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
|
|---|---|---|---|---|---|---|
Q4A738 | TRMD_MYCS5 | tRNA [GM37] methyltransferase | Mycoplasmopsis | MKINFLTLFPRYFEPLINESIIKKAVDKKILEFNVVDFRDFTKSKHRKVDDEIYGGGHGLLLQVEPIDLALDSLENRGGYKILVTPQGKIFDQKMANKLAKYDQITLISGRYEGFDERVTYLVDEEISIGDYVLTGGELPAMVIADSICRLVPGVIKKESVENDSFQNEGLLDYPQYTRPREYKNMKVPEVLFNGNHKEISEWKLKAQLEKTKKNRPDILERIKNEK | Specifically methylates guanosine-37 in various tRNAs. | Q4A738 |
Q12059 | ULA1_YEAST | Ubiquitin-like activation protein 1 | Saccharomyces | MERYDRQLRLWGALGQDSLNRSRVCVVGPATPLLQEVFKNLVLAGISSLTWLKVECAVQSGSLFLAELKKDLEPLASKQLEYEENDLRKTLQQPQYDWTRFSVVILTCIGEQTAMLDLNEIRRQRGTKFPPVLNTFVSGFYGYIYLVLSETHFVLQAHPDSKKYDLRLQNPWPELINYVDTFDLSKMDTATFSGIPYTVLLMKCIAKLERDGNNGRITIDQMKKVLDQICLPLGNDVIYEPNYVEAKRYAYLACSQNDCCKELEDLLRNLEISDYGNDWHDTYNYEILTLLLTLKNIAKENGELSFQPLTGTLPDMESTTENYIRLKKLYEVKAKLDKSRVEESLARSKKIVSQDVLETFCSHYGEVRKILPPKSDLLGIFSTSNALLDALVMVQFWEQPAVTAEDKDEFIGLRVDDNYSVMAFFGGAVVQEAIKLITHHYVPIDNLFLYNGINNSSATYKI | Regulatory subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12. | Q12059 |
A4F7F9 | UREG1_SACEN | Urease accessory protein UreG 1 | Saccharopolyspora | MLPEHHDHGHEHGGNGHGHGHRHQVNFDPTAAEPDPYGVAPRGGRAFRLGIGGPVGSGKTALTAALCRALGSEVNLAVVTNDIYTTEDADFLRRAGVLDTDRIEAVQTGACPHTAIRDDITANLDAVEKLEERHPGLELVIVESGGDNLTAVFSRGLADSQVFVVDVAGGDKVPRKGGPGVTTADLLVINKVDLAEQVGADMAVMVADAHRMRGELPVITQSLTRTPNAPDVSAWVRQQLAAGVVVGA | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | A4F7F9 |
B6EHA7 | TATA_ALISL | Sec-independent protein translocase protein TatA | Aliivibrio | MGGISIWQLLIIAVIIVLLFGTKKLRGVGSDLGSAVKGFKKAISEDESAKDAKKDADFVPQNLEKKEAETVEKQKQNDKEQA | 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. | B6EHA7 |
A6H6Q4 | TKTI1_MOUSE | Tektin bundle interacting protein 1 | Mus | MENVRREATRPSVPSGTLELYFPDHLYRNDYVSLEGPRWAPAIKQAVRWKFTPMGRDAAGQVWFTGLTNSEPGDAWYKLPRALDTPYREAHTRWHGCFQSRQRGLPPAYTQHLREMAFWDPAITAQYLNSGPRWGCMQWRDRQIRGKEFVVTRNQFGAKLPWRSDYVPLLSLPQRPRFTAQDFRQRGLQRPCPAIGQPPPAFTPAL | Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. Located at the center of the tektin bundle where may function to recruit tektins or stabilize the bundle. | A6H6Q4 |
P57289 | THRC_BUCAI | Threonine synthase | Buchnera | MKLYNLKNHNEQVNFEAAVKLGLGQQQGLFFPVELPTITPIELSKILKMDFITRSTEILSKFICHEISKEELYKHVKQAFSFKHPLKIKITKDIHCFELFHGPTLAFKDFGARFMAQMILLLNKKNESVTILTATSGDTGAAVANAFYGMKNVRVIILYPKGKISELQEKLFCTLGRNIKTISINGSFDDCQKLVKEAFNDKKLKESIGLNSANSINISRLLAQICYYFEAFSLISEEQRKNLVIAVPCGNFGNLTAGLLSKSLGLPIKSFIACTNANDTVPRFLNNGTWNPKKTVSTISNAMDISQPNNWTRIEELFYRKKWDLKKLRFGSVSDHTTEETLKELFKLGYVSEPHAAIAYRLLRDQLKENEFGLFLGTAHPAKFKNTVEKILKNKISLPSELQNRIDLPLLSHNINPVFSKLKTFLLEK | Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. | P57289 |
Q2LVM4 | TATA_SYNAS | Sec-independent protein translocase protein TatA | Syntrophus | MFGIGMPEMLIILVIILIIFGAGKLPEIGGAIGKGIKNFKKASNESEEIDENSRPKKIEPK | 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. | Q2LVM4 |
E7F021 | ZD12B_DANRE | Zinc finger DHHC domain-containing protein 12-B | Danio | MFKNVFGSGFLVRTAHVILTWVITLILFLHDTDLRRQEETGELTLPVLFVLLVLVSVLLYFAVSLMDPGFVLTDDCDLQFTLGIAEETQDMIPQTTKSIRLRRCGHCLVQQPMRSKHCQTCQHCVRRYDHHCPWIENCVGERNHRWFVLYLAVQFVVLLWGLYMAWSGFSHASTWQQWLRTNGVLLGAAAVVAILALTVLLLLGSHLYLVSLNTTTWEFMSRHRISYLKHCGADENPFDKGILRNLWGFFCAWEPVVWEHVYFKQGNDPI | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. | E7F021 |
Q6AVD0 | YSL3_ORYSJ | Protein YELLOW STRIPE LIKE 3 | Oryza sativa | MDAMIGDPMSATSVEAVFEKQPSPEFRELVTPRAMAVAVVLSVVICFVGMRIQMTAGIVPALNMPASILSFFLLKWLIRLLQSCGFPMLPFTRQENMFLLTCIITCLNLALTSGFATNIIGMTSTVARSLADDPDPRDIMDHVPIGKWIVYLFLVGMTGVLINVPFNQVMIIDYKLLFPTGTVIAQLINSFHTPEGAYVAKMQVATIFKVFFGSFSWSMFQWFYTAGDDCGFQHFPTFGLGLYKHRFYFDFSATYIGLGMICPHIVNFGLFFGAIISWGFLYPFLETKRGQWYQTDSPTSLNGQNGYKVFISVTLIITDGMINFLTLITTASINFYQLRKEHDLGLANYFKKHPSLNYDDRKRIEVFLANRIPIPVPVAAYITCAAISTIAIPAMFNQIKFYHLAVLYMVIPVVTFCNTYATGLTDWSVAPTYAKFTTFVFAAWIAKPGAVVASLLASGVIVAALHISSQAMQDLKSGHMTLTSPRAMVTGQIFGVAVGSILCPCVFLAFQSTTKPNAPVGSKQSDYPCPFAGLYRAIGVIGTGGVKELPKHCMTFCVVAFCVTVIIDAVVLVSQKRGWSIHRYIPSMTVIALPFFAGSYFTIDMCVGSLLLLAWTRMNAKSAEMLSSAVAAGLICGEGLFTLPSALLNMFKVQPPMCMKFLSGGEEVEAADSFLNNLGTSRT | May be involved in the transport of nicotianamine-chelated metals. | Q6AVD0 |
P25591 | VAC17_YEAST | Vacuole-specific MYO2 receptor VAC17 | Saccharomyces | MATQALEDITERLLIRSQEAILQLDLWIQRQQRSSICQTTDQESLDKLSQQYNQYMSQLNSLYVRSESVRDKLSKEQQRRLITEDNEHQRIEDLVREFQDITLRLNELATVPNEAPNDSPQSQSTRSSLGSFQPRPLKIIERQRLCMVTPSKPPKKSVGFNPINEVDCPSKTNSLPCSPKKQPARNRTLRAAKSHDTGLNKSKKPSSSDTYESFFKNRQRLSLTFFDEMDDEDFDSDQDTIILPNISTPPHVGVTAKGAEFEPLRRYNSHESILSNKPAPSKSLNLGSFSASFFRPSNPTFGTSISNVQVNCHPTVAATMAPSRNGPRISSSKALLSSFIARSDTHTVKENNTNLKHASFMDKFNSSLSTISESFQSKRGRKNKGMNEERISNHNVAQEQKNNMDISVSIEELQDALNTELLF | Vacuole-specific MYO2 receptor required for vacuole inheritance. Binds simultaneously to MYO2 and to VAC8, a vacuolar membrane protein, forming a transport complex which moves the attached vacuole membrane along actin cables into the bud. Once the vacuole arrives in the bud, VAC17 is degraded, depositing the vacuole in its correct location. | P25591 |
Q54DL6 | Y2140_DICDI | SET and MYND domain-containing protein DDB_G0292140 | Dictyostelium | MDGVIESPSNNTIKISPSTSDSSTTTPIITTPPTQSTATVTTKAAATTTTTEASTTPPPPQPTPTPTQSTATVTKEVETTTETIPPIVTKGKIKKSKKSIKKPTIVKRPTTPIDYKQWHTEWPIHVYSHPINGRYLVATKDLDEQTVILRDLPYTWAVDHATCDSVCQHCFLEVPLNQQILPTDFYMCEGCQRVGYCSANCRCIDYSQHRFECQIFKELDTEEYSPFLMSEIKLLVRTLSRKWLEDSITQTAGIDINDETIKKQNTYNQYKNPQSLIPQDNGLRYNDYAELVSNVENYNESLKESLSYWICKYVVKLSAKLGKIEDEFDLLNILLRNRCNAFYIQGRPRDGSSGESRGCGVYVRNSFFNHSCDPNVNYWVVNNTLEVECTLLKNVKEGDELTISYIDTTSPLNKRREKLLEGYLFNCLCTKCVADESLPLDQTGTLEKDDDDNDDEKEKMDEDDDEKDDDINNKNDKKSKYKSDGSTDDEEDEDNNNNKNNNKNKNNNSNNQDHQNNDKSN | Probable methyltransferase. | Q54DL6 |
Q5D7J0 | TRIM5_COLGU | TRIM5alpha | Colobus | MASGILVNIKEEVTCPICLELLTEPLSLHCGHSFCQACITANHKKSMLYKEGERSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDRKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVLADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELVSDLEHRLQGSVMELLQGVDGIIKRIEDMTLKKPKTFPKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRRVSSPNPQIMYRAQGTLFQSLKNFIYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDAMYNIEQNENYQPKYGYWVIGLQEGVKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5D7J0 |
P28119 | WNT51_EPTST | Protein Wnt-5(I) | Eptatretus | SGSCSLKTCWMQLSPFREVGNRLKQKYDQAAAVRLARRRRLEPVNQRFSPPTKMDLVYLETSPDYCMRNDTTGAAGTAGRQCERGSAGTGGCELMCCGRGYDSFRATSTERCHCKF | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | P28119 |
A6WPW9 | TRPD_SHEB8 | Anthranilate phosphoribosyltransferase | Shewanella | MSTNPIQPLLDVLYQGKSLNREQTAELFGALIRGEMSEAAMAGMLVALKMRGETIDEISGAADAMRAAAKPFPCPERNNNPLHNGIVDIVGTGGDGFNTINISTTAAFVAAAAGAKVAKHGNRSVSSKSGSSDLLAQFGIDLTMSPETASRCLDALNLCFLFAPHYHGGVKHAVPVRQALKTRTLFNVLGPLINPARPEFMLLGVYSPELVLPIAKVLKALGTKRAMVVHGSGLDEVALHGNTQVAELKDGDIVEYQLTPADLGVPLAQITDLEGGEPAQNALITEAILKGRGTEAHANAVAINAGCALYVCGIADSVKAGTLLALATIQSGKAFELLSQLAKVSGEALVNGQEKGR | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A6WPW9 |
A9AF28 | UBID_BURM1 | Polyprenyl p-hydroxybenzoate decarboxylase | Burkholderia cepacia complex | MKYKDLRDFIQRLEALGELRRVTQPVSPVLEMTELCDRVLRAGGPALLFEAPPGYAFPVLGNLFGTPRRVALGMGVDAGDDAALDSLRDLGRLLSALKEPDPPRSLKDAGKLLSLAKAVWDMAPKTVSSPPCQEIVWEGADVDLHKLPIQTCWPGDAGPLVTWGLTVTRGPNKPRQNLGIYRQQLIGRNKLIMRWLAHRGGALDFREFALKNPGKPYPVAVVLGADPATTLGAVTPVPDSLSEYQFAGLLRGSRTELAKCLTPGVDTLQVPARAEIVLEGFIYPQDGTPAPAPAGAPPRPAGQAAAAYEHALEGPYGDHTGYYNEQEWFPVFTVERITMRRDAIYHSTYTGKPPDEPAILGVALNEVFVPLLQKQFAEITDFYLPPEGCSYRMAIVQMKKSYAGHAKRVMFGVWSFLRQFMYTKFIVVVDEDVNIRDWKEVIWAITTRVDPVRDTVMVDNTPIDYLDFASPVAGLGSKMGLDATNKWPGETNREWGRPIEMDAKVKARVDRLWQDIGL | Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. | A9AF28 |
A5FPF2 | TATA_DEHMB | Sec-independent protein translocase protein TatA | Dehalococcoides | MPKIGPMEILIIVLLVVVVFGVGKLPQVGDAIGKGIRNFRKASTGEDAKEEVETKEETKPAEKSE | 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. | A5FPF2 |
Q8U3D3 | Y535_PYRFU | Putative transcriptional regulatory protein PF0535 | Pyrococcus | MKTFLTEQQIKVLMLRAKGYKQSEIAKILGTSRANVSILEKRAMEKIEKARNTLLLWEQINSKVIVEIKAGEDIFSIPEKFFKKADKVGVKVPYSTAEIITFLVEHAPVEDRLAKRDFVLFLDSKNKLRIGDCLVIEEIKED | Putative transcriptional regulator. | Q8U3D3 |
P60012 | ZAPD_CHRVO | Z ring-associated protein D | Chromobacterium | MISFEFPVTERTRILLRLEYLYGRLAYFIGKDHPHDHHAALQVLFELMETASRADLKADLLQELERQKQMLEALRDNPNVAEETLEGVLEEIERASSQLLALTGKFGQNLRENEWLMAIKQRAGIPGGTCQFDLPSYHLWQQRSAEVRRQDLRRWAAPLMPTADAAEILLHLLRDSGKTYHYVARKGAFQQMSGGKVVQLIQVAYDDNLELLPELSANKYALNIRFVSAVTGEARPRQTEQDVEFQLTNCKF | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | P60012 |
B0KL24 | THIC_PSEPG | Thiamine biosynthesis protein ThiC | Pseudomonas | MTKQEKAINLSESAQVDQQSVQPFPRSRKVYVEGSRPDIRVPMREISLDDTPTDFGGETNAPVLVYDTSGPYTDPNVIIDVRKGLADVRSAWIDARGDTERLDGLSSDFGQQRLNDAELAKLRFAHVRNPRRAKAGANVSQMHYARRGIITAEMEYVAIRENMKLQEARAAGLLKEQHAGHSFGANIPKEITPEFVRQEIARGRAIIPANINHPEVEPMIIGRNFLVKINGNIGNSALGSSIEEEVAKLTWGIRWGSDTVMDLSTGKHIHETREWIIRNSPVPIGTVPIYQALEKVNGVAEDLIWELFRDTLIEQAEQGVDYFTIHAGVLLRYVPLTAKRVTGIVSRGGSIMAKWCLAHHKENFLYTHFDEICEIMKAYDVSFSLGDGLRPGSIADANDAAQFGELETLGELTKIAWKHDVQCMIEGPGHVPMQLIKENMDKQLECCDEAPFYTLGPLTTDIAPGYDHITSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKTGIITYKIAAHAADLAKGHPGAQIRDNALSKARFEFRWEDQFNLGLDPDTARAFHDETLPKESAKVAHFCSMCGPKFCSMKITQEVREYAAKIEAVDVTVEEGMREQAERFRQEGSQLYHKV | 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. | B0KL24 |
Q47539 | TAUC_ECOLI | Taurine transport system permease protein TauC | Escherichia | MSVLINEKLHSRRLKWRWPLSRQVTLSIGTLAVLLTVWWTVATLQLISPLFLPPPQQVLEKLLTIAGPQGFMDATLWQHLAASLTRIMLALFAAVLFGIPVGIAMGLSPTVRGILDPIIELYRPVPPLAYLPLMVIWFGIGETSKILLIYLAIFAPVAMSALAGVKSVQQVRIRAAQSLGASRAQVLWFVILPGALPEILTGLRIGLGVGWSTLVAAELIAATRGLGFMVQSAGEFLATDVVLAGIAVIAIIAFLLELGLRALQRRLTPWHGEVQ | Part of a binding-protein-dependent transport system for taurine. Probably responsible for the translocation of the substrate across the membrane. | Q47539 |
A5ERU7 | UREF_BRASB | Urease accessory protein UreF | unclassified Bradyrhizobium | MTASERPHVSAAMTELDHPALYRLMTWLSPAFPVGGFAYSSGIEWAVEAGDVDDAASLRGWLSTMLTDGSGFCDAVFLVHAHRAMELGDIDRLREVAELAAAFVPSRERQLETTAQGRAFIEIARSAWNSPGLDDAVSQCEAMVYPVAVGVVGAAHGIQSSLLLHAYLHAVTSNWISAGSRLIPLGQTDSQRVLAALEPVVTATAVRAISASLDDIGSATFRADLASLRHETQYTRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A5ERU7 |
Q9UGI8 | TES_HUMAN | TESS | Homo | MDLENKVKKMGLGHEQGFGAPCLKCKEKCEGFELHFWRKICRNCKCGQEEHDVLLSNEEDRKVGKLFEDTKYTTLIAKLKSDGIPMYKRNVMILTNPVAAKKNVSINTVTYEWAPPVQNQALARQYMQMLPKEKQPVAGSEGAQYRKKQLAKQLPAHDQDPSKCHELSPREVKEMEQFVKKYKSEALGVGDVKLPCEMDAQGPKQMNIPGGDRSTPAAVGAMEDKSAEHKRTQYSCYCCKLSMKEGDPAIYAERAGYDKLWHPACFVCSTCHELLVDMIYFWKNEKLYCGRHYCDSEKPRCAGCDELIFSNEYTQAENQNWHLKHFCCFDCDSILAGEIYVMVNDKPVCKPCYVKNHAVVCQGCHNAIDPEVQRVTYNNFSWHASTECFLCSCCSKCLIGQKFMPVEGMVFCSVECKKRMS | Scaffold protein that may play a role in cell adhesion, cell spreading and in the reorganization of the actin cytoskeleton. Plays a role in the regulation of cell proliferation. May act as a tumor suppressor. Inhibits tumor cell growth. | Q9UGI8 |
Q87M23 | TYPH_VIBPA | TdRPase | Vibrio | MYLPQEIIRKKRDGEVLTADEINFFIQGVANNTVSEGQIAAFAMTIFFNEMTMDERIALTCAMRDSGMVIDWSHMNFGGPIVDKHSTGGVGDVTSLMLGPMVAACGGFVPMISGRGLGHTGGTLDKLEAIPGYNITPTNEVFGQVTKDAGVAIIGQTGDLAPADKRVYATRDITATVDNISLITASILSKKLAAGLESLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTKTTAILTDMNQVLASSAGNAVEVREAVRFLTGEYRNPRLLEVTMASCAEMLVLAKLAENTDDARAKLMEVLDNGKAAACFGKMVAGLGGPADFVENYDNYLEKAEIIKPVYATETGIVSAMDTRAIGMAVVSMGGGRRVATDEIDYAVGFDNFIRLGEVADSDKPLAVIHARSEGQWEEAAKALRSAIKVGGEYTPTPEVYRQIRAEDI | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q87M23 |
C0HJF6 | TY01_PHYSA | Tryptophyllin-1 | Phyllomedusa | MDILKKSLFLALFLGLVSISFCDEEKRQDDDESNESEEKKEIHEEGSQEERREKPPPWVPV | The synthetic peptide inhibits bradykinin-induced relaxation of rat tail artery smooth muscle, and also has anti-proliferative effects on the human prostate cancer cell lines LNCaP, PC3 and DU145. | C0HJF6 |
P07198 | XENO_XENLA | Xenopsin | Xenopus | MYKGIFLCVLLAVICANSLATPSSDADEDNDEVERYVRGWASKIGQTLGKIAKVGLKELIQPKREAMLRSAEAQGKRPWIL | XPF has antimicrobial activity. | P07198 |
Q96LB4 | VATG3_HUMAN | Vacuolar proton pump subunit G 3 | Homo | MTSQSQGIHQLLQAEKRAKDKLEEAKKRKGKRLKQAKEEAMVEIDQYRMQRDKEFRLKQSKIMGSQNNLSDEIEEQTLGKIQELNGHYNKYMESVMNQLLSMVCDMKPEIHVNYRATN | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. | Q96LB4 |
Q2LMP0 | XY11A_BOTFU | 1,4-beta-D-xylan xylanohydrolase 11A | Botrytis | MVSASSLLLAASAIAGVFSAPAAAPVSENLNVLQERALTSSATGTSGGYYYSFWTDGSGGVTYSNGANGQYAVSWTGNKGNFVGGKGWAVGSERSISYTGSYKPNGNSYLSVYGWTTSPLIEYYIVEDFGTYDPSSAATEIGSVTSDGSTYKILETTRTNQPSVQGTATFKQYWSVRTSKRTSGTVTTANHFAAWKKLGLTLGSTYNYQIVAVEGYQSSGSASITVS | Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Required for planr infection and the appearance of secondary lesions. | Q2LMP0 |
F6P6X0 | UBAP1_DANRE | Ubiquitin-associated protein 1 | Danio | MAARKSGSDIHNNGPVSYLDDVPFKLNEKFRCPSKVGLPIGFCLSDCNAILSDLQYDFNLERRTVQWGEELAKARAAEARAAEAIRTDSESERQAASQDAEVGLVGGKKARPSDEQDIVPPALKPVLAGLSHNAILTPLPAPSFGQTRPAPSNPAPQYLNLADFEREEDPFDKLELKTLDDKEELRTILQSQPQSSVSPPQLPPAEHRPVSPSTTPPLQAKTGIFHKPNGLVGLLDLDRGGVLGGQIDADRPCNIRSLTFPKLSDPGDSPLETPLSVYPVAPPRNLSNGTPPSLQRTASNNNTTLPQEQPVFAQNGTPKQSNPVTVTSHPPAGTTLLSLSPSERQCVETIVGMGYSYEGVLKAMQRQGQNVEQVLEYLFTHSRLCDRGFDATAVEECLEMYQGSEEKALEFLQLMSRFGEMGFERDTIKEVLLVHNNDQDKALEDLMTRATAS | Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). | F6P6X0 |
Q7MI39 | TYPH_VIBVY | TdRPase | Vibrio | MYLPQEIIRKKRDGEALTADEINFFIQGVANNTVSEGQIAAFAMTIFFNEMTMPERIALTCAMRDSGMVIDWSHMNFGGPIVDKHSTGGVGDVTSLMLGPMVAACGGFVPMISGRGLGHTGGTLDKLEAIPGYNITPSNDVFGQVTKEAGVAIIGQTGDLAPADKRVYATRDITATVDNISLITASILSKKLAAGLESLVMDVKVGSGAFMPTYEASEELAKSIVAVANGAGTKTTAILTDMNQVLASSAGNAVEVREAVRFLKGEYRNPRLLEVTMASCAEMLVLGKLAENTEDARAKLMEVLDNGKAAECFGKMVAGLGGPVDFMDNYDNYLDKAEIIKPVYAKETGVVSAMDTRAIGMAVVAMGGGRRVATDSIDYAVGFDQFIRLGEIASSEKPLAMIHARNEAQWQEAANALQAAIKVGGEYTPTPDVYRQIRQEDI | The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | Q7MI39 |
Q5RF29 | UROK_PONAB | Urokinase-type plasminogen activator chain B | Pongo | MRALLARLLLCVLVVSDSKGSNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTCYEGNGHFYRGKASTDTMGRPCLAWNSATVLQQTYHAHRSDALQLGLGKHNYCRNPDNRWRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQKTLRPRFKIVGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVVSATHCFIDYPKKEDYIVYLGRSRLNSHTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIHSKEGRCAQPSRTIQTICLPSMYNDPPFGTSCEITGFGKENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSYFLPWIRSHTKEENGLAL | Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin. | Q5RF29 |
P08321 | TRAL1_ECOLI | Protein TraL | Escherichia | MSGDENKLKKYRFPETLTNQSRWFGLPLDELIPAAICIGWGITTSKYLFGIGAAVLVYFGIKKLKKGRGSSWLRDLIYWYMPTALLRGIFS | Membrane protein involved in F pilin formation. | P08321 |
Q87NA5 | YCIB_VIBPA | Inner membrane-spanning protein YciB | Vibrio | MKQILDFIPLIIFFALYKMYDIYVATGALIVATAVQLIVTYALYKKVEKMQLITFVIVTIFGSMTIFFHDDNFIKWKVTIIYVVLAVGLTASHLMGKSVVKGMLGKEITLPDAIWAKINWAWVGFFSFFAGLNIYIAYELPLDVWVNFKVFGMLIATFAYMIATGVYIYKHMPKEEKNNSSDVSVDD | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | Q87NA5 |
Q2UPG7 | YPI1_ASPOR | Type 1 phosphatases regulator ypi1 | Aspergillus subgen. Circumdati | MSRSRQIAPSGTSQVESVPQQPNNTSTVRVPGTLRLRAENEPTVESNTEGRGLHRHIRWSEDVIDNEGMGKRSSKVCCIYHKARPVGESSSESESSDSESSDADSDNEIDNPRNTLGRSSVHHITDNHSHEQESEHDRERGRLTCCPNHGHRKLKRRRPSPNAYEKMPKTTKGR | Regulator of type 1 phosphatases which maintains protein phosphatase activity under strict control. | Q2UPG7 |
Q7Z0T3 | TEMPT_APLCA | Temptin | Aplysia | MEQKRTLRVFLAVSLLCALANAYPQYQAVIPNGSSVPNPCNTSQIAQGVGHINFQGTGPLNPFGEDFKAAGKQWTTDLCDMDSDGDGRSNGVELGDPECVWSQGETPARTTDLSHPGFDEATVSC | A component of the complex of water-borne protein pheromones that stimulates attraction and mating behavior. Modulates pheromone signaling by direct binding to attractin. | Q7Z0T3 |
Q1GHJ3 | TRPD_RUEST | Anthranilate phosphoribosyltransferase | unclassified Ruegeria | MSDALKPLIGLAADRALTRTEAETAFAALFNGEATPSQMGGLLMALRTRGETVDEYAAAAAVMRAKCNKVSAPADAMDIVGTGGDGKGTLNISTATAFVVAGAGVPVAKHGNRNLSSKSGAADALTEMGIQVMVGPKVVEKSLKEAGICFMMAPMHHPAIAHVMPTRQELGTRTIFNILGPLTNPADVKRQLTGAFSRDLIRPMAETLKQLGSEVAWLVHGSDGTDELTITGVSWVAGLSEDGNISEFEVHPEEAGLPEHPFEAIVGGTPAENAAAFRALLEGTPSAYRDAVLLNSAAALKVAGVVSSLKEGAERAAESIDSGAALGKVTAVARITSEAS | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q1GHJ3 |
Q47NB6 | Y2020_THEFY | Nucleotide-binding protein Tfu_2020 | Thermobifida | MATSRGDDLLPEIVVVTGMSGAGRSTAARALEDLDWFVVDNLPPALLPTMIDLAARTRGAVPQIAAVVDVRSMAFTEDLLSTVEDLRSRGIGARVVFLEASDETLVRRFESVRRPHPLQGDGRLTDGISRERELLRSIRGEADLVVDTSQLNVHQLKAKMVGFFGKARETRLRANVVSFGYKHGLPVDADLVLDCRFLPNPHWVPELRPLTGQDEPVRDYVLAQRGAKEMLDSYTEVLRLLVSGYQREGKHYMTLAVGCTGGKHRSVAMSEQLAARLRDEGVEVNIIHRDLGRE | Displays ATPase and GTPase activities. | Q47NB6 |
O15060 | ZBT39_HUMAN | Zinc finger and BTB domain-containing protein 39 | Homo | MGMRIKLQSTNHPNNLLKELNKCRLSETMCDVTIVVGSRSFPAHKAVLACAAGYFQNLFLNTGLDAARTYVVDFITPANFEKVLSFVYTSELFTDLINVGVIYEVAERLGMEDLLQACHSTFPDLESTARAKPLTSTSESHSGTLSCPSAEPAHPLGELRGGGDYLGADRNYVLPSDAGGSYKEEEKNVASDANHSLHLPQPPPPPPKTEDHDTPAPFTSIPSMMTQPLLGTVSTGIQTSTSSCQPYKVQSNGDFSKNSFLTPDNAVDITTGTNSCLSNSEHSKDPGFGQMDELQLEDLGDDDLQFEDPAEDIGTTEEVIELSDDSEDELAFGENDNRENKAMPCQVCKKVLEPNIQLIRQHARDHVDLLTGNCKVCETHFQDRNSRVTHVLSHIGIFLFSCDMCETKFFTQWQLTLHRRDGIFENNIIVHPNDPLPGKLGLFSGAASPELKCAACGKVLAKDFHVVRGHILDHLNLKGQACSVCDQRHLNLCSLMWHTLSHLGISVFSCSVCANSFVDWHLLEKHMAVHQSLEDALFHCRLCSQSFKSEAAYRYHVSQHKCNSGLDARPGFGLQHPALQKRKLPAEEFLGEELALQGQPGNSKYSCKVCGKRFAHTSEFNYHRRIHTGEKPYQCKVCHKFFRGRSTIKCHLKTHSGALMYRCTVCGHYSSTLNLMSKHVGVHKGSLPPDFTIEQTFMYIIHSKEADKNPDS | May be involved in transcriptional regulation. | O15060 |
P63384 | UVRA_STRPN | Excinuclease ABC subunit A | Streptococcus | MQDKIVIHGARAHNLKNIDVEIPRDKLVVVTGLSGSGKSSLAFDTLYAEGQRRYVESLSAYARQFLGNMEKPDVDAIDGLSPAISIDQKTTSKNPRSTVGTTTEINDYLRLLYARVGTPYCINGHGAINASSVEQIVDKVLELPERQRLQILAPVIRKKKGQHKSVIEKVQKDGYVRVRVDGEVYDVTEVPELSKSKQHNIDVVVDRIVIKEGIRSRLFDSIEAALRIAEGYVIIDTMDDSELLFSEHYACPVCGFTVPELEPRLFSFNAPFGSCSECDGLGIKLEVDTDLVVPDASKTLREGALAPWNPISSNYYPNMLEQAMKVFGVAMDKPFEDLSEEDKNLILYGSDGKEFHFHYENEFGGVRDIDIPFEGVINNIKRRYHETNSDYTRTQMRLYMNELTCGTCQGYRLNDQALSVRVGGQQGPHIGEISDLSIADHLDLVSQLTLSENEAIIARPILKEIKDRLTFLNNVGLNYLTLSRSAGTLSGGESQRIRLATQIGSNLSGVLYILDEPSIGLHQRDNDRLIASLKKMRDLGNTLIVVEHDEDTMREADYLIDVGPGAGVFGGEIVAAGTPKQVARNSKSITGQYLSGKRVIPVPEERRVGNGRFIEVIGARENNLQNVTARFPLGKFIAVTGVSGSGKSTLINSILKKAIAQKLNRNSDKPGKFKTITGIEHVDRLIDIDQSPIGRTPRSNPATYTGVFDDIRDLFAQTNEAKIRGYKKGRFSFNVKGGRCEACSGDGIIKIEMHFLPDVYVACEVCHGTRYNSETLEVHYKEKNISQVLDMTVNDAVEFFQHIPKIQRKLQTIKDVGLGYVTLGQPATTLSGGEAQRMKLASELHKRSTGKSFYILDEPTTGLHTEDIARLLKVLARFVDDGNTVLVIEHNLDVIKTADHIIDLGPEGGVGGGTIIVTGTPEEVAANEASYTGHYLKGKLHHE | The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. | P63384 |
B3PXN0 | UPP_RHIE6 | UPRTase | Rhizobium | MDGVTVIDHPLVQHKLTIMRRKETSTGSFRRLLREISTLLCYEVTRDLELTMETIETPLQTIESPILEGKKLVFASILRAGNGLLEGMLDLVPSARVSHIGVYRDHETLQPVEYYFKAPEDVAERLIIVVDPMLATGNSSIAAIDKLKERGAHNIRFLCLLAAPEGIRNFRAAHPDVPVFTAAIDSHLNEKGYIVPGLGDAGDRMYGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | B3PXN0 |
Q4UNZ5 | TTCA_XANC8 | tRNA 2-thiocytidine biosynthesis protein TtcA | Xanthomonas | MTAVLPLPLPLADPAPRTPRLQREPLRLAKRLRHAVGQAIADFGMIAPGDKVMVCLSGGKDSYTLLDMLLQLQRSAPVPFTLVAVNLDQKQPDFPADVLPTYLRAQQVPFDIIEQDTYSVVSRVIPQGKTMCSLCSRLRRGALYAYAQAHGVTKIALGHHRDDIVATFFMNLFHHARLAAMAPKLRSDDGAHVVIRPLAYVREADIAAYAQARQFPIIPCNLCGSQENLQRQQVGRMLQQWDREQPGRVDQIARALGDVRPEQLADRTLFDFPGLGGGADAPLPDAAGWLAGSAAEHARD | 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. | Q4UNZ5 |
Q0CJV3 | VPS27_ASPTN | Vacuolar protein sorting-associated protein 27 | Aspergillus subgen. Circumdati | MAGWFSSASPLDEQVERATSSSLEDIALNLEISDLIRSKSVQPKEAMRSLKRRLENKNPNVQLATLKLTDTCVKNGGTHFLAEIASREFMDNLVSLLKTEGLQLNTEVKEKMLELIQDWAMAAQGRMDLSYVGQTYQRLQEEGFRFPPKTQISGSMLESSAPPEWIDSDVCMRCRTAFSFMNRKHHCRNCGNVFDAQCSSKTLPLPHLGILQPVRVDDGCYAKLTSKAAQSSGLSDRTSFKNNSITKSSAMEPRTARAEGGFDDDLRRALQMSLEEAQNKGSSGYVPQPKVAQEPPKPSGQPTAEEEEDADLKAAIEASLRDMEEHKQKHAAALKNTTSETPSHQPQNTTTLPKNPYELSPVEVENIHLFAALVDRLQHQPPGTILREPQIQELYESIGTLRPKLARSYGETMSKHDTLLDLHSKLSTVVRYYDRMLEERLSSAYSQHSLGYGSIPSGPGYPNVYPSMPPTAEGKAGAENFYYGNSVVENPLTASNPQYPQAAPDMMSREKDTHARRPYEPQYVYTALHSLSTTILQWNGAPATDLHSPPPSANVP | 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. | Q0CJV3 |
Q5D7I1 | TRIM5_ATEGE | TRIM5alpha | Ateles | MASEILLNIKEEVTCPICLELLTEPLSLDCGHSFCQACITANHKESTLHQGERSCPLCRVSYQSENLRPNRHLANIAERLREVMLSPEEGQKVDRCARHGEKLLLFCQQHGNVICWLCERSQEHRGHSTFLVEEVAQKYQEKLQVALEMMRQKQQDAEKLEADVREEQASWKIQIENDKTNILAEFKQLRDILDCEESNELQNLEKEEENLLKTLAQSENDMVLQTQSMRVLIADLEHRLQGSVMELLQDVEGVIKRIKNVTLQKPKTFLNEKRRVFRAPDLKGMLQVFKELKEVQCYWAHVTLVPSHPSCTVISEDERQVRYQEQIHQPSVKVKYFCGVLGSPGFTSGKHYWEVDVSDKSAWILGVCVSLKCTANVPGIENYQPKNGYWVIGLQNANNYSAFQDAVPGTENYQPKNGNRRNKGLRNADNYSAFRDTFQPINDSWVTGLRNVDNYNAFQDAVKYSDFQDGSCSTPSAPLMVPLFMTICPKRVGVFLDCKACTVSFFNVTSNGCLIYKFSKCHFSYPVFPYFSPMICKLPMTLCSPSS | Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. | Q5D7I1 |
B3DN87 | ZDH12_ARATH | Zinc finger DHHC domain-containing protein At3g56920 | Arabidopsis | MSSQNLERQRIYQVWPAKNKFYCGGRLVFGPDASSLLLTTCMIGGPAIAFSIRMAYLISHRHPFFHSLTLIGAILLTFMAFTFLFLTSSRDPGIIPRNKQVSEAEIPDVTTQSTEWVTSKLGSVKLPRTKDVMVNGFTVKVKFCDTCQLYRPPRAFHCSICNNCVQRFDHHCPWVGQCIALRNYPFFVCFLSCSTLLCIYVFVFSWVSMLKVHGEFYVVLADDLILGVLGLYCFVSVWFVGGLTVFHFYLICTNQTTCENFRYHYDKKENPYRKGILENFKELFFAKIPPPLINFRDWSPEEEDDVEVGSIASELVRAFGPKDTKMSSGKSDSEARER | Palmitoyl acyltransferase. | B3DN87 |
Q56837 | XECA_XANP2 | Epoxyalkane:CoM transferase | Xanthobacter | MLIRGEDVTIPTSMVGNYPNPRWWDAQFARTWTGDQEPPDALIQESLEDAVAAIARDQERAGLDIISDGRVHGDNYAEQALYYYYRRLGYDLKGGYLGFPIYSRLHAGTLTGEVRRHGAIMVEQAKALKKATGKPTKVQYTGVQALTQATNDLHYKSSRDRAMAIAKAINEDIREVDALGVDFIQIDEFTWPYFFEDWAIEAFNAAVDGVKNAKIIAHVCWGNWGGTPAYYPDETAASGEIFDLTKRKAEATKATATGSIVPKAYEARLDVLNLESCGRRSDDLSGLHVMKNHPLPDNVSFWAGVIDVKSTITETADEVANRIRRLLEIVPADRLGVTTDCGLILLQRYIAQDKLHALVEGTKIVRAELAKAKQAA | Involved in aliphatic epoxide carboxylation . Catalyzes the addition of coenzyme M (CoM) to either R- or S-epoxypropane to form the thioether conjugate 2-hydroxypropyl-CoM . Catalyzes the reaction of CoM with R-epoxypropane at a rate approximately twice of that with S-epoxypropane . The CoM analogs 2-mercaptopropionate, 2-mercaptoethanol and cysteine substitute poorly for CoM as the thiol substrate . | Q56837 |
C4K3E8 | TRUB_HAMD5 | tRNA-uridine isomerase | Candidatus Hamiltonella | MKSKRRHSGRDVNGILLLDKPKNFSSNQVLQKVKSLFAARRAGHTGALDPLATGMLPICLGEATKFSPFLLNADKRYRVTAYLGHKTETSDAEGSVINKREITFTQPQLEEALEKFRGPILQIPSMYSALKHQGRPLYEYARQGVTLDREARRITVFDLQCLRWEGHELELEIHCSKGTYIRTIVDDLGEVLGCGAYVSDLRRLQVADYTHDSMVTLEKLEELTLKNNTLGSAIDLLLLPIESTALHLPEVNLESGAAACIKQGQPVSFFDNPTDTMVRLTEGGERHFIGIGIIDAHGRIAPKRLLRNVSDAL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | C4K3E8 |
Q32KN8 | TBA3_BOVIN | Detyrosinated tubulin alpha-3 chain | Bos | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKLDLMYAKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGVDSVEAEAEEGEEY | 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 . | Q32KN8 |
Q3YXI5 | UPPP_SHISS | Undecaprenyl pyrophosphate phosphatase | Shigella | MSDMHSLLIAAILGVVEGLTEFLPVSSTGHMIIVGHLLGFEGDTAKTFEVVIQLGSILAVVVMFWRRLFGLIGIHFGRPLQHEGESKGRLTLIHILLGMIPAVVLGLLFHDTIKSLFNPINVMYALVVGGLLLIAAECLKPKEPRAPGLDDMTYRQAFMIGCFQCLALWPGFSRSGATISGGMLMGVSRYAASEFSFLLAVPMMMGATALDLYKSWGFLTTGDISMFAVGFITAFVVALIAIKTFLQLIKRISFIPFAIYRFIVAAAVYVVFF | Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. | Q3YXI5 |
Q20Z78 | UREG_RHOPB | Urease accessory protein UreG | Rhodopseudomonas | MSDYHGPLRVGIGGPVGSGKTALMDLLCKTLRDRYQIAAITNDIYTKWDAEFLVRSGSLTQDRIVGVETGGCPHTAIREDASMNLAAVADMRAKFPDLDLVLIESGGDNLAATFSPELADLTIYVIDVAAGDKIPSKGGPGITRSDLLVINKIDLAPYVGASLDKMQIDAKRMRGERPFVMTNLKTQEGLDRIVGFIEAKGGLRAGS | Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG. | Q20Z78 |
Q0I0Z1 | YIDC_HAES1 | Membrane protein YidC | Histophilus | MDSKRSLLFMALLFISFLIYQQWQVDYNTPKPEMTEQAQVSEVNSTALTATSDIANDTQAKGRVITLENDVFRLKVNTLGGDVIGSELLNYDAELHSSAPFVLLQNNADKVYIAQSGLVGKNGIDSRAGRANYQVEGDVFKLAEGQQELKVPLVFEKDGVIYRKVFVLKPGSYALEVNFEITNQSPKPIEVVPYAQLTHTLVESSGSMAMPTYTGGAYSSSETNYKKYSFEDMEKADLDIHTKAGWVALLQHYFVSAWIPNQDANNTLYTLTNTKKHLGSIGYRSAPIVIENGATETIHTQLWTGPKLQDQMADVANHLDLTVDYGWAWFIAKPLFKLLTLIQSLVQNWGLAIIGVTLVVKAILYPLTKAQYTSMAKMRMLQPKLQEMRERFGEDRQRMSQEMMKLYKEEKVNPLGGCLPILLQMPIFIALYWTFMEAVELRHAPFFGWVQDLSAQDPYFILPILMGASMFLLQKMSPTPVADPMQQKVMTFMPLIFMVFFLFFPAGLVLYWLASNLITIAQQWLIYRGLEKKGLHTRVKK | 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. | Q0I0Z1 |
A5VLH4 | TRUA_LIMRD | tRNA-uridine isomerase I | Limosilactobacillus | MYRYKITFAYDGTNFSGFQIQPNKRTVEQTLKNAVNKIAKHPTPAIPVIGSGRTDAGVHALNQVAHFDIPYHLSNESMRKALNSILPLDILIKKAELVDNDFHARYSAHRKTYRYRVDQGEFVNPFKRNYTSHFKYPLNLEKMRKAADDLVGTHDFTSFVASGSQAKSNVRTIENITIKRDEVRNEVVFDFTGNGFLYNQVRIMVAFLLEIGSNQRPVDDVSRVLKAKDRTLARMTAPASGLYLVNVDYGTNDEKD | Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. | A5VLH4 |
Q7N8P2 | UPPS_PHOLL | Undecaprenyl pyrophosphate synthase | Photorhabdus | MILSSDHHQNDLSSLLPKHVAIIMDGNGRWAKKRGKLRAFGHRAGIKAVRSAVSFSAKHNIESLTLYAFSSENWNRPEQEVSSLMELFIFALDSEIKSLHKHNIRLSVIGDIGRFSERLQDRIHRSVKLTANNTGLQLNIAANYGGRWDIVQSVQKIAQQIKDNSLEQQDITEELVNNYMNLSQQPQVDLVIRTGGEHRISNFLLWQIAYAEFYFTDILWPDFDENVFEGAINAFAKRERRFGGTIPDDADVGS | 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. | Q7N8P2 |
P60513 | U6A_CONER | Delta-conotoxin EVIA | Chelyconus | DDCIKPYGFCSLPILKNGLCCSGACVGVCADL | Delta-conotoxins bind to site 6 of voltage-gated sodium channels and inhibit the inactivation process. This toxin inhibits sodium channel inactivation in neuronal membranes from amphibians and mammals (Nav1.2a/SCN1A, Nav1.3/SCN3A and Nav1.6/SCN8A) upon binding to receptor site 6. | P60513 |
O25701 | TATC_HELPY | Sec-independent protein translocase protein TatC | Helicobacter | MFEDLKPHLQELRKRLMVSVGTILVAFLGCFHFWKSIFEFVKNSYKGTLIQLSPIEGVMVAVKISFSAAIVISMPIIFWQLWLFIAPGLYKNEKKVILPFVFFGSGMFLIGAAFSYYVVFPFIIEYLATFGSDVFAANISASSYVSFFTRLILGFGVAFELPVLAYFLAKVGLITDASLKAYFKYAIVVIFIVAAIITPPDVVSQIFMALPLVGLYGLSILIAKMVNPAPKDNENNNENNNENNTKENTKSES | 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. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. | O25701 |
B2I782 | TPIS_XYLF2 | Triose-phosphate isomerase | Xylella | MRPKIVAGNWKLHGSHAFAQALVAQVAAGLPLPGVSVIILPPLLYLSDLAQRFKGEGLAFGAQNVSHHDKGAYTGEVSAAMVADVGAHYTLVGHSERREYHHEDSELVARKFAAALSAGLRPILCVGESLPQREAGQAEVAIAMQLAPVLALVGPQGVARGLIAYEPVWAIGTGRHADPSQVQAMHAFIRGEIARQDARIGDSLLILYGGGIKPCNAAELFSQQDVDGGLIGGASLVADDFLAIARATV | Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). | B2I782 |
Q5RFR0 | TTPAL_PONAB | Alpha-tocopherol transfer protein-like | Pongo | MSEESDSLRTSPSVASLSENELPPPPEPPGYVCSLTEDLVTKAREELQEKPEWRLRDVQALRDMVRKEYPNLSTSLDDAFLLRFLRARKFDYDRALQLLVNYHSCRRSWPEVFNNLKPSALKDVLASGFLTVLPHTDPRGCHVVCIRPDRWIPSNYPITENIRAIYLTLEKLIQSEETQVNGIVILADYKGVSLSKASHFGPFIAKKVIGILQDGFPIRIKAVHVVNEPRIFKGIFAIIKPFLKEKIANRFFLHGSDLNSLHTNLPRSILPKEYGGTAGELDTATWNAVLLASEDDFVKEFCQPVPTCDSILGQTLLPEGLTSDAQCDDSLRAVKSQLYSCY | May act as a protein that binds a hydrophobic ligand. | Q5RFR0 |
A7MQI7 | WZYE_CROS8 | Probable ECA polymerase | Cronobacter | MSLLQFSGLFIVWLLATLFIGTLTWFEFRRVRFNFNVFFSLLFLLTFFFGFPLTSILVFRFNVAVVPAEVLLQALLSAGCFYAVYYVTYKTRLRTARAQAASSGGGLFTMNRVETHLAWMVMMAVALVSVGIFFMHNGFLLFRLHSYSQIFSSEVSGVALKRFFYFFIPAMLVVYFLRQSSRAWLFFLVSTVGFGLLTYMIVGGTRANIIIAFAIFLFIGIIRGWISPGMLAAAGVMGIVGMFWLALKRYGLNVSGDEAFYTFLYLTRDTFSPWENLALLLQHYGDIEFQGLAPIARDFYVFIPSWVWPDRPHIVLNTANYFTWEVLNNHSGLAISPTLLGSLVVMGGVWFIPPGAVVVGLIIKWFDWLYERGNHEPNRYKAAILHSFCFGAIFNMIVLAREGLDAFVSRVIFFMVVFGACLVVAKLIYWLLDSAGLIQPRRRRAAPLSPTETL | Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. | A7MQI7 |
B3EII6 | TAL_CHLL2 | Probable transaldolase | Chlorobium | MKFFIDTANLDEIRSAAELGVLDGVTTNPSLIAKIVGDPSNFTYGDFKEHIRRICEIVDGPVSAEVTCLKAEEMIAQGEDLAAIHENVVVKCPLTIDGLKAIKHFSASGIRTNATLVFSPNQALLAAKAGADYVSPFVGRLDDISTDGMELVEQIVTIYDNYGYPTEVIVASVRHPQHVVTAAMMGADIATIPYSVIKQLANHPLTDAGLTKFMDDAAVMKK | Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | B3EII6 |
P27242 | WAAU_ECOLI | Lipopolysaccharide 1,2-N-acetylglucosaminetransferase | Escherichia | MRLGTFHKKKRFYINKIKINFLSFLFRNKINNQITDPAQVKSCLIIHDNNKLGDLIVLSSIYRELYSKGVKITLLTNRKGGEFLSNNKNIFEFCIKESTGFLEMLTLCKHLRDLQFDIVLDPFETMPSFKHSLILSSLKDSYILGFDHWYKRYYSFYHPHDECLKEHMSTRAIEILKHIYGEGKFSTNYDLHLPVDVEDKIKEFIGDTRIVIINPLGAKKICRLTFEQIKVIYQEVKTHFENYRIIFTGLPQDLLTIPILEIETLPFDEFIYTVALTKYSDFVISVDTALVHIAAAYHKPTLAFYPNSRTPEYPSHLIWSPNHHKSIQIVSPTYTVKDIDTETLTNSVKRLSCIDKK | Adds the terminal N-acetyl-D-glucosamine group on the glucose(II) group of LPS. | P27242 |
Q80TB7 | ZSWM6_MOUSE | Zinc finger SWIM domain-containing protein 6 | Mus | MAERGQQPPPAKRLCCRPGGGGGGGGGGGGSSGGGAGGGYSSACRPGPRAGGAAAAAACGGGAALGLLPPGKTQSPESLLDIAARRVAEKWPFQRVEERFERIPEPVQRRIVYWSFPRSEREICMYSSFNTGGGSAGGPGDDSGGGGGRQHGRGAAAGGSSSSPAATSAAAAAVAAGTGTPSVGAASAADGGDETRLPFRRGIALLESGCVDNVLQVGFHLSGTVTEPAIQPEPETVCNVAISFDRCKITSVTCSCGNKDIFYCAHVVALSLYRIRKPEQVKLHLPISETLFQMNRDQLQKFVQYLITVHHTEVLPTAQKLADEILSQNSEINQVHGAPDPTAGASIDDENCWHLDEEQVQEQVKVFLSQGGYHGSGKQLNMLFAKVREMLKMRDSNGARMLTLITEQFMADPRLSLWRQQGTAMTDKYRQLWDELGALWMCIVLNPHCKLEQKASWLKQLKKWNSVDVCPWEDGNHGSELPNLTNALPQGANANQDSSNRPHRTVFTRAIEACDLHWQDSHLQHIISSDLYTNYCYHDDTENSLFDSRGWPLWHEHVPTACARVDALRSHGYPREALRLAIAIVNTLRRQQQKQLEMFRTQKKELPHKSITSITNLEGWVGHPLDPVGTLFSSLMEACHTDGDAFSGFSDCTDNMGQCKSLEYHHLPAHKFLEEGESYVTLAVEVALIGLGQQRIMPDGLYTQEKVCRNEEQLISKLQEIELDDTLVKIFRKQAVFLLEAGPYSGLGEIIHRESVPMHTFAKYLFTSLLPHDAELAYKIALRAMRLLVLESTAPTGDLSRPHHIASVVPNRYPRWFTLSHIESQQCELASTMLTAAKGDVRRLETVLESIQKNIHSSSHIFKLAQDAFKIATLMDSLPDITLLKVSLELGLQVMRMTLSTLNWRRREMVRWLVTCATEVGVYALDSIMQSWFTLFTPTEATSIVATTVMSNSTIVRLHLDCHQQEKLASSARTLALQCAMKDPQNCALSALTLCEKDHIAFETAYQIVLDAATTGMSYTQLFTIARYMEHRGYPMRAYKLATLAMTHLNLSYNQDTHPAINDVLWACALSHSLGKNELAAIIPLVVKSVKCATVLSDILRRCTLTTPGMVGLHGRRNSGKLMSLDKAPLRQLLDATIGAYINTTHSRLTHISPRHYSEFIEFLSKARETFLMAHDGHIQFTQFIDNLKQIYKGKKKLMMLVRERFG | involved in nervous system development, important for striatal morphology and motor regulation. | Q80TB7 |
P17717 | UDB17_MOUSE | UDP-glucuronosyltransferase 2B5 | Mus | MPGKWISALLLLQISCCFRSVKCGKVLVWPMEFSHWMNIKIILDELVQRGHEVTVLRPSAYYVLDPKKSPGLKFETFPTSVSKDNLENFFIKFVDVWTYEMPRDTCLSYSPLLQNMIDEFSDYFLSLCKDVVSNKELMTKLQESKFDVLLSDPVASCGELIAELLQIPFLYSIRFSPGYQIEKSSGRFLLPPSYVPVILSGLGGQMTFIERIKNMICMLYFDFWFQMFNDKKWDSFYSEYLGRPTTLVETMGQAEMWLIRSNWDLEFPHPTLPNVDYVGGLHCKPAKPLPKDMEEFVQSSGDHGVVVFSLGSMVSNMTEEKANAIAWALAQIPQKVLWKFDGKTPATLGHNTRVYKWLPQNDLLGHPKTKAFVTHGGANGVYEAIYHGIPMIGIPLFGEQHDNIAHMVAKGAAVALNIRTMSKSDVLNALEEVIENPFYKKNAIWLSTIHHDQPMKPLDRAVFWIEFVMRHKRAKHLRPLGHNLTWYQYHSLDVIGFLLSCVATTIVLSVKCLLFIYRFFVKKENKMKNE | UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol). | P17717 |
P83303 | TXH4_CYRSC | Mu-theraphotoxin-Hs2a | Cyriopagopus | MVNMKASMFLALAGLVLLFVVCYASESEEKEFSNELLSSVLAVDDNSKGEERECLEIFKACNPSNDQCCKSSKLVCSRKTRWCKYQIGK | This lethal neurotoxin (without cyclization at position 53) inhibits neuronal voltage-gated sodium channel Nav1.2/SCN2A (IC(50)=10-150 nM), rNav1.3/SCN3A (IC(50)=338 nM), Nav1.6/SCN8A (IC(50)=117 nM), and hNav1.7/SCN9A (IC(50)=9.6-33 nM) . It inhibits activation of sodium channel by trapping the voltage sensor of domain II (DIIS4) in the closed configuration . The toxin neither shifts the Nav1.7/SCN9A activation curve nor modifies the slope factor . It does not slow fast-inactivation of hNav1.7/SCN9A channels . In addition, it has only a weak affinity for lipid membranes . This toxin also exists with a pyroglutamate at position 53 . The sole difference observed between modified (mHwTx-IV) and unmodified toxins is that moderate or high depolarization voltages (200 mV) permit the unmodified toxin to dissociate, whereas mHwTx-IV toxin does not dissociate, even at high depolarization voltages . These data indicate that mHwTx-IV strongly binds to voltage sensor of sodium channel even at extreme depolarization voltages . | P83303 |
Q928B9 | Y2617_LISIN | Nucleotide-binding protein lin2617 | Listeria | MASKQLKLVIITGMSGAGKTVAMQSLEDLGYFCVDNLPPSLLPKFWELMKESDKMDKIALVMDLRGREFFDSIEPALDELDNTNFITTKILFLEADDKVLVSRYKETRRHHPLEPNGSVLDGINAERELLSDLKGRSQLVINTSNMAPRELRERINNEFQTEDKDVFNVQLMSFGFKYGIPIDADLVFDVRFLPNPHYIDKMRPLTGLDEDVYEYVMKWPETMAFLDKLVDLLMFTLPFYKREGKTQLVIAIGCTGGQHRSVALTEYVGKAIQQKYETTISHRDMKRRKER | Displays ATPase and GTPase activities. | Q928B9 |
Q720Y7 | TARI_LISMF | Ribitol-5-phosphate cytidylyltransferase | Listeria | MIYAQILAGGKGTRMGNVSMPKQFLPLNGKPIIVHTVEKFILNTRFDKILISSPKEWMNHAEDNIKKYISDDRIVVIEGGEDRNETIMNGIRFVEKTYGLTDDDIIVTHDAVRPFLTHRIIEENIDAALETGAVDTVIEALDTIVESSNHEVITDIPVRDHMYQGQTPQSFNMKKVFNHYQNLTPEKKQILTDACKICLLAGDDVKLVKGEIFNIKITTPYDLKVANAIIQERIAND | Catalyzes the transfer of the cytidylyl group of CTP to D-ribitol 5-phosphate. | Q720Y7 |
Q9X1H9 | Y1468_THEMA | Fatty acid-binding protein TM_1468 | Thermotoga | MKVKILVDSTADVPFSWMEKYDIDSIPLYVVWEDGRSEPDEREPEEIMNFYKRIREAGSVPKTSQPSVEDFKKRYLKYKEEDYDVVLVLTLSSKLSGTYNSAVLASKEVDIPVYVVDTLLASGAIPLPARVAREMLENGATIEEVLKKLDERMKNKDFKAIFYVSNFDYLVKGGRVSKFQGFVGNLLKIRVCLHIENGELIPYRKVRGDKKAIEALIEKLREDTPEGSKLRVIGVHADNEAGVVELLNTLRKSYEVVDEIISPMGKVITTHVGPGTVGFGIEVLERKR | Binds long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | Q9X1H9 |
A8I4T0 | UREF_AZOC5 | Urease accessory protein UreF | Azorhizobium | MTMAETGAPPSALALFAWLSPGFPVGAYAYSHALEWAAEAGDITDESSLESWLRDLMLLGFGRADGILLAHAYGAGAAGDVPALAQVNARAVALSPTAELRLETCQQGRSFLDAVRAAWPHGGLDAAAAHLPPDVAYPVAVGYAAALHGVPRAAVLEAYLFAVTQTLVSAALRIAPIGQTAGTRVVARLMPAVQALAGDIPTLTLDDLGTATFRADLGSMRHETQYTRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A8I4T0 |
Q8EUW1 | Y807_MALP2 | Nucleoid-associated protein MYPE8070 | Malacoplasma | MNMQKMLQQAKALQSKMEKKIKEFEQEEFEFVYQKSITIQIKGNYEIIKMDINKELIDPEDKTMLEEMISEAINEAISAITEEKEKITKGAMPF | Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection. | Q8EUW1 |
Q8I7H9 | TTR33_CAEEL | Transthyretin-like protein 33 | Caenorhabditis | MSRLACISSLFILCAIGSEAVFTQSAGVKGVLMCGDKPLANTKVKLYDDDTGPDLDDLLAEGTTDSLGQFLLTGHTSEVMTIDPKLNIYHDCDDGLKPCQRRVTFNIPKSFVSSGENPKTFFNIGTINMQIEFESESRDCLHR | Protects dopaminergic neurons from degeneration caused by oxidative stress. | Q8I7H9 |
A7GRE0 | TRUB_BACCN | tRNA-uridine isomerase | Bacillus cereus group | MEGVVLLHKPKGMTSHDCVFKLRKILREKRIGHTGTLDPDVTGVLPICVGRATKIAQFLTSETKTYEGEVTLGFSTTTEDASGEVVEKQDVNRTITRKEIEAVLAELTGTLEQVPPMYSAVKVNGKKLYEYARAGQEVKRPVRIITIHEFTLLDNRETFEGANISFRFRVTCSKGTYVRTLAVMIGEKLGFPAHMSDLVRTASGEFQLHDCVSFEEIEENMQNGTVESVFISIDEALSKFPKIVVDEKQAEKIKNGMFLKNEIQAETPFITVFDRNNHCLAIYEHHPKRPGMLKPMKVLVNNQELKL | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | A7GRE0 |
C6E9G2 | UVRC_GEOSM | Excinuclease ABC subunit C | unclassified Geobacter | MITQAMIENFPSSPGVYLMKSADDTVIYVGKARNLKKRVRSYAGDTRDSRIHIRFMVQLVHSVDYLVTDTEKEALILENTLIKQHRPKYNINLRDDKTYFSLRMDMKEQFPRLSIVRKIPSDGARYFGPYASATAAKEVLKQLYKMFPLRHYPLATCMARKRPCLYHQIKQCSAPCCGLISAAEYAALAQGAALFLEGKNNEVARLYRSKMNLASEQMRYEDAARYRDLLRAIEVTVERQKMVAQSGDSDVFGVHREADRMQIALLHIRGGTLTGGRSFLFDWELETEEGLASFLNEYYDLDAPIPPQVLIPLPIAEPAALEELLSEKAGKKVTIAVPQRGPKLEMVKLAGKNAETAAQERLARESSSATLLTELAEKLNLPHPPRRIECYDISNIQGEMAVGSRVVFIDGRADKSLYRRYRIKGVLQSDDFAMMREVLSRRFKADSHEEKPDLIVVDGGLGQLGVLNAVLDELEVTGVEAAGLAKSRVARDMESEEIERSDERVFRPGRKNAIALRQSSAPLLLLVRIRDEAHRFAVTYHKDVRSKVLTGSELDGVAGIGEKRKKALLKHFGSLKRVKEATLEELKGAPGMTESAARALVERLHGGPLPNPPPPGEGAMGDGSIPSPRNGVMDDSIPSPSGRGWPKAG | 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. | C6E9G2 |
Q144Q1 | YQGF_PARXL | Putative pre-16S rRNA nuclease | Paraburkholderia | MSLAAGREATLLAFDYGEKRIGVAVGNSLTKSARPLVIVQNRSREYRFEAVGKLIAEWKPNALVVGLPMHPDGTPHEMTQLAKRFGNQLNGRFNLPVTWIDERYSSVEAKAEIRAGNGRADMLDAEAASIILQQYLDGLSDDHEFH | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | Q144Q1 |
B5DFN3 | UQCC2_RAT | Mitochondrial protein M19 | Rattus | MAALRYRRFLKLCEEWPVDETKRGRDLGAYLRQRVAQAFREGENTQVAEPEACDQMYESLARLHSNYYKHKYPRPRDTSFSGLSVEEYKLILSTDTLEEFQEMNKSVWRKLQEKFAPTRPEEKHRAWTRVLSRPRT | Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex). Plays a role in the modulation of respiratory chain activities such as oxygen consumption and ATP production and via its modulation of the respiratory chain activity can regulate skeletal muscle differentiation and insulin secretion by pancreatic beta-cells. Involved in cytochrome b translation and/or stability. | B5DFN3 |
P48615 | WNT11_MOUSE | Protein Wnt-11 | Mus | MRARPQVCEALLFALALHTGVCYGIKWLALSKTPAALALNQTQHCKQLEGLVSAQVQLCRSNLELMRTIVHAARGAMKACRRAFADMRWNCSSIELAPNYLLDLERGTRESAFVYALSAATISHTIARACTSGDLPGCSCGPVPGEPPGPGNRWGGCADNLSYGLLMGAKFSDAPMKVKKTGSQANKLMRLHNSEVGRQALRASLETKCKCHGVSGSCSIRTCWKGLQELQDVAADLKTRYLSATKVVHRPMGTRKHLVPKDLDIRPVKDSELVYLQSSPDFCMKNEKVGSHGTQDRQCNKTSNGSDSCDLMCCGRGYNPYTDRVVERCHCKYHWCCYVTCRRCERTVERYVCK | Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters. | P48615 |
Q65TF2 | TRPD_MANSM | Anthranilate phosphoribosyltransferase | Basfia | MRIKTRNFIMQTQQILTQLFDNQPLSQEQAAFIFGNIVKGELSNEQLAGALIALKIRGETIDEITGAVTALLAAAEPFPAPDYPFADIVGTGGDNADTINISTASAIVAASMGLKIAKHGNRSVSSKTGASDVLTALGVNIRMSTEQARKALDEIGIAFIFAQQYHLGFKYAGPVRQALKTRTIFNILGPLINPANPKRQLLGVYSPELLKPYAETNLRLNHEHSIIVHGCGLDEVAIHGLTQVAELRDGKIEYYNLSPKDFGFEPQPLESLRGGAPEENAKILTALLQGKGSEQQAQAVAMNTALLMKLFGHEDIKQNAQQVLEQLTTGKAFETLTKLTTY | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | Q65TF2 |
B1ZVE0 | YQGF_OPITP | Putative pre-16S rRNA nuclease | Opitutus | MRCLGIDYGTRRIGLAYGDELGVATPLPALVEADPAKRWQSLLATARQRRVTDLVVGHPLNMDDTAGPKAKEAEAVAARLRTELAGVDVHLVDERLTSYEAEATISKTQRRAVRASGVIDSRAATLILQDFLDQRFPPPLPHPAE | Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA. | B1ZVE0 |
B8D4P0 | TRPB_DESA1 | Tryptophan synthase beta chain | Desulfurococcus | MELRSTQTPDILPSYWYNIVPDLPEPLPPMIHPSGEPVKRSELEVLFPRSLVDQEISTQSRIPIPEAVRETLLMLGRPTPLIRARRLEEALKTNARIFFKYEGVLPTGSHKINTAVAQAYYNAVESVERVSTETGAGQWGSALSLAGNIYGLKVRVFMVRASYLQKPYRRILMEAYGAEVYPSPSTKTNTGRKLLAENPDHPGSLGIAISEAIEDVVLSGGRAKYSLGSVLNHVLLHQSVIGLEAIKQLELLGVERVDYVIGCVGGGSNFAGLSYPFIGYNYNNGEPPVFIAVEPETVPSMTRGEYRYDYGDTAGLTPLLKMYTLGHDYIPPPIYAGGLRYHGVAPSLSILVKNNIVKPVAYPQDEVLEAGLVFARTQGILPAPESSHAVKAVIDVALKYRGASEKPTILFNLSGHGLLDLSAYTRNH | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | B8D4P0 |
Q0BGZ5 | UVRC_BURCM | Excinuclease ABC subunit C | Burkholderia cepacia complex | MTSPEAVDIPFEPKKILAQLPHMPGVYRYYDTAGAVLYVGKARDLKKRVSSYFTKTQLSPRIAMMVTRIARIETTVTRSEAEALLLENNLIKALAPRYNILFRDDKSYPYLKLTAHRFPRMAYYRGSVDKQNQYFGPFPSAWAVRESIQILQRVFQLRTCEDSVFNNRTRPCLLHQIGRCTAPCVGAISADDYAIDVSNAARFLLGRQSEVMKELEQKMHAFAAELKFEQAAAVRNQMSSLATVLHQQAIEVGSDSDVDILAVVAQGGRVCVNLAMVRGGRHLGDKAYFPAHVESALTLAEGGLGDEADGADGADEAAAALPGEPADEAAAARDAASSASGASSASVEAEVLDAFIAQHYLGNRVPPVLVVSHAPASRDLLELLSEQAGHKVSLVRQPQGQRRAWLSMAEQNARLALARLLSEQGSQQARTRALAETLSFECDDLAMLRIECFDISHTMGEATQASCVVYHHHKMQSGEYRRYNITGITPGDDYAAMRQVLTRRYEKMVEQAAQAAAADAAAGIDGESTREAEASSLLPNIVLIDGGKGQVEIARQVFTELGLDTSMLVGVAKGEGRKVGLETLVFADGRTPLELGKESAALMLVAQIRDEAHRFAITGMRAKRAKARQTSRLEELEGIGAKRRQRLLARFGGLRGVVAASVEELASVEGISHALAEQIYKQLH | 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. | Q0BGZ5 |
Q7RZJ2 | VPS27_NEUCR | Vacuolar protein sorting-associated protein 27 | Neurospora | MMSWWSSGANTALDEQIEKATSSSLEDIALNLEISDVIRSKTVQPKEAMRSLKKRINHKNPNTQLSALNLTDTCVKNGGAHFLAEIASREFMENLVGLLKAVGPAAPNPDVRNKILDLIQSWAMAAEGRYELSYIGEVYKTLQREGYSFPPKPTVASSMIDSSAPPEWVDSDVCMRCRTAFTFTNRKHHCRNCGNCFDQQCSSKSLPLPHLGIMQAVRVDDGCYAKLTDKGGKSGGSDRKHHSSSRHHHHHHKHKSSSSMQPRDARVDDSFDEDLKRALAMSLEEVKSYSRGHSEPANSTQYKPDKQSTSVSKIAEEEDEDLKAAIAASLADMEEQKKRHAAALKEQTSNVGSSSSAAPFTLPKNDYELTPVEAENINLFATLVDRLQTQPPGTILREPQIQELYDSIGALRPKLARTYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSKAYGQHSIGGYNLPAPRQPTGPYPTLDPSAPSAPGAAENFYTGEQQADYSHAPYGQYPPQPPQSQYMPYDRRSSMVGPPNPQYPQQQMPQRTGSWGNAPPAQAPQYNYSGNEVAPSQPGHAQQAQPGAPESAPGAPNNDPNASYYYNPGQPQQQQQQSAQQAPAAAPDHSYPTLPQQGHSYQPSVPQTPASVPVQPSQTPQQAHQRVPPPQQAPQQPYWQHSAAQQTPLPPVWQAPQQTTTYPGYDQEAFPSAPQHAPAPKQPVVEEALIEL | 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. | Q7RZJ2 |
A1KBB2 | UREF_AZOSB | Urease accessory protein UreF | Azoarcus | MSTNPAGGLLPLIRLLQLASPALPVGAYTYSQGLEWAVECGTVRTEADARRWIGDVLEWSLARFEAPLVARLLAAWADGDDAEVARLNEDFLASRETSELRAETVQMGYSLVRLLADLDAFAGLPGWKARLVALDTPAFPVAWTAAAAAWRIPADQALSAYLWAWLENQVMAAVKAVPLGQSAGQRLLADLGAAVPALVEAAQCLPEAEWSNFTPGLAIASSRHETQYTRLFRS | Required for maturation of urease via the functional incorporation of the urease nickel metallocenter. | A1KBB2 |
Q8XIU5 | YBEY_CLOPE | Endoribonuclease YbeY | Clostridium | MIFIDNRQNKFDVTEELTTKLEEVISFVLKEEKVKEDCEVSLVFVDNEEIRGINNETRGIDKATDVLSFPMIDYPEDKVYKDVYLEHEFDKCYFDGDELILGDIVLSLERTKEQSIEFNHSFEREACYLVTHSVLHLLGYDHMEEEEKARMRGREEELLGKLNITRES | Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. | Q8XIU5 |
A4VLX7 | UBIG_PSEU5 | 3-demethylubiquinone 3-O-methyltransferase | Pseudomonas | MSNVDHAEIAKFEALAHRWWDRESEFKPLHEINPLRVNWIDEHISLAGKKVIDIGCGGGILSEAMAQRGAQVTGIDMGEAPLSVARLHLLESGLEIDYRQITAEAMAAEAPEQFDVVTCLEMLEHVPDPASVIRACATLVKPGGQVFFSTINRNPKAYAFAIIGAEYVLQLLPRGTHDFKKFIRPSELGAWSRDAGLAVKDIIGLTYNPLTKHYKLSADVDVNYMVQTVKES | O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. | A4VLX7 |
B1XRV6 | UBIA_POLNS | 4-HB polyprenyltransferase | Polynucleobacter | MSLKERFISYGYLIRLDKPIGTLLLLWPTLWALWLASSGVLDLSILLIFVAGTFLMRSAGCAINDYADRDFDRHVKRTQGRPVTSGKISAKEAVAVASFLALCAFLLIQPLNAFTKQLSVLALLVAFIYPFTKRFFAMPQTVLGIAFGFGIPMAYAAILDFIPLEAWFLFTGNIFWAIAYDTAYAMVDRDDDLRLGLRTSAITFGQYDVVVIAISYGMLFLSHLWVAQLANLSNYFLVGWFAALACAIYHLKLVSTRNRENCFKAFRHNNWLGGFLFLGIVLGLGVH | 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. | B1XRV6 |
P10878 | TBB_TOXGO | Beta-tubulin | Toxoplasma | MREIVHVQGGQCGNQIGAKFWEVISDEHGIDPTGTYCGDSDLQLERINVFYNEATGGRFVPRAILMDLEPGTMDSVRAGPFGQLFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAEGCDCLQGFQITHSLGGGTGSGMGTLLISKVREEYPDRIMETFSVFPSPKVSDTVVEPYNATLSVHQLVENADEVQVIDNEALYDICFRTLKLTTPTYGDLNHLVSAAMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFLIGFAPLTSRGSQQYRALSVPELTQQMFDAKNMMCASDPRHGRYLTASAMFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNMKSSVCDIPPKGLKMSVTFVGNSTAIQEMFKRVSDQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEGEFDEEEGEMGAEEGA | 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. | P10878 |
B3Q606 | TRPA_RHOPT | Tryptophan synthase alpha chain | Rhodopseudomonas | MTTRIDTRFADLKQQGRPALVTFVMAGDPDLDTSLQILKALPAAGADVIEIGMPFTDPMADGPAIQAAGLRALKAGTTLKKTLGLVRDFRATDNATPLVLMGYYNPIYIYGVDAFLADAKAAGVDGLIIVDLPPEEDEELCLPAMKAGLNFIRLATPTTDEKRLPAVLANTSGFVYYVSITGITGSASADASAVGAAVQRIKRHTNLPVCVGFGIRTPDAAQAIAAQANGAVVGSALIDALKASLDAEGRATKGTVGAVADLVASLAAGVRGAKQAAE | The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | B3Q606 |
Q46IK0 | THIC_PROMT | Thiamine biosynthesis protein ThiC | Prochlorococcus | MRNSWVASRKGKTNVSQMHFARKGEITEEMRYVAKRENLPESLVMEEVARGRMVIPANINHMNLEPMAIGIASTCKVNANIGASPNASDISEELKKLDLAVKYGADTLMDLSTGGVNLDEVRTEIINASPIPIGTVPVYQALESVHGSISRLNEDDFLHIIEKHCQQGVDYQTIHAGLLIEHLPKVKGRITGIVSRGGGILAQWMLYHYKQNPLFTRFDDICEIFKRYDCTFSLGDSLRPGCLHDASDEAQLAELKTLGELTRRAWKHDVQVMVEGPGHVPMDQIEFNVRKQMEECSEAPFYVLGPLVTDISPGYDHISSAIGAAMAGWYGTAMLCYVTPKEHLGLPNPEDVREGLIAYKIAAHAADVARHRSGARDRDDELSKARKEFDWNKQFELSLDPERAKQYHDETLPEEIFKKAEFCSMCGPNHCPMNTKITDEDLDKLNDQIQSKGAAELTPVKLNKEN | 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. | Q46IK0 |
P28103 | WNT5A_ALOVU | Protein Wnt-5a | Alopias | SGSCSLKTCWLQLADFRKVGNALKEKYDSATAMKLNGRGKLVQVNSRFNTPTTLDLVYVDQSPDYCVRNESTGSLGTQGRLCNKTSEGMDGCALMCCGRGYDQFKTVRTERCHCKF | Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. Required during embryogenesis for extension of the primary anterior-posterior axis. | P28103 |
Q64707 | U2AFL_MOUSE | U2(RNU2) small nuclear RNA auxiliary factor 1-like 1 | Mus | MASRQTAIPEKLSRKQYKAAMKKEKRKKRRQKMARLRALEAPPEEDDDVSANEELAERLLEIERQRLHEEWLLREEKAQEEFRIKKKKEEAARKQKEEQERQIKAEWEEQQKKQREEEEQKLQEKREREEAVQKMLDQAENERIWQNPEPPKDLRLEKYRPSCPFYNKTGACRFGNRCSRKHDFPTSSPTLLVKSMFTTFGMEQCRRDDYDSDANLEYSEEETYQQFLDFYHDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKVAICGLFEMQKCPKGKHCNFLHVFRNPNNEFREANRDIYMSPPAWTGSSGKNSDRRERKDHHEEYYSKSRSYHSGSYHSSKRNRESERKSPHRWKKSHKQTTKSHERHSSRRGREEDSSPGPQSQSHRT | Plays a role in splicing of the U12-type introns . Implicated also in removal of U2 introns positioned adjacent to a U12 intron . | Q64707 |
C0QHT9 | UPP_DESAH | UPRTase | Desulforapulum | MAVYVEDHPLIKHKLGLMRQKDISTKDFRDLASEVAGLLTYEATQDMETEVATIDGWAGPVQVERIKGKKITIVPILRAGLGMMDGVINLIPSAKVSVVGFYRDEKTLQPVQYYVKTASAMDERIALILDPMLATGGTLLATIELLKASGCTRIKGLFLVAAPEGIEKIQKAHPDVDIYVAAIDERLNEVGYILPGLGDAGDKIFGTK | Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | C0QHT9 |
B0S5D5 | ZD12A_DANRE | Zinc finger DHHC domain-containing protein 12-A | Danio | MNKSLFKSGCLVRTAHVILTWIITLILFLHNTDLRRCQERGDLLQPLVFSSVLLLSVLLYFTVSLMDPGFVLSDSQTETASGDGDEELEAMIPQEQNSIKQRRCGYCFLLQPMRARHCKWCKRCVRRFDHHCPWIDNCVGELNHRWFLLYLCVQFTAVCWGLQSAWSGFISAPSWQQWFTQNVFLLVAFAVTAVFSVVLLLLLCIHAYLASVNCTTWEFMSRHRILYLKHVDSEENPFDRGVFCNLWSFCCVCGTVAWEKMYIRHNNASV | Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. | B0S5D5 |
A6VU64 | TRPD_MARMS | Anthranilate phosphoribosyltransferase | Marinomonas | MDIKKAIAAVVERQDLSGGEMQVVMHDIMTGKATPAQIGGFLIGLRMKGETVEEITAAAQVMRSLSSKVHLDLEHVVDTCGTGGDGGNLFNVSTASAFVVASAGGKVAKHGGRSVSSKSGSADVLEQAGIYLGLDAEQVCRCVEEIGLGFMFAPNHHSAMKYAVGPRKEMATRTIFNLLGPLTNPANAKCQVMGVFHQKWVRPIAEVLKALGSEHVMVVHSEDGLDEISIAAPTYVAELKNGEILEYKISPEDFGIPLQSIDTIQAADASESLALVKMALDGKGKINPARDIVALNAGAAIYVSGIADTLAEGVNIAEDVIGGGTAKVKMSELASFTRCFMSPDSL | Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA). | A6VU64 |
D5V9A9 | TSAC_MORCB | tRNA threonylcarbamoyladenosine biosynthesis protein TsaC | Moraxella | MAGSKQIFGADELDLVANYLQAGGVLAYPSESVWGLGCDAFNTDAINQIINLKHRDIGKGLIVLTDAAERLKSLIDVSHETSLLDYMQNFSDEFTHKHSRALTWLMPIQSSVLPSVLIGSHDTLAVRITTHPLLKDLCHALISPTNPYGFLVSTSCNLSKSTPAKNLTQAMGYFGDQIAYLDTDGLGFAQPSCIKDLLAGHILR | 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. | D5V9A9 |
Q07XP8 | Y3380_SHEFN | Nucleotide-binding protein Sfri_3380 | Shewanella | MKLVIVSGRSGSGKSVALRVLEDLGYYCVDNLPLPLIGTLLAQLKGSNDLVAISVDVRNIAEQGKVLQDQLALLENDTEIISFFLNSNDKVLLKRYSETRRLHPLSKNHISLQEAIKLEGRLLEPIAKIVDHYIDTSALNIYELSDQVRQILLGSVDKELVINFESFGFKHGMPTEADFMFDVRFLPNPHWEIELRPFTGLDEPVQEFLGRQPLVNKFIWQIENLFETWMPHLERNNRSYLTIAIGCTGGQHRSVYIADQLAKRFRQGSKHTVNARHRELNISDTNN | Displays ATPase and GTPase activities. | Q07XP8 |
B7NHK6 | ZAPD_ECO7I | Z ring-associated protein D | Escherichia | MQTQVLFEHPLNEKMRTWLRIEFLIQQLTVNLPIVDHAGALHFFRNVSELLDVFERGEVRTELLKELDRQQRKLQTWIGVPGVDQSRIEALIQQLKAAGSVLISAPRIGQFLREDRLIALVRQRLSIPGGCCSFDLPTLHIWLHLPQTQRDSQVETWIASLNPLTQALTMVLDLIRQSAPFRKQTSLNGFYQDNGGDADLLRLNLSLDSQLYPQISGHKSRFAIRFMPLDSENGQVPERLDFELACC | Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. | B7NHK6 |
G3Y418 | YANG_ASPNA | Yanuthone D biosynthesis cluster protein G | Aspergillus subgen. Circumdati | MSTTKRSVTTRPSTSSRNVPRGIWELARLHTRESWLCWYPSIWGACVAAGVSDTVLEPLAFARFLFGIWASVTATHCAFCTFKSVPFCFFVVPRYSSDYWHLDKHVQRCKVRPLPSGMISTPEALLAFVCWVPFTFAITWATLGPAVTVSFIPVWVLSVIYPFMKRLMPFPQVVLGAIIGGAVFPGWVGVTGDLDHLDQALPLFFATAAWVVYFDVFYATQDLPDDKKAGVKSLAVWMGPNVKILLAGLGILQIAFFAMTALRADLSLIFWILGIGVWAVSVPWHVLSLNLKDRHSGGSVFKANIKLGLYMTGVSLLELVLLRVHHAPMKVY | Polyprenyl transferase; 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 . YanG is also involved in the synthesis of yanuthone X1 which does not have 6-methylsalicylic acid (6-MSA) as precursor . | G3Y418 |
B8E6N4 | TRUB_SHEB2 | tRNA-uridine isomerase | Shewanella | MARRPKGRFIDGIVLLDKSTGMSSNFALQRVKRFFNANKAGHTGALDPLATGMLPVCLGEGTKFSQHLLDADKRYLVTAKLGERTDTSDSDGEVVQTRAIDFTEAQLLTALDFFRGETQQVPSMYSALKYQGQPLYKYAREGIEVPRESRPITVFELNFIGLEGDELTLDIHCSKGTYIRTIIDDLGEMLGCGAHVIMLRRTQVAQYPYARMVTLEQLEALVAQAHEQQIDPSVLLDPLLLPMDTAVADFPEVNVPDAIAPYLMQGQAVRVPVNADLKTDELVRITLGDIRRFVGIGTMNEDGLLAPKRLIVIHDEPAETD | Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs. | B8E6N4 |
Q9NPG3 | UBN1_HUMAN | Ubiquitously expressed nuclear protein | Homo | MSEPHRVQFTSLPGSLNPAFLKKSRKEEAGAGEQHQDCEPAAAAVRITLTLFEPDHKRCPEFFYPELVKNIRGKVKGLQPGDKKKDLSDPFNDEEKERHKVEALARKFEEKYGGKKRRKDRIQDLIDMGYGYDESDSFIDNSEAYDELVPASLTTKYGGFYINSGTLQFRQASESEDDFIKEKKKKSPKKRKLKEGGEKIKKKKKDDTYDKEKKSKKSKFSKAGFTALNASKEKKKKKYSGALSVKEMLKKFQKEKEAQKKREEEHKPVAVPSAEAQGLRELEGASDPLLSLFGSTSDNDLLQAATAMDSLTDLDLEHLLSESPEGSPFRDMDDGSDSLGVGLDQEFRQPSSLPEGLPAPLEKRVKELAQAARAAEGESRQKFFTQDINGILLDIEAQTRELSSQVRSGVYAYLASFLPCSKDALLKRARKLHLYEQGGRLKEPLQKLKEAIGRAMPEQMAKYQDECQAHTQAKVAKMLEEEKDKEQRDRICSDEEEDEEKGGRRIMGPRKKFQWNDEIRELLCQVVKIKLESQDLERNNKAQAWEDCVKGFLDAEVKPLWPKGWMQARTLFKESRRGHGHLTSILAKKKVMAPSKIKVKESSTKPDKKVSVPSGQIGGPIALPSDHQTGGLSIGASSRELPSQASGGLANPPPVNLEDSLDEDLIRNPASSVEAVSKELAALNSRAAGNSEFTLPAPSKAPAEKVGGVLCTEEKRNFAKPSPSAPPPASSLQSPLNFLAEQALALGQSSQEKKPESSGYKELSCQAPLNKGLPEVHQSKAKHHSLPRTSHGPQVAVPVPGPQVKVFHAGTQQQKNFTPPSPFANKLQGPKASPTQCHRSLLQLVKTAAKGQGFHPSAPATSGGLSASSSSSHKTPASSSSALSHPAKPHSVSSAGSSYKNNPFASSISKHGVSSGSSSSGGTPVQSSVSGSLVPGIQPPSVGQATSRPVPSSAGKKMPVSQKLTLVAPPGGPNGDSSGGTQGVAKLLTSPSLKPSAVSSVTSSTSLSKGASGTVLLAGSSLMASPYKSSSPKLSGAMSSNSLGIITPVPIPVHVLSFSADSSAKAGVSKDAIVTGPAPGSFHHGLGHSLLAGLHSSPPHAAPLPHAAVPTHIPQSLPGASQLHGKGPAVPRKL | Acts as a novel regulator of senescence. Involved in the formation of senescence-associated heterochromatin foci (SAHF), which represses expression of proliferation-promoting genes. Binds to proliferation-promoting genes. May be required for replication-independent chromatin assembly. | Q9NPG3 |
Q6Y0Z3 | XYL1_CANPA | NADH-dependent D-xylose reductase | Candida | MSTATASPAVKLNSGYEIPLVGFGCWKLTNDVASDQIYRAIKSGYRLFDGAEDYANEQEVGEGIKRAIKEGIVKREELFITSKLWNSFHDKKNVEVALMKTLSDLNLDYVDLFYIHFPIAQKPVPIEKKYPPGFYCGDGDKWSIEEVPLLDTWRALEKLVDQGLAKSIGISNFSAQLIYDLIRGCTIKPVALQIEHHPYLTQPKLVEYVQLHDIQITGYSSFGPQSFLEMDLKRALDTPVLLEEPTVKSIADKHGKSPAQVLLRYQTQRGIAVIPRSNSPDRMAQNLSVIDFELTQDDLQAIAELDCNLRFNEPWDFSNIPVFV | Reduces D-xylose into xylitol. Preferentially utilizes NADH as a cosubstrate. | Q6Y0Z3 |
Q5YPL7 | TYSY_NOCFA | Thymidylate synthase | Nocardia | MATDRQYEDLLRLVLDTGTAKGDRTGTGTRSIFGHQLRYDLSAGFPLITTKKVHLKSIVYELLWFLRGDSNVGWLREHGVTIWDEWADPQGELGPVYGVQWRSWPTPDGTHIDQISQVLQTLRTDPDSRRMIVSAWNVAELDRMALAPCHAFFQFYVADGKLSCQLYQRSADLFLGVPFNIASYALLTHMVAQQTELEPGEFIWTGGDCHIYDNHVEQVTEQLGREPYPFPRLELRPAPSLFDYRFEDVTVTDYRHHPAIKAPVAV | Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. | Q5YPL7 |
B6EJA1 | YCIB_ALISL | Inner membrane-spanning protein YciB | Aliivibrio | MKQILDFIPLIIFFALYKMYDIYTATGALIVATAVQLILTYVLYKKVEKMQLITFIMVTVFGGMTIFLHDDNFIKWKVTIVYAVFAAGLIIAQILGRPIIKGMLGKEVTLPDNKWNKINYAWILFFTACSIANLYVAFEMPLDVWVNFKVFGLLGLTFIYTLLTGMYVYKHMPKEKKEEQE | Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis. | B6EJA1 |
Q9V157 | UPPS_PYRAB | Undecaprenyl pyrophosphate synthase | Pyrococcus | MIYGILSHVPKIFFKPAYDLYERYLLEKVKAGVLPKHVAIIMDGNRRWAKKREKPPWYGHLFGSKKLEEILEWCHELGIRILTVYAFSTENFKRSKEEVERLMQLFEQKFRELVTDKRVHEYGVRVNVIGRKELLPKSVRDAAEEAERATRKYNNYVLNVAIAYGGRSEIVDAVKDIVRDVMDGKLRVEDIDEELLKKYLYVPNMPDPDIVIRTGGEVRISNFLLYQIAYSELFFVDVYFPEFRKIDFLRIIREFQKRERRFGR | Catalyzes the sequential condensation of isopentenyl diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate (tritrans,heptacis-UPP). It is probably the precursor of glycosyl carrier lipids. | Q9V157 |
Q6FBS0 | TRMA_ACIAD | tmRNA (uracil(341)-C(5))-methyltransferase | Acinetobacter | MSQTYQQQLQSKIERITHQFAEFNPPALEVFESPEQHFRMRAEFRIWHTDNDLFYAMFERNEDGKQKEVIRVDEFPIADQSINQLMPRLLEELKANPTLSQRIFEADFLTTLSGEMLVTLIYHRKLDTEWESAAKALAEKLNIKIMGRSRGQKVIIGDDYVVEQLNVHGRTFKYKQIESSFTQPNAEVCQKMLTWACDVIQGSNQDLLELYCGNGNFTLPLSLHFRRVLATELAKSSVYAAQWNIEQNQIENIQIARLSAEEFTQAYQGEREFRRLQEANIDIQSYEFDTIFVDPPRAGIDDETLKLLKGFKRILYISCNPDTLYNNLKTLSQTHKITRFALFDQFPFTHHVESGVLLELI | Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA). | Q6FBS0 |