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
B7LNJ1
LPLT_ESCF3
Lysophospholipid transporter LplT
Escherichia
MSESVHTNTSLWSKGMKAVIVAQFLSAFGDNALLFATLALLKAQFYPEWSQPVLQMVFVGAYILFAPFVGQVADSFAKGRVMMFANGLKLLGAASICFGFNPFVGYTLVGIGAAAYSPAKYGILGELTTGDKLVKANGLMEASTIAAILLGSVAGGVLADLHVLVALAACALAYAGAVAANIYIPKLAAARPGQSWNVLKMTCSFKSACTSLWQNGETRFSLVGTSLFWGAGVTLRFLLVLWVPVALGITDNATPTYLNAMVAIGIVLGAGAAAKLVTLETVSRCMPAGILIGVVVLFFSLQHELLPAYALLMLIGVLGGFFVVPLNALLQERGKKSVGAGNAIAVQNLGENSAMLLMLGIYSLAVLVGIPVVPIGIGFGTLFALAITALWIWQRRH
Catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell.
B7LNJ1
Q6LG09
OTC_PHOPR
Ornithine carbamoyltransferase
Photobacterium
MSFNLRNRNFLKLLDFTGKEIEHLIALAQDLKHAKYAGTEQQKLKGKNIALIFEKTSTRTRCAFEVAAHDQGAHVTYIGGGSQMGHKESTKDTARVLGRFYDGIEYRGFGQDVVETLGEHAGVPVWNGLTDEWHPTQIIADWMTMLEHGNGKRLNQMKLAYMGDAKNNMGNSLMVGAAKVGMEIRLVGPKAYWPDPALVAECNELCKISGGKIVITDNVQEGVDSVDFIYGDVWVSMGEPEELWATRINDLAPYQVNMSVITATQNPAVKYMHCLPAFHNDETRVGKKIEEKFNMKGLEVTEDVFESSYTICFDEAENRMHSIKAIMVATLGD
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q6LG09
Q01345
NHEB_ONCMY
Na(+)/H(+) antiporter
Oncorhynchus
MPAFSCAFPGCRRDLLVIVLVVFVGIGLPIEASAPAYQSHGTEGSHLTNITNTKKAFPVLAVNYEHVRKPFEIALWILLALLMKLGFHLIPRLSAVVPESCLLIVVGLLVGGLIKVIGEEPPVLDSQLFFLCLLPPIILDAGYFLPIRPFTENVGTILVFAVIGTLWNAFFMGGLLYALCQIESVGLSGVDLLACLLFGSIVSAVDPVAVLAVFEEIHINELVHILVFGESLLNDAVTVVLYNLFEEFSKVGTVTVLDVFLGVVCFFVVSLGGVLVGAIYGFLAAFTSRFTSHTRVIEPLFVFLYSYMAYLSSEMFHLSGIMALIACGVVMRPYVEANISHKSYTTIKYFLKMWSSVSETLIFIFLGVSTVAGPHAWNWTFVITTVILCLVSRVLGVIGLTFIINKFRIVKLTKKDQFIVAYGGLRGAIAFSLGYLLSNSHQMRNLFLTAIITVIFFTVFVQGMTIRPLVELLAVKKKKESKPSINEEIHTEFLDHLLTGVEGVCGHYGHYHWKEKLNRFNKTYVKRWLIAGENFKEPELIAFYRKMELKQAIMMVESGQLPSVLPSTISMQNIQPRAIPRVSKKREEEIRRILRANLQNNKQKMRSRSYSRHTLFDADEEDNVSEVRLRKTKMEMERRVSVMERRMSHYLTVPANRESPRPGVRRVRFESDNQVFSADSFPTVHFEQPSPPSTPDAVSLEEEEEEVPKRPSLKADIEGPRGNASDNHQGELDYQRLARCLSDPGPNKDKEDDDPFMSC
Involved in pH regulation to eliminate acids generated by active metabolism or to counter adverse environmental conditions. Major proton extruding system driven by the inward sodium ion chemical gradient.
Q01345
Q54ME1
GMSA_DICDI
Gamete and mating-type specific protein A
Dictyostelium
MKLILVLLCLISTLFVVKGGLSPTEQQIIVSYHNKWRSSPIGPTPSTTIPALKWNATIAAALQSSLDKCDGKFSTMSQYGTNSEWQSWWTPNTYFNLNATLDNIQKGASFYDWNAKGCNSSANYNCQLWTYAVWSKSTSYGCAKTICPDKSEVSCSYYPAGGFKGVLPYTPKTTTPAPTTPAPTTPKPTTPAPTTPKPTTPAPTTPKPTTPAPTTPKPTTPAPTTPKPTTPAPTTPAPTSTLTVDWTSYQTPIRDQGQCGSCWAFASSAALESRYLIKYGTAQKSTLQLSNQNAVNCIASGCNGGWSGNYFNFFKTPGIAYEKDDPYKAVTGTSCITTSSVARFKYTNYGYTEKTKAALLAELKKGPVTIAVYVDSAFQNYKSGIYNSATKYTGINHLVLLVGYDQATDAYKIKNSWGSWWGESGYMRITASNDNLAIFAYNSYYPTF
Thiol protease that seems to be involved in the sexual development.
Q54ME1
Q8UIE8
SYW_AGRFC
Tryptophanyl-tRNA synthetase
Agrobacterium tumefaciens complex
MNAFKPLVFSGVQPTGNLHLGNYLGAIRKFVALQEDNDCIYCVVDMHAITAQLVHSDLKAQTRSIAAAFIAAGIDPVKHIVFNQSAVPQHAELAWVFNCVARIGWMERMTQFKDKSGKNAEQVSLGLLAYPSLMAADILVYRATHVPVGDDQKQHLELARDIAQKFNIDFGGHIRNAGLGVNITVGDEPVHAYFPMVEPLIGGPAPRVMSLKDGTKKMSKSDPSDLSRINLMDDVDAISKKIKKAKTDPDALPSEVEGLKGRPEAENLVGIYAALSDKTKADVLAEFGGQQFSTFKPALVELAVNVLAPVNNEMRRLLDDPTHIDAILSQGGERARTIAEKTMNEVRDIIGFLR
Catalyzes the attachment of tryptophan to tRNA(Trp).
Q8UIE8
A6UYL3
PYRR_PSEA7
Uracil phosphoribosyltransferase
Pseudomonas
MSLPNPAELLPRMASDLRAHLAERGIERPRYVGIHTGGIWVAEALLKALGNEEPLGTLDVSFYRDDFTRNGLHPQVRPSALPFEIDGQHLVLVDDVLMSGRTIRAALNELFDYGRPASVTLVCLLDLNARELPIRPDVVGQTLSLGRDERVKLVGPAPLALERKVLSPAS
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
A6UYL3
B7GFF3
RECR_ANOFW
Recombination protein RecR
Anoxybacillus
MYYPEPISKLIDSFMKLPGIGPKTAVRLAFFVLNMKEDVVLDFAKALVNAKRNLTYCSSCGHITDKDPCYICEDDKRDRSIICVVQDPKDVIAMEKMKEYNGLYHVLHGAISPMEGIGPEDIKIAELLRRLQDETVQEVILATNPNIEGEATAMYISRLLKPTGVKITRIAHGLPVGGDLEYADEVTLSKALEGRREL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
B7GFF3
O42807
FAEA_ASPNG
Ferulic acid esterase A
Aspergillus subgen. Circumdati
MKQFSAKYALILLATAGQALAASTQGISEDLYNRLVEMATISQAAYADLCNIPSTIIKGEKIYNAQTDINGWILRDDTSKEIITVFRGTGSDTNLQLDTNYTLTPFDTLPQCNDCEVHGGYYIGWISVQDQVESLVKQQASQYPDYALTVTGHSLGASMAALTAAQLSATYDNVRLYTFGEPRSGNQAFASYMNDAFQVSSPETTQYFRVTHSNDGIPNLPPADEGYAHGGVEYWSVDPYSAQNTFVCTGDEVQCCEAQGGQGVNDAHTTYFGMTSGACTW
Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-galactose ester bond in pectin. Binds to cellulose.
O42807
B1IA76
RIMP_STRPI
Ribosome maturation factor RimP
Streptococcus
MDAIATIVELVREVVEPVIEAPFELVDIEYGKIGSDMILSIFVDKPEGITLNDTADLTEIISPVLDTIKPDPFPEQYFLEITSPGLERPLKTKDAVAGAVGKYIHVGLYQAIDKQKVFEGTLLAFEEDELTMEYMDKTRKKTVRIPYSLVSKARLAVKL
Required for maturation of 30S ribosomal subunits.
B1IA76
P40283
H2B11_ARATH
HTB4
Arabidopsis
MAPKAEKKPAEKKPASEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQEASKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
P40283
Q5L3D3
PURQ_GEOKA
Phosphoribosylformylglycinamidine synthase subunit I
Geobacillus thermoleovorans group
MKFAVVVFPGSNCDVDMYHAIADELGEEVEYVWHDEDNLDRFDAVLLPGGFSYGDYLRSGAIARFSKVMAAVKKAAEAGKPVLGVCNGFQILLEAGLLPGAMRRNQGLKFICRPVQLTVENHETMFTSAYEKGEVITIPIAHGEGNYYCDEQTLERLVENRQIVFRYHGENPNGSLADIAGIVNEQGNVLGMMPHPERAVDALLGSADGLKLFRSIVNYWRETHVVTA
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Q5L3D3
Q90WG1
SPINZ_CHICK
Spindlin-Z
Gallus
MKTPFGKSPGQRSRADAGHAGVSASMMKKRTSHKKHRNNVGPSKPISQPRRNIVGCRIQHGWKEGSGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELHKDERVSALEVLPDRVASSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPIMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS
May play a role in mitosis.
Q90WG1
A4WVP0
PCKA_CERS5
Phosphoenolpyruvate carboxykinase (ATP)
Cereibacter
MNFGRVNPAQTLDAQGITGLGEVHYNLIEPALVEAAVKRGEGRLGRGGAFLCSTGAFTGRSPKDKFVVRTPSVEDTIWWENNAPMDPEAFDRLHADMLEHMKGRTYFVQDLFAGADPELRLDVRMVTELAWHGLFIRHMLRRPERTELDSFVPEWTVINCPSFKADPARHGCRTDTVITLNFDKKLILIANTEYAGENKKSVFTLLNYILPGKGVMAMHCSANHAIGNTDDAAVFFGLSGTGKTTLSADPSRTLIGDDEHGWSDKGTFNFEGGCYAKTINLSPEAEPEIYATTSKFATVVENMVYNEETLELDFDDDSLTANTRCAYPLEYISNASATGMGGHPKNVIMLTCDAFGVLPPIARLTPAQAMYHFLSGFTSKVAGTERGVTEPQPTFSTCFGAPFMPRRPEVYGKLLQEKITSLGATCWLVNTGWTGGAYGTGKRMPIKATRALLTAALDGSLANVTFRKDPNFGFEVPTELHGVDSSLLDPRSTWADPAAYDAQAKKLVEMFANNFAQYVPYIDADVKAAAIG
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
A4WVP0
Q9CY34
UB2FA_MOUSE
Ubiquitin-conjugating enzyme E2 F
Mus
MLTLASKLKRDDGLKGSRTSASTSDSTRRVSVRDKLLVKEVAELEANLPCTCKVHFPDPNKLHCFQLTVSPDEGYYQGGKFQFETEVPDAYNMVPPKVKCLTKIWHPNITETGEICLSLLREHSIDGTGWAPTRTLKDVVWGLNSLFTDLLNFDDPLNIEAAEHHLRDKEDFRDKVDEYIKRYAR
Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.
Q9CY34
Q8EGW8
SSRP_SHEON
Small protein B
Shewanella
MVKKNSKKAAPATIARNKRATFEYRFEEKMEAGLSLMGWEVKSIRMGKVNLSDCYVFLKNGEAFMHGCTIIPLNTASTHVVCDPIRLKKLLLSRKELDKLAGLVERQGYSIIPISMYWRKGAWVKVEIGLGKGKKDHDKREDTKAREWEVEKARVMKKEKTRG
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q8EGW8
Q5WH37
DEOB_ALKCK
Phosphodeoxyribomutase
Alkalihalobacillus
MKKRFERIFLIVMDSVGIGEAPDAKEFGDEGANTLGSIAEAFNGLHVPELEKLGLGKIAPLKGVKNVPTPLASYGIMQEASLGKDTMTGHWEIMGLHITKPFQVFPDGFPTELLEQLKSETGRGIIGNKVASGTEILDELGEEHVKTGDLIVYTSADSVLQIAAHEEVVPLEELYDICEKARKLTLAPEYMVGRVIARPFVGEPGKWKRTANRHDYALKPFGRTVMNTLEDAGLASIALGKISDIYDGEGVTKAVRTTSNEDGMDKLAEQINTSFEGLCFLNLVDFDALYGHRRDVIGYGEAIMAFDQRLGEILPQLGDEDLLIVTADHGNDPTHTGTDHTREYVPLLVYNKGIKPVNLGKRRTFADIGATVADNFQVERPSNGTSFLTELKPE
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
Q5WH37
Q5QYV0
RUVC_IDILO
Holliday junction resolvase RuvC
Idiomarina
MAIILGIDPGSRLTGYGVIEQRGRQLNYLGSGCIKVIGTTKEPLTLAEKLRRIHDSVSELITQFKPNEFAIEQVFMAKNPDSALKLGQARGAAIVAAACAELPVAEYSARQIKQSVVGNGGAEKSQVQHMVMALLNLQRCPQEDAADALAVALCHAHSSQNLIKMAGAARKTVRGRLR
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
Q5QYV0
P0AE71
MAZF_ECO57
mRNA interferase MazF
Escherichia
MVSRYVPDMGDLIWVDFDPTKGSEQAGHRPAVVLSPFMYNNKTGMCLCVPCTTQSKGYPFEVVLSGQERDGVALADQVKSIAWRARGATKKGTVAPEELQLIKAKINVLIG
Toxic component of a type II toxin-antitoxin (TA) system. MazF is a sequence-specific endoribonuclease that inhibits protein synthesis and induces bacterial stasis. It is very stable, single-strand specific and cleavage is independent of the ribosome. The endoribonuclease activity (a toxin) is inhibited by the labile cognate antitoxin MazE. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. Both MazE and MazE-MazF bind to the promoter region of the mazE-mazF operon to inhibit their transcription.
P0AE71
A0A1W2PPG7
GBG14_HUMAN
Putative guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-14
Homo
MSSKVAINSDIGQALWAVEQLQMEAGIDQVKMAADLLKFCTEQAKNDPFLVGIPAATNSFKEKKPYAIL
Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
A0A1W2PPG7
Q8XXL5
ADE_RALSO
Adenine aminohydrolase
Ralstonia
MPISPALAERIATSPKAELHIHIEGSLEPELMFALAERNGVKLPYASVDEVRAAYAFNDLQSFLDLYYAGASVLLTEQDFYDMTAAYVARAVADNVRHAEIFFDPQTHTARDVPMHVVIGGIVRALDDAERAHGFSSRLILCFLRHLSEADAFDTLEAALPYIQDPANRIIGVGLDSSERGNPPEKFARVFARCKALGLRLVAHAGEEGPAQYVIDALDILQVERIDHGVRAIDDAALVKRLAASRVALTVCPLSNEKLKVYPDLRDHSLKQLLDAGCAVTLHSDDPAYFGGYMNTNWLATFNALGLSAADAHTLARNSFEASFLPEQDKALWLNAVDIHWRAHT
Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Q8XXL5
A7ZSM0
TUSD_ECO24
tRNA 2-thiouridine synthesizing protein D
Escherichia
MRFAIVVTGPAYGTQQASSAFQFAQALIVEGHELSSVFFYREGVYNANQLTSPASDEFDLVRGWQQLNAQHGVALNICVAAALRRGIVDETEAGRLGLASSNLQPGFTLSGLGALAEASLTCDRVVQF
Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Accepts sulfur from TusA and transfers it in turn to TusE.
A7ZSM0
B4S433
DER_PROA2
GTP-binding protein EngA
Prosthecochloris
MKPLVALVGRPNVGKSTLFNRITHQKSAIVDSTPGVTRDRHIMPAEWIGKEFLVMDTGGYCHDSDGISKAMLEQTLTAIGEADVIIFLVDVRSGLTYLDLDMAKLLKRDFNDKPVYFAVNKVESPQLAYEGESFRKTGFTEPWFISARDGSGVADLLDAVVDSFEEKSGQEEEDDSIRLAIIGRPNVGKSSFVNALLGTNRNIVSNKPGTTRDAIDTRFKRNGREIVLIDTAGLRKRARIDAGIEFYSSLRTERAIERCDVALVLIDAEQGLEKQDMKIIEMAAERKKGVLLLVNKWDLIEKDSKTSKLYSDRMYDDMGNLGWIPIQFISAMTKKNLYRAIDAALDIQEQRSQQITTSDLNRFLQDTLLQAPPSSKSGKELKIKYMTQIRAPWPVFAFFCNDPKLLQNNYKRFLEKRIRQNYNLSGVPFSLRFMQK
GTPase that plays an essential role in the late steps of ribosome biogenesis.
B4S433
J7FK10
IDTM_CLAPA
Indole-diterpene biosynthesis cluster protein M
Claviceps
MADDFKVVIVGGSVAGLSLAHCLERLGVSYVVLEKGSQIAPQLGASIGILPNGGRILDQLGIFRDVEDEIEPLNFAVIRYADGFSFRSQYPKALHSSYGYPVSFLERQKFIQILYDKLRGKNHVHTRKRVVSIVDGPGKALIRTDDGDEYDADMVVGADGVHSVVRSEIWRHAKEAAGTAVTEEEPNADIKYDYACVYGISVNVPHADTGVQLSSLSDGVSIHLFAGKGSKFFWFIMVRTSRDEFLELKKDSAHMARRTCEGLGSKRLSDAVYFRDVWSRCTVYQMTPLEEGVFRQWNRGRLVCIGDAIRKMAPNIGQGANMAIEDAAQLSNLIREMLASPRKASATTVEKMLRDFAAMQKARTKSMCGQSEFLVRMHANEGFGRRLLGRYLIPSLQDAPAGLAGLSIRGAVKLECAGVPSRTLGKAWEGSWGSSLRNLMYLRPRLGILSLVYVVAGLAMMYMSIYLVVPARLAAQAFDVSRDGTEGKGGG
FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations of isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP (Probable). Condensation of indole-3-glycerol phosphate with GGPP by the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI) (Probable). Epoxidation of the two terminal alkenes of the geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and cyclization by the terpene cyclase idtB then leads to the production of paspaline (Probable). The cytochrome P450 monooxygenase idtP then catalyzes oxidative elimination of the pendant methyl group at C-12 of paspaline and generates the C-10 ketone to yield 13-desoxypaxilline . The cytochrome P450 monooxygenase idtQ may catalyze the C-13 oxidation of 13-desoxypaxilline to afford paxilline (Probable). Considering that both paspalicine and paxilline were detected in C.paspali, idtQ also catalyzes the formation of paspalinine from 13-desoxypaxilline via paspalicine as an intermediate (Probable). Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the C-20 or the C-21 positions to yield paspalitrems A and C, respectively . The hydroxylation of paspalitrem A at C-32 by a still unknown oxidase affords paspalitrem B (Probable).
J7FK10
Q98LX2
GLMU_RHILO
Glucosamine-1-phosphate N-acetyltransferase
Mesorhizobium
MSQRSCLSVILAAGEGTRMKSALPKVLHQIAGLPMVAHVVKAADAAGASSDAIVIGHGAEEMRKAVTKFSPKAETFVQEERLGTAHAVLAAREAISRGYDDILVMFGDTPLIDAEALNLARLKLAEGAAVAVIGFRPPLPNGYGRLVEKGGKLIAIREEKDCSEAEKKIGFCNAGMMAVAGAHALKLLDAVGNKNAKGEYYLTDIVEIAGAQGLDVVATEASFENALGINNRAELAQAEGIWQARRRQEAMLSGVTLIAPETVYFSHDTEIGADTVVEPNVWFGPGVKIAGGAKIHAFSHIEGATIAANCDVGPFARLRPGADLRNKAKVGNFCEVKQAVIEEGAKVNHLTYIGDARVGAGANIGAGTITCNYDGFSKFFTDIGEGAFVGSNSSLVAPVSIGKGGYIASGSVITESVPDDALAFGRARQKTIPGKGKELRERFASAAAAKKKAAGADH
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
Q98LX2
B1ZND9
RS17_OPITP
30S ribosomal protein S17
Opitutus
MSSSPAQRHTRKTQIGFVSSRSGDKSIKVTVPYKSPHPLYHKIVNRQTVLHVHDEKNEAKLGDTVEVMETRPMSRLKRWRIVSIVQRAVTTDAVAISETDVAAQVPTKTTASNTPAPAEQPAPQA
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
B1ZND9
B0TUD3
TRMN6_SHEHH
tRNA m6A37 methyltransferase
Shewanella
MPFTFKLFHVDDSRCGMPVSTDGVLLGAWAPLVQAKTILDIGAGSGLLSLMAAQRSQAKITAIELDNDAALDCQQNFDASHWSERLEIICCDIQAYCQREQARQFDHIICNPPYFANGPQSSKFSRATARHTDSLSFDALLQAIKQLLAPEGQASLILPTESVSLLEAILSTYNLRLCHKLLAASVEGKAPNRQILVLGHDLKAKKIHNFGTELQAVAQQQLYIREKTGHYSLAFTLLSQDFYLKL
Specifically methylates the adenine in position 37 of tRNA(1)(Val) (anticodon cmo5UAC).
B0TUD3
Q8UVQ4
KAISO_XENLA
Zinc finger and BTB domain-containing protein 33
Xenopus
METKKLITATDTQYSGILLNALNDQRIQGLYCDVTVIVEDRKFRAHRNILSACSTYFHQLFSVAGQVVELNFVKADIFAEILNYIYSSKIVRVRCDMLEELIKSGKLLGVPFIAELGIPLSQVKSISGAGGKDGGTDAPSNPDHKAPEPQKSSDSPLPCTVKIKADVKTEMPVITESFSLSSDDYKDKKASGSQDHNSEKEDDDDDVIFCSEIVSSKQAPAERKEAAQTQIPPDNEQVPEVKKVTPSSQVQLTQNSLPTNQQSSKNTSSTTQKFTPPVNANISKNPTPAANGFLSPTAQKQGTPNAVQNQHSQNITSGNALPQQKPVVNFSSIKPQQISAIKPKTEVIIHGNGLSPPSSSVIPLGQQPVTPKHISFDGVQKKQVVTFTQGSPSKPGEFKIKIADVVSGSSLDSFKDSEPRRIIDGKKIITLDTASEIEGLSTGCKVYANIGEDTYDIVIPIKEDPEEGEAKLDLDGLPNRKRMKLKHDDHYELIVDGRVYYICIVCKRSYVCLTSLRRHFNVHSWEKKYPCRYCERVFPLAEYRTKHEIHHTGERRYQCLTCGSSFINYQVMASHIRSVHSLDPSGDSKLYRLNPCKTLQIRQYAYVNNSTNGTVINDGAINVPVITDGGINVPVINDGGIVYDIDPDEPQQPASEGNHANSATKPVNWDNIFIQQSNQNMFKLNTSEGGTEFEFVIPESY
Transcriptional regulator with bimodal DNA-binding specificity. Binds to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' and also binds to the non-methylated consensus sequence 5'-CTGCNA-3'. May recruit the N-CoR repressor complex to promote histone deacetylation and the formation of repressive chromatin structures in target gene promoters. Contributes to the repression of target genes of the Wnt signaling pathway and to the methylation-dependent repression of zygotic transcription prior to the mid-blastula transition (MBT). Also required for gastrulation movements.
Q8UVQ4
B0BAF4
PSD_CHLTB
Phosphatidylserine decarboxylase beta chain
Chlamydia
MAAREMLYVNRETGKVEQERIICSSLVKFFIETRIGRALYSVLCKNSLFSRIVGWCQRLRVTRYFIKPFVTKYRICIEESASPLHDYASFNDFFVRKLKPDARPICQGEDICVTPADGAYLVFPSMADLSLFTIKNKPFSLESFLGDPQLAHQYAQGSMAIARLAPFDYHRFHFPIAGIAEAPRRINGHLFSIHPLMLKRNFEVFTENKREITIITSKEFGEVAYVEVGALNVGSIHQTFSPGSYVKKGAEKGFFAFGGSTVVLLFQPQRIIFDADLVGYSAQGLETRCRMGQSLGKHFSS
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
B0BAF4
Q8Y4B6
ATP6_LISMO
F-ATPase subunit 6
Listeria
MEEEFPTISLLGIDFNLSNILMITVTCVIVLLIAIICTRNLQRRPTGKQNFIEWVMDFVRGIINSNMDWKTGGRFHVLGITILMFVFVANMLGLPLQIAVNDEVWWRSPTADPIVTLTLAIMVLGLTHYYGIKMRGFKHYFVGTYLSPMKFLFPLKLVEEFANTLTLGLRLYGNIFAGEVLLTIIATQLAHINIFVGVLAIIPAIIWQAFSLFIGAIQAYIFTMLTMVYMSHKVSDEH
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
Q8Y4B6
A2DZE8
ALG5A_TRIVA
Dolichyl-phosphate beta-glucosyltransferase ALG5A
Trichomonas
MKFWRFVQILFFLGVAAVGLVVAVMIANADDTTLFDRMQLPDGDPNKLNYYIQPAPNGNEKVPFPTIFDPASVYLSLVVPAYNEEKRLPKMLDETLNYLKSREEKDKSFTWEIVIVNDGSKDKTKEVVLNYAKEYPNIFLLNQPVNMGKGAAIQAGCLHVRGELVLMLDADGATKIDDFEVLEKEIKSLMKTTNQAIVIGSRAQNEKAKRTPLRKFLSIGMHTLIVLSGVHGIRDTQCGFKLFTRESCKMIFMNQHVQRWCCDPEILVIARRLGMKISELPVEWNEIDGSKMKISGMIKMATDLIKIAIFHRVGAWKIRDRRH
Dolichyl-phosphate beta-glucosyltransferase involved in the glycosylation of glycoproteins through the synthesis of dolichyl beta-D-glucosyl phosphate which serves as a sugar donor for transfer of three glucose residues to the Man-9-GlcNAc-2-PP-dolichol precursor to N-glycans.
A2DZE8
O46392
CO1A2_CANLF
Alpha-2 type I collagen
Canis
MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPTGDRGPRGERGPPGPPGRDGDDGIPGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGASGAPGPQGFQGPAGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGPVGNPGPAGPAGPRGEVGLPGVSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGIVGEPGPAGSKGESGNKGEPGSAGAQGPPGPSGEEGKRGPNGEAGSAGPSGPPGLRGSPGSRGLPGADGPAGVMGPPGPRGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGAPGNVGPAGKEGPMGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPAGTAGEVGKPGERGLPGEFGLPGPAGPRGERGPPGESGAAGPSGPIGSRGPSGPPGPDGNKGEPGVLGAPGTAGASGPGGLPGERGAAGIPGGKGEKGETGLRGEIGNPGRDGARGAPGAMGAPGPAGATGDRGEAGPAGPAGPAGPRGTPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPIGSAGPSGPNGPPGPAGSRGDGGPPGATGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGLRGPRGDQGPVGRTGETGASGPPGFTGEKGPSGEPGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGSVGEPGPLGIAGPPGARGPPGAVGAPGVNGAPGEAGRDGNPGNDGPPGRDGQAGHKGERGYPGNIGPVGAVGAPGPHGPVGPTGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGLAGQHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGQPGTVGPAGIRGSQGSQGPAGPPGPPGPPGPPGPSGGGYDFGYEGDFYRADQPRSPPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRNSKVKKHIWLGETINGGTQFEYNVEGVTTKEMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWRKTIIEYKTNKPSRLPILDIAPLDIGDADQEFRVDVGPVCFK
Type I collagen is a member of group I collagen (fibrillar forming collagen).
O46392
C5CFW2
MURA_KOSOT
UDP-N-acetylglucosamine enolpyruvyl transferase
Kosmotoga
MSEIVVEGGRKLIGEVPISGSKNAALPILAAAVMIDEPVVLDNVPELKDVFTMLTILQRIGKKVSFRDNRVVVEPGNVLMGDVPYELVRMMRASFNVLGPLTMVCGWAKVGKPGGCNIGQRPVDFHIEGLKALGFLIKEEHGDVIAKKPSSFKEELYYKLPFPSVGATEQLMTVAALMSESKTIIENVAREPEIQDLQNFLNKAGAKIKGAGTDRIEIEGVEKLHGIEYHIIPDRIEAGTYLLAGVSTRGRVKVSNVIPEHLEALLKVLDELGVSITCDKNSIEVSVSGELKPIRVSTAPYPGFPTDLQPMLTAVLCTVPGESIIEEKVFENRFGYVDEMNRMSANIKVMNRVAHIVGVEKLSGAQIYAPDIRATAGMLIAALSAEGQTVIKNAAHIFRGYEKLKEKFTTIGAQIEVYPEE
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
C5CFW2
Q31G53
FABZ_HYDCU
Beta-hydroxyacyl-ACP dehydratase
Hydrogenovibrio
MLNVKEIFEYLPHRYPFLLVDRVTEFKSGESLKAYKNVTYNEPQFTGHFPDNPIMPGVMIIEAMAQCTGILAFKTQDVKPDGTSMYYLAAVDNCRFRKPAIPGDKLEFEVKTVNNKKGIWKFECTTSVDGKLIASCDMLCAERKV
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q31G53
B9ME46
PTH_ACIET
Peptidyl-tRNA hydrolase
Diaphorobacter
MIKLFVGLGNPGPEYEATRHNAGFWWIDALARELKVTLVPERSYHGLVARASVAGHSVWLLQPQTFMNLSGKSVAALARFFKIPPEEILVAHDELDIPPGQAKLKRGGSHAGHNGLRDIHAQLGTSDYWRLRIGIGHPGVKAEVVNWVLKKPAPDQRTLIEDSILHSLKAYPALLAGDMDKATLLVHTTKPPRPKATRPAQAQAAPQAGAD
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
B9ME46
B0BR79
FTSP_ACTPJ
Cell division protein FtsP
Actinobacillus
MMNLTRRQLLTRSAVAATMFSAPKTLWAAERQPLKIPPIIDVGRGRPVRLDLRPAQTQFDKGKLVDVWGVNGQYLAPTVRVKSDDFVKLTYVNNLPQTVTMNIQGLLAPTDMIGSIHRKLEAKSSWSPIISIHQPACTCWYHADTMLNSAFQIYRGLAGMWIIEDEQSKKANLPNKYGVNDIPLILQDQQLNKQGVQVLDANQKQFFGKRLFVNGQESAYHQVARGWVRLRIVNASLSRPYQLRLDNDQPLHLIATGVGMLAEPVPLESITLAPSERVEVLVELNEGKTVSLISGQKRDIFYQAKNLFSDDNELTDNVILELRPEGMAAVFSNKPSLPPFATEDFQLKIAEERRLIIRPFDRLINQKRFDPKRIDFNVKQGNVERWYITSDEAVGFTLQGAKFLIETRNRQRLPHKQPAWHDTVWLEKNQEVTLLVRFDHQASAQLPFTFGVSDFMLRDRGAMGQFIVTE
Cell division protein that is required for growth during stress conditions. May be involved in protecting or stabilizing the divisomal assembly under conditions of stress.
B0BR79
A2RJS5
RIMM_LACLM
Ribosome maturation factor RimM
Lactococcus cremoris subsp. cremoris
MENFYKVGTIVNTQGLQGEVRILPSTDFANERFSKGAVLALFDDKDNYIQDLKVKSGRLQKNFYVVKFEGFYHINDVEKYKGYVVKIAQENQEELNDGEFYYHEIIGSDVYDNDILIGQISEILQPGANDVWVVKRKGKRDLLLPYIPPVVLKVDVAQHRVDVDIMEGLDD
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
A2RJS5
B3QBR5
GLNE_RHOPT
Adenylyl transferase
Rhodopseudomonas
MIFSAITADLDNTALAARFGAGPRLYDPVLAAERWAGWLVDLAPEQADAIAALGNAFPDLQIALQSIAEASPYLFDLIRGDPVRLLRVLRGAPEQRLAKLLEDAETFVAAASAEDEVMAALRRLKAEAALLIALCDIGGIWPVMQVTQALTDLAGRSVQMALRFLLRLEAGRGRIVPPNPDCPEQGSGLIVLAMGKMGAGELNYSSDIDLIVFYELDAPTLAPDIEPQPFFVRVTQGLSRILQQRRGDGYVFRVDLRLRPDPASTPVALSTVSALDYYEREGRTWERAAMIKARPCAGDLVAGDALLSEIAPFVWRKHLDFAALSDVHDMKRQMQTYRGQTEIAVEGHNVKVGRGGIREIEFFAQTQQLIAGGRHPELRVRPTLEALEILAARNWITIQARDELTEAYLFLRKVEHRVQMIADEQTHALPDTVEAIERFSRFLGYDSRDSFARDLLGYLERVQGHYAKLFEGDPTGTAKLPPVDYGAGPEDTRLLDHLLSLGYKKPLMIATTLQQWMTGGYRVLKVETTQRAFREFVPALIEELARAEQPDDAVNAFDRLLQALHRGGRLISLLSQNRELLTLVALVLGAAPRLGDMLARQPQILDGLIDPRFFGAMPDQAELSARLAVTLADAGSYEEFLDRLRLFGQESLFLIGTRILSGTVPTQQAAVAFADVAEGIVGTVHGLVSEQFASTYGRVKGQQTAILAMGKLGSREMTASSDLDLILIYDFDDDQPDSDGERSLHGAQYFARFTQRLISAFTTRTNYGVLYDVDMRLRPSGRAGPVASRLDAFAAYQEQEAWTWEHLALTRARVISAPPEFRSRIEQVIRAVLTRPRDAAIIANDVAEMRRAIAQEKGEDDVWDLKYAAGGMVDIDFIAQYLQLVHAHEAPDILHVNTLSALDNATRLGLLAQADAEVLRPAARLYQNLTQILRLCVSEKFNPDTAGDDLLRVMVRAGDAPDFSSLQARVKETQSDVRAIFNRLIGGEDA
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
B3QBR5
Q0UK52
STHC_PHANO
Stemphyloxin II biosynthesis cluster protein C
Parastagonospora
MAPAETTGNVQRPEAGKQSMGSFWTQMFPPKPTYTEEQVPDLTGKIFIVTGSSSGVGKEAARMLYAKNAKVYMAARPGPKLPAAINSVQEAVPKSGGALIPLELDLADLAVVKKAVEKFTSLETKLHGLINNAAVQALKDTDGDARTAQGHEIHMGVNVLAPFLFTRLLTGVLTATARQEPPGTVRVVWVSSMGTETIGEKRRGLSPDYVDYWPLMSPLERYGLSKAGNWLHGVEFARRYAADGIASFPINPGHLKSDLYREGGALFKFALKPVLYPPTYGAYVELFAALSPTLTLKDSGAWSKYVEMVYFPDC
Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of the phytotoxin stemphyloxin II . The first step of the pathway is the synthesis of dehydroprobetaenone I by the polyketide synthase sthA and the enoyl reductase sthE via condensation of one acetyl-CoA starter unit with 7 malonyl-CoA units and 5 methylations . The C-terminal reductase (R) domain of sthA catalyzes the reductive release of the polyketide chain . Because sthA lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase sthE . The short-chain dehydrogenase/reductase sthC then catalyzes reduction of dehydroprobetaenone I to probetaenone I . The cytochrome P450 monooxygenase sthF catalyzes successive epoxidation, oxidation (resulting from epoxide opening) and hydroxylation to install a tertiary alcohol in the decaline ring to yield betaenone C from dehydroprobetaenone I and betaenone B from probetaenone I . The FAD-linked oxidoreductase sthB is responsible for the conversion of betaenone C to betaenone A via an intramolecular aldol reaction between C-1 and C-17 to form the bridged tricyclic system in betaenone A . Finally, the cytochrome P450 monooxygenase sthD catalyzes the hydroxylation of C-15 to afford the final metabolite stemphyloxin II .
Q0UK52
P00457
NIFH1_NOSS1
Nitrogenase reductase
Nostoc
MTDENIRQIAFYGKGGIGKSTTSQNTLAAMAEMGQRIMIVGCDPKADSTRLMLHSKAQTTVLHLAAERGAVEDLELHEVMLTGFRGVKCVESGGPEPGVGCAGRGIITAINFLEENGAYQDLDFVSYDVLGDVVCGGFAMPIREGKAQEIYIVTSGEMMAMYAANNIARGILKYAHSGGVRLGGLICNSRKVDREDELIMNLAERLNTQMIHFVPRDNIVQHAELRRMTVNEYAPDSNQGQEYRALAKKIINNDKLTIPTPMEMDELEALLIEYGLLDDDTKHSEIIGKPAEATK
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
P00457
B7IE21
PANC_THEAB
Pantoate-activating enzyme
Thermosipho
MKVIEKIEEMKKISREILESKKAIGFVPTMGFLHEGHLSLVKAAKSENDITVVSIFVNPTQFGPNEDYNNYPRDLERDLSMLKDMEVDYVFVPSVEEMYPDSFSTYVEEIKLSRFLCGASRPGHFRGVCTVVTKLFNIVKPTRAYFGQKDAQQFRVLRRMVRDLNMDVELVEMPIVREPDGLALSSRNTYLNDEERKEAVRLYKSLLKAKELIESGEKDVEIIKNEMKKILTHPLLRIDYIEIVDEENLEPVEKIDRRVIIAIAVFVGRARLIDNMII
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
B7IE21
Q9NX24
NHP2_HUMAN
snoRNP protein NHP2
Homo
MTKIKADPDGPEAQAEACSGERTYQELLVNQNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMVLAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVKPHEEYQEAYDECLEEVQSLPLPL
Required for ribosome biogenesis and telomere maintenance. Part of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Each rRNA can contain up to 100 pseudouridine ('psi') residues, which may serve to stabilize the conformation of rRNAs. May also be required for correct processing or intranuclear trafficking of TERC, the RNA component of the telomerase reverse transcriptase (TERT) holoenzyme.
Q9NX24
B8GT00
MINE_THISH
Cell division topological specificity factor
Thioalkalivibrio
MNFFNYFRSQKKKSAQVAKERLQVIVARERVHRDGPDYLPRLQEEILNVIRKYVQVDEDAVSIQLERDGDCEVLELNVTLPEHKA
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
B8GT00
Q6A1G2
FUT11_XENTR
Galactoside 3-L-fucosyltransferase 11
Silurana
MSAGCTQLVWGGRLHWGASHLLSCLLALCALWVLAAAEPTEGGSANVQGVGEAALYQGRGQHRVPSEDNVAVLSDQWEPSSFQPSSAFSGTDLGTMVADSYRGPGNSDRRSNKELPILLWWSENLFPHFPGDAERIDCPLSSCMVTKNKSVKLHKRTKSIIFYGTDFRAYEAPLPRLPHQTWALFHEESPMNNYVLSHLPGIRLFNYTATFSRESDYPLTLQWLPTIGYLHNPALSMAEKNRWRKNGYAPVLYMQSHCDVPSDRDRYVKELMKHLEIDSYGQCMKNREHPNKRLEDTSTATTEDPEFMAFTARYKFHLAMENAICADYMTEKLWRPMHLGAIPIYRGSPSVRDWMPNNHSIIMIDDFASPKELAEFIMTLDSDDEQYLKYLEYKKPGGTTNTFLLSSMEKREWGVNDMTAPNYLNGFECFVCDKENSRIKAEKTYKKSQQGGAAPEPHIADFNHMGCPMPTPGFGSAQEIPESDSWKQMWLQDYWQSFDQGEALTAMIQRNETNQDRFWDYMHETYIKRSMNH
Probable fucosyltransferase.
Q6A1G2
Q9CG33
SCPA_LACLA
Segregation and condensation protein A
Lactococcus
MIKEINIKIKNFEGPLDLLLHLVSQYEMDIFEVPLVPVIEQYLIYIQTMKELELEVAGEYMLMASQLMLIKSRRLLPTVTETFIEDTEQLEYDLLAQIDEYRKYKMLSQDLDELHQERSHFYSKAKTEIITDETVLLQDKSALDLFLAFTKILELQRQHFQDENTKIAAEKFTIADKILELSTRFTEQKICKFSDLFSSSTNKDELVTTFMALLELIKNQQISFSQGELFGEIILERKETSE
Participates in chromosomal partition during cell division. May act via the formation of a condensin-like complex containing Smc and ScpB that pull DNA away from mid-cell into both cell halves.
Q9CG33
Q2JFF1
RS13_FRACC
30S ribosomal protein S13
Frankia
MARLSGVDLPREKRVEIALTYIFGIGRSRSRDTLAATAVNPDTRVRDLSEEEIVRLRDWIDANYRVEGDLNREIKQDIRRKMEIGCYQGLRHRRNLPVHGQRTHTNARTRKGPRRAIAGKKKAGKK
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
Q2JFF1
B2HUM8
HEM1_ACIBC
Glutamyl-tRNA reductase
Acinetobacter calcoaceticus/baumannii complex
MSFFALGVNHQTASVELREQIAFNAERLSNLLAEQRHHESLKDLVVVSTCNRTEVYAMAEDAESLLKWLADANNIDVKQLIHHVYRYENAQAITHLMRVASGLDSLMLGEPQILGQVKSALALSKEAQTVSPELNSVFEYAFYAAKRVRSETAVGSHAVSMGYAVAQLALQVFSKPEKLTVMVVAAGEMNSLVAKHLAEMGVAKMIICNRSRERADQLAQEIAHQVEVEIIDFSDLAENLYRADVVSSCTGSLHQVIAYADVKTALKKRRYQQMLMVDLAVPRDIDPKVESLDGVYLYGVDDLQSVIDENLAQRRQAAVEAEVMVNQLATQLITHQKVKEAGSTIHAYRQHSEEISQRELTQALEALHHGGNPEQVLQQFAHRLTQKLIHPTSMLLREAAKAESPDYFEWLQQHLQDVFDHERKPKR
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
B2HUM8
O94811
TPPP_HUMAN
p25-alpha
Homo
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath . Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath . Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes . Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear . In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network . Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 . Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility . Plays a role in cell proliferation by regulating the G1/S-phase transition . Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 .
O94811
P25033
HEMO_HYACE
Protein P4
Hyalophora
MAFKSIAVLSACIIVGSALPVDKYPVLKDQPAEVLFRENNPTVLECIIEGNDQGVKYSWKKDGKSYNWQEHNAALRKDEGSLVFLRPQASDEGHYQCFAETPAGVASSRVISFRKTYLIASPAKTHEKTPIEGRPFQLDCVLPNAYPKPLITWKKRLSGADPNADVTDFDRRITAGPDGNLYFTIVTKEDVSDIYKYVCTAKNAAVDEEVVLVEYEIKGVTKDNSGYKGEPVPQYVSKDMMAKAGDVTMIYCMYGSNPMGYPNYFKNGKDVNGNPEDRITRHNRTSGKRLLFKTTLPEDEGVYTCEVDNGVGKPQKHSLKLTVVSAPKYEQKPEKVIVVKQGQDVTIPCKVTGLPAPNVVWSHNAKPLSGGRATVTDSGLVIKGVKNGDKGYYGCRATNEHGDKYFETLVQVN
Insect-immune protein. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.
P25033
B2GDT7
RL13_LIMF3
50S ribosomal protein L13
Limosilactobacillus
MRTTYMAKPGQVDRKWYVVDAKGISLGRLASTVASILRGKNKPTFTPHVDTGDYVIVINAAEVKLTGKKATGKIYYRHSNHPGGLKQRTAGDFLAKDPEKMVEQTIKGMLPHTSLGRKMGMKLHVYAGESHNQAAQKPEVLDITNLI
This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
B2GDT7
Q62K72
NODI_BURMA
Nodulation ATP-binding protein I
pseudomallei group
MSVAPIDFQQVEKRYDDKLVVDGLSFHVQPGECFGLLGPNGAGKTTTLKMLLGITHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPDFTVRENLLVFARYFGLTAHAARALVPPLLEFAKLESKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCHRLCVIEEGRKIAEGAPRMLIEAEIGCDVIEIYGPDPVQLRDELAPFAERTEISGETLFCYVDNPEPIHARLKGRAGLRYLHRPANLEDVFLRLTGREMLD
Part of the ABC transporter complex NodIJ involved in the export of the nodulation factors (Nod factors), the bacterial signal molecules that induce symbiosis and subsequent nodulation induction. Nod factors are LCO (lipo-chitin oligosaccharide), a modified beta-1,4-linked N-acetylglucosamine oligosaccharide. This subunit is responsible for energy coupling to the transport system.
Q62K72
Q9I7M2
GTPBA_DROME
GTP-binding protein 10 homolog
Sophophora
MVQIFKFLLKSSKSTGRAHFRPTFLDTLRLAVRGGHGGNGLPKYGGVGGQGGCVYLVAKEGLTLRKVVQGLKDKRVAASSGEDSSKASIFGRRGADQRIEVPVGVQVYDDQQKLIADLDEHEATCIVAGGGTGGCTATNFLGRPGENRTVNLDLKLIADVGLVGFPNAGKSTLLKAVSNAKPKIAAYPFTTIRPQIGTIEYRDLRSITVADLPGLIEGAHANFGMGHKFLKHIERTRLLVFMVDIFGFQLSPKHPHRDCLANVYALNKELELYDPSLLEKPSVLLLNKMDKEGAHEIFTKVKPLVSDLASGLEQCPEELRPKQVLNFDSIVPISAMNSSKITQVKSQLRRTLVRLAEKQFLADEDQVKEKLRQRVGVVGPKIT
May be involved in the ribosome maturation process.
Q9I7M2
Q15NG5
DAPF_PSEA6
PLP-independent amino acid racemase
Pseudoalteromonas
MQVQFSKMHGLGNDFVVIDNVTQNVFFSKEKISQLADRNFGIGFDQLLVVEPPYDPEQDFHYRIFNSDGSEVSQCGNGARCFARFVKMKGLTNRNKIVVSTKAGRIVLYHERDGQITVNMGEPIFEPAKIPLKANKQENIYIIRENDHTFFCGAVSMGNPHCVLLVDDVETADVEGIGKTLVAHERFPEGANIGFMQILNSGHIKLRVYERGVGETLACGSGACAAVAVGQMQKKLNKEVTVDLPGGTLKIRWQGPGSILKMTGTAEHVFDGNITL
Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L-lysine and an essential component of the bacterial peptidoglycan.
Q15NG5
A7H026
FMT_CAMC5
Methionyl-tRNA formyltransferase
Campylobacter
MNIIFMGTPAYARTILDALVRAGIGVAGVFTQPDKPVGRKQILTPSEVKIYAQQNLPHAKIFQPKTLKEGTVAAEILALKPDFIVVAAYGKILPKSVLDIAPCINLHASILPKYRGASPIQAALLNGEKNTGVTAMLMDEGLDTGDMLGFTHVSCEGKRSAEMFEILGELAGELAVKTLFDFKNLTPQKQDDALATHCKKIQKSDGLVNLSEDAEQIYNKFRAFHEWPGVFLESGLKFLELNLAEGSGAAGEILRIEKDGFVVACGTGALKILALQEAGKKALDAKAYINGKRLVAGNKIS
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
A7H026
C4L176
HIS6_EXISA
ImGP synthase subunit HisF
unclassified Exiguobacterium
MLKRRIIPCLDVKEGRVVKGIEFVQLRDIGDPVEIAKYYDESGADELVFLDITASTERRQTMLDVVSAVARKVFIPLTVGGGIRSLEDISSLLKAGADKVSLNTLAVESPSLIREAADRFGSQCIVVAIDVKFKDGEYYVYTYGGKQKTDLLAVEWAKQVAALGAGELLVTSMNQDGKQSGYDLSILEQLREVVDIPIIASGGAGNAEHVVEALEKVDAALLASILHDRKTTVEEVKHVCKSHNLPMRFVSTKMD
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
C4L176
P0A5Y5
MABA_MYCBO
Beta-ketoacyl-acyl carrier protein reductase
Mycobacterium tuberculosis complex
MTATATEGAKPPFVSRSVLVTGGNRGIGLAIAQRLAADGHKVAVTHRGSGAPKGLFGVECDVTDSDAVDRAFTAVEEHQGPVEVLVSNAGLSADAFLMRMTEEKFEKVINANLTGAFRVAQRASRSMQRNKFGRMIFIGSVSGSWGIGNQANYAASKAGVIGMARSIARELSKANVTANVVAPGYIDTDMTRALDERIQQGALQFIPAKRVGTPAEVAGVVSFLASEDASYISGAVIPVDGGMGMGH
Part of the mycobacterial fatty acid elongation system FAS-II, which is involved in mycolic acid biosynthesis. Catalyzes the NADPH-dependent reduction of beta-ketoacyl derivatives, the second step of the FAS-II elongation cycle.
P0A5Y5
P0A9G7
ACEA_ECOL6
Isocitratase
Escherichia
MKTRTQQIEELQKEWTQPRWEGITRPYSAEDVVKLRGSVNPECTLAQLGAAKMWRLLHGESKKGYINSLGALTGGQALQQAKAGIEAVYLSGWQVAADANLAASMYPDQSLYPANSVPAVVERINNTFRRADQIQWSAGIEPGDPRYVDYFLPIVADAEAGFGGVLNAFELMKAMIEAGAAAVHFEDQLASVKKCGHMGGKVLVPTQEAIQKLVAARLAADVTGVPTLLVARTDADAADLITSDCDPYDSEFITGERTSEGFFRTHAGIEQAISRGLAYAPYADLVWCETSTPDLELARRFAQAIHAKYPGKLLAYNCSPSFNWQKNLDDKTIASFQQQLSDMGYKFQFITLAGIHSMWFNMFDLANAYAQGEGMKHYVEKVQQPEFAAAKDGYTFVSHQQEVGTGYFDKVTTIIQGGTSSVTALTGSTEESQF
Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates.
P0A9G7
P45783
GSPN_AERSA
General secretion pathway protein N
Aeromonas
LQANRQYLFQGSLKPGPELPEEMKQGLPFLGQPDGQGRFPLRYQGRI
Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of proteins.
P45783
Q59500
ILVC_MYCAV
Ketol-acid reductoisomerase type I
Mycobacterium avium complex (MAC)
MFYDDDADLTIIQGRKVGVIGYGSQGHAHSLSLRDSGVQVKVGLKEGSKSRAKVSEQGLDVDTPAAVAKWADVIMLLAPDTAQADIFKNDIEPNLSDGDALFFGHGLNIHFGLIKPPAEVTVAMVAPKGPGHLVRRQFVDGKGVPCLIAVDQDPTGKGEALALSYAKAIGGTRAGVIKTTFKDETETDLFGEQAVLCGGTEELVKAGFDVMVESGYPPEMAYFEVLHELKLIVDLMYEGGIARMNYSVSDTAEFGGYLSGPRVIDAGTKDRMREILRDIQNGDFVKKLVANVEGGNKQLEQLRKENVEHPIEVVGKRLRDLMSWVDRPITETA
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
Q59500
A4SDE2
END4_CHLPM
Endonuclease IV
Chlorobium
MKRVGAHVSIAGGVENAPLNATAIGAKAFALFTRNQRQWHSPPLQKASVDAFRRHCEAGGFDARHILPHDSYLINLGNPDPDKLERSRKAFIEEMERAETLGLVLLNFHPGSHLNAIGEEECLGLIADSINLAIKATDRVTAVIENTAGQGTNLGSRFEHLRAIIDRIEDRSRIGVCLDTCHLFASGYDLGTAEAAERTFEEFDRTVGMQYLKGMHLNDALRPLGSRLDRHACIGKGMIGIEGFRYIMQSPLFEEIPLILETPDSEGWKEEIELLYSLE
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
A4SDE2
B3R0P2
TRMD_PHYMT
tRNA [GM37] methyltransferase
16SrX (Apple proliferation group)
MIIEIITIFPKFFDSFFEHSIIKRAIKKNKIIFQVHDLRNYSNNKHNQVDDSPYGGGAGMLLKFPPFYECLKKIKKSFSKVILLSPQGTLLNQKMAFEYVNEIKHLIILNGNYEGIDARILNYIDAEISIGDYILTGGEIATIVLIDVLVRLLPGVINSESYLEDSHQKDLLKYPQYTKPKIYQNQKVPEILLSGNHKNIKDWRYNQSLKNTFFKRPDILKKINLTEKQQKILLEIKKKLKEG
Specifically methylates guanosine-37 in various tRNAs.
B3R0P2
Q9FF78
PME46_ARATH
Pectin methylesterase 46
Arabidopsis
MSSYGRLDEHEQAKLEASRKTKKRIAIIAISSIVLVCIVVGAVVGTTARDNSKKPPTENNGEPISVSVKALCDVTLHKEKCFETLGSAPNASRSSPEELFKYAVKVTITELSKVLDGFSNGEHMDNATSAAMGACVELIGLAVDQLNETMTSSLKNFDDLRTWLSSVGTYQETCMDALVEANKPSLTTFGENHLKNSTEMTSNALAIITWLGKIADTVKFRRRRLLETGNAKVVVADLPMMEGRRLLESGDLKKKATIVVAKDGSGKYRTIGEALAEVEEKNEKPTIIYVKKGVYLENVRVEKTKWNVVMVGDGQSKTIVSAGLNFIDGTPTFETATFAVFGKGFMARDMGFINTAGPAKHQAVALMVSADLSVFYKCTMDAFQDTMYAHAQRQFYRDCVILGTVDFIFGNAAVVFQKCEILPRRPMKGQQNTITAQGRKDPNQNTGISIHNCTIKPLDNLTDIQTFLGRPWKDFSTTVIMKSFMDKFINPKGWLPWTGDTAPDTIFYAEYLNSGPGASTKNRVKWQGLKTSLTKKEANKFTVKPFIDGNNWLPATKVPFNSDF
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Q9FF78
Q9LSS7
RUBP1_ARATH
Deneddylase-1
Arabidopsis
MGNTSDDDKILSYEDVVLRRSDLDILNGPIFLNDRVIEFYLSFLSTVHSSTTISLIPPSIAFWISNCPDTEYLKDFMKPLNLRDKDLLILPVNDNSNVEVAEGGLHWSLLVYYKEANTFVHHDSYMGVNRWSAKQLFKAVSPFVSNGDASYKECTDTPQQKNGYDCGVFLLATARVICEWFSSGGMKNRDELWFANVKETVPDLVNHLREEILALIKKLMSESVSK
Processes the pre-form of the ubiquitin-like protein NEDD8/RUB1. Has the capacity to discriminate between NEDD8/RUB1 and ubiquitin. Has no SUMO protease activity.
Q9LSS7
A1S212
RPOC_SHEAM
Transcriptase subunit beta'
Shewanella
MKDLLKFLKQQGKTEEFEGIKIGLASPDLIRSWSFGEVKKPETINYRTFKPEREGLFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTKVRRERMGHIELASPVAHIWFLKSLPSRIGLMLDMTLRDIERVLYFESYVVIEPGMTSLERGQMLTEENYLDALEEYGDEFEAKMGAEAVLDLLRAIDLEKEIEQMREELPSINSETRRKKVTKRLKLIEAFYTSGNKPEWMILKVLPVLPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEKRMLQESVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQGRFRQNLLGKRVDYSGRSVITVGPTLRLHQCGLPKKMALELFKPFIYGKLEGRGLATTIKAAKKMVEREVAEVWDVLDEVIREHPVMLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAAYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANGEPIIVPSQDVVLGLYYISRERVNGRGEAMAFESVAEAEKAYRVGAAELHARVKVRITETIIGENGERTKQRRIVDTTVGRAILSQILPAGLSFDLVNQDMGKKQISKLLNTCYRQLGLKDTVIFADQLMYTGFQYATISGASVGINDMVIPEEKYSLVADAEAEVIEIQEQFQSGLVTAGERYNKVIDIWASANEKVSKAMMENLSSETVINRHGEEEKQKSFNSIYMMADSGARGSAAQIRQLAGMRGLMAKPDGSIIETPIVANFREGLNVLQYFISTHGARKGLADTALKTANSGYLTRRLVDVAQDLVIIEDDCGATEGLSMKPLIEGGDVVEPLRERVLGRVVAEDVMYPGTDEVLAPRNTLLDEAWCDKLEQHSVDEVQVRSVITCETDFGVCAKCYGRDLARGHIINMGEAIGVVAAQSIGEPGTQLTMRTFHIGGAASRASAENSVQVKNAGTLKLHNAKYVTNSDGKLVIVSRSSELAIIDELGREKERYKVPYGTVLDTKEGAEVNAGQIIANWDPHTHPIITEVAGSIKFVDMIDGVTITRQTDELTGLSSIVVLDVGQRTSAGKEMRPAVRLVDDNGNDLTIPGTDVPAQYFLPGNAIVNLDDNAKISVGDALARIPQESSKTRDITGGLPRVADLFEARRPKEPAILAEISGTISFGKETKGKRRLVITPNDGGDAYEEMIPKWRNLNVFEGEKVERGEVIADGPESAHDILRLRGIHNVANYIVNEVQDVYRLQGVKINDKHIEVIIRQMLRKCIITQAGDSEFLEGEQVEVARVKIANRDLEAAGKQPAKFERELLGITKASLATESFISAASFQETTRVLTEAAVGGKSDNLRGLKENVIVGRLIPAGTGFAYHKNRAKARASGEETAAPTITASEAEQNLADLLNLAGSQE
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A1S212
Q86W10
CP4Z1_HUMAN
Laurate 7-monooxygenase
Homo
MEPSWLQELMAHPFLLLILLCMSLLLFQVIRLYQRRRWMIRALHLFPAPPAHWFYGHKEFYPVKEFEVYHKLMEKYPCAVPLWVGPFTMFFSVHDPDYAKILLKRQDPKSAVSHKILESWVGRGLVTLDGSKWKKHRQIVKPGFNISILKIFITMMSESVRMMLNKWEEHIAQNSRLELFQHVSLMTLDSIMKCAFSHQGSIQLDSTLDSYLKAVFNLSKISNQRMNNFLHHNDLVFKFSSQGQIFSKFNQELHQFTEKVIQDRKESLKDKLKQDTTQKRRWDFLDILLSAKSENTKDFSEADLQAEVKTFMFAGHDTTSSAISWILYCLAKYPEHQQRCRDEIRELLGDGSSITWEHLSQMPYTTMCIKECLRLYAPVVNISRLLDKPITFPDGRSLPAGITVFINIWALHHNPYFWEDPQVFNPLRFSRENSEKIHPYAFIPFSAGLRNCIGQHFAIIECKVAVALTLLRFKLAPDHSRPPQPVRQVVLKSKNGIHVFAKKVC
A cytochrome P450 monooxygenase that catalyzes the in-chain oxidation of fatty acids . Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates lauric and myristic acids predominantly at the omega-4 and omega-2 positions, respectively . Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA). Displays an absolute stereoselectivity in the epoxidation of arachidonic acid producing the 14(S),15(R)-epoxyeicosatrienoic acid (EET) enantiomer . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) .
Q86W10
P54045
RS5_METJA
30S ribosomal protein S5
Methanocaldococcus
MRFNIDEWEPKTTIGRMVKEGQITDIDYILDNNLPILEPEIVDALLPDLEEKVLDVKLVQRMHKSGRRARFRATVVVGNRNGYVGVGKGKAKEVGPAIRKAIAQAKKNIIRVKRGCGSWECGCGTPHSIPYKGYGKCGSTAIEILPAPKGVGLVAGDVAKAVLGLAGIKDVWTKTFGETRTTYNFAMATFEALKSLNFTRTMEKHKEKLGIVEGRVL
With S4 and S12 plays an important role in translational accuracy.
P54045
A4QJM2
RK20_AETGR
50S ribosomal protein L20, chloroplastic
Aethionema
MTRIKRGYIARRRRTKIRLFASSFRGAHSRLTRTMTQQRIRALVSAHRDRGRRKRDFRRLWITRINAVIQEMEVFNSYNRFIHNLYKKQVLLNRKILAQIALLNRSCLYTISNEIIK
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
A4QJM2
Q8CDT7
CBCO1_MOUSE
Ciliary-associated calcium-binding coiled-coil protein 1
Mus
MNFSIEQYSKFMTLLDMLLHNLQTLHMSLEDSIKWLGEVMAEIGPNHSQKSEDFHVFEVKEANAIIDYLKISLFQHYRLYEFLFYSTREEIVIGTEQTIEVVKPADYPFPAPLEEGISLDTYSTFIEPLPTPDMEQKVLDQEQGTQEALLESEMREEDPLGGFTIDDVKSALERVTDEVLISMQKEISEKLQVQEEAFNARIEKLKKA
Calcium-binding protein . May be involved in the control of sperm flagellar movement .
Q8CDT7
Q9VE04
RM55_DROME
39S ribosomal protein L55, mitochondrial
Sophophora
MLLKQLPQAVQQIRCISSATTAVTRLHRSVYCRLYPTVVVQPDGSTINIRYHEPRKIIKLPLDLSTLTDAERRARLEARKPRKKVKIMEEVEDNFNAKKYMKYIKKK
Involved in mitochondrial biogenesis and G2/M phase cell cycle progression.
Q9VE04
A1V9E1
ILVD_DESVV
Dihydroxy-acid dehydratase
Desulfovibrio
MRSKKMTHGLEKAPHRSLLHALGLTREELARPLVGVVNAANEVVPGHIHLDDIAEAVKAGVRAAGGTPLEFPAIAVCDGLAMNHEGMRFSLPSRELIADSIEIMATAHPFDALVFIPNCDKSVPGMLMAMLRLDVPSVMVSGGPMLAGATLAGRADLITVFEGVGRVQRGDMTEAELDELVEGACPGCGSCAGMFTANSMNCLAETIGLALPGNGTTPAVTAARIRLAKHAGMKVMEMLERNIRPRDIVTEKAVANAVAVDMALGCSTNTVLHLPAVFAEAGLDLTLDIFDKVSRKTPNLCKLSPAGHHHIQDLHAAGGIPAVMAELDSIGLIDRSAMTVTGRTVGENLDALGAKVRDADVIRSVDAPYSPQGGIAILKGSLAPGGAVVKQSAVAPEMMVREAVARVFDSEEAACEAIMGGRIKAGDAIVIRYEGPKGGPGMREMLTPTSAIAGMGLGADVALITDGRFSGGTRGAAIGHVSPEAAEGGPIGLVQEGDRIRIDIPARALDLLVDEDELARRRAVFVPVEKEITSPLLRRYARMVSSAATGARQR
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
A1V9E1
B2UQL7
G1092_AKKM8
Glycosyl hydrolase family 109 protein 2
Akkermansia
MSIFSSRRQFLKSLGLAAGAAAAGNALPGKAVEIPAGDHLWKSASPAAPRPSGSTYMGGFKAPRLGRIRLAFIGVGGRGFSHLAQMCVMDGVEIVGICDLKEELTKRGVDRVLSRMGKSPLGYSGGDMEYLTMLKELKPDAVIISTDWSSHARIACDSMKHGAHAFVEVPLAVSLEELWSLVDTSEATRKHCMMMENVNYGRDELMFLNMVRQGVIGDLLHGEAAYIHCLVTQLGDTRGEGAWRPEYHTRINGNLYPTHGLGPVAQYMNLERGEDRFCRVAAFASPALGRNAYAKKHLPADHRWNNTPFICGDMNTAVVKTQLGRTILVQLDETSPRPYSRANLIQGTEGTLAGFPTRVAGEKLGNGNYHEWIEGREKLAAIYEKYDHPLWKRIGELATKMGGHGGMDFVMLSRIVECLRNGEPMDQNVYEGASWSSLLPLTARSIAQGGMPVEFPDFTRGDWKTTMPLAVVS
Glycosidase.
B2UQL7
B0VNK1
ATPD_ACIBS
F-type ATPase subunit delta
Acinetobacter calcoaceticus/baumannii complex
MAELLTLARPYAKAAFAYASEQGATDNWSNALQVLSAAVQDEAFSAYLNRPEHTPAEQVKLFAKVLGEDQSQAVSNFLTLLADNDRLVLLPEIAAEYEQLKSQNNNNVDVVIESAFPLTAEQEQLLKSALEKRFNSTVTVSVEVKPELIAGVVIRAGDQVIDDSALNKLEKMRTRLLA
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
B0VNK1
B9DUP5
RNZ_STRU0
tRNase Z
Streptococcus
MELQFLGTGAGQPAKQRNVSSLVLKLLDEINEVWMFDCGEGTQRQILETSIKPRKIQKIFITHLHGDHIFGLPGFLSSRAFQASEEQTDIEIFGPLGIKSFVQNSLAISGTRLPYKIHFHEFTDKDMGKIMETDKFLVYAEKLAHTIFCMGYRVVQKDLEGTLDAEALKKAGVPFGPLFGKIKNGQDIVLDDGRQILAKDYISEPKKGKVITILGDTRKTPASQRLALNADVLVHESTYGKGDDRIARNHGHSTNMQAAQIAKDANVKRLLLNHVSARFLSRDCRQMEKDAASLFENVKIVKDLEEVTI
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
B9DUP5
C6E7L6
RLMH_GEOSM
rRNA (pseudouridine-N3-)-methyltransferase RlmH
unclassified Geobacter
MRLKLLWVGKTQESWVRTGIEEYAGRIRRYAPLEILEAREEKGAQAAAMRERECERLAKLIPKGGRLVLLDERGEAMTSPELASFLSKNRDQGTQDLVFAIGGAYGFTDAFRSQAFKSISLSRMTLTHQMVRVFLLEQIYRGFTIINGEPYHHE
Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA.
C6E7L6
A8YXL4
RS17_LACH4
30S ribosomal protein S17
Lactobacillus
MSETNERNRRHVYQGRVVSDKMDKTIVVVVDTYKNHPVYSKRIRYSKKYYAQDENNEAKVGDTVRIMETRPLSRKKRFRLVKIVKKSV
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
A8YXL4
P48145
NPBW1_HUMAN
G-protein coupled receptor 7
Homo
MDNASFSEPWPANASGPDPALSCSNASTLAPLPAPLAVAVPVVYAVICAVGLAGNSAVLYVLLRAPRMKTVTNLFILNLAIADELFTLVLPINIADFLLRQWPFGELMCKLIVAIDQYNTFSSLYFLTVMSADRYLVVLATAESRRVAGRTYSAARAVSLAVWGIVTLVVLPFAVFARLDDEQGRRQCVLVFPQPEAFWWRASRLYTLVLGFAIPVSTICVLYTTLLCRLHAMRLDSHAKALERAKKRVTFLVVAILAVCLLCWTPYHLSTVVALTTDLPQTPLVIAISYFITSLSYANSCLNPFLYAFLDASFRRNLRQLITCRAAA
Interacts specifically with a number of opioid ligands. Receptor for neuropeptides B and W, which may be involved in neuroendocrine system regulation, food intake and the organization of other signals. Has a higher affinity for neuropeptide B.
P48145
B2VFA0
YIHI_ERWT9
Der GTPase-activating protein YihI
Erwinia
MKQPARTSQVKKPAARVKRKTREEINQEARDRKREKKHSGHASGSRANPATVSQKGDKSQSVKDPRIGSKKAIALGTDAPVRQPANPVKAAKPAVEKKPRLTPEEELAKLENDERLDALLDRLENGEALSAEDQAWLDQSLDRIDVLMEQLGIALDDDAEDEKAEEDMYRLLKGSHRTPE
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
B2VFA0
A6TBX4
NUOA_KLEP7
NUO1
Klebsiella
MRMSTSTEVIAHHWAFAIFLIIAIGLCCLMLVGGWYLGGRARARSKNTPFESGIDSVGSARLRLSAKFYLVAMFFVIFDVEALYLYAWSTSIRESGWVGFVEAAIFILVLLAGLVYLVRIGALDWTPARSRRTLVNPETDSPTNRHMQ
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
A6TBX4
Q8GSM3
LOX22_HORVU
LOX2:Hv:2
Hordeum
MQTATKPLVGARAVPLSRRASFLVAEARRKPSTNARRTRVGSTSTTTTTTTILTDVNGPALTTVAKPGHQYDLKQTVEMKATVSVHMKSFWWSDEKKERARDWAYDLILGSWLTLELVSSELDPKTGQEHDVISGKLKHSRETEKDYDLYEAIFTCRHRLAPSGAVRLVNYHHTEMLLGEVKIFPAGEDPTKSSAVTLFHCQSWIDPSHCSPDKRTFFPVEKSYIPSQTPKGVEKLRKSELEALRGNGCGERKKHDRIYDYDVYNDLGKPESKRPVLGGKEHPYPRRCRTGRPRSKTDPSSEEESHKKGEMYVPRDETFTERKEQAFLTKQLLSQLHGLCTGLKVNKDILPSFPTLASIDALYDDDFRNQPVQPEGGKVRLILDLLAKELVHLVKLEGAEFVEGIRRVFKFETPEIHDMDKLAWFRDEEFARQTLAGMNPLSIQLVTELPIVSKLDELKYGPADSLITKELIEKQINRIMTAEEAVAQKKLFMLDYHDLLLPYVHRVRKLDNKTMYGSRTLFFLADDGTLRPIAIELTRPKSPHKQQWRKVFTPGSGYSGSVTGSWEWQLAKIHVLSHDTGYHQLVSHWLRTHCCVEPYVIAANRQLSQMHPIYRLLHPHFRFTMEINAQARGMLICADGIIEKTFSPGEFSMEISSAAYDKQWRFDMEALPEDLIRRGMAVRGEDGKLELAIEDYPYANDGLLVWDAIKQWASDYVAHYYPCAVDIVDDEELQDWWTEVRTKGHPDKQDEPWWPELDCHESLVQVLATIMWVTSAHHAAVNFGQYPMAGYVPNHPSIARRNMPCEMGPEEMLAFKAAPEKVWLDTLPSQLQTVMVMATLDLLSSHASDEEYMGTHQEPAWQRDGEVDKAFQVFQKKMRDIAEQVEEWNKDDSRRNRHGAGVVPYVLLRPLNGNPMDAKTVMEMGIPNSISI
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This enzyme exhibits linoleate 13-lipoxygenase activity.
Q8GSM3
Q9Y597
KCTD3_HUMAN
Renal carcinoma antigen NY-REN-45
Homo
MAGGHCGSFPAAAAGSGEIVQLNVGGTRFSTSRQTLMWIPDSFFSSLLSGRISTLRDETGAIFIDRDPAAFAPILNFLRTKELDLRGVSINVLRHEAEFYGITPLVRRLLLCEELERSSCGSVLFHGYLPPPGIPSRKINNTVRSADSRNGLNSTEGEARGNGTQPVLSGTGEETVRLGFPVDPRKVLIVAGHHNWIVAAYAHFAVCYRIKESSGWQQVFTSPYLDWTIERVALNAKVVGGPHGDKDKMVAVASESSIILWSVQDGGSGSEIGVFSLGVPVDALFFIGNQLVATSHTGKVGVWNAVTQHWQVQDVVPITSYDTAGSFLLLGCNNGSIYYIDMQKFPLRMKDNDLLVTELYHDPSNDAITALSVYLTPKTSVSGNWIEIAYGTSSGAVRVIVQHPETVGSGPQLFQTFTVHRSPVTKIMLSEKHLVSVCADNNHVRTWTVTRFRGMISTQPGSTPLASFKILSLEETESHGSYSSGNDIGPFGERDDQQVFIQKVVPITNKLFVRLSSTGKRICEIQAVDCTTISSFTVRECEGSSRMGSRPRRYLFTGHTNGSIQMWDLTTAMDMVNKSEDKDVGGPTEEELLKLLDQCDLSTSRCATPNISPATSVVQHSHLRESNSSLQLQHHDTTHEAATYGSMRPYRESPLLARARRTESFHSYRDFQTINLNRNVERAVPENGNLGPIQAEVKGATGECNISERKSPGVEIKSLRELDSGLEVHKIAEGFSESKKRSSEDENENKIEFRKKGGFEGGGFLGRKKVPYLASSPSTSDGGTDSPGTASPSPTKTTPSPRHKKSDSSGQEYSL
Accessory subunit of potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3 (HCN3) up-regulating its cell-surface expression and current density without affecting its voltage dependence and kinetics.
Q9Y597
Q72HM3
FABZ_THET2
Beta-hydroxyacyl-ACP dehydratase
Thermus
MDIREILKVLPHRYPFLLVDRVLEADERRFKALKNVTFNEPHFQGHFPGHPVMPGVLILEAMAQAAVGALVRQPGFPQGGLAFLAGVEGARFRRPVYPGDTLILEGELLAFRRGVGKVAVRALVEGEERASATLTFVLQGAS
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
Q72HM3
Q8JI40
CRVP_GLOBL
Cysteine-rich venom protein ablomin
Gloydius
MIVFIVLPILAAVLQQSSGNVDFDSESPRKPEIQNEIVDLHNSLRRSVNPTASNMLKMEWYPEAAANAERWAYRCIEDHSSPDSRVLEGIKCGENIYMSPIPMKWTDIIHIWHDEYKNFKYGIGADPPNAVSGHFTQIVWYKSYRAGCAAAYCPSSEYSYFYVCQYCPAGNMRGKTATPYTSGPPCGDCPSACDNGLCTNPCTQEDVFTNCNSLVQQSNCQHNYIKTNCPASCFCHNEIK
Blocks contraction of smooth muscle elicited by high potassium-induced depolarization, but does not block caffeine-stimulated contraction. Since high potassium-treatment activates voltage-gated channels and caffeine exposure activates ryanodine receptors, this toxin may target L-type voltage-gated calcium channels (Cav) (and not ryanodine receptors) on smooth muscle . This toxin also shows a little inhibition on cyclic nucleotide-gated CNGA1 channel .
Q8JI40
A0KF26
RL22_AERHH
50S ribosomal protein L22
Aeromonas
MEAIAKHRYARTSAQKARLVADQVRGLSVDKALNILTFSPKKAAALVKKVLESAIANAEHNEGADIDALRVATIMVDEGPSMKRIRPRAKGRADRILKRTAHITVVVSDAKAGR
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
A0KF26
Q635G3
BIOD_BACCZ
Dethiobiotin synthase
Bacillus cereus group
MSGFFITATDTEVGKTVVAGALAGVFRELGYNIGVYKPLQSGHVASNPEGDAARLKALSGVPTKEDEICPYSIEEPLAPRLAMKRAGRTVTLKDIIHHYNERLKEFNSLFVEGAGGLAVPYTEDALVIDFAKELQLPLIVVARPTLGTVNHTVLTIAYAKAHGLTVAGVILSGCKECEMERVQENKVMIEELSGVPVLGLLPFFEGEFTKKEVLESAKEYIMISKLEECIRNESTVAHTSSN
Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring.
Q635G3
Q04KR9
DAPA_STRP2
4-hydroxy-tetrahydrodipicolinate synthase
Streptococcus
MSYQDLKECKIITAFITPFHEDGSINFDAIPALIEHLLDHHTDGILLAGTTAESPTLTHDEELELFAAVQKIVNGRVPLIAGVGTNDTRDSIEFVKEVAEFGGFAAGLAIVPYYNKPSQEGMYQHFKAIADASDLPIIIYNIPGRVVVELTPETMLRLADHPNIIGVKECTSLANMAYLIEHKPEEFLVYTGEDGDAFHAMNLGADGVISVASHTNGDEMHEMFIAIAESDVKKAAAIQRKFIPKVNALFSYPSPAPVKAVLNYMGFEAGPTRLPLVPAPEEDAKRIIKVVVDGDYEATKATVTGVLRPDY
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
Q04KR9
B7IGQ4
PLSX_THEAB
Phosphate-acyl-ACP acyltransferase
Thermosipho
MKKIAIDLMGGDYAPEEILAGALSFAKENEDVELYLVGIEENFKDVQLPKNCVKVVTDDFLPMDVKPTEAVRRRKSTMYVSCQLAREKKVDAVVSAGNTGALLACATFVVGRIKGIERPTLAVPIPTKNDFCVLADAGANIDVKPSNLLQFAIMGVEYAKLLGKDNPTIGLLNVGTEENKGTQKEKEAFQILKERFGNQFVGNVEGNDLNAGKVDVVVADGFHGNIAMKTMEGAAKMITELIKSEVKKNIISALGALLMKPVFSSLKNKLDPKKYGGTFFIGVEGVVVKAHGNSNRTAIFNALKVAKKGVEEKLPLKIKEALLKCAE
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
B7IGQ4
A2C6X2
ATPF2_PROM3
F-type ATPase subunit b'
Prochlorococcus
MTSLLLFGAGGLFDFDATLPLMALQVVLLTFILNALFFRPVGRVVEEREVYVTTSRAEAKQKLAEAEKLELELKEQLKSARIAAQQLIQEAEKDSEQLYREALAIANADANAAREKARREIDAQRDSALTQLKGDAEKLGDLIVNRLLAAK
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). The b'-subunit is a diverged and duplicated form of b found in plants and photosynthetic bacteria.
A2C6X2
Q4KLT6
FL2D_XENLA
Wilms tumor 1-associating protein
Xenopus
MTNEEPLPKKVRLNESDFKVLPREDLLQRWKQYEAYVQALENKYTDLNSNDVTGLRESEEKLKQQQQESARRENILVMRLATKEQEMQECTNQIQHLKQVQQPSVAQLRATMVDPAINLFFIKMKAELEQTKDKLEQAQNELSAWKFTPDSQTGKKLMAKCRMLIQENQELGRQLSQGRIAQLEAELALQKKYSEELKSSQDELNDFIIQLDEEVEGMQSTILVLQQQLKDSRQQLSQFQQQIQISGNRTPSSEPKDEGETSGKDCGRILNGPSNGGSSLQRTHSSAGLYREGSSTEDDFSASPINEGKLSNHSQERTSRDGSSYINPLSTGYESVDSPTGSENSLTHQSNDTDSNHDSQEEKPVSGKGNRTVSSRHLQNGLDSSVNVQGSVL
Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing.
Q4KLT6
Q1GVN5
RS11_SPHAL
30S ribosomal protein S11
Sphingopyxis
MAREPQRLRRRERKNISSGVAHVNATFNNTMITITDAQGNAIAWSSAGMMGFKGSRKSTPYAAQVCAEDAGKKAAEHGVRTLEVEVKGPGAGRESALRALQAVGFHITSIRDVTPIPHNGVRPAKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
Q1GVN5
C0K3N1
TXVE_BITAR
VEGF-F
Bitis
MAAYLLAVAILFCIQGWPSGTVQGEVRPFMEVYQRSVCQPRETLVSILEEYPDKISKIFRPSCVAVLRCGGCCSDESLTCTSVGERTVELQVMQVTPKTLSSKIKVMKFREHTACECRPRSGSRVNIGKHKRSPEEGEREPSSPLTPGSL
Snake venom VEGFs that may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. This protein induces an increase in capillary permeability after intradermal injection, as well as a drastic hypotensive effect after intravenous injection. The hypotension is mediated by nitric oxide (NO), which is produced by VEGF-activated endothelium NO synthase. Also induces angiogenesis in vitro, probably through VEGF receptor (KDR/VEGFR-2) signaling.
C0K3N1
Q8DSD7
RS6_STRMU
30S ribosomal protein S6
Streptococcus
MAKYEILYIIRPNIEEEAKNALVARFDAVLTDNGATIVESKDWEKRRLAYEIQDFREGLYHVINVETEDAHALNEFDRLSKINNDILRHMIVKLDA
Binds together with S18 to 16S ribosomal RNA.
Q8DSD7
C3P8M5
LEPA_BACAA
Ribosomal back-translocase LepA
Bacillus cereus group
MNKEERAKRQSKIRNFSIIAHIDHGKSTLADRILEKTNALTQREMKAQLLDSMDLERERGITIKLNAIQLNYKAKDGEEYILHLIDTPGHVDFTYEVSRSLAACEGAILVVDAAQGIEAQTLANVYLALDNNLEILPVINKIDLPSADPERVRQEVEDVIGLDASEAVLASAKAGIGIEEILEQIVEKVPAPTGDSEEPLQCMIFDSLYDPYRGVIAYIRVVNGTVKVGDKVRMMATGKEFEVTEVGVFTPKTTQRDELTVGDVGFLAASIKNVGDTRVGDTITHAKRPAAEPLAGYRKLNPMVFCGLYPIDSARYNDLRDALEKLELNDSALEFEPETSQALGFGFRCGFLGLLHMEILQERIEREFKIDLITTAPSVIYKVFLTNGEDMIVDNPSNMPDPQTIDRVEEPFVKAAIMVPNDYVGAVMEICQGKRGTFIDMQYLDETRVTLTYEIPLSEIVYDFFDQLKSNTKGYASFDYELIGYKPSKLVKMDILLNSEQVDALSFIVHRDSAYDRGKVIVEKLKELIPRQQFEVPIQATIGNKVVARSTIKAMRKNVLAKCYGGDISRKRKLLDKQKEGKKRMKSVGSVEVPQEAFMAVLKMDDN
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
C3P8M5
O35652
LHX8_MOUSE
LIM/homeobox protein Lhx7
Mus
MYWKSDQMFVCKLEGKEVPELAVPREKCPGLMSEECGRPAALAAGRTRKGAGEEGLVNPEGAGDEDSCSSSAPLSPSSSPQSMASGSVCPPGKCVCSSCGLEIVDKYLLKVNDLCWHVRCLSCSVCRTSLGRHTSCYIKDKDIFCKLDYFRRYGTRCSRCGRHIHSTDWVRRAKGNVYHLACFACFSCKRQLSTGEEFALVEEKVLCRVHFDCMLDNLKREVENGNGISVEGALLTEQDVNHPKPAKRARTSFTADQLQVMQAQFAQDNNPDAQTLQKLAERTGLSRRVIQVWFQNCRARHKKHVSPNHSSSAPVTAVPSSRLSPPMLEEMAYSAYVPQDGTMLTALHSYMDAHQQLLDSSPCYPIQ
Transcription factor involved in differentiation of certain neurons and mesenchymal cells.
O35652
B4U741
EFG_HYDS0
Elongation factor G
unclassified Hydrogenobaculum
MPRTVPIQDLRNIGIVAHIDAGKTTTTERILYYTGKTYKIGEVHEGAATMDWMPQEKERGITITAATTACYWAGKQINIIDTPGHVDFSVEVVRSMRVLDGIIFIFSAVEGVQPQSEANWRWADKFNVARIAFINKLDRLGADFYRVYDEIVKKLTIKPVAIQIPIGTEDNFVGVVDLMNMNAIIWLEETLGAKYEIRDIPEEYKAKAQEWREKMVESIAETDDTLMEKYLEGQEISTDELKQALRKATINKQLVPVLCGSSFKNKGVQPLLDAVVDYLPSPLDVPSVVGINPKTVQEETRLPEDDQPFCAYIFKVVSDPYAGQLSYFRVFSGKVQAGSYVLNSTKDKKERVGRLLLMHANTREDITEVAAGEIAAAVGVDAATGDTICDEKSPIILEKLEFPEPVISMAIEPKTKKDQEKLSQVLNKFMKEDPTFKASMDPETGQTLIHGMGELHLEIMVDRMKREYNIEVNVGKPQVAYKEAIKGKAVAEGKFIRQTGGRGQYGHVVIEVEPLERGSGFVFENAIVGGVIPKEFIPPVEEGIKEAMENGVLAGYPVVDVKVKLFDGSYHEVDSSEIAFKIAGSMAFKEAAKKASVVLLEPIMEVEVETPDDYVGDVIGDLNSRRGKIMGMENKGIITSIKAHVPLSEMFGYATNLRSLTQGRGTFIMKFSHYSEAPQSITEKVVGERTHT
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
B4U741
B9DN91
RS4_STACT
30S ribosomal protein S4
Staphylococcus
MARFRGSNWKKSRRLGISLSGTGKELEKRPYAPGQHGPNQRKKLSEYAIQLREKQKLRYLYGITERQFHNTFIEAGKQSGVHGENFMRLLARRLDAVVYALGLARTRRQARQLVGHGHIEVDGKRVNIPSYTLKPGQVVSVREKSQKLDIIQESVEINNFVPEYLDFDEEKLSGTFVRVPERSELPAEINEQLIVEYYSGK
With S5 and S12 plays an important role in translational accuracy.
B9DN91
A4X491
GATB_SALTO
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Salinispora
MTTTLPAYDEVVARYEPVIGLETHVELGTNTKMFCGCPTDFGGAPNTRVCPVCLGLPGSLPVANRAAVEATIRIGLALNCSIAEWCRFARKNYYYPDMPKNYQISQYDEPLCVDGYLDVEVDGEPVRISIERVHMEEDTGKTLHVGGATGRIHGATESLVDYNRAGIPLVEIVTKPIPGAGAMAPEVARAYVTELRDVLRSLGVSDVRMEEGSLRCDVNTSLNLPGEQWGTRTETKNVNSLRSVERAVRSEMIRQASVLEGGGRITQETRHFHEDTGDTTSGRSKETATDYRYFPEPDLVPVAPDPTWVAELKAALPELPRLHRRRLQQEWGLSDLDMQSILNAGAVELIEATIAAGATPTAARKWWLGELSRRANEAGVELADIGATPEQVAELQGLVDAGKLTDKLARTVLEHVVAGEGSPAKIMADRNLEVVSDTGALTAAVDEAIAANPAIADKVRGGKVAAAGALVGAVMKTTRGQADAKTVRELILERLGVQG
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
A4X491
B4SBU6
RS10_PELPB
30S ribosomal protein S10
Pelodictyon
MAVQQKIRIKLKSYDHSLVDKWALRIIDVVKQTDAIIFGPIPLPTKSHVYTVNRSPHVDKKSREQFSFSSHKRLIEIINPTSRTIDMLMKLELPSGVDVEIKS
Involved in the binding of tRNA to the ribosomes.
B4SBU6
B6JN80
NTPP_HELP2
Nucleotide pyrophosphatase
Helicobacter
MELILGSQSSARANLLKEHGIKFEQKALYFDEESLKTTDPREFVYLACKGKLEKAKELLANNCVIVVADSVVSVDNRMQRKAQSKREALEFLKRQNGNEIEVLTCSALISPKLEWLDLSVFRARLKAFDPSEIEKYLESGLWQESAGCVRLEDFHRPYIKSSSKNLSVGLGLNVEGLLGALKLGAKIASL
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
B6JN80
A6UC30
UREF_SINMW
Urease accessory protein UreF
Sinorhizobium
MAEHADTQALLRLVTWLSPAFPVGSFSYSGGLEQAIHQGLVTSADDLRLWCETLLERGNTWNDALLLSESYRAYGDAQRLIAVSELAEALAGSRERHMETMLLGEAFLAAAGHWPHPSLAVLGTKAAYPVSVGAVAGAHRTGLKPALAAFLNATVSNAVSVAIRCGITGQRDGVGVLARVEDTIGAVVARAAAASLEDLGGATFIAEIASLKHENLHSRLFRS
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
A6UC30
P0CW31
VPB16_MYCTU
Putative antitoxin VapB16
Mycobacterium tuberculosis complex
MALWYQAMIAKFGEQVVDAKVWAPAKRVGVHEAKTRLSELLRLVYGGQRLRLPAAASR
Putative antitoxin component of a possible type II toxin-antitoxin (TA) system. The cognate toxin is VapC16.
P0CW31
A0ZZ18
PSBK_GOSBA
Photosystem II reaction center protein K
Gossypium
MLNIFNLICICFNSALFSSSFLFAKLPEAYAFLNPIVDFMPVIPVLFFLLAFVWQAAVSFR
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
A0ZZ18
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