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2.75k
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5.51k
AlphaFoldDB
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10
P55069
CITM_BACSU
Mg(2+)/citrate complex secondary transporter
Bacillus
MLAILGFLMMLVFMALIMTKRLSVLTALVLTPIVFALIAGFGFTEVGDMMISGIQQVAPTAVMIMFAILYFGIMIDTGLFDPMVGKILSMVKGDPLKIVVGTAVLTMLVALDGDGSTTYMITTSAMLPLYLLLGIRPIILAGIAGVGMGIMNTIPWGGATPRAASALGVDPAELTGPMIPVIASGMLCMVAVAYVLGKAERKRLGVIELKQPANANEPAAAVEDEWKRPKLWWFNLLLTLSLIGCLVSGKVSLTVLFVIAFCIALIVNYPNLEHQRQRIAAHSSNVLAIGSMIFAAGVFTGILTGTKMVDEMAISLVSMIPEQMGGLIPAIVALTSGIFTFLMPNDAYFYGVLPILSETAVAYGVDKVEIARASIIGQPIHMLSPLVPSTHLLVGLVGVSIDDHQKFALKWAVLAVIVMTAIALLIGAISISV
Proton motive force-driven secondary transporter that mediates the transport of citrate complexed to Mg(2+). Cotransports at least two protons per Mg(2+)-citrate complex. Can also transport citrate in complex with Ni(2+), Mn(2+), Co(2+), and Zn(2+).
P55069
C3LQP9
PRMA_VIBCM
Ribosomal protein L11 methyltransferase
Vibrio
MPWIQIKLNATNDNAEAIGDMLMEETGAVSVTFLDAKDTPVFEPLPGETRLWGDTDVVALYEADMDTSLILQQIKASNMLAEGFAHKVEQVEDKDWEREWMDNFHPMQFGRRLWICPSWREVPDPQAVNVMLDPGLAFGTGTHPTTALCLEWLDNLDLTGKTVIDFGCGSGILAIAAIKLGAAKVIGIDIDPQALLASKDNAARNGVEDQIEVYLPKDQPEGLVADVVVANILAGPLRELSPIIKGLLKPGGQLAMSGILDTQAESVAEFYRDDLELDPIAEKSEWCRISGRKLG
Methylates ribosomal protein L11.
C3LQP9
C0HKX7
APDP_SPHSE
Apidaecin Ck P
Sphecius
NRPTYVPPPPRPPHPRL
Antimicrobial peptide active against many Gram-negative enterobacterial and plant-associated bacterial species. Not active against other bacterial species like H.pylori, P.mirabilis, B.pertussis or N.gonorrhoeae.
C0HKX7
Q03AZ5
MUTS2_LACP3
Endonuclease MutS2
Lacticaseibacillus
MNEKILKTLEYDKIQQALLGQVVTANGRQLVQAMQPLTDPVAVQQALDETADGASALRLKGGIPVPQLENIDPALKRVDIGAVLNGQELASISRVLQTVSAIDKFLTDLQDQIDFRQLYTLQESLTVLPQLSRRLKTAVDPDGTLTDEASPQLHGVREQIKSIEGEIRGKMTNYTRGAQSKYLSDPIVTIRDDRYVIPVKAEYRAKFGGVVHDQSATGQTLFIEPQAIVALNNRLREAQLAEVAEINRILAELSNELAPYTGQIKANAAVLGHFDFINAKARLAKAEKATEPLVSADNDVLLRDARHPLIDPHKVVGNDIPLGDKYQAMVITGPNTGGKTITLKTLGLLQLMGQSGLFIPADDESRIGIFDEVFADIGDEQSIEQNLSTFSAHMDNIVHILKQLSQNSLVLFDELGAGTDPQEGAALAIAILDAVGEVGAYVVATTHYPELKLYGYNTAKTINASMEFDSKTLQPTYRLLVGVPGRSNAFDISARLGLPGVIVERAKSMISSDSHELNNMISDLEKQRKAAETAYEAARRQLADAQSVHDELAAAYKKFTTERDAQLQQAKDKANTLVDKAQTKADKIIKQLRQMQLTNPGTVKENQLIAAKTALKQLHQDEPLQKNRILRREREKQALHVGDEVKVASYDQTGTLLEQFDKKHWQVQLGILKMKVPTDELKKIKSSKQSAAQRPVVKVSGGGMSGPSTTLDLRGERYDQAMADLDQYIDAALLAGYPSVTIIHGLGTGAIRNGVTQYLKRNRQVKTYGFAPQNAGGSGATIVNFK
Endonuclease that is involved in the suppression of homologous recombination and may therefore have a key role in the control of bacterial genetic diversity.
Q03AZ5
Q5JD26
THIC_THEKO
Thiamine biosynthesis protein ThiC
Thermococcus
MTQLEEARKGVVTEEMKFIAEREGIDAEKLRRNVAKGYTVIFRNVRHDWVKPVAVGAGVRVKVNANIGTSRDIVDVKAEIEKAKVAVKYGADTIMDLSTGGDLDEIRKTIMHAVDVPVGTVPIYQAAEEMLAKGKAIIEMSEEDMWRAVEKHFKDGVDYTTIHVGVTKEVVEKMKRTKRAVGMVSRGGTFLAAWILHWGEENPFYKDYDYLLELAREYDVVLSLGDGLRPGGLPDAGDELQIAELYTLGRLVRRAREAGVQTMVEGPGHVPIDQIAAQVKLAKVATDNAPFYVLGPIVTDIFPGYDHITAAIGGAIAALNGADFLCYVTPAEHLGLPDVEHVRQGVIAAKIAAHAVNLTRFEADFKKDYLMALARGKLNWARQFELSMDKERFVEIRKERPTKTEACSMCGDLCAIKLINDMLAGERK
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.
Q5JD26
Q19V59
NDHH_CHLAT
NADH-plastoquinone oxidoreductase subunit H
Chlorokybus
MTMLETKTDPMVISMGPHHPSMHGVLRLIVTLDGENVIDCEPVLGYLHRGMEKIAENRTIVQYLPYVTRWDYLATMFTEAITVNAPERLANIEVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREMIYDLFEAATGMRMMHNYFRIGGVAADLPYGWVDKCLDFCDYFLPKVDEYERLITNNPIFLKRVKDIGKISKEDAINWGLSGPMLRASGVKWDLRKVDNYECYDELDWSIQWQSDGDCLARYQVRIGEMRESIKIIQQALKAIPGGPYENLEARRLSKGRKSEWNNFEYQFIGKKPSPTFKMPKQEHYVRVEAPKGELGVFLIGDDNVFPWRWKIRAPGFINVQILPQLVQGMKLADIMTILGSIDIIMGEVDR
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Q19V59
P18287
APOE_RABIT
Apolipoprotein E
Oryctolagus
MKVWWAVLAAAILAGCRAQTEQEVEVPEQARWKAGQPWELALGRFWDYLRWVQSLSDQVQEELLSSQVTQELTMLMEETMKEVKAYKSELEEQLSPMAQEHRARLSKELQVAGALEADMEDVCNRLAQYRGEAQAMLGQSTEELARAFSSHLRKLRKRLLRDAEDLQKRMAVYGAGAREGAERGVSAVRERLGSRLERGRLRVATVGTLAGRPLRERAQAWGERLRGHLEEVGSRARDRLNEVREQVEEVRVKVEEQAPQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKLQAAMPSKAPAAAPIENQ
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apoliproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE has also a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
P18287
P0CV02
RLR31_PLAVT
Secreted RxLR effector protein 31
Plasmopara
MRHCACLFHLFLIGFLCNVYFSACTHTSSLKESDDESPRAEHWGSDGKRILRANDSEFLLTEERILLILLWSPLGR
Secreted effector that dos not suppress the host cell death induced by cell death-inducing proteins.
P0CV02
A0JX41
YBEY_ARTS2
Endoribonuclease YbeY
Arthrobacter
MSIEVNNESGVTVDEAQLVALARFVFERLYIHPQAELSILLVDEPAMEKLHLELMDEPGATDVLSVPMDELTPGTPDKPTPQGMLGDIAVCPQVAEVQARNAGHSTQDEMLLLTTHGILHLLGYDHADPEEKEEMFGLQRELLEGFTGKEAPSETMQ
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
A0JX41
Q8XYZ0
BPT_RALSO
Aspartate/glutamate leucyltransferase
Ralstonia
MSKLKELPLSALQFYATAPYACSYLEGRLARSQVATPAHLINADVYSKLVRAGFRRSGIFTYRPHCDDCHACTPCRVVVAPFVPSRAQRRAAERHQSLEALVAPLTYVEEHYQLYLLYQSVRHAGGGMDHDSRDQYEQFLLQSRVNSRLVEFREPPESESAGRLRMVSMIDVLEDGLSSVYTFYDPLERKASYGTYNVLWQIAQAQALELPYVYLGYWIEQSRKMAYKAQFQPLELLVNGEWRRFEDVAPAAARPAE
Functions in the N-end rule pathway of protein degradation where it conjugates Leu from its aminoacyl-tRNA to the N-termini of proteins containing an N-terminal aspartate or glutamate.
Q8XYZ0
B5DMC9
WUHO_DROPS
tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit wuho
Sophophora
MATIFFAEPELVIGHGRKVLFLNPGDLQIFKEIELPPDLTTCGLKTVEPVPAPGHPASSSKQQPAALKEATGSVKVEVSIQNVTYSPDRQLLALTTAGQKAVLLYKSRPENAQLLSIRPLARASSALRFCSDGSSVLVTDKTGDCYQYDCVEVDASPRLLLGHLSIVYDVLWSEDQQYIITCDRDDKIRVTNYPATFDIHSYCLGHKEFVSGLAMLTEQHIISASGDKTLRVWNYTCGKELLLHELPAPAVRMLVRQLEPEKTYEVAVLFYDYVDAIGVYRLEQTTTESWSITSTQLVRAEAGTWNICNFALTDDRIYVTGAENERLTLRVYDSRNGERASGLPEGWLKMVLDNLDVAAFMPEDLSVWFKKRFDNVSEYLERKKRRIEEQKQQKCG
Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Required during gametogenesis.
B5DMC9
Q6ZG85
NRAT1_ORYSJ
Protein NRAMP ALUMINUM TRANSPORTER 1
Oryza sativa
MEGTGEMREVGRETLHGGVVQSVSETDEYKEKTIDSEKDGQFRVQPRWRKFLAHVGPGALVAIGFLDPSNLETDMQAGADFKYELLWVILVGMVFALLIQTLAANLGVKTGRHLAELCREEYPHYVNIFLWIIAELAVISDDIPEVLGTAFAFNILLKIPVWAGVILTVFSTLLLLGVQRFGARKLEFIIAAFMFTMAACFFGELSYLRPSAGEVVKGMFVPSLQGKGAAANAIALFGAIITPYNLFLHSALVLSRKTPRSDKSIRAACRYFLIECSLAFIVAFLINVSVVVVAGSICNANNLSPADANTCGDLTLQSTPLLLRNVLGRSSSVVYAVALLASGQSTTISCTFAGQVIMQGFLDMKMKNWVRNLITRVIAIAPSLIVSIVSGPSGAGKLIILSSMILSFELPFALIPLLKFCNSSKKVGPLKESIYTVVIAWILSFALIVVNTYFLVWTYVDWLVHNNLPKYANGLISVVVFALMAAYLVAVVYLTFRKDTVATYVPVPERAQAQVEAGGTPVVDASAADEDQPAPYRKDLADASM
Metal transporter that transports the trivalent cation aluminum (Al(3+)), but does not seem to transport divalent cations such as iron (Fe(2+)), manganese (Mg(2+)) or Cadmium (Cd(2+)). Involved in Al tolerance by taking up Al in root cells, where it is detoxified by chelation with organic acid anions and sequestration into the vacuoles.
Q6ZG85
E7F9T0
MICA1_DANRE
Molecule interacting with CasL protein 1
Danio
MVNPLDSVNPSHALFEGFVQAQTCKETQQNFTELCRHLQVDPKDYKHFYSKLKDRLNYWKAKDLWQKIDKRAAHPDYDQGKACHQNKCLVLGAGPCGLRTAIELALLGAQVVVLEKRSSFTRNNVLHLWPFTIKDLLNLGAKKFYGRFCSGSIHHISIRQLQLILLKVALFLGVEVHTGVAFEGLNEPSGSAGWRANVSPKSHPVADFQFDVFISAGGGKYVPDGFKIKELRGKLAIGITANFVNRHTKQEAQVQEISGVARIYNQQFFQALQSEIGVDLENIVYYKDDTHYFVMTAKKASLLKKGVIKQDFSDADKLLAPSNVNQEALQDYAFEACDFSTEHLLPNLEFAKNHKGQADVAMFDFTCMQRAESASLVKERNGKRLLIGLVGDSLVEPFWPLGTGIARGFLGAFDAAWMVRSWGKGVQPMEVLAERESVYQLLSQTTPENTSKNYMAYSIDPSTRYPNINLSSIKPRQVKRLYEAEEQESKPNKLKKPDIKAKPRKDSMKRLEELLSWCQKNTVGYEHVKVKDLSESWRSGLALCALIHSFRPELVDMSALDEYNIIKNNKLAFDLMEKEFGITPIMRPGDMMTCGKIDQLSMVVYLTQIRNALTEKDTPAAQSNTLSLSRKRSAVAFLNTLKRNSLQRHKDRLASVKGPRQQNMKEKEEKKDVKEESLSSETSACEPCYFCKKHLYVVERESAEGKFFHRSCFNCFQCGSTLRQGGYSFHSDNGRFYCELHSLAEEEEGDEGHGGAQNHTENGSKEDKNGETTAASSPPAHLSIKRKGSYKISVDPDFDESTEFPAPDQDEPPDLEESHQPPKPSELSAENTNMENQQHNINPVPAPRGSRAPLPKPRTVHNVVHEPCNIPEEAEQIPEEPKPKPSLRKLQQSEEEKVDLLSQDSDSETRGSSSAASTSSSSKQHEEEGYWSGGTTWGKSHREQRNRPCIRRKSEPPLPLTGHSQHGKMRSKFSPWNLSSPRLQQRFSVHRVPAGQSQPDQYVSEDDNEDDEDEDEEDLQAEHYLDCEGADFEFSDSEKRNLKRMKTLERKAKMTEIQRFHKAQSIQRRLEEIEVTFKELEEKGVELERALRGETGTGDPEIIDQWIELVQEKNNLLSEESDLMVASRQLELEDKQSMLEMELRRYMEMDDSEKSPEQQKHEAEILQEMLDVVDMRDSLVAFLEEKRLKEVNDQFNSSLDAKRRSTTASQVHWE
Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and prevent repolymerization.
E7F9T0
Q8K087
CML2_MOUSE
G-protein coupled receptor 1
Mus
MEVSKEMLFEELDNYSYALDYYSQESDPEEKVYLGLVHWISLFLYALAFVLGIPGNAIVIWLMGFKWKKTVTTLWFLNLAIADFIFVLFLPLYISYVALSFHWPFGLWLCKVNSFIAQLNMFSSVFFLTVISLDRYIHLLHPGLSHRHRTLKSSLVVVILVWLLASLLGGPTLYFRDTMEVNNHIICYNNFQEHELTLMRHHVLTWVKFLFGYLFPLLTMSSCYLCLIFKMKKRNILISRKHLWMILSVVIAFLVCWTPYHLFSIWELSIHHNSSFQNVLQGGIPLSTGLAFLNSCLNPILYVLISKTFQARFRASVAEVLKRSLWEASCSGTVSEQLRSAETKSLSLLETAQ
Receptor for chemoattractant adipokine chemerin/RARRES2 suggesting a role for this receptor in the regulation of inflammation and energy homesotasis . Signals mainly via beta-arrestin pathway. Binding of RARRES2 activates weakly G proteins, calcium mobilization and MAPK1/MAPK3 (ERK1/2) phosphorylation too. Acts also as a receptor for TAFA1, mediates its effects on neuronal stem-cell proliferation and differentiation via the activation of ROCK/ERK and ROCK/STAT3 signaling pathway .
Q8K087
Q7MVQ5
SYT_PORGI
Threonyl-tRNA synthetase
Porphyromonas
MIKITFPDGNFREYEAGITGWDIAGSISPRLQQDVLAAGVNGQVWDLHRQINEDAEVKLFKWDDAEGKHAFWHSSAHLMAEALEELYPGIKFGIGPAIENGFYYDVDPGEGISIKDADLPAIEKRMQDLAARKETIIRRDIAKADALRMFGDKDDQYKVELISELADGTITTYTQGGFTDLCRGPHLPNTGYIKAIKLLSVAGAYWRGDEKRKQLTRIYGISFPKKKMLDEYLELLEEAKKRDHRKIGKELELFAFSQNVGAGLPLWLPRGTQLRLRLEDFLKQIQKHFGYQQVITPHIGNKNLYITSGHYAKYGQDSFRPINTPQEGEEFMLKPMNCPHHCEIFKITPHSYRDLPIRLAEFGTVYRYEQSGELHGLTRVRGFTQDDAHLFCRPDQLKEEFCKVMDIIFIIFKALDFKNFEAQISLRDKVNREKYIGSEENWERAERAIIEACEEKGLPAVIEYGEAAFYGPKLDFMVKDALGRRWQLGTIQVDYNLPERFDLEYTGEDNKKHRPVMIHRAPFGSMERFVAVLIEHTAGKFPLWLTPDQVVVLPVSERFNEYAHRVAKELNQRDIRVQVDDRNEKVGRKIRDNELKRIPYMLIVGENESREEEVSVRKQGEGDMGIMKITTFAELIEKEVDDMISAWRKDYQN
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
Q7MVQ5
B2A259
AROB_NATTJ
3-dehydroquinate synthase
Natranaerobius
MKNKFDTLTVETGVKSKKKYPIYIGKAILNLLDKVIPRNVSVLIVIDSRIARLHRDKITRLIEFLTESRTVNQIIIPGEEDSKSLSVSESLYEKAASLNLDRSSWFIGIGGGVVGDLTGFVAATYMRGANLLHVPTTLLAQVDSSVGGKVAINQSGYKNLVGNFYQPKAVIIDTNFLDTLPIRELRAGLAEVFKYGILCDRELFLTVKSLFEDCEPLNNVSWERYSYLIHKSCEIKADIVSQDEIDTGIRMLLNLGHTFAHALEGATSYNYFKHGEAVMWGLAMSAELSYKLNKLTYKDYQAIAELPELTKVPEVPIQVKDPNIIEELLLRDKKKTGEELTVILPTSIGSAEICKCPATALIKVILES
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
B2A259
Q4G3A6
RPOC1_EMIHU
Plastid-encoded RNA polymerase subunit beta'
Emiliania
MDRSFDYVKINLASPSRIREWGERKLPNGQVVGEITKPETINYRTLKPEMNGLFCERVFGPVNDWECHCGKYKRIRHKGIVCERCGVEIIDSKVRRHRMGFIELASSVTHVWYVKGRPSKIALILGMTVKELEQIVYFNSYVVTKANKDLNLSYQQLLSEADWLAIDYNDDFSLKENTISIGAEAIKTLLKNVDLQQSASEIRELLPFAKRFFSEKLIRRLRVINQFIASKFDPTWMILDILPVLPPDLRPMVQLDGGRFATSDLNDLYRRVINRNNRLARLQEIVAPELIIRNEKRMLQEAVDALIDNGKRGRAVVGLNNRPLKSLSDIIEGKQGRFRQNLLGKRVDYSGRSVIIVGPELKLNQCGLPSEMAIELFQPFVIHRLIYEGLVNNIKAAKSIIQKNGPLAWEILANVMEGHPILLNRAPTLHRLGIQSFEPILVSGRAIRLHPLVCPAFNADFDGDQMAVHIPLSLEAQSEARLLMLAPNNFLSPATGDAILTPSQDMVLGCFYLTANNPSQQLNKNHYFSDFEDAILAYQNSQIHLHTFIWVRCNNVDLTEDETCSQTQSGNLILTHGADIKSKQSSSQDTKTKYIRTTPGRILLNEIFQ
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q4G3A6
Q1DC95
OBG_MYXXD
GTP-binding protein Obg
Myxococcus
MKFVDEVRIFVKAGDGGNGAVSFRREKYIERGGPNGGDGGNGGSVVFVADPQLTTLLDYRYQQHHRARNGEHGMGSDCNGRAAEDMVLKVPVGTLVKDANTGELLVDLSEAGQRWVAAKGGRGGLGNMNFATSTRQTPRFAQDGTKGEELTLRLELKLLADVGLLGFPNAGKSTFISRVSRARPKVADYPFTTLVPNLGMVQYKDGLSFVMADIPGIIEGASEGVGLGHQFLRHVERCKVLIHLIDMGAEGEGRAPLHDFDVLNAELGKYSPELASKPQVVAANKLDLPDAQARLEGFTEALRERGIRVYPVSCATGEGMQPLMDSVAEVLFTGRTEKLHVEIPAKAARAGKAKTKAAEKKALARNAGAAAATKSATKKSAAAKKAVTKKAPARKAGAVAKTSAARKAGTAAAKKAPARKSGTAPVKKAAAKKAPARKSGTAPAKKSAVKKASARKSGSSGKAAAKKASAATKRAPARKSGGGRS
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q1DC95
P02851
BAR2_CHITE
Giant secretory protein I-B
Chironomus
SKHSKPSKHSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRCTCTSVGKPSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRCTCTSVGKPSKPSKHSKPSKHSKPSKHSKPSKHSKPSKHSKPEKCGSAMKRTEAAKCARKNGRFNSKRSTCNSVGKPSKPSKH
Used by the larvae to construct a supramolecular structure, the larval tube.
P02851
Q2YQA5
CHPT_BRUA2
Histidine phosphotransferase
Brucella
MSLPVTLSALDLGALLCSRICHDIISPVGAINNGLELLEEGGADEDAMALIKSSARNASARLQFARIAFGAAGSAGVQIDTGDAQNVATEYFRNEKPEFTWEGARVLLPKNKVKLLLNMLLIGNGAIPRGGSLAVRLEGSDTDPRFVITVKGRMLRVPPKFLELHSGAAPEEPIDAHSVQPYYTLLLAEEAGMKISIHATAEDIVFSAE
Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. ChpT efficiently and specifically shuttles phosphoryl groups from the CckA kinase to the receiver domains of both CtrA and CpdR. Does not bind ATP. Overexpression of chpT results in a defect in cell morphology, DNA content, and intracellular survival in human macrophages.
Q2YQA5
B0REJ6
Y1991_CLAMS
Nucleotide-binding protein CMS1991
Clavibacter
MHARMSVEIPQQDVMIVTGMSGAGRSTVGNALEDLGWYVVDNLPPQMLKPLVELAGRAGTSLPKIAAVVDVRGGDFFSELRDILHTFGTGPRLRVLFLEATDAALVRRFEQVRRPHPLQGNGTLLDGIAAERARMIEIREASDLVIDTSELNIHQLATTITEQFSGADDAGVRVTVMSFGFKYGTPADADMVADMRFLPNPFWTPELRPLTGRDKAVSDYVLGQEGAEEFVHAYARALAPVLAGYQRENKRHATIAIGCTGGKHRSVAVSEELSSLLRALPGVAVSTKHRDLGRE
Displays ATPase and GTPase activities.
B0REJ6
Q0MQE6
NDUB8_GORGO
NADH-ubiquinone oxidoreductase ASHI subunit
Gorilla
MAVARARVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPISWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Q0MQE6
P14019
DCOR_CRIGR
Ornithine decarboxylase
Cricetulus
MNSFNKDEFDCHILDEGFTAKDILDQKINEVSSDDKDAFYVADLGDVLKKHLRWLKALPVTPFYAVKCNDSRALVNTLAAITVDCASKTEIQLVQGLGVPPERVIYANPCKQVSQIKYAASNGVQMMTFDSEIELMKVARAHPKVTKLVLRIATDDSKAVCRLSVKFGATLRTSRLLLERAKELNIDVIGVSFHVGSGCTDPETFVQALSDARCVFDMGTEVGFSMYLLDIGGGFPGSEDTKLKFEEITSVINPALDKYFPPDSGVRVIAEPGRYYVASAFTLAVNIIAKKIVSKGSDDEDESSEQTFMYYVNDGVYGSFNCILYDHAHVKPLLPKRPKPDEKYYSSSIWGPTCDGLDRIVERCNLPEMHVGDWMLFENMGAYTVAAASTFNGFQRPSIYYVMSRPMWQLMKQIQNHGFPPEVEEQDVGTLPISCAQESGMDRHPAACASASINV
Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis.
P14019
Q6GP81
TM258_XENLA
Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
Xenopus
MELEAMSRYTSPVNPAVFPHLTVVLLAIGMFFTAWFFVYEVTSTKYTRDVYKELLISLVASLFMGFGVLFLLLWVGIYV
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Q6GP81
Q8S0S6
G2OX3_ORYSJ
Gibberellin 2-oxidase 3
Oryza sativa
MVVLAGPPAVDHIPLLRSPDPGDVFSGVPVVDLGSPGAARAVVDACERYGFFKVVNHGVATDTMDKAESEAVRFFSQTQPDKDRSGPAYPFGYGSKRIGFNGDMGWLEYLLLALDDASLADACTVPSCAVFRAALNEYISGVRKVAVRVMEAMSEGLGIAQADALSALVTAEGSDQVFRVNHYPPCRALQGLGCSVTGFGEHTDPQLVSVLRSNGTSGLQIALRDGQWVSVPSDRDSFFVNVGDSLQVLTNGRFKSVKHRVVANSLKSRVSFIYFGGPPLAQRIAPLPQLLGEGEQSLYKEFTWDEYKKAAYKSRLGDNRLAQFEKK
Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development . In vitro, converts GA1, GA20, and GA29 to the corresponding 2-beta-hydroxylated products GA8, GA29-catabolite, respectively .
Q8S0S6
A5D451
ENGB_PELTS
Probable GTP-binding protein EngB
Pelotomaculum
MKIKNAEFITSAAKTADYPAGNIPEVALAGRSNVGKSSLLNRLVNRKSLARISSTPGRTRLINFFLVNGLFRLVDLPGYGYAKVSARERQGWRRMVEEYLKTRENLKGVVLLVDSRHPPTVLDVQMYEWLKYQGIPAAVAATKADKISRSKRAQSLKVIREVLNLTAKEPLVFFSAETSEGREEMLEVIGRWVGLSGR
Necessary for normal cell division and for the maintenance of normal septation.
A5D451
Q80ZU9
G137A_MOUSE
Transmembrane 7 superfamily member 1-like 1 protein
Mus
MESNLSGLVPAAGLVPALPPTVTLGLTAAYTALYALLFFSVYAQLWLVLLYGHKRLSYQTVFLALCLLWAALRTTLFSFYFRDTPRANRLGPLPFWLLYCCPVCLQFFTLTLMNLYFVQVVFKAKAKRRPEMSRGLLAVRGAFVGASLLFLLVNVLCAVLSRQRQAQPWVLLLVRVLVSDSLFVICALSLAACLCLVARRAPSTSIYLEAKGTSVCQAAAIGGAMVLLYASRACYNLAALALAPRSRLDAFDYDWYNVSDQADLVNDLGNKGYLVFGLILFVWELLPTTLLVGFFRVHRPPQDLSTSRILNGQVFGSRSYFFDRAGHCEDEGCSWEHSRSESTSMSGSLGSGSWYGAIGREPGWGGASQTRTTPLLFSQVPGPGSHHHSLYSTPQT
May activate Wnt/beta-catenin signaling to modulate epithelial cell function.
Q80ZU9
B2IT24
MIAB_NOSP7
tRNA-i(6)A37 methylthiotransferase
Nostoc
MTTSKRHYHITTFGCQMNKADSERMAGVLEDMGFEWSEDPNNADVILYNTCTIRDNAEQKVYSYLGRQAKRKHDQPDLTLIVAGCVAQQEGEALLRRVPELDLVMGPQHANRLKDLLESVFDGNQVVATESVHIIEDITQPRRDSKVTAWVNVIYGCNERCTYCVVPNVRGIEQSRTPSAIRAEMEELGRQGYKEITLLGQNIDAYGRDLPGTTPEGRHLHNFTDLLYYVHDVPGIERLRFATSHPRYFTERLIKACAELPKVCKHFHIPFQSGDNELLKAMARGYTHEKYRRIIDTIRRYMPDASISADAIVGFPGETEAQFENTLKLVEDIGFDMLNTAAYSPRPGTPAALWDNQLSEEVKSDRLQRLNHLGNLKVAERSQRYFGRIEEVLVEDQNPKDQTQVMGRTDGNRLTFFSGDIKELKGQLVKVKITEVRPFSLTGQPVEVRQAIPV
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
B2IT24
A9BJ54
IF2_PETMO
Translation initiation factor IF-2
Petrotoga
MSKTRIYEVAKELGMNSKELMEFLEKELNISVKSHMSTIEEETVQVIMDLIEEERQTKKEVKKQKEPSKEKGKSSEQVKVKEKSKEEPVEEKFLREVTITSHDLSLDILAKQIGLEQNDIIKDMFMKGVVLRPGQKLDITMAENIAMNYNVILNFEIEKKETEEGKEQDIEAILAKKWNDIYEKEKDKLAPRPPVVTIMGHVDHGKTTLLDKIRNTHVADKEEGGITQSIGAYQIEYNGQKITFIDTPGHEAFTEMRARGAQVTDIVVLIIAADDGVMPQTIEAYNHAKSANVPIIVAINKIDKPNANVELTKQQMVSKLNLIPEDWGGDTITVLVSAKTGEGIDELLEMILLVSEMQEIRCIPDGKARAVIIESRVDKAMGPLGTVIVKDGILKVGDDFISGSTYGRVRRLINDKGESLIKAVPSTPVQVLGFNDVPNTHSILYVIDSKEEARTLAEKVKEKEEEKSKGPAKRHVKLEDIMQKMEEEEKKKLNILLKASTYGEIEALRNAIQKFENPEIDIEIIHAGIGPVSTSDIMLASASDAIVLGFRVKADSKALKMAEAEGIEVRRYNIIFDLIDDIKKALEGMLEPIQKEELTGNGVIKEEFKIKGVGKIAGVQVNEGYVQRDGGVRIYRNGGLIADVKIKSLKHYKDEVKSIEAPKECGIQFENFEDFTKGDELEFYKHVFVKRELGLEQKTK
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
A9BJ54
A5A6M2
ANXA1_PANTR
Annexin Ac2-26
Pan
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTRRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2.
A5A6M2
A7Z8Y2
GPMI_BACVZ
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Bacillus amyloliquefaciens group
MSKKPAALIILDGFGLRNETVGNAVAQAKKPNFDRYWNQYPHQTLTASGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVNVAIREGEFERNQTFLDAIKNAKDNDKALHLFGLLSDGGVHSHINHLFALLKLAKSEGLTKVYIHGFLDGRDVGPQTAKTYIQQLNEQVEEIGVGEIASISGRYYSMDRDKRWDRVEKAYRAMAYGEGPSYRSAMDVVDDSYANGIHDEFVIPSVITKENGEPVAKIHDGDSVIFYNFRPDRAIQISNTFTNKDFRDFDRGENHPKNLYFVCLTHFSESVDGYVAFKPVNLDNTVGEVLAQHGLKQLRIAETEKYPHVTFFMSGGREEEFPGEERILINSPKVATYDLKPEMSAYEVKDALVKEIAADKHDAIILNFANPDMVGHSGMVEPTIKAIEAVDECLGEVVDAIIAKGGHAIITADHGNADILITETGEPHTAHTTNPVPVIVTKEGVTLREGGILGDLAPTLLDLLGVEKPKEMTGTSLIQK
Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
A7Z8Y2
Q82V20
OBG_NITEU
GTP-binding protein Obg
Nitrosomonas
MKFIDEVKIQISAGDGGNGVASFRREKFIPRGGPDGGDGGHGGSIYALADHNLNTLIDYRFTPVFRAKRGENGRGSDCYGKGAEDIVLRMPVGTIITNDLTGELVADLEHDQQKVLLAKGGRGGLGNLHFKSSTNRAPRQFTHGEAGEQFELRLELRVLADVGLLGLPNAGKSTLIRAVSAARPKVADYPFTTLYPNLGVVRVDAGHSFVMADIPGLIEGAAEGAGLGHRFLKHLGRTRLLLHVIDVAPFDENVDIVHSARALVDELRKFDETLYRKPRWLVFNKVDMLPEDEQQAVCTRLLQAMNWQERWFAISALTGRGCQALIYAIMGHLQQLQSDSEET
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
Q82V20
Q0AC01
LOLB_ALKEH
Outer-membrane lipoprotein LolB
Alkalilimnicola
MRRGRLLIAGLAALVLSACATLPEPVDDPKARYQEAVERLRAQTDWDASGRAALRTADDAGSLSLEWRQRGETYQVDLRAPLGAGSARLEGGPEGVWLTTSAGDREYAPDPETLVAWFTGYQVPVSALRYWLRGLDAPGPEVERLDLDPAGRPERLHQAGWEVVYRDWSQTNGLPLPRRLDISRGEDSVRVVIRDWSLAP
Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein.
Q0AC01
O95169
NDUB8_HUMAN
NADH-ubiquinone oxidoreductase ASHI subunit
Homo
MAVARAGVLGVQWLQRASRNVMPLGARTASHMTKDMFPGPYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPKLPDRSQHERDPWYSWDQPGLRLNWGEPMHWHLDMYNRNRVDTSPTPVSWHVMCMQLFGFLAFMIFMCWVGDVYPVYQPVGPKQYPYNNLYLERGGDPSKEPERVVHYEI
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
O95169
Q3Z888
ILVD_DEHM1
Dihydroxy-acid dehydratase
Dehalococcoides
MKSEDVKLGIERAPHRSLLRALGLNTESFQKPFIGIVNSFTEVVPGHIHLRRISEAVKEGINAAGGVGFEFNTIAVCDGIAMNHAGMKYSLPSREIIANTVEIMAMAHAFDGLVFIPNCDKVVPGMLMAACRLNIPSIFVSGGPMLAGRLRKNDQVSCVDLNSVFEAVGQVAKGQMTEEELLELEKVACPGCGSCAGMFTANTMNCLTEALGMALPGNGTIPAVDSRRTQLAKDTGRQILKLIKDNTCPKDIITPDAIYNAFSLDVALGGSTNSVLHVMAVAHEAGADFSLEEINRVSDTTPNLCKLRPSGPYHIENLDQAGGIGSVLKELKPWLKNDARTVSGKTIGQMADAAPKADNKVIRFASNPYSPKGGLAILFGNLAPSGSVVKRSAVAPEMMVHRGPARIFDSEELATKAIMGGKIIPGDVLVIRYEGPKGGPGMREMLTPTSLLAGMGLDKEVALITDGRFSGATRGAAMGHVSPEAAARGPIAALQDGDMINIDIHNYKLSVELSDEEIQKRLANVPAFKPKITSGYLKYYTENVTSASTGAVFKD
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.
Q3Z888
B1YLS1
TRPD_EXIS2
Anthranilate phosphoribosyltransferase
Exiguobacterium
MKDVLTKLANANHLRFEEMQQAARELFAEDVTDSEIAAFLIALKAKGETAEELAGLASIMREVAVDIPVSGTDFIDNCGTGGDGSQSFNISTTAAFVLAGAGAKVAKHGNRSVSSKTGSADVLESLGVPLDVSTEEIATLLETNGIAFLFAQRMHPRVKQIMKVRRDLRIPTIFNLIGPLTNPVPLKTQLLGIYREDLLETIALTLHRLGRKRAIVLHGACGMDEASLAGTNQLVLLDQGELIRFSLHPEEVGLSVAPIEAIRGGTAAENAEILLRVLRGEAGPYRDTVLLNAGIALFAEGRVETIREGIERSAESIDSGRALEKLQYLQRMKQQEAIG
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
B1YLS1
A5CW26
RL7_VESOH
50S ribosomal protein L7/L12
Candidatus Vesicomyosocius
MAKLTNEDILNAIADMSVIDVVELVSAMEEKFGVSATAVTPVAVVADVDNTVVEKDEFDIMLTSFGEKKVAVIKAVRSITGLGLKESKDMVESAPVVIKESASKIEAEDIERQLKEVGASVELK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
A5CW26
C5BD00
RECR_EDWI9
Recombination protein RecR
Edwardsiella
MQTSPLLESLMEALRCLPGVGPKSAQRMAFHLLQRDRSGGMRLAQALTRAMSEIGHCRDCRTFTEQEVCTICTNARRRENGQICVVESPADIHAIEQTGQYSGRYFVLMGHLSPLDGIGPQDIGLDRLEVRLSQEAVSEVILATNPTVEGEATANYIAEMCAAHGVLASRIAHGVPVGGELEMVDGTTLSHSLAGRHPVTR
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.
C5BD00
Q7VKY2
DSBB_HAEDU
Disulfide oxidoreductase
Haemophilus
MLSYFKELSLRRPAWLLLATLACTLEVTGLYFQHKLGLIPCVMCIYERVALTGLLIAGLIALIAPNFFLFRWLALVLWGFSAFKGLSLSIKHYDYQANPSPWNQCEFKPQFPQTIPLDEWFPNIFAAGTVNCSEKQWQMLGWGMPEWLIVAFSLFMLFFLIVFMSQFKRAKPQYRSVFR
Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein.
Q7VKY2
B5RQN4
TPIS_BORRA
Triose-phosphate isomerase
Borrelia
MRKVFLAGNWKMHYTSVEAADVAKQIVDGVYNINNNVVVMVTPTFTSLCKVCRVTKGTNVLLGAQNMSYENSGARTSEIAPSMLLEFGVDYVILGHSECRTYLGENDEIINKKVLTGLKHPFKYLILCVGETLEEREKGKTLDVVLNQVRNGLASVYESDLQRIILAYEPVWAIGTGKTATKEEAQEVHKAIRLEIQSLYSKSAADNIIIQYGGSVNVDNVEGLMGENDIDGALIGGSSLKADSFLKIINKISK
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
B5RQN4
B1Y9M9
PELO_PYRNV
Protein pelota homolog
Pyrobaculum
MKYEIDAKRRTVRVVPEREEDLYFVYLLVERGDVVRGWTVREYKPEGAKEGERVKMYLAVRVESLEYHKFRGSLRIRGPVVEVQEGVEGVKGRRHTFDVVPGREIEIEKAAEFPLDVVEEILKMAQALMPKVLLVSIDDEEAAFAYITALGVELIQVVHNASKGEESLFDGYLESVRKQVDELSRRLKPDKLVVAGPAMLVEHIARYIRGDKAPQGSGGLAGVYEFIRSGLYDELKTQMGVKAYEKLIHMAATSRESVAIGPQEVEEAASLGRVDFVLVLDSYIKESPEKAWVLLSQIYKTKGRIYIVREDTEVGAGIRAMGGIAAVLRW
May function in recognizing stalled ribosomes, interact with stem-loop structures in stalled mRNA molecules, and effect endonucleolytic cleavage of the mRNA. May play a role in the release non-functional ribosomes and degradation of damaged mRNAs. Has endoribonuclease activity.
B1Y9M9
Q14K49
GATA_FRAT1
Glutamyl-tRNA(Gln) amidotransferase subunit A
Francisella
MSYIKKLRARLDSGEISAVELTKEYLAKIKEQDKRINSVITLCEAEALKEAEDADAIISAGKQGLLTGIPILHKDLFCTKGIRTTAASKMLDNFVAPYDSTVTKNCKDQGMVTLGKLNMDEFAMGSTNEYSYYGAVSNPWDLERVPGGSSGGSAAAVAAGFAPISTGSDTGGSVRQPASFCGLTAMKPSYGSTSRFGMVAFASSFDQAGVLGHYAEDVAIMLDAIAGECEFDSTCVGVKQNHFTQDLEKDISGKVIGVDESLIKDLPAQIQEAVSKTLDNFKKLGAEIKSVKVPDLKEALSTYYIITPAEAAANLARYDGIRYGYRNPEARDLDELYRKSRTDGFGAEVKRRIMIGNYVLASSQYDSYYNKAQQLRKVMTDQINQIFTQVDAIFMPASPSEAFKKGDKLDPVSAYLSDIYTIPANISGLPAIAFPIGFANNLPVGGQLMAKAFNDNILTQMVVQYQKHYGIEEFILQQARI
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Q14K49
Q3S8P6
OXYT_STRRM
SAM-dependent methyltransferase
Streptomyces
MTTTPLAPVAQARSLLQLTTAYHQAKALHSAVELGLFDLLADGPATAEEVKDRLRIVHPLAKEFLDALVALELLEADGDRYRNSPAAQAFLVSGASEYLGGTVLQHARKHYHVWAGLTTALQEGEAGSGAEAHGPEAYPKHYEDPERARQVMAHFDTFSSFTAEELARRVDWSGYGSFIDIGGARGNLATRVALAHPHLHGAVFDLPALAPLAGELIRERGLEGRVRFHGGDFLTDPLPSADAVVTGHVLPDWPVPQRRKLLARIHEALPSGGALVVYDLMTDPATTTVHDVLQRLNHGLIRGDSSSSSVEEYRAEIEEAGFRVRQAERIDNLLGDWLIVAVKP
Involved in the biosynthesis of the tetracycline antibiotic, oxytetracycline. Catalyzes the dimethylation of 4-amino-4-de(dimethylamino)anhydrotetracycline (4-amino-ATC) to yield anhydrotetracycline (ATC) . Also able to catalyze the dimethylation of 7-chloro-, 6-demethyl-, 2-decarboxamido-2-nitrile-, and 4-methylamino-derivatives of 4-amino-4-de(dimethylamino)anhydrotetracycline .
Q3S8P6
B8B8I3
ALFL2_ORYSI
PHD finger protein ALFIN-LIKE 2
Oryza sativa
MEMAAPVSPAPRTVEDIFKDFSGRRAGLVRALTVDVDEFYGFCDPEKENLCLYGHPNGRWEVALPAEEVPPELPEPALGINFARDGMHRRDWLSLVAVHSDSWLLSVAFFFGARLNGNERKRLFSLINDHPTVLEALSDRKHGRDNKSGADNGSKSRHSGKRANDVQTKTSRPAVVDDGYDEEEHSETLCGTCGGRYNANEFWIGCDICERWFHGKCVRITPAKAEHIKHYKCPDCSSSKKSRQ
Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
B8B8I3
Q758W7
RAD17_ASHGO
DNA damage checkpoint control protein RAD17
Eremothecium
MLESTALFSATTIHLDRLMCAFNCMTPFGQRDDVLITIDRDGLTFIRQNNHAAEIQLFLAKELFQYYSIREGFEGEIQLCMKLNHLLDTVSVANRDKDDVVECTLSYDGEGTPFMLILEDSMITEQVEYATYLVGEMDRTGLELDRARLEFECILKGDVLYSALRDLREIGCKECYLYIVTSSRARPMFALVSRGQLGLSKIILPSERSVLEKLEVYENDSTTLIHDAPVIGLFDFAALDKLRPSTKIASKVLIRKDVHGLLAVNILSDTNAILVPEKRELIRASRSVSAEYPTVVIEVFLLEKASVGDIDVRDVHQLMLTSPAHRRSGFADSGSRIVSVTPTATSAAHTGAGSLLGLAPPSAFPAEETQDPDESYHPAPSNTDIPLFL
Component of the checkpoint clamp complex involved in the surveillance mechanism that allows the DNA repair pathways to act to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes.
Q758W7
B3DP37
ISPE_BIFLD
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
Bifidobacterium
MSPVISHPRSAAARHQSDELSPITITVDCPAKTNLTLEVGPAHDEWGGRHELDTTYCAIGVYDTVTATAKQPGAGFSLELEGAYLGDLASSRSDMRRNHAVLALFAMAQAAEREPDVALTITKRIPVGAGLGGGSADAAATMLAVNRLWELNWPIERLRTIAATLGADMPFCLTGGLAYGTGFGERITDIAPGSRDELALIEQGFSGEVLVGAYQSQLSTPEVYHTFDIVGAAEGDRNHLQAAAISLHPRSGQAIDAATQAGASHAFVSGSGPSVVAFAADEAAAQRIIEVWRDTAVVDRIIRAKSPEHPNISVRQ
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
B3DP37
Q6YQV1
RNY_ONYPE
Ribonuclease Y
Candidatus Phytoplasma asteris
MKGDYWRTHCIMDCSLLVFALICGSIIGYFLYSFFNQKKLEEKKQAFDDKLKEKEKDLQQREQEMMRNAKIEITSLRQKLELDLEQRTNTIVDLESKNNRREELFNNRTESLNKREEHLDSEQQIISHTKKNLEQQIKEQETILNTQKQQLEKIASLTQDQARQIIMKETRDQTTYEMMSYIKQEEEKAKSEASKKAKTLLVLAMQKYAGDITGEKNISVVNIPNEDMKGRIIGRQGRNIKSLEVLTGVDLIIDESPCTIILSSFDPIRREIAKKTLEFLVSDGRIHPSRIEKALETSTIEVDNFIKEMGEEAAFITKIGEVHPDLIKILGKLHFRISYSQNVLKHSLEVAFLAGKLASEIGENEILARRAGLFHDIGKALDHEMEGSHVEIGVFIASKYKEKKEVIDAIASHHEDQEPQSIIAVLVAIADTLSSARPGARKESVENYIQRLTKLETIANATEGVAKSYAIQAGREIRVIVEPDKIADNFIFQTARTIKEQIEKDISYNGVIKVTVIRETRAVEMAKL
Endoribonuclease that initiates mRNA decay.
Q6YQV1
Q8E2K7
RECF_STRA3
DNA replication and repair protein RecF
Streptococcus
MWIKNISLKHYRNYEEAQVDFSPNLNIFIGRNAQGKTNFLEAIYFLALTRSHRTRSDKELVHFKHHDVQITGEVIRKSGHLNLDIQLSEKGRITKVNHLKQAKLSDYIGAMTVVLFAPEDLQLVKGAPSLRRKFLDIDIGQIKPTYLAELSNYNHVLKQRNTYLKTTNNVDKTFLTVLDEQLADYGSRVIEHRFDFIQALNDEADKHHYIISTELEHLSIHYKSSIEFTDKSSIREHFLNQLSKSHSRDIFKKNTSIGPHRDDITFFINDINATFASQGQQRSLILSLKLAEIELIKTVTNDYPILLLDDVMSELDNHRQLKLLEGIKENVQTFITTTSLEHLSALPDQLKIFNVSDGTISINEKKATD
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
Q8E2K7
P0C5H5
GAOX2_ORYSI
Protein semidwarf-1
Oryza sativa
MVAEHPTPPQPHQPPPMDSTAGSGIAAPAAAAVCDLRMEPKIPEPFVWPNGDARPASAAELDMPVVDVGVLRDGDAEGLRRAAAQVAAACATHGFFQVSEHGVDAALARAALDGASDFFRLPLAEKRRARRVPGTVSGYTSAHADRFASKLPWKETLSFGFHDRAAAPVVADYFSSTLGPDFAPMGRVYQKYCEEMKELSLTIMELLELSLGVERGYYREFFADSSSIMRCNYYPPCPEPERTLGTGPHCDPTALTILLQDDVGGLEVLVDGEWRPVSPVPGAMVINIGDTFMALSNGRYKSCLHRAVVNQRRERRSLAFFLCPREDRVVRPPPSAATPQHYPDFTWADLMRFTQRHYRADTRTLDAFTRWLAPPAADAAATAQVEAAS
Key oxidase enzyme in the biosynthesis of gibberellin that catalyzes the conversion of GA53 to GA20 via a three-step oxidation at C-20 of the GA skeleton.
P0C5H5
B7N2G7
YIHI_ECO81
Der GTPase-activating protein YihI
Escherichia
MKPSSSNSRSKGHAKARRKTREELDQEARDRKRQKKRRGHAPGSRAAGGNTTSGSKGQNAPKDPRIGSKTPIPLGVAEKVTKQHKPKSEKPMLSPQAELELLETDERLDALLERLEAGETLSAEEQSWVDVKLDRIDELMQKLGLSYDDDEEEEEDEKQEDMMRLLRGN
A GTPase-activating protein (GAP) that modifies Der/EngA GTPase function. May play a role in ribosome biogenesis.
B7N2G7
O22886
DCUP2_ARATH
Uroporphyrinogen decarboxylase 2, chloroplastic
Arabidopsis
MSILQVSTSSLSSSTLLSISPRKSLSSTKSCRIVRCSVEGTTVTERKVSATSEPLLLRAVKGEVVDRPPVWLMRQAGRYMKSYQTLCEKYPSFRDRSENADLVVEISLQPWKVFKPDGVILFSDILTPLSGMNIPFDIVKGKGPIIFNPPQSAADVAQVREFVPEESVPYVGEALRRLRNEVNNEAAVLGFVGAPFTLSSYVIEGGSSKNFTQIKRLAFSQPKVLHALLQKFTTSMITYIRYQADSGAQAVQIFDSWATELSPVDFEEFSLPYLKQIVEAVKQTHPNLPLILYASGSGGLLERLARTGVDVVSLDWTVDMAEGRDRLGRDIAVQGNVDPGVLFGSKEFITSRIHDTVKKAGRDKHILNLGHGIKVGTPEENVAHFFEVAQEIRY
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
O22886
B2B674
SLX1_PODAN
Structure-specific endonuclease subunit SLX1
Podospora anserina
MTPQPRPIPALYCVYILRSTVRHSSLYIGSTPNPPRRLSQHNGVVKGGAVRTSRNSLRPWEMVALVSGFASSTAALKFEWALTNPHTSLHIPSESRLAFSTQRKRNGQPKRPPKSLSSILSNLHLLLSVPSFARWPLRVHFFKRDVHAAWGRWCGKVERELRGSLPVVTDFGEDEGAVVARASASEPLGVVGEGLDGDGGGEEVPTWGIYGLPLDYAPLKEYVAKGQDIFEFERQGSCVVCKEEIDPEEGGLHAVCSNEGCEGVGHLRCWGRYLLKSEEGGGEGAILPVGGRCPRCKGEVHWGTMMKELTLRVRGQKEVENLLKVKRKRAPRKKTAKTKETREEDG
Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
B2B674
Q8VYZ5
PWP2_ARATH
Periodic tryptophan protein 2
Arabidopsis
MEFRFENLLGAPYRGGNAVITKNTQLISPVGNRVSVTDLSKNHSVTLPLETSTNICRLASSPDGTFLLAVDEQNRCLFINLPRRVVLHRITFKDKVGALKFSPNGKFIAVGIGKLVEIWRSPGFRRAVLPFERVRTFANSDDKVVSLEWSLDSDYLLVGSRDLAARLFCVRKLKGVLNKPFLFLGHRDSVVGCFFGVDKMTNKVNRAFTIARDGYIFSWGYTEKDVKMDESEDGHSEPPSPVTPDRADEVMVENGGGVGTELKKRKEYDGKGLESDEEGDDDDEEYMHRGKWVLLRKDGCNQASAKVTACDYHQGLDMVVVGFSNGVFGLYQMPDFICIHLLSISRQKLTTAVFNERGNWLTFGCAKLGQLLVWDWRTETYILKQQGHYFDVNCVTYSPDSQLLATGADDNKVKVWNVMSGTCFITFTEHTNAVTALHFMADNHSLLSASLDGTVRAWDFKRYKNYKTYTTPTPRQFVSLTADPSGDVVCAGTLDSFEIFVWSKKTGQIKDILSGHEAPVHGLMFSPLTQLLASSSWDYTVRLWDVFASKGTVETFRHNHDVLTVAFRPDGKQLASSTLDGQINFWDTIEGVLMYTIEGRRDIAGGRVMTDRRSAANSSSGKCFTTLCYSADGGYILAAGTSRYICMYDIADQVLLRRFQISHNLSLDGVLDFLHSKKMTEAGPIDLIDDDNSDEEGGIDKQSRGNLGYDLPGSRPNRGRPIIRTKSLSIAPTGRSFAAATTEGVLIFSIDDTFIFDPTDLDIDVTPEAVEAAIEEDEVSRALALSMRLNEDSLIKKCIFAVAPADIKAVAISVRQKYLERLMEALVDLLENCPHLEFILHWCQEICKAHGSSIQRNYRTLLPALRSLQKAITRAHQDLADMCSSNEYTLRYLCSVPNNH
Involved in nucleolar processing of pre-18S ribosomal RNA. Plays a role early in ribosome biogenesis, especially in the maturation of 5.8S rRNA . Required for guard cell functions .
Q8VYZ5
Q1WSR2
NADE_LIGS1
NH(3)-dependent NAD(+) synthetase
Ligilactobacillus
MRPLQERIINELKVKPEINAEEEIRRSVDFLKDYLKKHPFLKALVLGISGGQDSTLAGKLSQMAISELREETGDDAYQFIAVRLPYGDQADEQDAMDAIEFMQADKTVRVNIKQAADAMVQSIEENGLEISDFNKGNIKARERMIAQYGIAGAVSGAVVGTDHAAEAITGFYTKYGDGGADITPLWRLDKRQGRAMLELLNAPEHLYKKVPTADLEEDRPALPDEVALGVTYNDIDDYLEGKEVADNVAEKIENWFLKTEHKRHMPINVYDTFWK
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Q1WSR2
Q06GQ0
PSAI_PIPCE
Photosystem I reaction center subunit VIII
Piper
MTDFSLPSILVPLVGLVLPAIAMASLSLHVQKNKIV
May help in the organization of the PsaL subunit.
Q06GQ0
B0RMB4
ILVD_XANCB
Dihydroxy-acid dehydratase
Xanthomonas
MPEYRSKTSTHGRNMAGARALWRATGMKDGDFHKPIIAIANSFTQFVPGHVHLKDLGQLVAREIERVGGVAKEFDTIAVDDGIAMGHDGMLYSLPSREIIADSVEYMVNAHCADALVCISNCDKITPGMLMAALRLNIPTVFVSGGPMEAGKTKLADHNLDLIDAMVIAADDSASDEKVAEFERSACPTCGSCSGMFTANSMNCLTEALGLSLPGNGTVVATHADREQLFLRAGRVAVELCHRWYGGEDPTALPRGIATFEAFENAMTLDIAMGGSTNTILHLLAAAQEGEVPFGMRDIDRLSKRVPQLCKVAPNTPKYHIEDVHRAGGIMSILGELARGGLLHTNAATVHTRTLADAIAQWDVTQVDDDKVHTFYKAGPAGIPTQIAFSQATRWDTLDTDRSEGCIRDVAHAFSQEGGLAVLYGNIARDGCVVKTAGVDESIHVFEGNARVYESQDSAVKGILADEVKAGDVVVIRYEGPKGGPGMQEMLYPTSYLKSKGLGKHCALLTDGRFSGGTSGLSIGHASPEAAAGGAIGLVRNGDKILIDIPKRSIDLLVSDEELAARRTEQDAKGWKPVEVRPRKVTTALKAYALLATSADKGAVRDKAMLDG
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.
B0RMB4
P25670
3L21_ASPSC
Toxin S4C6
Aspidelaps
RICYIAPYDHKTCAAGENICYLKAWCDAWCSSRGKKLEFGCAATCPTVKPGVDISCCDTDNCNPHPKL
Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.
P25670
Q2A1V2
COAX2_FRATH
Pantothenic acid kinase 2
Francisella
MLLVMDMGNSHIHIGVFDGDIIVSQIRYATSSVDSTSDQMGVFLRQALRENSVDLGKIDGYGISSVVPHLNYSLGSAVIKYFNIKPFFISMDTTDLDMSAVEAHQVGADRIASCISAIADHPNKDLLIIDLGTATTFDLVTKDKKYLSGSIMPGVKLSLNALCQGASQLSSVTIVKPEVAIGYDTKTNIRSGLYYGHLGALRRSVEEFGSPVYTIATGGFAGLFKEEDIFNEISPDLILRGIRIAFLENNKKGV
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Q2A1V2
A4WCS0
5DNU_ENT38
Nucleoside 5'-monophosphate phosphohydrolase
Enterobacter
MSQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFNGNVNAERIALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAALIDEHQCSEEERLLVKQADALCAYLKCLEELSAGNNEFLLAKSRLEKTLESRRSEEMDYFMQVFVPSFQLSLDEISQDSPL
Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates.
A4WCS0
P24856
ANP_NOTNE
AFGP8-like
Notothenia
VTAAPAATAATAATPATAALNFAATAATPATPATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAAAAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAACNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATPAFNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALHFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAAFNFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATPAFHFAATAATPATAATPALIFAATAATAATPATAALNFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAALNFAATAATPATAATPALIFAATAATAATPATAAFNFAATAATAATPATAATPALIFAATAATAATPATPATPALIFAATAATAATPATPALNFAATAATAATTAARG
Antifreeze proteins lower the blood freezing point.
P24856
A2RKS3
HIS1_LACLM
ATP phosphoribosyltransferase
Lactococcus cremoris subsp. cremoris
MIRVAMTKGRIQKQVTILLEQAGFDMTAVREMGRELVVTIPDDLEIIFGKANDVITFLEHGIVDIGFVGKDTLDENDFDDYYELLDLKVGQCIFALASYPDFLNKKFHRRKRIASKYPRITKNYFAQKQEDIEIIKLEGSVELGPVVGLADAIVDIVETGNTLSANGLVVIEKISQISTRMIVNKVSFKFKKDKIIEIVERLENAQTN
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
A2RKS3
P40513
MAM33_YEAST
Mitochondrial acidic protein MAM33
Saccharomyces
MFLRSVNRAVTRSILTTPKPAVVKSSWRVFTVANSKRCFTPAAIMRNQETQRVGDILQSELKIEKETLPESTSLDSFNDFLNKYKFSLVETPGKNEAEIVRRTESGETVHVFFDVAQIANLPYNNAMDENTEQNEDGINEDDFDALSDNFANVNVVISKESASEPAVSFELLMNLQEGSFYVDSATPYPSVDAALNQSAEAEITRELVYHGPPFSNLDEELQESLEAYLESRGVNEELASFISAYSEFKENNEYISWLEKMKKFFH
Not known. Binds to the sorting sequence of cytochrome b2.
P40513
Q89AE4
SRP54_BUCBP
Fifty-four homolog
Buchnera
MFNNLTQRFLKIIKKISNKGRLTEKNIKETLREIRIALLEADVALPVVKNFIPSIQKSVIGNQVNKSLTPGQELIKIVKKELTLILGKENHSLNLSVTPPAIILMIGLQGSGKTTTTAKLGQLIRTKYKKKVIVTSIDIYRLAAIKQLKMLSKQAKISFFPSNNTQSPKDIVQHAIQHAKLKFYDVLLIDTAGRLQIDKKMMNELLDVYNISHPIETFFVADAMFGQDSINVINEFNKYLPVSSFIITKTDSDTRAGIILSIKYLTKKPIKFIGTGEKLEELELFYPDRIASRILGMGDMLSLIENIENKIDKKHIKKFSNTIKKYNTFNFNDMLLHINQIKKIGGVNSILGKLPKTQTIFNSFQNNIDENILLKMKTIINSMTISERHQPELIKGSRKRRISLGSGIPIPEINQLLKQFNNIKKIMKTIKKGGVTKIMQGINNIIKNKF
Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY. Interaction with FtsY leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components.
Q89AE4
B4RC51
RBFA_PHEZH
Ribosome-binding factor A
Phenylobacterium
MKRPSSHGRRPPQGPSQRQLRAGELVRHALVEIFREEEINDPVLAGVSVTVTEVRVSPDLRHATVFVEPLGGEHADEVVQALNRHARFLRGHLGRAIELRFTPELKFLHDESFNEAARMAKLFDDPKVRQDLTPQPPSDSWKDED
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
B4RC51
A9BHW9
MIAA_PETMO
Isopentenyl-diphosphate:tRNA isopentenyltransferase
Petrotoga
MNKVLVIAGPTAVGKTEISIEIARRINGEIICMDSRQIYSHLIIGTATPDEETKKLVPHHLYGSVDPRTHFTAFDYKKLAEKKIGEVLNRGNTPVLVGGTGLYLDALRKGFLNVKSDYGLRTYLRKLETNNPGVLRKILVDLDPQRAQKIHPNDLKRIIRAIEIYVITGIKMGEIVKENRQDENSFDYHIIVLDRERQELHERINKRVHQMIDEGLIEEVRNLLSLGYSTTLNALNTIGYKEVVQYLYGKIDFNEMVHQIKVNTRNYARRQIIYFRKIEGAKWINLSKTSQEEVVDQILSEFI
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
A9BHW9
Q96PL5
ERMAP_HUMAN
Scianna blood group antigen
Homo
MEMASSAGSWLSGCLIPLVFLRLSVHVSGHAGDAGKFHVALLGGTAELLCPLSLWPGTVPKEVRWLRSPFPQRSQAVHIFRDGKDQDEDLMPEYKGRTVLVRDAQEGSVTLQILDVRLEDQGSYRCLIQVGNLSKEDTVILQVAAPSVGSLSPSAVALAVILPVLVLLIMVCLCLIWKQRRAKEKLLYEHVTEVDNLLSDHAKEKGKLHKAVKKLRSELKLKRAAANSGWRRARLHFVAVTLDPDTAHPKLILSEDQRCVRLGDRRQPVPDNPQRFDFVVSILGSEYFTTGCHYWEVYVGDKTKWILGVCSESVSRKGKVTASPANGHWLLRQSRGNEYEALTSPQTSFRLKEPPRCVGIFLDYEAGVISFYNVTNKSHIFTFTHNFSGPLRPFFEPCLHDGGKNTAPLVICSELHKSEESIVPRPEGKGHANGDVSLKVNSSLLPPKAPELKDIILSLPPDLGPALQELKAPSF
Possible role as a cell-adhesion or receptor molecule of erythroid cells.
Q96PL5
C4YL78
CHO2_CANAW
Phosphatidylethanolamine N-methyltransferase
Candida
MTFTINNTNSTVFDSTNNENMTISEPVQPVSKGPKGITFSGETFIVPETHDMVKTLFDPTVKKSNFELIILSCLFSNLLVFLIPNNQIRIYIFIALYIFWRLSYNFGIGWLLQNQSNHNLLVSWSQKYHLFDPENKGALAQSIQNEIKSQRGENYDIKSMPVEFNTWLIFRKFVDLILMSDFITFCCVVYCSAIKDDYQFINNQSFWLVYSRIVLGSGLILFNLWVKVNAHNTIKDYAWYWGDFFFRQINNEELIFDGVFEMVPHPMYSVGYVGYYGFALIAKSYVVLAIAIFGHFLQMIFLHYIENPHIDKIYGPSKNEINLIKILKLKDLKNFDNLKPLVGLTNFNWMRASDIVNLVLSLTYGIIIPLFANSIKSLFILTVGMKLFESISINLSLTLQSYFKIVTKWSLSNDIPVEKSFSNWAVLYNSLINLTYSSLFGMNLGYFLQKSGSGSSSGGLLFSDWFYLRVFLGLLLIYTQFWINFSIIDSIGYFGWFYGDFFIPKSQSSIKNITTAGVYRYLNNPEQIFGVCGVMGIFLIYPTVENFVCVGLWVVNNFIRINFIEKSHMVKLYGEQEVNRDSGVTKTVKKHLLPEVIQRRMSNDEAYTRVNGTTHERRRRRSSNLHGNSVADSLDNFIRDLRNSSTKLSQQKLIELSQNLSFANSDYKLTIDGLKMQSTESDELKYTTIGTPVTVSWTSPTENHSVRDWIGLYKIVQTSYSRNKTILSSAGRWTWCKEPKGSFIFDKEKLFWEEGVYEFRYHLDGKHDVAYISEPFEIKSIELKVPEFKEDAIKFAENLKLEIFDKVIKLTDINEAISPIANQSDNVIEVYKLISSMISKSTKINITYKIFLNQGDDDLLSIKDVAIKLINIKHVLEELSYNITDKKDV
Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME).
C4YL78
P70712
KYNU_RAT
L-kynurenine hydrolase
Rattus
MEPSPLELPVDAVRRIATELNCDPTDERVALRLDEEDKLKRFKDCFYIPKMRDLPSIDLSLVNEDDNAIYFLGNSLGLQPKMVKTYLEEELDKWAKIGAYGHEVGKRPWIIGDESIVSLMKDIVGAHEKEIALMNALTVNLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRMIKPREGEETLRMEDILEVIEKEGDSIAVVLFSGLHFYTGQLFNIPAITQAGHAKGCFVGFDLAHAVGNVELHLHDWDVDFACWCSYKYLNSGAGGLAGAFIHEKHAHTIKPALVGWFGHELSTRFNMDNKLQLIPGVNGFRISNPPILLVCSLHASLEIFQQATMTALRRKSILLTGYLEYLLKHYHGGNDTENKRPVVNIITPSRAEERGCQLTLTFSISKKGVFKELEKRGVVCDKREPEGIRVAPVPLYNSFHDVYKFIRLLTAILDSTERN
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
P70712
A1APN8
TPIS_PELPD
Triose-phosphate isomerase
Pelobacter
MRTPLIAGNWKLHKTIAESLAMVDELKPLVAGSRGVEIVVAPVFTALKSVSFALNGSDIGLAAQDCFWEEQGAFTGEVSPAQLRDAGCSHVIIGHSERRQLFGETDEGVNRKARAAVAVGLTAIICVGETMEERESRATFTVVGRQVTAALAGFLSHEFSRIVIAYEPVWAIGTGKTATDQQAQEVHCYIRNLVTMSISQAIADSLRILYGGSVKPDNIRGLMAQPDIDGALIGGASLKAASFAEMVNFRG
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
A1APN8
B9LR64
DEOC_HALLT
Phosphodeoxyriboaldolase
Halorubrum
MDRDEFAASIDHTVLGPETTWGDVETILNEAADHGMNACIPPCYLPEAADYENAPKTIATVVGFPHGQHAPGVKRDEAVTAWDDGADEIDLVINVGRLKAGEDDAVAAEISDVVAAVPVPVKVIIETALLSDDEKRRACEAAVEADADMVKTSTGFADGGATIRDVELMSEYLPVKASGGVGSYEEATAMLDAGAVRIGASSGVAIVEGHPGDGD
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
B9LR64
B8CNX4
CMOB_SHEPW
tRNA U34 carboxymethyltransferase
Shewanella
MISFSSFYKQISDSSLQHWLETLPAILGEWQREHKHGSLPKWEKVLNKLHYPQPDTIDFTTSVTIGSGEQLSAGEREKLENLLAIFKPWRKGPYSIHGVEIDTEWRSDWKWERIAPHISPLANRTVLDVGCGSGYHMWRMLGEGAKHVVGIDPSPMFMCQFEAVKRIAGNEHPVHFLPLGIEELPPLDAFDTVFSMGVLYHRRSPIDHLIQLRDQLRTGGELVLETLVIDGDENTVLVPEDRYGKMNNVWFLPSVKALMLWLKKSDFIDIRCVDVDVTSLAEQRSTHWMPNESLVDYLDPNDVSLTVEGYPAPKRATIIATKNQPNKETK
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
B8CNX4
O18087
NH127_CAEEL
Nuclear hormone receptor family member nhr-127
Caenorhabditis
MKITFSPELSIPCEVCKNQSNGYHFEVLSCGACASFFRRSVVSKIKYQCKDGKKRCQIRYLDRHFCRYCRFSKCVKAGMKAEKIQKNRDLDSSPTPTDQNNCIPSDVLHDDGILIKDIRGLFKQFNPHNASEGCSKLEKLTEGLQFIRRNQERECIKIIDEMDSESLKDVQFKVIGSCATWLLFSSFFQKLEENEKVVILERLWHGWTVLEFLSRSLEIFGNKVIDEKIVFISDNTAIRLITAFENSLKTASPKKSESIKKKLELSFSVIFDELALHFINWKPTEIEISYMQWQIVWSVAEQLLSGNSLEKGEHFTEQLSKDLHEYYVRELKLENYAFRIEKMMDIVQIVQNNFY
Orphan nuclear receptor (Probable). May play a role in modulation of lifespan and immunity .
O18087
Q3YJT3
PT2K1_SOLTU
Patatin-2-Kuras 1
Solanum
MILATTGSTCATLGEMVTVLSIDGGGIKGIIPATILEFLEGQLQEVDNNKDARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAAKDIVPFYFEHGPHIFNSSGTIFGPMYDGKYLLQVLQEKLGETRVHQALTEVAISSFDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPIYFPPHYFVTHTSNGDRYEFNLVDGAVATVGDPALLSLSVATRLAQEDPAFSSIKSLDYKQMLLLSLGTGTNSEFDKTYTAEEAAKWGPLRWLLAIQQMTNAASSYMTDYYLSTVFQARHSQNNYLRVQENALTGTTTEMDDASEANMELLVQVGETLLKKPVSKDSPETYEEALKRFAKLLSDRKKLRANKASY
Probable lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens.
Q3YJT3
B1XT48
PRMA_POLNS
Ribosomal protein L11 methyltransferase
Polynucleobacter
MSYRELIFTVAAETAEPLGDALLDLGALSVTVEDDAAGGYDENPLYEEPGLSPEVQAWDRSAVTALFNPEIDTSGSAEFIPELLASLKEVGFNLAPPQEKTIEEQDWVRLTQSQFSPIQIGERIWVVPSWHDAPNDPNAICLAVDPGLAFGTGSHPTTHLCLLWLEQQSHLKNQSLLDYGCGSGILAIAAAKLGCNPVIGTDIDPQAMVAARSNADINHTAVTFVLPNEGATELAAETKYDIVMANILANPLQVLAPALVNKMKLGGRIVLSGVLARQAEEVIATYSQWLTPSVWKESEGWVCLHGTLNQDKQNTASTVFAAPAQKKF
Methylates ribosomal protein L11.
B1XT48
Q6P5F6
S39AA_MOUSE
Zrt- and Irt-like protein 10
Mus
MKVHIHTKFCLICLLTFIFHHCNHCHEDHDHGPEELHRHHRGMTESESSKFSVQDAENEKKYYIEKLFDRYGENGRLSFFGLEKLLTNLGLGEIKVVEINHEDLGHDHVSHLDILAVQEGKHFHSHTHQHFHNHLNAENHTTTSVTSKRNHKCDPEKEAAELPIKADDKHLHDRNHRFHHRHRLHHHLDHNTTRHVHNDSVAHSEHGEPGHSPSPETNKTQEQSEVKSVKVRRKEKGKRKKENSEVNTPGFLPNHDHSEQYEHNRVHKLDRVHSPGHPHAHLPEHSGHELGHGHQELDPDNEGELRHTRKREAPHVRKSAIYSTPSHKDQSEDDRQHECLNVTQLLKHFGLGPNSPISPDLFTYLCPALLYQIDSRLCIEHFDKLLVEDLNKDKTLVPEDKTNIGASAWICGIISITVISLLSLLGVILVPIINQGCFKFLLTFLVALAVGTMSGDALLHLLPHSQGGHDHSHQHTHGHGHSHGHESKEFLEEYDAVLKGLVALGGIYLLFIIEHCIRMFKHYKQQRGKQKWFMKQSTEESTIGRKLSDHKLNSTPDADWLQLKPLAGTDDSVVSEDRLNETELTDLEAQQESPPKNYLGVEEEKIMDHSHSDGLHTIHEHEVHVTSHNHHDEDKAVLRKHSHQWHHRHAHHSHGPCHSGSDLKETGIANIAWMVIMGDGIHNFSDGLAIGAAFSAGLTGGISTSIAVFCHELPHELGDFAVLLKAGMTVKQAIVYNLLSAMMAYIGMLIGTAVGQYANNITLWIFAITAGMFLYVALVDMLPEMLHGDGDHEEHGFCPVGQFILQNLGLLFGFAIMLVIALYEDKIVFDIQF
May act as a zinc-influx transporter.
Q6P5F6
B8DP81
MURD_DESVM
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
Desulfovibrio
MTCDKHTAQTIGKGDLVVVVGAGRSGMAAARLLHRMGARVRLLERNADGVPADFVRWAAEAGVEIATGDHAPTQFEGARAVVPSPGMAVSKLRPLLAQGPDAPEIMAEMELAWRQLDGEPVLAVTGTSGKTTTVSLCAAMLRAQGLSVFLGGNIGTPLSEYVLSVAHGGADGQGRADVLVIEISSFQLQACTTFRPRVAMLLNISENHLDYHADMAEYIDAKFRLFRCMEEGDLAIFGQGVRDLVAARDLKPRTLFFDAAARRFPRTCLLGGHNQANIEAAWQACREFGVTPEAAEKAVADFAPMEHRLEAVAERNGVLWVNDSKCTTVEALRVALQAFDRPVVLMVGGKFKGGDLASLLPLLCGRVRAVVGFGASREHFEGAWMGQGDFPMSWHPALEPAVAEAAALARPGDAVVMAPATSSFDLFANYKERGHAFRRAVEALP
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
B8DP81
C6A179
RL18_THESM
50S ribosomal protein L18
Thermococcus
MAHGPRYRVPFRRRREGKTNYHKRLALLKSGKPRLVVRKTLNHHVAQIVLYAPEGDKTVVSAHTRELMRDFGWKGHGGNTPSAYLLGLLIGYKALEKGIEEAILDIGLHPPTKGSSIFAVLKGAVDAGLNVPHSEEIYPGEERINGKHIAEYAKMLKEDDENYKKQFGGYLVKGLEPEKLPEHFEEVKARIIEKFEKVRA
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
C6A179
A3PIC9
CH10_CERS1
Chaperonin-10
Cereibacter
MAFKPLHDRVLVRRVQSDEKTKGGLIIPDTAKEKPAEGEVVSCGEGARKDSGELIAMSVKAGDRVLFGKWSGTEVTIDGAELLIMKESDILGILS
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
A3PIC9
Q12V31
NADE_METBU
NH(3)-dependent NAD(+) synthetase
Methanococcoides
MDIIQAKDIIIDFIGTKLEGTGIEGAVVGISGGIDSALVAYLSVEALGAENVLGIHMPEASTPKSEIEDASKVAEALGIDFKVINITNVLEVYRTAMPDIDGASAHVDGNLKARIRMSMLYYYANMFGRVVMGTGNKSEILLGYFTKYGDGGVDIEPIGDLYKTEVREMSKMLGVPESILEKAPSAGLWEGQTDEDDLGVTYETIDKVLQPILAGEGQERVHLKLGVPMEEISSILLRVRSNLHKRTTPQIAYLDDLRGDWLS
Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Q12V31
Q1B4S9
GLGC_MYCSS
ADP-glucose synthase
unclassified Mycobacterium
MRELPHVLGIVLAGGEGKRLYPLTADRAKPAVPFGGAYRLIDFVLSNLVNARYLRICVLTQYKSHSLDRHISQNWRLSGLAGEYITPVPAQQRLGPRWYTGSADAIYQSMNLIYDEDPDYIVVFGADHVYRMDPEQMVQFHIESGAGATVAGIRVPRAEATAFGVIDADESGRIRSFVEKPADPPGTPDNPDEAFVSMGNYIFTTKVLIDAIRADADDDDSDHDMGGDIIPRLVSDGMAAVYDFSNNEVPGATERDHGYWRDVGTLDAFYDAHMDLVSVHPIFNLYNKRWPIRGESENLAPAKFVNGGSAQESVVGAGSIISAASVRNSVLSSNVYIDDGAIVEGSVIMPGTRIGRGAVVRHAILDKNVVVGPGEMVGVDLEKDRERFSVSAGGVVAVGKGIWI
Involved in the biosynthesis of ADP-glucose, a building block, required in the biosynthesis of maltose-1-phosphate (M1P) and in the elongation reactions to produce linear alpha-1,4-glucans. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc.
Q1B4S9
A3MRR3
HSLU_BURM7
Unfoldase HslU
pseudomallei group
MSTMTPAEIVSELDKHIIGQAKAKKAVAVALRNRWRRQQVAEPLRQEITPKNILMIGPTGVGKTEIARRLAKLADAPFIKIEATKFTEVGYVGRDVDSIVRDLIEISVKQTRETEMRKVRSKATDLAEDRILDVLLPQPRAVGFGASAEHANDDNNATRQTFRKRLREGQLDDKEIELDIEQPAVGMDIMAPPGMEEMTEQIRSMFSNLGSGKKQRRKVKIREALKLLTDEEAAKMLNDEEVKTKAVQNVEQNGIVFLDEIDKITSRNHEGGGGEVSRQGVQRDLLPLVEGTTINTKYGMVKTDHILFIASGAFHLAKPSDLIPELQGRFPIRVELDSLSVKDFEAILVATDASLVKQYQALLATEDVKLEFADDGIRRLAEIAYAVNEKTENIGARRLYTVIEKLLEEVSFAAGNHAGQSVTIDSAYVDRALGEVSKDEDLSRYVL
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
A3MRR3
B0UHC4
GATB_METS4
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Methylobacterium
MNAPVTPKKLIKGALGDWEVVIGMEIHAQVTSRSKLFSGASTAFGAEPNAHVSLVDAAMPGMLPVINRECVAQAVRTGLGLKAQINHRSVFDRKNYFYPDLPQGYQISQYKSPIVGEGEVLVDLPDGETIRVGIERLHLEQDAGKSLHDQHPSLSFVDLNRSGVALMEIVSKPDLRSSEEAKAYVTKLRTILRYLGTCDGDMEKGNLRADVNVSVRRPGEPFGTRCEIKNVNSIRFIGQAIETEARRQIAILEDGGWIEQETRLYDPNRNETRSMRSKEEAHDYRYFPDPDLLPLEIEQAFIDGLRTELPELPDAKKARFVAEYGLSAYDATVLVAERASADYFEAVAKGRDGKAAANWVINELFGRLNKEGHGIEGSPVSAAQLGAIIDLIADGTISGKIAKDLFEIVWGEGGDPRAIVESRGLKQVTDTGAIEAAVDQIIAANPDKVAQAKAKPTLLGWFVGQTMKATGGKANPAAVNALLKTKLGIE
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).
B0UHC4
Q12218
TIR4_YEAST
TIP1-related protein 4
Saccharomyces
MAYSKITLLAALAAIAYAQTQAQINELNVVLDDVKTNIADYITLSYTPNSGFSLDQMPAGIMDIAAQLVANPSDDSYTTLYSEVDFSAVEHMLTMVPWYSSRLLPELEAMDASLTTSSSAATSSSEVASSSIASSTSSSVAPSSSEVVSSSVAPSSSEVVSSSVAPSSSEVVSSSVASSSSEVASSSVAPSSSEVVSSSVASSSSEVASSSVAPSSSEVVSSSVAPSSSEVVSSSVASSSSEVASSSVAPSSSEVVSSSVASSTSEATSSSAVTSSSAVSSSTESVSSSSVSSSSAVSSSEAVSSSPVSSVVSSSAGPASSSVAPYNSTIASSSSTAQTSISTIAPYNSTTTTTPASSASSVIISTRNGTTVTETDNTLVTKETTVCDYSSTSAVPASTTGYNNSTKVSTATICSTCKEGTSTATDFSTLKTTVTVCDSACQAKKSATVVSVQSKTTGIVEQTENGAAKAVIGMGAGALAAVAAMLL
Component of the cell wall. Required for anaerobic growth.
Q12218
A9GBF1
LON2_SORC5
ATP-dependent protease La 2
Sorangium
MPTGDPSSRTPPSPDADSVPILPLRNSVLFPMSVVPINVGRPRSVRLVEDLLGRERALVGVISQRSPDVDEPTFKELYSVGTVARVVKVIRLGPNNYSVVLNGLGRFRVKSAFSLEPYMRARIERIPESLVRDVELEALGAGLREATREVLGLMPNLPRDTAGILDNVREPGALADLIASNFPQAQASVGDKQEILEAFDVKARVRLVLAMVGRQLEVLRVKKEISSMVQEEMGKSQREYILRQQMKSIKEELGEGGDDDEIEELRERIRRAKVPAEVDKVVRKQLSRLRSMAQQSAEFNVTKTYLEWIADLPWSKTTVDKLSVESVRRCLDEDHLGLEKVKKRIVEYSAIRQLRTDKKGPILLFIGPPGVGKTSLGKSIARSMGRRYERIALGGVRDEAEIRGHRRTYVGALPGRILQALKKAGTKNPVLVLDEVDKMGVDLRGDPAAALLEVLDPEQNSTFQDHYLDLPFDLSQVMFLATANNWDGIPGPLVDRMEVIEVPGYTRTDKLGIAREFLVPKQLSAHGLTDERLEFTEPGIEAVVDHYTREAGVRGLERQIAAVCRATAVKVAEGNDVREVATPEHVEQVLGPHKHRPEIAERTLQPGVATGLAWTPAGGEILFIEATKMPGKGNVVLTGNMRNVMQESASTAVSFVRSKADRLHLDPEWLKEIDLHVHIPQHGTPKDGPSAGVTMFAAVASLLLGAPVRSDVAMTGEISLRGRVMPVGGVKEKLLAAHRAGIRHVLIPAKNRRDLEDVPQDVKDQIKITMVSSMEEILPLVLEPPRRAPAQSASPEELEEQAGV
ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
A9GBF1
B0U0Y0
RS17_FRAP2
30S ribosomal protein S17
Francisella
MSDKIRLLEGKVSSVAMDKTVVVRAERYVKHPLYGKFVKKTTKYYVHDEKNECKEGDVIKFKETRPYSKTKKWCLVDIINREK
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
B0U0Y0
A1BJF5
ATPA_CHLPD
F-ATPase subunit alpha
Chlorobium
MSTTVRPDEVSSILRKQLAGFESEADVYDVGTVLQVGDGIARVYGLSKAAAGELLEFPNKVMGMALNLEEDNVGAVLFGESNLVKEGDTVKRTGILASIPVGEAMLGRVINPLGEPIDGKGPIETQIRLPLERRAPGVIYRKSVHEPLQTGLKAIDSMIPIGRGQRELIIGDRQTGKTAVAIDTIINQKGKGVFCIYVAIGLKGSTVAQVVNTLEKFGAMEYTTVITATASDPAPLQFIAPFAGATLGEYFRDTGRHALVVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKITDDIEVARKMNDLPDALKSMVKGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLESNLFNSGQRPAINVGISVSRVGGSAQIKAMKKVAGTLRLDLAQFRELEAFSKFGSDLDKTTKAQLDRGARLVEILKQGQYIPMAVEKQVAIIFLGTQGLLDAVDVTRIRKFEEEFLGLLEHKHPEVLKAIAETGTLETDTANKIKEAAQKFIASFNQKAKA
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
A1BJF5
Q8EIV5
KATG2_SHEON
Peroxidase/catalase 2
Shewanella
MKINTLPTLSALTLAMSLALGAGMATAQEQATGNQFWWPEKLNLSPLRQNAIESNPYGSDYRYAEAFNTLDLDAVKKDIKALMTESQDWWPADYGHYGPFFIRMAWHSAGVYRIFDGRGGAAGGQQRFEPLNSWPADNVSLDKARRLLWPIKQKYGSKLSWGDLMVLTGNVALESMGFKTFGFGGGRVDDWEAEMVNWGSEKAWLDNKRHNGKGELAKPMGATQMGLIYVNPEGPNGVPDPLASAKEIRDTFGRMAMNDEETVALIAGGHTFGKAHGAHDPAKCVGADPAAAGIEEQGLGWKNKCGKGHSEDTVTSGLEGAWSSNPTKWTMEYLTWLYTFDWVQTKSPAGHIQWTPADGKAANLVPDAHLPDKRHAPIMFTSDIALKADPIYREITTRFLKNPQEFELAFAKAWFKLTHRDLGPKARYLGADVPAEALIWQDPIPALDHPLIDNADIKALGNKILASGLTVPELVRTAWASASSFRGTDMRGGANGARIRLEPMMNWQANNPKELAKVLAKLEKVQKDFNGSLKGSKKVSLADVIVLGGSVAVEKAAKEAGVVISVPFTPGRMDATQVQTDVNSFAVLEPAADGFRNYYSKDSSLSPAEMLIERANMLNLTVPEMTVLVGGLRALDANSAGVKHGVFTDKPGVLSNDFFVNLLDMSTKWRKSDKQEGIYEGQDRNSGKLKWTATPVDLIFGSHSELRAVSEVYGAQDGQDRFIQDFVKAWNKVMNADRFDI
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
Q8EIV5
F5CPD5
3S151_MICAT
MALT0051C
Micrurus
MKTLLLTLVVVTVVCLDFGHTMICYNQQSSQPPTTTTCSEGQCYKKTWSDHRGTIIERGCACPNVKPGVKISCCSSDKCNG
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
F5CPD5
B4E9P3
COAX_BURCJ
Pantothenic acid kinase
Burkholderia cepacia complex
MSEPHLLIDAGNSRIKWALADARRTLVDTGAFGHTRDGGADPDWSRLPRPRGAWISNVAGADVAARIDALLDARWPGLPRTTIRSRPAQCGVTNGYTTPEQLGSDRWAGLIGAHAAFPGEHLLIATFGTATTLEALRADGCFTGGLIAPGWALMMRALGTHTAQLPTLTTDIASGLLAGAQAEPFQVDTPRSLSAGCLYAQAGLIERAWRDLVAAWQAPVRLVLAGGAADDVARALTIAHTRHDTLILSGLALIAADAADPATAPD
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
B4E9P3
A0PPM4
WHIA_MYCUA
Probable cell division protein WhiA
Mycobacterium
MAMTTEVKDELSRLVVKSVSARRAEVTSLLRFAGGLHIVAGRVVVEAEVDLGSIARRLRKDIFDLYGYSAVVHVLSASGIRKNTRYVLRVANDGEALARQTGLFDMRGRPVRGLPAQVVGGSIGDAEAAWRGAFLAHGSLTEPGRSSALEVSCPGPEAALALVGAARRLGVGAKAREVRGADRVVVRDGEAIGALLTRMGAQDTRLVWEERRMRREVRATANRLANFDDANLRRSARAAVAAAARVERALEILGDTVPDHLASAGKLRVEHRQVSLEELGRLADPPMTKDAVAGRIRRLLSMADRKAKVEGIPDTESAVTPDLLEDA
Involved in cell division and chromosome segregation.
A0PPM4
Q31EM1
TSAD_HYDCU
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Hydrogenovibrio
MQTTHSNPSSPSLTLGIETSCDETGIALYHSEKGLIAHTLYSQIKLHAEYGGVVPELASRDHIRKITPLIQETLKKGQVSAKDITGIAYTAGPGLMGALLSGASVARSLAFAWQIPAIAIHHMEGHLLAPMLEETQPEFPFVCLLVSGGHTMIIRVDGIGRYKLLGDTLDDAAGEAFDKTAKMLGLGYPGGPEVSKLALHGQTDRYKFPRPMVDRPGLDMSFSGLKTFTLNTWLKAKESGDDSEQTKADICRAFEVAVADTLSIKCKRALEQEGLNRLVVSGGVSANREIRAKLDALMAKRKGSAFYPRLEFCTDNGAMIAYAGSKRLEAGQFSDLNFACQPRWDLESLEPIDPIEVV
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
Q31EM1
Q0SN23
RS3_BORAP
30S ribosomal protein S3
Borreliella
MGQKVHPYSLRVKINKDWKSKWYFDKKLYSTILHEDFLIRLEIMKFLKGIKFDISDIEIIRNNPQKVTVVIVTPRPGSVIGLKGSNLEKIGQLLTKKISKKISIKIKEVKRPELDAQIIANGIAKQVENRVSYRKVLKSALSTSMLKGAQGLKIKIAGRLGGAEIARSFEVKEGRVPLHTLRANIDYGFSEAHTTYGIIGVKVWLFKGEVLGRQTNSDAGQVINKKPFRERGETVKNFDKILNNREKINEKQTRALNKKDGLSKDEASLLNKLSSSFSKERVDSNEQNIGG
Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation.
Q0SN23
A4J103
RPOB_DESRM
Transcriptase subunit beta
Desulforamulus
MAYPEKVGNRVRWNYGKLREVLDLPNLIEVQRNSYEWFLQEGLREVFHDISPIQDFTGNLILEFLDYTLGEPKYSVEECKERDVTYAAPLRVKVRLINKETGEVKEQEVFMGDFPLMTSKGTFIINGAERVIVSQLVRSPGVYFADQIDPSGKRLFATTMIPNRGAWLEFETDVNDHIFVRIDRTRKIPATVLIRALGYGSNALIMELFENDKFVQETLTRDNTDTEEEALVEIYKRLRPGEPPTVESARSLLNTLFFDPKRYDLAHVGRYKLQKKLKHGILYRYPNGEEGPKEWDRLLNKEVPVDREFIRELTKEDIIATFRYLLNLMQGEGIVDDIDHLGNRRLRSVGELLQNQFRIGLSRMERVVRERMTIQDVDVITPQVLINIRPVVASIKEFFGSSQLSQFMDQTNPLAELTHKRRLSALGPGGLSRERAGFEVRDVHHSHYGRMCPIETPEGPNIGLIGSLSTYARINSFGFMEAPYRKVDKENKRVTDEIVYLTADEEEDHIIAQANAPLDENGYFVEERVNARRGHDTLLVPTDRVEYMDVSPKQVFSVATSLIPFLEHDDANRALMGANMQRQAVPLLRCQAPVVGTGIEHRAAKDSGVCIVAERGGEVVRVTATEVAVRTDEGRTDTYKLLKFTRSNQGTCINQKPIVNKGDRVEEGQILADGPATEQGELALGRNILVAFMTWEGNNYEDAILISEKAVKEDFFTSIHIEEYECDARDTKLGPEEITRDIPNVGEDILKDLDERGIIRVGAEVRPGDILVGKVTPKGETELTAEERLLRAIFGEKAREVRDTSLRVPHGEAGKIVDVKVFSRENGDELPPGVNHLVRCYIAQKRKISEGDKMAGRHGNKGVVARILPEEDMPFMADGTPVQIVLNPLGVPSRMNIGQVLETHLGWAAKTLGFNVATPVFNGASEESIWETLRRAELPEDGKTVLYDGRTGEPFDNRVTVGYIYMIKLHHLVDDKIHARSTGPYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEILTVKSDDVVGRVKTYEAIVKGENVPEPGVPESFKVLIKELQSLGLDVKVLAEDEKEIEIKEIEEDITETAKELGIELPEERRVSSSKEEIEEEEEVEDNSDEFDETFLEEAEDDFSLDDED
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
A4J103
Q9VGC3
COG1_DROME
Component of oligomeric Golgi complex 1
Sophophora
MTANLLNLNVDTLFEQHSVSEIDEVHKKIQSVVENKREELRTHVGERYRDLLQAADTIAAMQTSAGTLMEQVRHVQANCRSLNEQQLLGFQSTANASAKDAALKERNAGKKLQTYYGTMAQIKLLTALPELIWTHLDNDRFYAATELFIFSRHISTGLQLDGQSALMQKLPVARKQWEILRPFHVTIKQAILTALEREELLQEMTVDCLQSLLLLDKSDLSTVLKSFLNLRSSAFLNCLQSGPSEPRRVKDRILASLNVLNSTVELLDKCLLGYSLLFSRLEECASSTCPPSINRMESSERQLVHLLPEIIAGFKPQFDVPQLTPEQLGSSLQQWLDKMNALAAAHLQQVFALVTNMQTIQDIKSAARTNGRPDFVRLEQQLHLKRSQLDFYARKYVPLINARVREIIRSSWASAMKLTYEQVLLLIEAGQSQPPLQIWREQSDDLPLSLAAALSDQPKRLANRTKGYDGATIELCKRFDSHLADIVQELNVMLQEQTTRAEDKVSLIEFLRETAEEQLTEYLSNLKGLELRERPALLLALRNSLALVELCPNLKLCFCQPSSWRQWTDNSAGLGIEHWQRICGLIEKEMLSFWLVIVDDVLAGHNCEEKLPKVINHEVVLSDFALWQTLTLEQRDEDQEQSVQSTIRIPSQPRLSLQTYLHQLIQALNSVVPQTLPPKVLQAFIQRLIGKLLCHYEGLAHAECTKASQNIALQLYFDLKFLERVFAISREERTLYDQIHAQQNQLRDYIDPFDFELFAEHITAHVSRAASRLQGELGVLTPSAAAPSQGAAAASSLAHEADPNVLCLSSSGSTSLWFPLLPIVMPQAAGRVTSAERKSPIQEPVEKTATTTPTRKSGGNGARKGDSSKSKSSAASFFGMSQEWFR
Required for normal Golgi function.
Q9VGC3
A2RNP3
RL5_LACLM
50S ribosomal protein L5
Lactococcus cremoris subsp. cremoris
MTNRLKEKYTNEVVPALTEQFNYTSIMAVPKVDKIVINMGVGDAVNNSKNLDKAVAELALISGQKPLITKAKKSVAAFRLREGMPIGAKVTLRGERMFEFLDKLVTVSLPRVRDFHGVSNKAFDGRGNYTLGVKEQLIFPEINYDDVDKVRGMDIVIVTTANTDEESRELLAKLGMPFAK
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
A2RNP3
A4JCP7
PLSX_BURVG
Phosphate-acyl-ACP acyltransferase
Burkholderia cepacia complex
MTVKLTIDCMGGDHGPSVTVPAAVKFVRAHPDAHLMLVGIESAIRAQLKKLKALDDPALTIVPATEVVAMDDPVEVALRKKKDSSMRVALNHVKEGAAQACISAGNTGALMAVSRYVLKTLPGIERPAIAFALPNPTGYTMMLDLGANVDCEPQHLLQFAEMGHALVAALEGKERPTIGLLNIGEEVIKGNETIKRAGELLRASTLNFRGNVEGNDIYKGTVDVIVCDGFVGNVALKTSEGLAQMLSDIIREEFGRSLMSKLMALLALPVLMRFKKRVDHRQYNGAALLGLKSLVIKSHGSADAYAFEWAIKRGYDAVKNGVLERLTRAMADNSVSLGDGEHDAGGAGHTGPAAGQHAEPPAAQSSKA
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.
A4JCP7
Q2JQL5
RECO_SYNJA
Recombination protein O
unclassified Synechococcus
MSGVTYRVTGINLKAMPLGEADRIITILTREQGLIRAVAKGSRKQLSKWGGRMEPFVVNDLLVARGRWSAQTDPSQCLQRIAQAETLQSFPRLGRSLAHLTAAQYLAEVALLLALPNQPQEELFVLLVEHLERIEQAPATEAVLPLLVHGLYHLLVVGGVAPSVQACYSCGEELAGEAFFSPHAGGLVCDPCRLAQRLSPVAWVSSSVLQALGSLPNPTLPSLAERALPLASWLAAERLLRRVLELHADRAIRSAGLLASCYSVPVAETLPPTPSGQGSPVAAAAFSEEDSETLGSNLKKL
Involved in DNA repair and RecF pathway recombination.
Q2JQL5
Q59PD6
MAD1_CANAL
Spindle assembly checkpoint component MAD1
Candida
MSTGSSPFVDHKSNNSTISINNNSSILNESSISKAYVSKLEFQLDTIKTENRILQQEKDQITSDYRKIIDEKNQELENLKLNFKYVYDEKNQLESKLTNQEQVSTNNINQLSDEIQTYKRENLKLTKDYNSLLDKFNKLNRKNQQIMHDLNKEIEVNDKLHQELKIKEKTNQELQKASDTAINELEQYSKILDKKNGSDNLLYKNLTTKSNNLQNINHQLQNKIDQLLQNKTSNELLKQQNQSLLHKLQNLENIESKYLQLEIEKLQLETKYNDLFKALDTAIASSNEYKDNENTDDTIHTSKVKSFIEYCNNLQAKNLTLQEKYDSKIIQVKELTKELEDHAREIETDFLPTITDLESKLKVYADQNTKLERTKSLREKEITFLRNSLKQMEQIHANQQHKQQEQEKEENTENKSISQYMTNLEKLVDEYKTKIDELEKKNLEYNKSSIITNEKTPSNKRQRLESNYTFKTQAIELEKENIEISSKLKQAESTIEQLKFKISELDKVETRKEQYRILQLKNNLISQDQFIKQTTLIALRKENEELINKYIKNLPIEEQIPKGVFQRQEDDKQRLQAQIDHLTKRSTRLREVFTKKSKDIITVIAKYFGFIIEFLPNPINPTDLFSRIKLRSRYIPSEEDCYLIIDVENRGLKAHGNFQFKQICEELAQYWVNENNQFPCLLSAVNLKLYEIYASK
Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis.
Q59PD6
A0PJ29
D4FAD_REBSA
Delta-4 desaturase
Rebecca
MPPSAAKQMGASTGVHAGVTDSSAFTRKDVADRPDLTIVGDSVYDAKAFRSEHPGGAHFVSLFGGRDATEAFMEYHRRAWPKSRMSRFHVGSLASTEEPVAADEGYLQLCARIAKMVPSVSSGFAPASYWVKAGLILGSAIALEAYMLYAGKRLLPSIVLGWLFALIGLNIQHDANHGALSKSASVNLALGLCQDWIGGSMILWLQEHVVMHHLHTNDVDKDPDQKAHGALRLKPTDAWSPMHWLQHLYLLPGETMYAFKLLFLDISELVMWRWEGEPISKLAGYLFMPSLLLKLTFWARFVALPLYLAPSVHTAVCIAATVMTGSFYLAFFFFISHNFEGVASVGPDGSITSMTRGASFLKRQAETSSNVGGPLLATLNGGLNYQIEHHLFPRVHHGFYPRLAPLVKAELEARGIEYKHYPTIWSNLASTLRHMYALGRRPRSKAE
Fatty acid desaturase that introduces a cis double bond at the 4-position in 22-carbon polyunsaturated fatty acids that contain a Delta(7) double bond, resulting in the production of delta-4 desaturated fatty acid docosahexanoic acid (DHA).
A0PJ29
Q2NW23
IF2_SODGM
Translation initiation factor IF-2
Sodalis
MTDVTVKSLAAEIQTPVDRLVQQFADAGIDKTAVDSVTQQEKETLLAHLNRDRGAAPNKLTLQRKTRSTLNIPSTGGKSKSVQIEVRKKRTYVQRDPQAQEQAEAEEQARREAEELAQHQVQRDAEEKAKRAAEDKAKREAAEQAKRVAAESDKLTNQQTNTMTKSPQATEKARREAEAAELRRKAEEETRRKVEEKARQVAEEARRMAEERGGNWDNAPEPAEEDTTDYHVNTSHHAREAEDENDRKVEGDRRSRTRGGKATKQKKTSRLSESKADREEARAVGRGGKGKRRPSTLTQGFNKPAQAVNRDVVIGETITVAELANKMAVKGSQVIKAMMKLGAMATINQVIDQETAQLVAEEMGHKVILRRENELEESVMSDRDTGSSAAAESRAPVVTIMGHVDHGKTSLLDYIRSTKVAAGEAGGITQHIGAYHVETDNGMITFLDTPGHAAFTAMRARGAQATDIVVLVVAADDGVMPQTIEAIQHAKAAKVPVVVAVNKIDKPEADPDRVKNELTQYGVIPEEWGGESQFVHVSAKSGAGIDELLDAILLQAEVLELKAIRNGMASGVVIESFLDKGRGPVATVLVREGTLNRGDIVLCGFEYGRVRAMRDEVGRDVASAGPSIPVEILGLSGVPAAGDEATVVRDEKKAREVALYRQGKFREVKLARQQKSKLENMFANMTEGEVSELNIVLKSDVQGSAEAISDALEKLSNDEVKVKIVGSGVGGITETDATLAAASNAILLGFNVRADASARRVIEAENLDLRYYSVIYDLIDEVKQAMSGMLAPEYKQEIIGLAEVRNVFRSPKFGAIAGCMVTEGVVKRHNKIRVLRENVVIYEGELESLRRFKDDVNEVRNGMECGIGVKNYNDVRSGDVIEVFETIEIQRTIA
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
Q2NW23