVLPLPHPLADPAPRDPRQRLQREQLRLGKRLQRQVGQAIADFGMISPGDKIMVCLSGGKDSYTMLDMLLQLQRKAPVPFTLVAVNLDQKQPDFPAHVLPAYLDALGVPFDIVEQDTYSVVSRVVPAGKTMCSLCSRLRRGALYAYAQTHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREAHIAAYAQARQFPIIPCNLCGSQENLQRQQVGKMLQQWDHEQPGRVEQIARALGDVRPEQLADRTLFDFLALGRSGDAPPDLAPDPGAWLTASDATHDSD | Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. | B2SIG7 |
Q6GJQ9 | XPT_STAAR | Xanthine phosphoribosyltransferase | Staphylococcus | MELLGQKVKEDGVVIDERILKVDGFLNHQIDAKLMDEVGRTFYEQFKDKGITKILTIEASGIAPAIMAALHFDVPCLFAKKAKPSTLTDGYYETSIHSFTKNKTSTVIVSKEFLSEEDTVLIIDDFLANGDASLGLYDIAQQANAKTAGIGIVVEKSFQNGHQRLEEAGLTVSSLCKVASLEGNKVTLVGEE | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | Q6GJQ9 |
B9KNX7 | TRMD_CERSK | tRNA [GM37] methyltransferase | Cereibacter | MLKGAWQARIVTLFPEAFPGTLGLSLTGKALEMGLWSLETIDLRPFGEGRHRNVDDNPAGGGAGMVLRADIVARALDAASVGTPSERSRWPVVYLSPRGKPFSQAMARDWAGAEGLTLLCGRFEGVDQRVLDAYAVEEVSLGDFVLTGGEIAAQALIDATVRLIPRVLGNHASTEEESFSEGLLEFPQYTRPTVWQDRTIPEVLLSGHHANIARWRRAEAERLTKERRPDLWRAYCAARGRDPDEDREL | Specifically methylates guanosine-37 in various tRNAs. | B9KNX7 |
P75291 | ULAA_MYCPN | Ascorbate-specific permease IIC component UlaA | Mycoplasma | MLNKIKLQQKRKLIIGWSVFALINLVVILLTVLLRAGLPNLVSKGVTPFSAQAFGDAFIFLITRVYLDNFLRQPALLLGVITLIGYLALGRGGVQSVVGALKTVIGFILLSIGSGVLVSTARPVFDTIKGLGGTGVVLLDPYFSLASANDFFTNSFLNNDYVSLIAFSLLVGFIVNIIFVGLKRWTNTNSIMVTGHVMLQQAAVVTTLFYIVLFRQIPLLGTGIAYGAQAGLVIISGIFLGVYWSTASTGTYLVTNKVTNNAGFSIGHQQMLGIMTVAKLGKYFGDKNDSAEHKKLPKALKIFEDNIFTQTIIILSLFVVLFIVILASYKGDKPLLINWDKFGAINGLEIWNTTFGGANFTLNIIGGALKMVASLIAIMTGVRMFITELQQAFQGISEKVVPGAVVAVDIAAVYGFSINSVTFGFLSGVIGQFLAVAIMAGISYIPGNQFSFVAIPLFITLFFNSGAFGVYANAEGGWKAALLLPGIIGFLEIIVISFALRTVSNAYQASALLDAKQSFDLKALMGNSLDNNNGSALKTAVEKVVNATGVNRITEAQSFVKSDSFNSLKAVNSTLAQAIEWISKSASPVDNGFIGMADWNLYFGLLVWIGAYNVIGGWILVILATVGLILLAQIIDNGKQTKVTKLQQLLKINPQLDLNN | The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. | P75291 |
G3Y422 | YAND_ASPNA | Yanuthone D biosynthesis cluster protein D | Aspergillus subgen. Circumdati | MVKFFQPKIDPLPTGIDLTGKTAVITGASAGMGLEVTKQLLRLRLSTAILAVRNVTKGEACIKSLLQDRGIQTHNPKPTIKVMELDMDRYDSVQQFAKTLREEVPVVDLLILNAGVASLNFERSPSGHERVTQVNYCSNVLLVAELLPHLEAGAEQTGSPARISWVGSRSHETPSFEKKAPIEADEGVLEHMDKEEAFVPFQRYNDTKLLCVLFLYSLAPRLDPKKVVINTMCPGMVNTGMSNMLPLHLRLIFNVIKAIRARPVEVGGWIILNAALVAGPESHGKFLADKTITDKSAIVTSPMGQDIQKKLWEETITEMSKLTTLPPQFR | Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of yanuthone D, a fungal isoprenoid epoxycyclohexenone that acts as an antibiotic against fungi and bacteria . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase yanA . 6-MSA is then converted to m-cresol by the decarboxylase yanB . The cytochrome P450 monooxygenase yanC then catalyzes the oxidation of m-cresol to toluquinol . Epoxidation of toluquinol is then performed by the short chain dehydrogenase yanD, with the help of yanE, and a further prenylation by yanG leads to 7-deacetoxyyanuthone A . The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase yanH to yield 22-deacetylyanuthone A . O-Mevalon transferase yanI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E . Finally, the FAD-dependent monooxygenase yanF oxidizes the hydroxyl group at C15 of yanuthone E to form yanuthone D . Furthermore, several branching points in the pathway lead to the production of yanuthones F and G from 7-deacetoxyyanuthone A; yanuthones H and I from 22-deacetylyanuthone A; and yanuthone J from yanuthone E . YanD is also involved in the synthesis of yanuthone X1 which does not have 6-methylsalicylic acid (6-MSA) as precursor . | G3Y422 |
B2U0F2 | TRPB_SHIB3 | Tryptophan synthase beta chain | Shigella | MTTLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNYAGRPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMGKTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLMGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVCEFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETNVGLIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEDGQIEESYSISAGLDFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHALAHALKMMRETPEKEQLLVVNLSGRGDKDIFTVHDILKARGEI | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | B2U0F2 |
Q96NJ3 | ZN285_HUMAN | Zinc finger protein 285A | Homo | MIKFQERVTFKDVAVVFTKEELALLDKAQINLYQDVMLENFRNLMLVRDGIKNNILNLQAKGLSYLSQEVLHCWQIWKQRIRDLTVSQDYIVNLQEECSPHLEDVSLSEEWAGISLQISENENYVVNAIIKNQDITAWQSLTQVLTPESWRKANIMTEPQNSQGRYKGIYMEEKLYRRAQHDDSLSWTSCDHHESQECKGEDPGRHPSCGKNLGMKSTVEKRNAAHVLPQPFPCNNCGVAFADDTDPHVHHSTHLGEKSYKCDQYGKNFSQSQDLIVHCKTHSGKTPYEFHEWPMGCKQSSDLPRYQKVSSGDKPYKCKECGKGFRRSSSLHNHHRVHTGEMPYKCDECGKGFGFRSLLCIHQGVHTGKKPYKCEECGKGFDQSSNLLVHQRVHTGEKPYKCSECGKCFSSSSVLQVHWRFHTGEKPYRCGECGKGFSQCTHLHIHQRVHTGEKPYKCNVCGKDFAYSSVLHTHQRVHTGEKPYKCEVCGKCFSYSSYFHLHQRDHIREKPYKCDECGKGFSRNSDLNVHLRVHTGERPYKCKACGKGFSRNSYLLAHQRVHIDETQYTHCERGKDLLTHQRLHEQRETL | May be involved in transcriptional regulation. | Q96NJ3 |
A4VZL1 | TRHO_STRS2 | tRNA hydroxylation protein O | Streptococcus | MSKDIRVLLYYKYVPIENAKEYAAEHLAFCKSIGLKGRILIADEGINGTVSGDYETTQKYMDYVHANPLFSDLWFKIDEENEQAFKKMFVRYKKEIVHLGLEDNDFDNDIDPLVTTGAYLSPKEFKEALLDEDTVVLDTRNDYEYDLGHFRGAIRPDIRNFRELPQWVRDNKEKFMDKRVVVYCTGGVRCEKFSGWMVREGYKDVGQLHGGIATYGKDPEVRGELWDGKMYVFDERIAVDVNHVNPVVVGKDWFDGTPCERYVNCGNPFCNRRILTSEENEHKYVRGCSAECRAHERNRYISENGLTRQEWAERLEAIGETLTPANA | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | A4VZL1 |
Q54F34 | Y1141_DICDI | Probable zinc transporter protein DDB_G0291141 | Dictyostelium | MAGSLDDSIYNNGRSGGGGGGFKFSKGFNKDSISKRIIMMLFFSKGIRAWSCIILLYFLQSSISIISASFYMCLFSAIFSVVVEKPWNLLSSLRPSQIKKIIYHSIFNLLIIITWNSSIKFIGPIGSILASDYTFSTYPLIFNSLLQGNFLATDMSRGSIMLMIGYFLIPLFGISNRLDILGYTSSQVFMIGLFSLIVHNVLVLWKKTIVRSWNSGSSGGKNKLSSLGSCVSTIILFVFKLFEGFSSGSSGSDSINQVSYSQLFVIAIITFILYSLNQFIDDVSEKELTFNVLSKVSLTSSVIFGLLAALFIGFKDFFHPILILSFIFIINAIHILYSKSNDIQPMTFSNNMDGGNSSIKTYNSSGGGGGGSIINGNGSGNAIYYFEILKDVLRQIVDKPTSRRIFTFLVINLMFMFVEMAYGIWTNSLGLITDACHMFFDATALFIALVAEVISQWKQNDKYSYGYGRFQVLSGFVNGIFLIFIAVTILMESVERLLEPPEINTDKLLLVSVLGFIINLIGIFSFHGDHGHSHGGGGGHSHGGGEKKEKHHGHSHGGHGDHQQVTPILGEEKKKKRSVNIDGVFLHLLADTLGSVGVIVSSLIIQIWGYTLADPICSLLISILIFLSVLPLIANTAKTLLQCTPEPIQSSLYQINQFILSIDGVHNIISYHFWSHYDDMNIATLKIQLNETASSNSTLDTERIKKSISKYLNKDHNIHKCIIEFIPLLYNNNNQQQGNDVPLINHHIHNDIHHNHSSSSSSSSHHHRHN | May be involved in zinc transport from the cytoplasm to either intracellular organelles or extracellular spaces. | Q54F34 |
Q04BH0 | TPIS_LACDB | Triose-phosphate isomerase | Lactobacillus | MSRTPIIAGNWKLNMNPKETVEFVNAVKDQLPDPSKVESVICAPAVDLDALLKAAEGSNLHVGAENCYWENSGAFTGETSPAVLKEMGVQYVIIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETREAGKENEWVVSQIKAGLEGLTSEQVSKLVIAYEPIWAIGTGKTASSDQAEEMCKTIRETVKDLYNEETAENVRIQYGGSVKPANVKELMAKPNIDGGLVGGASLVPDSYLALVNYQD | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | Q04BH0 |
P59783 | YIDC_SHIFL | Membrane protein YidC | Shigella | MDSQRNLLVIALLFVSFMIWQAWEQDKNPQPQAQQTTQTTTTAAGSAADQGVPASGQGKLISVKTDVLDLTINTRGGDVEQALLPAYPKELNSTQPFQLLETSPQFIYQAQSGLTGRDGPDNPANGPRPLYNVEKDAYVLAEGQNELQVPMTYTDAAGNTFTKTFVLKRGDYAVNVNYNVQNAGEKPLEISSFGQLKQSITLPPHLDTGSSNFALHTFRGAAYSTPDEKYEKYKFDTIADNENLNISSKGGWVAMLQQYFATAWIPHNDGTNNFYTANLGNGIVAIGYKSQPVLVQPGQTGAMNSTLWVGPEIQDKMAAVAPHLDLTVDYGWLWFISQPLFKLLKWIHSFVGNWGFSIIIITFIVRGIMYPLTKAQYTSMAKMRMLQPKIQAMRERLGDDKQRISQEMMALYKAEKVNPLGGCFPLLIQMPIFLALYYMLMGSVELRQAPFALWIHDLSAQDPYYILPILMGVTMFFIQKMSPTTVTDPMQQKIMTFMPVIFTVFFLWFPSGLVLYYIVSNLVTIIQQQLIYRGLEKRGLHSREKKKS | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | P59783 |
Q98Q98 | TRMD_MYCPU | tRNA [GM37] methyltransferase | Mycoplasmopsis | MLKINFLTIFPKYFDCFLKESIIGKAIERKKISINVIDFREFSENKHKKVDDSVYGGGQGMLLQVQPIAKALKTLKGLKILVSPQGKLFNQEIAKEIVKNHSEITFVSGRYEGFDERILNYIDIELSIGDYILTGGELPSMVMADSIIRLWEDVIKKESYENESFENNLLDYPQYTRPRVFEGFEVPEILLNGNHKEIEKWRKQKQIEKTKINRPDLYERFKNEK | Specifically methylates guanosine-37 in various tRNAs. | Q98Q98 |
Q7VPM2 | YIDC_HAEDU | Membrane protein YidC | Haemophilus | MNSNRSLLVMGLLLVSFLIFTQWQQDFNPEIQAQKQAQQQSRDVPHATNTANAITEHMTKGKTITVESDVLRLVIDTLGGDVIESDLLAHKASLDSTDPLKLLTTEGLIYTAQSGLVGKNGIDTHIGRAPYQVTQDHFTLAKGQNEIVVPMTFEQDGVMYTKTFTLKRGSYDVAVSFDIQNNSANTIEVQPYGQIKHSLLDSSGNLAMPTYTGGAYSSSETNYKKYSFDEMTKANLNIDTKGGWVALLQHYFVSAWVPNQDASNTLYSRTHNGVATIGYRGPITTVKPNTKTTITSQLWTGPKDQKEMAQAATHLELTVDYGWAWFIAKPLFWLLIFIHSIIGNWGLAIMGVTLVVKSLLYPLTKAQYTSMAKMRMLQPKLQELRERYGDDRQQMSQEMMKLYKQEKVNPMGGCLPLILQMPIFIALYWTFMEAVELRHAPFFGWIQDLSAQDPYYIFPVLMGLSMFLLQKMSPTAVADPTQLKVMTFMPVIFTVFFLWFPSGLVLYWLTSNCITIVQQWLIYRNLEKKGLHTRKK | Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins. | Q7VPM2 |
B1W5H1 | UREG1_STRGG | Urease accessory protein UreG 1 | Streptomyces | MTRTPTGVPMHLGHTHDAPAAVSADATRPDGTRRALRIGLGGPVGSGKTATVAALCRELRDRLSIAVVTNDIYTREDADFLLKNAVLPPERIQAVETGACPHTAIRDDISANLEAVEDLEDAVGPLDLILVESGGDNLTATFSKGLVDAQIFVIDVAGGDDIPRKGGPGVTTADLLVVNKTDLAPYVGSDLERMALDAKKQRGDLPVAFTSLTSAEGVGPVADWVRAQLAAWAA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | B1W5H1 |
B4TQK0 | THIG_SALSV | Thiazole synthase | Salmonella | MLRIADKTFNSHLFTGTGKFASSQLMVEAIRASGSQLVTLAMKRVDLRQHNDAILMPLIEAGVTLLPNTSGAKTAEEAIFAAQLAREALGTHWLKLEIHPDARWLLPDPIETLKAAEALVKQGFVVLPYCGADPVLCKRLEEVGCAAVMPLGAPIGSNQGLETKAMLEIIIQQSTVPVVVDAGIGVPSHATQALEMGADAVLVNTAIAVADDPVMMATAFRLAVEAGVLARQAVPGNRSPYASATSPLTGFLEALA | Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. | B4TQK0 |
Q8NB15 | ZN511_HUMAN | Zinc finger protein 511 | Homo | MQLPPALCARLAAGPGAAEPLPVERDPAAGAAPFRFVARPVRFPREHQFFEDGDVQRHLYLQDVIMQVADVPEKPRVPAFACQVAGCCQVFDALDDYEHHYHTLHGNVCSFCKRAFPSGHLLDAHILEWHDSLFQILSERQDMYQCLVEGCTEKFKTSRDRKDHMVRMHLYPADFRFDKPKKSRSPASAEAPGDSGERSEGEAMEICSEPVAASPAPAGERRIYRHRIPSTICFGQGAARGFKSNKKKTKQC | May be involved in transcriptional regulation. | Q8NB15 |
Q11DI2 | TOLB_CHESB | Tol-Pal system protein TolB | unclassified Chelativorans | MRNFFKTAVAITSLVMGLVAMAVVPARALVEIDVNRGVVEPVPIAITDFLSAGGRGAEISAVIAADLKRSGLFAPIDRGAFIEKISNPDVAPRFEDWKVINAQAIVTGRVTEEPGGRLKAEFRLWDTFAGQQLVGEQFFAKPADWRRVAHIIADTIYEQFTGEKGYFDSRIVFVDESGSKENRVKRLAIMDQDGANYRALTDGRSIVLKPSFSPQRQEITYVSFEGGQPQVYLLQIETGQRELVGNNFPTMSFASRFNPVGDKIIMSLLRTDGNSNIYTMDLKTRTTARLTDTNAIDTSPSYSPDGNKVVFTSDRGGRAQIYVMNADGSNPQRISFGDGTYSEPVWSPRGDLIAFTKQSGGQFQIGIMRTDGSGERILSTGFQIEGPTWSPNGRVIMFFRQDAGAAGPKLYSIDLTGRNEQLIPTPNFASDPAWSPLLN | Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. | Q11DI2 |
Q8U0J5 | TRPB2_PYRFU | Tryptophan synthase beta chain 2 | Pyrococcus | MKVVLPDGRIPRRWYNILPDLPEPLAPPLDPETNEPVDPKKLERIFAKELVKQEMSTKRYIKIPEEVRKMYSKIGRPTPLFRATNLEKYLNTPARIYFKFEGATVTGSHKINTALAQAYYAKKEGIERLVTETGAGQWGTALSLAGALMGIKVRVYMARASYEQKPYRKVLMRIYGAEVFPSPSENTEIGKRFLSENPNHPGSLGIAISEAIEDVLKDEKARYSLGSVLNHVLMHQTVIGLEAKQQMEEFEEPDVIIGCVGGGSNFAGLAYPFVKEVLDGDNEYEFIAVEPKAAPSMTRGVYTYDFGDSGELTPKLKMHTLGHRYHVPPIHAGGLRYHGVAPTLSVLVNNGIVKPIAYHQTEVFEAAALFAKLEGIVPAPESAHAIKATIDKAIEAKREGKEIVILFNLSGHGLLDLHGYEEYLEGRLQDYEPKDLPISNPLNPKP | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | Q8U0J5 |
A7GTW9 | TRMB_BACCN | tRNA(m7G46)-methyltransferase | Bacillus cereus group | MRLRHKPYAMDRIKEYSQFVIGNPEEHRGNWKELFGNDHPIHIEVGTGRGRFVYEMAKANPDINYIGIEKFTSVIVDALDKLIEKELPNLKLINKDAEDLTVFFTKGEIDRVYLNFSDPWPKKRHAKRRLTYKTFLRNYEEVLVKDGEIHFKTDNQALFEYSLMSMAEYGMVFTFLSLDLHNSDFEGNIMTEYEEKFSSKGHRIYRVEAKYRTEPVQ | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | A7GTW9 |
Q3AX81 | TRHO_SYNS9 | tRNA hydroxylation protein O | unclassified Synechococcus | MSRLQVAAFYAFTPLNEQQRASLLSDLPDMAMTNSVLGSILVAHEGVNGTISGPEAGVEALLQSLRTSLALGCEHFERLEVKRSWADQAVFRRFKARAKKEIVTMGVTSVNPRQNVGTYVDPKDWNDLVDDPDTLVIDTRNSYETAIGSFEGSLDPSTESFRDFPAWAEASLRPLMNDQSPKRIAMFCTGGIRCEKASSYLQSNGFGEVLHLRGGILNYLGEIPEQESRWQGECFVFDQRVALNHQLEPGVHSLCHACGLPLSPSDRADPSYIKGVQCIHCIDRFSESDRARFLMRQQQFDQTPT | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q3AX81 |
Q39QP4 | TATA_GEOMG | Sec-independent protein translocase protein TatA | Geobacter | MFGIGMPELIVILVIVLVVFGAGRLPEIGGALGKSIRNFKKASDGKDEIEIKPEKKDDPSK | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | Q39QP4 |
Q10953 | WRM1_CAEEL | Worm armadillo protein 1 | Caenorhabditis | MDVDCAETFSQPCTPLNFNPMTPSTSRVSTPVRPSSTMSARQYSGSPFKAQPQNMEPSNSRVQELREAAVGKRSYTNAWMQGTYAPPQMAGQQQRFSRPPSVIGSTMSHMTNMSEMTAYSYGGLSMLSVNTEMGEFNNFVNQAPYQRALTRVSQVSENQDPTNRQYPMTAPEIIENLESTELINQAAAIRALEPIVKAGGMLQTWGPKGAEPIIRALFQVLIPRPVENENVIRKAFEILHHSILLSNKEIRRIDRMFFRLNAALMDPNGPPVFNVPKPYSIYEIVMTRAIQLDTKFESSAMVLLVHLCCKPHFMKIFFGEDETQQSPAHRRLHKIVIEFAIGNLRRPETKSKNKGLCVSIIKNLSNKNATIKDMSERLGVVSLFHQIMQNEVIHEDLLWSTMQALTVFCGDVKNGTHFVQMGGAQVLCGLLSHGSTRLLHELLKCLRRVSDLPAIQEQDMKESIHCIVQLIGCSDVTIVELATGTLRNIGLHNKMNKAFMVQDGVTSHAIAVLRTSEQFTYQPHANIDLYRKQILSIYENCLSVLNNVTSMAPQDIKESAVSACRMISENADSAYVLLHYFNVGNRKCRKLAVTVMKRVIETVPAFADPFVDLLGTTNEPLPILLLQRAFQSLDEWRKTSVEMMNCDGRSAEQRRELDDRRKDHEDIVKRSVGLLTNLCSQANPRFFHSLKLVLTNGTLNPFQWLTHEMSDGILQEWLAFILSICSRDESLQTFMMYRFLEQAKMTEAFFAELKARRQNSNIQTMLSKIIDLGRHQQRIVSQQHQQHQMQHHRQLM | Antagonistic role in the Wnt signaling pathway that operates in embryogenesis. When located at the cortex it has been shown to inhibit Wnt signaling during asymmetric cell division but when relocated to the nucleus it shows positive regulation. Has a role in blastomere signaling during endoderm specification. Component of the beta-catenin-lit-1 complex which promotes phosphorylation, down-regulation and subcellular relocation of pop-1 . Within the complex, activates lit-1-dependent kinase activity . Can substitute for bar-1 indicating functional redundancy. Appears to have a role in centrosome positioning and can activation transcription in yeast. Involved in the development of distal tip cells (DTC) by regulating the asymmetric distribution of cye-1 and cki-1 between the daughters of Z1.a and Z4.p cells . | Q10953 |
Q1BYC0 | UBID_BURCA | Polyprenyl p-hydroxybenzoate decarboxylase | Burkholderia cepacia complex | MKYKDLRDFIQRLEALGELRRVTQPVSPVLEMTELCDRVLRAGGPALLFNAPPGNAFPVLGNLFGTPRRVALGMGVDAGDDAALGSLRDLGRLLSALKEPDPPKSLKDAGKLLSLAKAVWDMAPKSVSSPPCQEIVWEGADVDLNKLPIQTCWPGDAGPLVTWGLTVTRGPNKSRQNLGIYRQQLIGRNKLIMRWLAHRGGALDFREFALQNPGKPYPVAVVLGADPATTLGAVTPVPDSLSEYQFAGLLRGSRTELAKCLTPGVDTLQVPARAEIVLEGFIHPQEGAPAPAPAGAPPRPAGNAAAAYEHALEGPYGDHTGYYNEQEWFPVFTVERITMRRDAIYHSTYTGKPPDEPAVLGVALNEVFVPLLQKQFTEITDFYLPPEGCSYRMAIVQMKKSYAGHAKRVMFGVWSFLRQFMYTKFIVVVDEDVNIRDWKEVIWAITTRVDPVRDTVMVDSTPIDYLDFASPVAGLGSKMGLDATNKWPGETSREWGRPIEMDAAVKARVDRLWQEIGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | Q1BYC0 |
O43298 | ZBT43_HUMAN | ZnF-x | Homo | MEPGTNSFRVEFPDFSSTILQKLNQQRQQGQLCDVSIVVQGHIFRAHKAVLAASSPYFCDQVLLKNSRRIVLPDVMNPRVFENILLSSYTGRLVMPAPEIVSYLTAASFLQMWHVVDKCTEVLEGNPTVLCQKLNHGSDHQSPSSSSYNGLVESFELGSGGHTDFPKAQELRDGENEEESTKDELSSQLTEHEYLPSNSSTEHDRLSTEMASQDGEEGASDSAEFHYTRPMYSKPSIMAHKRWIHVKPERLEQACEGMDVHATYDEHQVTESINTVQTEHTVQPSGVEEDFHIGEKKVEAEFDEQADESNYDEQVDFYGSSMEEFSGERSDGNLIGHRQEAALAAGYSENIEMVTGIKEEASHLGFSATDKLYPCQCGKSFTHKSQRDRHMSMHLGLRPYGCGVCGKKFKMKHHLVGHMKIHTGIKPYECNICAKRFMWRDSFHRHVTSCTKSYEAAKAEQNTTEAN | May be involved in transcriptional regulation. | O43298 |
C4ZA66 | XPT_AGARV | Xanthine phosphoribosyltransferase | Lachnospiraceae incertae sedis | MKELQDRILKDGQVIGTNILKVNKFINHQVDPVLMEHIGEDFANHFADKGITKVVTIESSGIAPALMAAAKMNVPLVILKKQPSKTLHNDLYQTQVTSFTTEKSYELTLSRDVISEDDNILLIDDFMADGEAATGAIRLLRMAHATVAGIGILIEKSFQPGRRKINEQGYEVYSLARIKYMDEYQIDFIEEN | Converts the preformed base xanthine, a product of nucleic acid breakdown, to xanthosine 5'-monophosphate (XMP), so it can be reused for RNA or DNA synthesis. | C4ZA66 |
Q6AFR0 | TRMB_LEIXX | tRNA(m7G46)-methyltransferase | Leifsonia | MEPAPLVRPRSYVVRGRKTDAQQRAIAEFWPAFGVDFAGGLLDLDALFGRTAPRTVEIGFGNGENLLALAERHPERDFLGVEVHGAGVGRVFAAMRERGLSNIRVIRHDAVEVFETGLSAGSVAEALLFFPDPWPKARHHRRRLVQPDVVRLLARALAADGVLRLATDWEPYADHMLAVLDAEPVLVNVAGPGAFIPRPEARPVTKFERRGEKLGHSIFDLEYRPLP | Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. | Q6AFR0 |
P31863 | TBB2_HYPRU | Beta-2-tubulin | Trichoderma | MREIVYIQTGQCGNQIGAAFWQTISGEHGLDSNGIYNGSSELQLERMNVYFNEASNNKYVPRAVLVDLEPGTMDAVRAGPFGQLFRPDNFIFGQSSAGNNWAKGHYTEGAELVDQVLDVVRREAEGCDCLQGFQITHSLGGGTGSGMGTLLLSKIREEFPDRMMATFSVVPSPKVSDTVVEPYNATLSVHQLVENSDETFCIDNEALYDICMRTLKLNNPAYGDLNYLVSAVMSGITTCLRFPGQLNSDLRKLAVNMVPFPRLHFFMVGFAPLTSPGAHSFRAVTVPELTQQMFDPKNMMAASDFRNGRYLTCCSIFRGKVAMKEVEDQMRNVQNKNSTYFVEWIPNNIQTALCAIPPRGLKMSSTFIGNSTSIQELFKRVGEQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAGIDEEEEYEDEAPMEAEE | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | P31863 |
Q9SUE0 | YMG12_ARATH | YGGT family protein YLMG1-2 | Arabidopsis | MASFTTNSLALRASILANPRLPPPIIRPRLSLPRKLSFNLSLHNARTIVSSAVTSSSPVLSSKPPSQFPFSDSTRSITTLVLLAGVVIKSLIQKLSVAIVNLSPQIQASFRTASPLFFASLRDRPAGYLNTPLTVVAAGLSKWLDIYSGVLMVRVLLSWFPNIPWDRQPLSAIRDLCDPYLNLFRNIIPPVFDTLDVSPLLAFAVLGTLGSILNNSRG | Not required for the biogenesis and accumulation of native cytochrome b6 in the thylakoid membrane. Not functionally involved in the pathway for covalent binding of the c-type heme to cytochrome b6. | Q9SUE0 |
B3QXJ6 | TRMD_CHLT3 | tRNA [GM37] methyltransferase | Chloroherpeton | MRVDIISVLPDFFDSPLANGLLRIAREKQRLQLHVHSLREYGLGKYKQVDDTPFGGGAGMVLRVEPVFACIEKLKADRDYDEVIFFTPDGKQFNQSEANRHALDRNLILLCGHYKAIDERIRETLITKEISLGDFVLSGGELPALIFLDSVARLLPGVLHDEESMLTDSFQDGKLDCAHYTRPSEFRGMKVPDVLLSGNHKKIEEWRLENAIERTRQRRPDLLKDINL | Specifically methylates guanosine-37 in various tRNAs. | B3QXJ6 |
Q9RDV3 | TRMD_MYCGA | tRNA [GM37] methyltransferase | Mycoplasma | MKIVVLTLFDDFVRSYYDFSIIKNALDKKAVELEVINFRQYANDKHKTVDDTIYGGSAGMLLKLEPLVNCLRDIKQNQFKDPNKIRTYLLSPQGEVYDQNKAVALSQSDHDLILIAGRYEGFDERIYHYVDGALSVGDFVITGGELAALIVVDSIVRLLPNVINKDSLSSESFNNYLLDYPMYTKPYDFEGYKVPDVLLSGNHQAIAAFNQQEAINNTKMKRPDLYLKYKSNLK | Specifically methylates guanosine-37 in various tRNAs. | Q9RDV3 |
Q8GBB2 | TRMI_THET2 | tRNA(m1A58)-methyltransferase | Thermus | MAWPGPLLLKDRKGRAYLVFPKEGGVFHHHKGSVPHEALLEAGPGGVVRTHLGEELSVHRPTLEEYLLHMKRSATPTYPKDASAMVTLLDLAPGMRVLEAGTGSGGLTLFLARAVGEKGLVESYEARPHHLAQAERNVRAFWQVENVRFHLGKLEEAELEEAAYDGVALDLMEPWKVLEKAALALKPDRFLVAYLPNITQVLELVRAAEAHPFRLERVLEVGWREWEVRLPVAHPRFQQVGHTAFLVALRRWKAS | Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 58 (m1A58) in tRNA. Is required for cell growth at extreme temperatures. | Q8GBB2 |
Q4WHN8 | VPS27_ASPFU | Vacuolar protein sorting-associated protein 27 | Aspergillus subgen. Fumigati | MAGWFSSTSPLDEQVERATSSSLEDMALNLEISDLIRSKSVQPKEAMRSLKRRLENRNPNVQIATLKLTDTCVKNGGSHFLAEIASREFMDNLVSLLTTEGAPLNTDVKEKMLELIQDWAMAAQGRMDLNYLGETYRKLQNEGFRFPPKNEISGSMLESSAPPEWIDSDVCMRCRTPFSFMNRKHHCRNCGNVFDAQCSSKTLPLPHLGILQPVRVDDGCYVKLTSKSSLPSNLSDRSAFKNHSITKANAMEPRGARAEGGFDDDLRRALQLSLEEAQSKGSSGYVPSTRINDEPAKTTTQTNHEEEEDADLKAAIEASLRDMEEHKKKHAAALKSNAAATDSSTRDSAAATPLPKNPYELSPVEVENIHLFAALVDRLQHQPPGTILREPQIQELYESIGALRPKLARSYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSSAYSQHSLGYATAPGGSPYPNIYPTMPSHIPEGKTGAENFYYGNPVADRAPPVGNTYGYPHSSRDIREPTAAPSGPISSGVYNQPGQAVPQNPPWNGNAPSVASPQPSAPSTPFPNNSSGYPGPSASTQYYASAPHPEQDSNAYSGPRPGETDVSHQSSPNMRRDSYYQSAGAPVTARASAPEQSPPTDQGQSPAYMQYGDSHSAQSTGQPTHQHQPTAPPPQSYYFQHQPPQSAPLPTHSQTPGAPYGTYPGGDVSPIGAPAPAVHYQPAAQTKPAVEESLIEL | Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane. | Q4WHN8 |
Q3AJ48 | TRHO_SYNSC | tRNA hydroxylation protein O | unclassified Synechococcus | MNPSNLEPGLANDSRLLVAAFYAFTPLDDERRETLLSSLPTLARNGSVLGSVLVAHEGVNGTISGPESAVDAVLDHLRTSFDLGDEHYARLEVKRSWAEKPVFRRFKARRKKEIVTIGVASVDPSTSVGTYVEAEHWNALVDDPDTLVIDTRNSYETAIGTFEGAIDPSTESFRDFPQWAESTLRPLIEQKSSKRIAMFCTGGIRCEKASSYLQQQGFGEVHHLRGGILKYLEQVPEAESRWQGECFVFDQRVALNHQLEPGEHSLCHACGLPVSAQQRELPSYIKGVQCLHCVDRFSDADRERFAMRQRQIDQRQIEQHKINRQQG | Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs. | Q3AJ48 |
Q31JQ7 | TSAC_HYDCU | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Hydrogenovibrio | MNCPLLTIKAAAKLITEGGVLAYPTEAVYGLGCDPLNKDAFQQLLRLKQRPLEKGVILIASSIAQIEPFVKLHNQAWTEKVLASWQVLNQPVTWVLPATDNVPEWITGGRNTVAVRVTQHPDVMALCNQLNFPIVSTSANLSGEDPVTTMEACCKAFPALAIMQGNLMGISAPSQIWEAQTQKRLR | Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Catalyzes the conversion of L-threonine, HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as the acyladenylate intermediate, with the release of diphosphate. | Q31JQ7 |
Q17VS4 | UREE_HELAH | Urease accessory protein UreE | Helicobacter | MIIERLTGNLRDLNPLDFKVDYVDLEWFETRKKIARFKTRQGKDIAIRLKDAPKLGLSQGDILFKEEKEIIAINILDSEVIHIQAKSVAEVAKICYEIGNRHATLYYGESQFEFKTPFEKPTLALLEKLGVQNRVLSSKLDSKERLTVSMPHNEPNFKVSLASDFKVVMK | Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly. | Q17VS4 |
Q1AVV7 | YBEY_RUBXD | Endoribonuclease YbeY | Rubrobacter | MPFRVEVLNETSGGARLTPERATELCRRAFVERGLDPERMGELSVALVEPEVIHDLNLKFRNKDAPTDVLSFEVDGPYGEMVGEIVICPGCAEMDLEELVVHGALHLSGMDHGENFEASEMARVQKRVMEAVRGR | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q1AVV7 |
B9MDW9 | TATA_ACIET | Sec-independent protein translocase protein TatA | Diaphorobacter | MGSFSIWHWLIVLLIVVMVFGTKKLKNIGSDLGGAVKGFKDGMKDGASTDDSATTSAPAGQVTNNSAAADKTTIDVEAKHKS | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. | B9MDW9 |
Q6NDN5 | TRPA_RHOPA | Tryptophan synthase alpha chain | Rhodopseudomonas | MTTRIDTRFGELKQQGRPALVTFVMAGDPDLDTSLQILKVLPAAGADVIEIGMPFTDPMADGPAIQAAGLRALKAGTTLKKTLGLVRDFRATDNATPLVLMGYYNPIYIYGVDAFLADAKAAGVDGLIIVDLPPEEDEELCLPAMKAGLNFIRLATPTTDEKRLPAVLANTSGFVYYVSITGITGSASADASAVGAAVQRIKRHTNLPVCVGFGIRTPDAAQAIAAQANGAVVGSALIDALKASLNAEGRATKATVGAVADLVASLAAGVRGAKQAAE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | Q6NDN5 |
Q9VM35 | U2QL1_DROME | E2Q-like ubiquitin-conjugating enzyme CG4502 | Sophophora | MSSRSKERVVTAFRKIFHKSSNNNNNNNNNHNNNINNNNNNDKVDGATGSSPNINNNNNNNNNNNNHDGAAAPSSAGGVAVAGGAVGSSGSSGAAKNAVVRMAAEQAVWDSPGKRRRQDHKVAPTTERQLVAAPDHTIRTRRLMKEYREMERLQAKNDAVFTVELVNDSLFEWHVRLHVIDPDSPLARDMAEMGVPAILLHLSFPDNFPFAPPFMRVVEPHIEKGYVMEGGAICMELLTPRGWASAYTVEAVIMQFAASVVKGQGRIARKPKSTKEFTRRQAEESFRSLVKTHEKYGWVTPALSDG | Catalyzes the covalent attachment of ubiquitin to other proteins. | Q9VM35 |
Q5HTL6 | UVRC_CAMJR | Excinuclease ABC subunit C | Campylobacter | MIKENLENELKTLPNSAGVYQYFNQEGKLLYVGKAKNLKNRVKSYFAFTPNLHANPRNSLRIQKMIEETVHLEFIATNSEADALILENSFIKQLHPKYNILLRDDKTYPYIYVDFEEEFPRFEITRKLVKKSKIKYFGPFFKGARELLDALYLYYPLKQKASCKSPCIFYQISRCLAPCDKLISREKYLEILDEAIHALLNPSVLLKNLEKQMLVLAQNENYEEAAKVRDQIAMIKDLEVKVEIDIAKLEDFEVFALAFKNSVLSTLRFVVQNGKIISANSKITPIRNDIQWDQNEIYKQLILENFSMDIPLLANVIYVYEEFEDRVLLEEILSQRFDKKISIKIPKIGEKRRICDLAFQNALLNIEKEQKNHDFTIQKELKFYFELENLPNDIEIFDNSHLQGVANVGAMVTYRINSWDKSKYRKFHLKHKNDYDQMREVLTRRALDFDKIPPPDLWLIDGGKALLDLAKEIIVSSGANVDILAISKEKIDAKAHRAKGGAKDKIHSLKGEFSLSINDKKLQFLQKLRDEAHRFAISFHQNTKKKQDLKSSKLANLGLSSGVIQKLLAYYGNFESIYKADFKDLTMLVGRKAAQKIKEN | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q5HTL6 |
Q9P6R0 | TF3B_SCHPO | TFIIB-related factor | Schizosaccharomyces | MGCPNCGSTTFESDTASGNTYCTQCGVVVEQDAIVSEVTFGEASTGAAVVQGSLVSNDQTHARTFGGPYRNQGSVESRELTIANGRRRISALAIALKLNERHIEAAVRYFTLAINNNFIKGRRSQYVVASCLYIVCRISKTSHMLIDFSDILQINVFKLGSTFLKLCRVLRPNLPLLDPSLYISRFASLLEFGPETHRVANDAIRLVARMNRDWMQIGRRPAGICGACLLIAARMNNFRRSVREVVHVVKVADITIQKRLDEFKLTESGDLSIADFRNIWLEGQSDPPSFTKNQKFQQYGAQKVSNIDHTQEYMSPIKRTPDFDGNEVKSEELSQTVKVESQETPVHLKADEREIRKEVTETLKGDELRKISLQVNVKFSEEEVTLEDVDDDEIEDILLDKDEILTKTQVWMELNKDYLAEEEAKNLKLQEDLKKGIVRQPRKRRRYRPRDSTSDGIADTAAESAKEMMQQRAFSKKINYEALDMLFDEEQS | General activator of RNA polymerase III transcription. | Q9P6R0 |
Q6PEY2 | TBA3E_HUMAN | null | Homo | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY | Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. | Q6PEY2 |
P0CM61 | VAC8_CRYNB | Vacuolar protein 8 | Cryptococcus neoformans species complex | MGSALSSCCSPRRKNAYEPLLLETEREAVADLLQYLENRSTTNFFAGSPLAALTTLSFSENVDLQRSAALAFAEITEKEVREVGRDTLDPVLYLLSSHDPEVQRAASAALGNLAVNAENKLLVVSLGGLEPLIRQMLSPNVEVQCNAVGCITNLATHDENKTQIAKSGALVPLTRLAKSKDMRVQRNATGALLNMTHSDENRQQLVAAGAIPVLVSLLNSPDTDVQYYCTTALSNIAVDAANRKKLAQSEPKLVQSLVQLMDSQSLKVQCQAALALRNLASDSKYQLEIVKFGGLKPLLRLLHSSYLPLILSAAACVRNVSIHPANESPIIESGFLQPLIELLSFDENEEVQCHAISTLRNLAASSEKNKGAIVEAGAVEKIKSLVLTVPLAVQSEMTACVAVLALSDDLKPQLLEMGICEVLIPLTNSPSVEVQGNSAAALGNLSSKAAEDYAPFNAVWNKPDGGLHAYLVRFLSSADITFQHIAVWTIVQLLEAEDEQLTNNIRSSPILISSIRQLAKSPPPSRAGGAPRHDPNDPSAGSSEDEFEDGLTDQEGEGEIVSLARRILDLTEVGEEGDEFGERAGRNVPVGSHGQAPGQGQTSQVGSMGSEHAALRASVHRALSGGGRDR | Functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. | P0CM61 |
O67409 | TRPB2_AQUAE | Tryptophan synthase beta chain 2 | Aquifex | MRKFLLSEGEIPKKWLNILPLLPEPLEPPLDPETMEPVKPEKLLAIFPEPLVEQEVSDKEWIDIPEEVLDIYSLWRPTPLHRAKNLEEFLGTPAKIFYKNESVSPPGSHKPNTAVAQAYYNKISGVKRLTTETGAGQWGSALSFATQFFDLQCRVYMVRVSYNQKPYRRILMETWKGEVIPSPSPYTNAGRKYYEENPEHPGSLGIAISEAIEEAASREDTKYSLGSVLNHVLLHQTVIGLEAKKQMEEAGYYPDVIIGAVGGGSNFAGLSFPFLADVLRGDKRKEDLKVLAVEPEACPTLTKGEYKYDFGDSVGLTPLIKMYTLGHDFVPSPIHAGGLRYHGDAPLVCKLYNLGYIDAVAYKQTEVFEAAVTFARTEGIVPAPESAHAIKAAIDEALKCKETGEEKVILFNLSGHGYFDLSAYDKYLHGELTD | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | O67409 |
Q54VP1 | VPS55_DICDI | Vacuolar protein sorting-associated protein 55 homolog | Dictyostelium | MGHDIKGFSCAFAVGLLFNILACIVSHSGYPIIVVASYFLAPFPNILCRNRDSFSSEKGTFEDIGLFLTGLFITSGFAIPMILAHSDIISGKALAFSMAGGVTVYATIITFLWFFNRHNDEDNNW | Involved in endosomal protein transport. | Q54VP1 |
Q2A2E9 | UVRC_FRATH | Excinuclease ABC subunit C | Francisella | MIVDNSKDFDLKSFLANLTTHSGVYRMLDKHGEIIYVGKAKNLKNRINSYFSKGAKDSKTLMMVEQIARIEITITPSDYEAYLLENNLIKQHRPKYNILFKDDKSYPYLVISRDKFPRVSFYRGKSAYKKGQCFGPYVSISSVKNTLNTIQKIFPIRQCENSYYKSRVRPCLQYQIKRCLAPCVGLVSQQQYDEQLAILKKFLAGKFSSVLEEISANMYQASEDMEYEKAQVYRDQLVVLRKLQQQQIVDIQEDKTFDVIGIYMQDSYASIALLQIQNGDVVADRHWSIDAKGQDKTSIMHAFLSHFYLGDEIRNIWPKNIILSKVEFADITDLMNSISQKIGQAINWIIAPAADNLKWLKLAEVNARQKLNIYTSSKSQYQKRLESLKEFLESEKDIKRIECFDISHFQGEATIASCVVYTDDGEDRKSHRRYNIKDIKSGDDYAAIHQAVSRRVSSGLEADNLPDVMIIDGGKGQIHQAEAVFREYGIQDKVQLVSLGKGVERISGKEKIYKGFDDTEYTLDEHNPGFLLLRQVRDSAHDHAIKGQRKKVSANRQSSIIEEIEGVGPKRRKALMMYFGGWQELSRASVDEIAKVKGISKKLAQEIWECFH | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q2A2E9 |
Q46LZ8 | YIDD_PROMT | Putative membrane protein insertion efficiency factor | Prochlorococcus | MLTKINKAIALVFVSLISFYQKWISPLFGPSCRFIPSCSAYGIEAVNKHGPWRGGWLTLKRLSKCHPLTPCGCDPVPEK | Could be involved in insertion of integral membrane proteins into the membrane. | Q46LZ8 |
Q7MZB6 | UBIA_PHOLL | 4-HB polyprenyltransferase | Photorhabdus | MAGSMAQSKWLAYCRLMRINKPIGALLLLWPTFWALWMAGKGIPDMHILLVFTAGVFLMRAAGCAINDFADRKFDGYVERTKTRPLPSGAISEKESKILFVVLALISFGLVLTLNKMAIWLSAVGLALAWLYPFVKRFSHFPQFVLGAAYGWAIPMGFAAVSESLPLECWLLFLVNIFWSVIYDTQYAMVDRNDDLKIGVKSTAILFGRFDKLIIGLLQLAMLLLLVLVGYLINLGGIYYWSLLLTGTLFIYQQKLIAGRERELCFQAFLNNNYVGLVLFLGIFFSYV | Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. | Q7MZB6 |
P75132 | TRMD_MYCPN | tRNA [GM37] methyltransferase | Mycoplasma | MKITVLTLFEQVVWPYLNASIMAQAQKAKLVEFEVINWRQYCKDKHQTVDDMAYGGGGGMVLKAEPILKALKACRTPQSKVVLLSPEGQQFSQPMAQALTQTEHLILICGHYEGFDYRLYKHVDQIISLGDFVLSGGELVALSVIDATVRLIKGVINDQSLIHESFNNYLLDFPAYTRPYDLDGDKVPEILLSGDHKKIEAYRKEQQLLRTAQYRPDLYKQYLAKKDEKNK | Specifically methylates guanosine-37 in various tRNAs. | P75132 |
Q896F1 | YQGF_CLOTE | Putative pre-16S rRNA nuclease | Clostridium | MRILGLDVGDRTIGVAISDPLGWTAQGVKTIKRSNLKNDIKEIEDICNEYKVDKIVSGLPKNMNGTLGPQSEKVTEFCDILKKELEKEIIMWDERLTTVAAHKAMIEGDLSRAKRKKIVDKIAAIYILQGYLDSVYNK | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q896F1 |
B7LV66 | THIM_ESCF3 | 4-methyl-5-beta-hydroxyethylthiazole kinase | Escherichia | MQPDLLSRKTAALTLQKFHTLSPLTHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAVASALLINVGTLTQARAHAMRAAVVHAKRVKTPWTLDPVAVGSLDYRRHFCTELLSLNPDAIRGNASEIMALAGVSNSGRGVDSTDVVANALPAAVMLAQETGAVVVVTGEVDYVTDGRRTVGVGGGDPLMTKVVGTGCALSAVVAACCALPGDRLLNVASACSWMKQAGERAIVRSQGPGTFVPYFLDALWQMTQEVEA | Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). | B7LV66 |
Q3T086 | TPC6A_BOVIN | Trafficking protein particle complex subunit 6A | Bos | MADPALFEFLHTEMVAELWAQDPDPGPGGQKTSLLVLEGMGFRVGQALGERLPRETLTFREELDILKFLCKDLWVAVFHKQMDSLRTNHQGTYVLQDNSFPLLVRMASGLQYLEEAPKFLAFTCGLLRGTLSTLGVKSLVTASVAALPACKFQVVIQKL | May play a role in vesicular transport during the biogenesis of melanosomes. | Q3T086 |
Q4FVG3 | UBIG_PSYA2 | 3-demethylubiquinone 3-O-methyltransferase | Psychrobacter | MAENTVNAINVDPSEVEKFNKLAGEWWNKTGAFATLHEINPLRLNWIEENVKCGYVSADHQKTAEMGLAGKKVLDVGCGGGILSEAMARRGADVTGIDLGTENLKAASLHAEQSNLQDTLRYQHIPVEALAATHAGQFDVVTCMEMLEHVPDPAAIVDACFKLLAPGGVCVLSTINRNPKSYLFAIVGAEYVLRLLDRGTHDYAKFITPAELDKMAIDAGFTRQDIIGLHYNPLTKRYWLAQNVDVNYMMAVQKPRA | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | Q4FVG3 |
Q6ITC0 | VKT2_PSEAU | Kunitz-type serine protease inhibitor mulgin-2 | Pseudechis | MSSGGLFLLLGLLTLWEVLTPVSSKDRPKFCELPPDSGSCKGSFQAFYYHPVHRTCLEFIYGGCEGNDNNFKTIDECKRTCAA | Serine protease inhibitor. | Q6ITC0 |
Q9P1Q0 | VPS54_HUMAN | Tumor antigen SLP-8p | Homo | MASSHSSSPVPQGSSSDVFFKIEVDPSKHIRPVPSLPDVCPKEPTGDSHSLYVAPSLVTDQHRWTVYHSKVNLPAALNDPRLAKRESDFFTKTWGLDFVDTEVIPSFYLPQISKEHFTVYQQEISQREKIHERCKNICPPKDTFERTLLHTHDKSRTDLEQVPKIFMKPDFALDDSLTFNSVLPWSHFNTAGGKGNRDAASSKLLQEKLSHYLDIVEVNIAHQISLRSEAFFHAMTSQHELQDYLRKTSQAVKMLRDKIAQIDKVMCEGSLHILRLALTRNNCVKVYNKLKLMATVHQTQPTVQVLLSTSEFVGALDLIATTQEVLQQELQGIHSFRHLGSQLCELEKLIDKMMIAEFSTYSHSDLNRPLEDDCQVLEEERLISLVFGLLKQRKLNFLEIYGEKMVITAKNIIKQCVINKVSQTEEIDTDVVVKLADQMRMLNFPQWFDLLKDIFSKFTIFLQRVKATLNIIHSVVLSVLDKNQRTRELEEISQQKNAAKDNSLDTEVAYLIHEGMFISDAFGEGELTPIAVDTTSQRNASPNSEPCSSDSVSEPECTTDSSSSKEHTSSSAIPGGVDIMVSEDMKLTDSELGKLANNIQELLYSASDICHDRAVKFLMSRAKDGFLEKLNSMEFITLSRLMETFILDTEQICGRKSTSLLGALQSQAIKFVNRFHEERKTKLSLLLDNERWKQADVPAEFQDLVDSLSDGKIALPEKKSGATEERKPAEVLIVEGQQYAVVGTVLLLIRIILEYCQCVDNIPSVTTDMLTRLSDLLKYFNSRSCQLVLGAGALQVVGLKTITTKNLALSSRCLQLIVHYIPVIRAHFEARLPPKQYSMLRHFDHITKDYHDHIAEISAKLVAIMDSLFDKLLSKYEVKAPVPSACFRNICKQMTKMHEAIFDLLPEEQTQMLFLRINASYKLHLKKQLSHLNVINDGGPQNGLVTADVAFYTGNLQALKGLKDLDLNMAEIWEQKR | Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD . Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling . | Q9P1Q0 |
B1ZHN6 | UREG1_METPB | Urease accessory protein UreG 1 | Methylorubrum | MASLNGPLRVGIGGPVGSGKTALMEQLCRRFRDRYEICAITNDIYTKEDARILTVAGALPEERILGVETGGCPHTAIREDASINLAAVAEMRRRFPKLDLVLIESGGDNLAATFSPELADITLYVIDVAGGEKIPRKGGPGITRSDLLIVNKTDLAPLVGADLSVMESDTQRMRGTRPYVFASLREGHGADRVATFIVEAGGLR | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | B1ZHN6 |
A0KYM0 | TIG_SHESA | PPIase | Shewanella | MQVSVEATQGLERRLTISVPAEQIEKLVKDSLQREAKRARIPGFRPGKVPVTVINKRYGAAIRQDITGEVMQRNFIEAIIAEKLNPAGAPTFVPGATDGEKFEFVATFEIYPEVELKGLDAIEVEQPKASVTDADVDSMIETLRKQHATFAAVEREAADGDKVKMNFVGSVDGVEFEGGKADDFELQLGSGRMIPGFEAGILGHKAGEEFVIDVTFPEEYHAENLKGKAAKFAITLTEVLAANLPEVNDEFAALFGISEGGLDALKTEIRKNMNRELEQALKANVKEQVITGLLANNDIELPKALIDGEVNVLRQQAMQRFGGQTANMPELPAELFTEQAARRVKIGLLLGEVIKTNELKAEDERVQALIASMASAYEDPSEVVAYYNSNKELMQNMRNVALEEQAVEALLKSAKVTEKEVAFEEFMNKATGRA | Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase. | A0KYM0 |
Q4FQ48 | UVRC_PSYA2 | null | Psychrobacter | MVNVSVLSPVDDKKARLKHLIQRLPNLPGVYKMLGKNGDILYVGKAKSLKSRVNSYFAKTIDHPKTRALVARIHNIETIITRSETEALLLEQNLIKEYRPPYNVLLRDDKSYLYVFISADQPYPRLAYGRGKVNHQKGCFFGPFPSAHAAKETLVLMQKMFQMRQCTNTFFKQRKRPCLEYQIKRCRAPCVGLVSAEEYSEDVNNTIRFLKGDSSDIHSALIEKMEASAEELDFEKAVFYRDQLSMLREVQAKQAVYTVQGEADVIAIASQVGMTCVNVLTVRGGRVLGGKNYFPDVDSSQPLADNLSAFITSFYFQVTDDLPAEIMLSHELPDQVAVSEALASHFGSKVVIKTNVREHRAEWLDLAKLNTNNALKTKLGDYLELHARFGALKDVLADITDRTIDRIECFDISHTMGEATIGGCVVFDQSGSRRRDYRQYAIHDIVGGDDYAAMKQVLTRRYKKQPLPDLLLIDGGKGQLGIAKEVLTELGMLGDTLLIGVAKGEGRKAGLEVLHFIDHEPLDLPMDSKALHLLMHIRDEAHRFAITAHRKKRDKRRSSSVLEVIPGLGEKRRRDLLNHFGGLQQLLGASQQELAGVQGIGPILAKTVYKVLHE | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. | Q4FQ48 |
Q6D8D8 | UPPS_PECAS | Undecaprenyl pyrophosphate synthase | Pectobacterium | MPSDNQKNTNDLPLAGPRHVAIIMDGNGRWAKSRGKMRIFGHQAGVKAVRRSVSFAVNHGLDALTLYAFSSENWNRPAQEVSALMELFVRALDSEVKSLHKHNVRLRVIGDIGRFSPRLQERIRRSEVLTEKNQGLTLNIAANYGGRWDIIQGVRQLAEQVQEGILRPDSINEASLCQYICLNDLAPVDLVIRTGGEHRISNFLLWQIAYAELYFTDVLWPDFDEQVFEGALNAFAQRERRFGGTTPIDADAS | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with (2E,6E)-farnesyl diphosphate (E,E-FPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E,38E)-undecaprenyl diphosphate (di-trans,octa-cis-UPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. | Q6D8D8 |
Q92ES8 | TATC_LISIN | Sec-independent protein translocase protein TatC | Listeria | MTEVSMSLTGHLKELRTRLLIILLSFFLAFFVGLFVSKPLILFLQKDDLPKEVILHVFKVTDAFQIYIEMAFIIGLILVFPVILYQLWAFVKPGLHASEQRITLRYIPITFLLFLCGVVFSYVITFPFILKFMFQFAAELGVETTIGLATYFQFLLQIVLSFGVLFELPMVIMLLTRLSLITPNGMRRARKYAYFCLLIIAAFIAPPEILSHLMITIPLIGLYEISIVVSGFTVRRMDKEMNMKKML | Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. | Q92ES8 |
P96579 | YDAF_BACSU | Putative ribosomal N-acetyltransferase YdaF | Bacillus | MFTCKVNEHITIRLLEPKDAERLAELIIQNQQRLGKWLFFAENPSSADTYRETIIPDWRRQYADLNGIEAGLLYDGSLCGMISLHNLDQVNRKAEIGYWIAKEFEGKGIITAACRKLITYAFEELELNRVAICAAVGNEKSRAVPERIGFLEEGKARDGLYVNGMHHDLVYYSLLKREWEGEK | Putative N-acetyltransferase. May act on ribosomal proteins (Potential). | P96579 |
Q750F0 | YPI1_ASHGO | Type 1 phosphatases regulator YPI1 | Eremothecium | MSSNNQESLANRSHTVTVSETSQILQLRANQTEQVPKLAKKEQKSKVRWDENVVDNEHMNKKKTKICCIFHPQQNFDDEDGGECEHASSSASSSSSSESENDTSMDFEARRQARIARRRQKLERKRSSSPNAYEYQPDYSQYRQKYLHGDK | Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. | Q750F0 |
O95159 | ZFPL1_HUMAN | Zinc finger protein MCG4 | Homo | MGLCKCPKRKVTNLFCFEHRVNVCEHCLVANHAKCIVQSYLQWLQDSDYNPNCRLCNIPLASRETTRLVCYDLFHWACLNERAAQLPRNTAPAGYQCPSCNGPIFPPTNLAGPVASALREKLATVNWARAGLGLPLIDEVVSPEPEPLNTSDFSDWSSFNASSTPGPEEVDSASAAPAFYSQAPRPPASPGRPEQHTVIHMGNPEPLTHAPRKVYDTRDDDRTPGLHGDCDDDKYRRRPALGWLARLLRSRAGSRKRPLTLLQRAGLLLLLGLLGFLALLALMSRLGRAAADSDPNLDPLMNPHIRVGPS | Required for cis-Golgi integrity and efficient ER to Golgi transport. Involved in the maintenance of the integrity of the cis-Golgi, possibly via its interaction with GOLGA2/GM130. | O95159 |
Q6R3K8 | YSL4_ARATH | Protein YELLOW STRIPE LIKE 4 | Arabidopsis | METEIPRSTEISETLLLPETNLDHGEYVPEWKEQITIRGLISSALLGILFCIITHKLNLTIGIIPSLNVAAGLLGFFFIKSWTGFLSKLGFLSKPFTKQENTVIQTCVVSCYGLAYSGGFGSYLIAMDERTYKLIGSDYPGNNPEDVINPGLWWMTGFLFVVSFLGLFCLVPLRKVMILDYKLTYPSGTATAMLINSFHNNTGAELAGKQVKCLGKYLSLSLVWSCFKWFFSGIGGACGFDHFPTLGLTLFKNTFYFDFSPTFIGCGMICPHLVNCSVLLGAIISWGFLWPFISQHAGDWYPADLKANDFKGLYGYKVFIAISIILGDGLYNLIKIIVVTVKEICNKSSRQHNLPVFTDILDKSKTSVLMREKKKRDIIFLKDRIPLEFAVSGYVGLAAISTAIIPLIFPPLKWYFVLCSYLVAPGLAFCNSYGAGLTDMSMPSTYGKTGLFIVASIVGNNGGVIAGLAACGIMMSIVSTAADLMQDFKTGYLTLSSAKSMFVTQLLGTAMGCIIAPLTFWLFWTAFDIGDPDGLYKAPYAVIYREMAILGVEGFAKLPKHCLALCCGFFIAALIVNLIRDMTPPKISKLIPLPMAMAGPFYIGAYFAIDMFVGTVIMLVWERMNKKDADDYSGAVASGLICGDGIWTIPSAILSILRINPPICMYFRPS | May be involved in the transport of nicotianamine-chelated metals. | Q6R3K8 |
Q9RP19 | UREG_SPOPA | Urease accessory protein UreG | Sporosarcina | MKTIHLGIGGPVGSGKTTLVKTLSEALKEEYSIAVITNDIYTREDANFLINENILEKDRIIGVETGGCPHTAIREDASMNFEAIEELKNRFDDLEIILLESGGDNLSATFSPELVDAFIYVIDVSEGGDIPRKGGPGVTRSDFLMVNKTELAPYVGVDLDTMKNDTIKARNGRPFTFANIKTKKGLDEIIAWIKSDLLLEGKTNESASESK | Facilitates the functional incorporation of the urease nickel metallocenter. Binds a maximum of 4 Ni(2+) and 2 Zn(2+) ions per homodimer. The affinity for Zn(2+) is 10-fold higher than that for Ni(2+). This process requires GTP hydrolysis. | Q9RP19 |
Q6PD29 | ZN513_MOUSE | Zinc finger protein 513 | Mus | MPRRKQSHPQPVKCEGVKVDTEDSFDEGPGALVLESDLLLGQDLEFEEEEEEDEGDGHNDQLMGFERDSEGDSQGARPGLPYGLSDDESGGGRALSAESEVEEPARGPGEARGERPGPACQLCGGPTGEGPCCGAGGPGGGPPLPPRLLYSCRLCAFVSHYSSHLKRHMQTHSGEKPFRCGRCPYASAQLVNLTRHTRTHTGEKPYRCPHCPFACSSLGNLRRHQRTHTGPPTPPCPTCGFRCCAPRPTRPPSPTEQEGTMPRRSEDALILPDLSLHVPPGGASFLPDCGQLRGEGESLCGTGSEPLPELLFPWTCRGCGQELEEGEGSRLGAAMCGRCMRGEAGGVATGGPQGPGDKGFACSLCPFATHYPNHLARHMKTHSGEKPFRCARCPYASAHLDNLKRHQRVHTGEKPYKCPLCPYACGNLANLKRHGRIHSGDKPFRCSLCNYSCNQSMNLKRHMLRHTGEKPFRCATCAYTTGHWDNYKRHQKVHGHGGAGGPGLSAPEGWAPPHSPPSVLSTRGPAALGATGSRALHSDSP | Transcriptional regulator that plays a role in retinal development and maintenance. | Q6PD29 |
Q39R76 | TRUD_GEOMG | tRNA-uridine isomerase D | Geobacter | MSGEKRYLTAGLPGTGGTIKETADDFVVEEIPLYLPCGEGEHVYALIEKRGVTTLDAIRRLARALKLSERDVGYAGMKDARGVTRQTVSLPRMKPEEVLALELPGIRILSAERHRNKLKLGHLAGNRFRIRVRGVVSDAVARAEAILAVLERRGVPNRFGEQRYGAQGNSHLIGRAMLAGDWCAAVDLLMGDPAKVTGEAWRSAIEAYQRGELEESQRLFPGHCRTERDVIQRLVKRPDDFEGAFRAVNPRLRKLYLSACQSALFDHVVEARLDSLDTVQEGDLAWKHANGACFLVTDPAAEAPRAEHFEISPTGPLFGCRMMMPEGEEGALERSLLAAEGVEPASFDLPGGLRMEGERRPLRVPLGDPRASADADGLVLEFSLPKGSYATAVLREVMKGGRPD | Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs. | Q39R76 |
O26979 | XERA_METTH | Tyrosine recombinase XerA | Methanothermobacter | MVDTMNMKRESEERQGLLERYNFPELIEDYLIELEIRNYSPNTIKTYKSIVKNFYEFLMNEDDLYDDRRVLRSFKRYIQYLKRDKKVTQNYIYLVTVVVKKFFEFSGIDCLEEVKAPKRTKSLPKSLNEDEVKSLINAVEVADDGSVIRRFIKTRDRLILSLLYSSGLRVSELVSLRINDIDPDERTIRIRGKGDKDRIVLFDENTRDLLMDYLKRRIHESEYLFLNRFGDPLTPRYVQMMIKNYARKAGIKKKVTPHILRHSFATHLLKNGVDIRAIQQLLGHSNLSTTQIYTSVDMQTLKNVYDRARLL | Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. | O26979 |