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
|
|---|---|---|---|---|---|---|
P35247
|
SFTPD_HUMAN
|
Lung surfactant protein D
|
Homo
|
MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF
|
Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
|
P35247
|
Q20849
|
KNTC1_CAEEL
|
Rough deal homolog
|
Caenorhabditis
|
MGRLGEAKAVDLEAETSTVGLYDVCTVGRILPLLNEMSIDKKSPAWKLKPKSNERFLVLASCSDLAVFSLGEKSDYSFNTGLGGAITDFEILGSSSFFVGVIEHRRIVILSLDKQEIYLNEPAPHEIDFVVCHTTSSVCQLIFGSRSDNWHTITLPGDVAASKETNRFENWHRDQIQEFFHQAMGKTVSKSVDMSKVAGDITLISNGPLQTFASIDQQRGIHWCGLVESEFEVIGMEKQFLQVRDGGRFSLHLDTDGWIHVFDSLVSSFCHEFDMKMSPDDKILDFVIIDKNEVEVPKMFAILVLPRDGDSTKMMIYDRLNKDNCFALDSSTSTTLFAYGGSDRVLIAVEELENSLADEQDGSQIVVRQVSQSRPEMRFESLLKNNRFEEAEKFAMAFMLDVQKVYKGHVHYLMDSCDESDESFETLMTKMGQIQDHNMVAETYFTLVGMSRRCDRIRTYLTHAKKRRITDLDILKMIEALCYTWGTYRIIAGPEENEPSRPQVNETIWDLFVEALHDANPWIEIYNEFISDAQFTQARVIFSRHGKSITDYMCDDEENTISRLETLFRMFIDAISSDISKWSNVIEHVTTDILPACVMITEELIPCLESLITSLISLLEYRDSTNWPENAIKAASSYDTMTKILSNNGNTPATQCILVMYGSKLGSSAGNKPSSMSRIKKIYYDLIELKRLKDVYECSISFSVFQNMSSEQICHKILQNALANPNMTHAKIEKFVKPFMAERHLDQEQTIVNYIQMMSGAAVTNANLFGWEKQCVQLCASLMDETRRCCSIISIASTAKIPWPAELNEAVEKILASRTLLRSEIEQMHLVCKRTELYKMLSSYGFSRQDIELLTTPDSNMDIILTIRCMLAHREKASRFVDVIKLVDLLKAMQGSSQPRTLRIEYVQSFAIIHMMSHQDVTISIINYIDSLGDRERVKTISLVFSFIECVANAPATGDNVLEREKILGVGEELMSHYTCRDNNFNDPERRLKDELVLLREVQKTETKAVLLSELKDEDWQRRFLERLIESNSSMSLNLGRCSYMGISPEHLIEMILTKATVENDMDTIVDSITNYVEFINSLTDSSREMLEPIVQILSWITFRLPKLLPNETEMARADYIAFVVKRIGRVVRETLRRFSFDVISDDLDYLLQLEAFYHLGEHIIKQSLRGQENENEKQEMFRSDDDTFLPTDSSNPFSNQSSLRIFEFKRPLGTFDFSNDPALFEGVQGVLALAMVAPSVARPYDSEISPDDANEFRSSWEQLNMFLAMHSQDLLDISARVFAGSLKCWAGEYLQGIVEMEQPILSVVERMLQQKKFDFWHAVTLLGGIPLERLDRAIIDLQKRQGVRSSTKATIQYLQLAFVMSLLARNMEKVPTIVSAYEQKYLVKKLAEEGIRVSITQDFVDKVLQQAIDLRQPLSPLRLHDYVKKYVEKLIRNSKISVGEYMVRYATLLIRKASVAGRHTDREIRKEEIEKYIEAARIALRIAEEEDASCICNYLHCLLYVVCPYNYEVIQFIVTSYGKYATETVEIEFNKNLKSIMAFLWAYQRTNHISNEESIWFTKRESVLMKDEKEFEKTGRMLDPFGHSLRVVYEDDGSNMSDSYNSDLALSSDAMVYERNSVIISDLPSLAEQYLPFHAFLLRKKEEIDEIVMGIVKAELSIFNVPIWQTFLREVSWLSSRFSRSQLLSSAIFAHANKYAKFGKSLPDGERNVIYELLNSASQRHVVVSTIALLFKRIILSDVKIELLQMGVNISERWTSDLTGEEQQEMEEQSARLKDGIAKFSTELELKKNGLYNEKTADNIENVSELCSLIYNEMVQWDDSRDVLKKCQVVDKIAKANGLDLTALHEQLVFSWVEDTQTIISINHVDMNESIGGTSFLDHKDETDDQNDLRIPLFDGILDKVVVLCQRIDKKRLLTRLGSILMRGGRKATGGYTAVVRATCIILRSFTDTEVSELLSGADMFALCSTLENQLYERLFEKAEVKGDCKTDKMQLIKSLLQCPSRTHPMTALIACLIIDHEFKDPKRDISLGWDVGCVPVSANSSNS
|
Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis . Required for chromosome segregation, the assembly of the dynein-dynactin and mdf-1-mdf-2 complexes onto kinetochores and spindle pole separation . Plays a role in nuclear envelope breakdown . Its function related to the spindle assembly machinery and kinetochore-microtubule attachments likely depends on its association in the mitotic RZZ complex . The RZZ complex recruits the spindly-like protein spdl-1 to kinetochores . To prevent irregular chromosome segregation, the complex also inhibits the attachment of the kinetochore-associated NDC80 complex to microtubules . The recruitment of spdl-1 to kinetochores relieves this inhibition . Required for embryonic development .
|
Q20849
|
A2XK30
|
HOX32_ORYSI
|
OsHox32
|
Oryza sativa
|
MAAAMVAAVHGVGRQDRSSPGGGGAPQVDTGKYVRYTPEQVEALERVYGECPKPSSLRRQQLIRECPILSNIEPKQIKVWFQNRRCREKQRKEASRLQTVNRKLTAMNKLLMEENDRLQKQVSRLVYENGYMRQQLHNPSVATTDTSCESVVTSGQHHQQQNPAATRPQRDANNPAGLLAIAEETLAEFLSKATGTAVDWVQMVGMKPGPDSIGIIAVSHNCSGVAARACGLVSLEPTKVAEILKDRPSWYRDCRCVDVLHVIPTGNGGTIELIYMQTYAPTTLAAPRDFWILRYTSGLEDGSLVICERSLTQSTGGPSGPNTPNFVRAEVLPSGYLIRPCEGGGSMIHIVDHVDLDAWSVPEVLRPLYESPKILAQKMTIAALRHIRQIAHESSGEMPYGGGRQPAVLRTFSQRLSRGFNDAVNGFPDDGWSLMSSDGAEDVTIAFNSSPNKLVGSHVNSSQLFSAIGGGILCAKASMLLQNVPPALLVRFLREHRSEWADPGVDAYSAAALRASPYAVPGLRAGGFMGSQVILPLAHTLEHEEFLEVIRLEGHSLCHDEVVLSRDMYLLQLCSGVDENAAGACAQLVFAPIDESFADDAPLLPSGFRVIPLDGKTDAPSATRTLDLASTLEVGSGGTTRASSDTSSTCNTRSVLTIAFQFSYENHLRESVAAMARQYVRTVVASVQRVAMAIAPSRLGGQIETKNPPGSPEAHTLARWIGRSYRFHTGADLLRTDSQSMDSSLKAMWQHSDSIMCCSLKAAPVFTFANQAGLDMLETTLIALQDISLEKILDDDGRKALCTEFPKIMQQGFAYLPGGVCVSSMGRPVSYEQAVAWKVLSDDDTPHCLAFMFVNWSFV
|
Probable transcription factor.
|
A2XK30
|
Q9RYK1
|
URED_DEIRA
|
Urease accessory protein UreD
|
Deinococcus
|
MTTLGTPVSLGRRTRTGRLELEFGVRHGQTALLRDLQKAPLMVVRPFRLPCGTLMVFIVNPTGGVLGGDHSEIHVEAGAGTRVLILTQSATRVQPSPGGEWATQELHFHVGVGARLEYYPERTLPFAGSRFRQHLRADLGAGAEFGLLETLASGRVQMGERLAWADYRSEVSVYAAQERVYLDRQHFRPGPHSRAPGVLGGNDYFASGVWVAGDSAAGRPAAESPTTAPGWASGLSAGGAVWARGVAATGPALDHAARQLREQVRHDLFGAAPLVLRR
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q9RYK1
|
Q9ZL45
|
MOG_HELPJ
|
Molybdopterin adenylyltransferase
|
Helicobacter
|
MQTIHIGVLSASDRASKGVYEDLSGKAIQEVLSEYLLNPLEFHYEIVADERDLIEKSLIKMCDEYQCDLVVTTGGTGPALRDITPEATKKVCQKMLPGFGELMRMTSLKYVPTAILSRQSAGIRNKSLIINLPGKPKSIRECLEAVFPAIPYCVDLILGNYMQVNEKNIQAFRPKQ
|
Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.
|
Q9ZL45
|
Q65ML0
|
BIOD_BACLD
|
Dethiobiotin synthase
|
Bacillus
|
MKGFFVTGTDTGVGKTFIACGLAALLKEQHVDVGVFKPFLSGELASDPQSDTALLKNMSETPLTDEEVTPFIFKEPLAPYTAAKLEGRTVGLEDAVNHWKKIKDRHECFIVEGAGGIAVPLGEDYFVSDLIKALDLPAVIVARPNLGTINHTYLTAQYAKQMGIRVIGIVINGISSRPGLDEQTNPDMIERFCGVPLLGVTPKLEDASPTQIHHMIKDHVDVSLIMNQMQMGAEK
|
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.
|
Q65ML0
|
Q8CY56
|
TRMD_BIFLO
|
tRNA [GM37] methyltransferase
|
Bifidobacterium
|
MKIDIVSVFPEYFEVMNLSLMGKAQAKGLLEIKAHNLRDWTHDVHHSVDDTPVGGGAGMVMKPEVWSECLDELLGFSQPSGSPAPSGAPVLIFPNPSAPLFTQRDATELSHADHLLFGCGRYEGYDARIPDYYRAQGVDVREYSIGDYVLNGGEVAVSVMLEAITRLMPGFMGNPDSIVEESYTGEGALLEHRQYTKPAVWRGIAVPDVLLSGDHGKVDRFRRDEALARTAEIRPDLIAALDCKALDKADRKTLMALGWEVSAAHPRRLAD
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q8CY56
|
Q80ZE4
|
PAQR7_MOUSE
|
Progestin and adipoQ receptor family member VII
|
Mus
|
MAMAVAQKFNHLLSSLWHVGQKPPQPEPVFTVDRAQVPPLFWKPYIYAGYRPLHQNWCFYFRTLFQRHNEAVNVWTHLLAALALLLRLIGLAASVDFREDPHALPLFFIVLASFTYLSFSAVAHLLQAKSEFWHYSFFFLDYVGVAVYQFGSALAHFYYAIEPSWHDKVQAIFLPTAAFLAWLSCAGSCYNKYSQKPGLLGRIFQEAPSALAYVLDISPVLHRIIVSPLPAEEDPALLYHKCQVVFFLLAAAFFSTVMPESWFPGSCHIFGQGHQVFHVFLVLCTLAQLEAVTLDYQARRGIYEPLHARWPHNFSGLFLLTVASSSLTALLLSQLVRRKLHQKTK
|
Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(i) mediated pathway. May be involved in oocyte maturation. Involved in neurosteroid inhibition of apoptosis. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone.
|
Q80ZE4
|
Q51676
|
HEMN_PARDP
|
Coproporphyrinogen III dehydrogenase
|
Paracoccus
|
MEQQSQLERLGLFDARVPRYTSYPTAPHFTPAVGEPVFRDWIAAIPAGAAISLYMHVPFCRRLCWFCACRTQGTQSDEPVRAYAKALLAELDMLKSALAPGVRLSRLHWGGGTPTLMPAEMMRLVAGAVLDAFPLAEGAEFSVEIDPNEIDEARMDALAEAGLNRASIGVQDFDPEIQKIIGREQSFEVTKRAVDMIRDRGIASLNADILYGLPHQDPHRIAESVQKLLALSPDRVALYGYAHVPWMAKRQVMIPSEALPDPHGRLRLFETARELFLADGYDEIGIDHFARPGDGLARAQKAGLLRRNFQGYTDDRAEVLVGLGASSISRFPQGYAQNAPATGAHLARIRDGRFSTTRGHAFSAEDRWRSRMIEALMCDFEIRAEEFIRDHGFDAESLSRILTPVAAHFGDMVDADASGLRITPRGRPLTRMIARMFDGYDMAASGHSAAI
|
Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
|
Q51676
|
Q562C2
|
BOP1_RAT
|
Block of proliferation 1 protein
|
Rattus
|
MAGACGKHHMSPGSLPGKRRLEPDQEPQIQEPLLLSDPDSSLSDSEESVFSGLEDSGSDTSDEDTEEVARAGCDKDNRTEKTSEEQEQAVPPCPRAEEAGALTRDEYEEDSSDEEDIRNTVGNVPLAWYDDFPHVGYDLDGKRIYKPLRTRDELDQFLDKMDDPDFWRTVQDKMTGSDLRLTDEQVALVHRLQRGQFGDSGFDPYEPAVDFFSGDIMIHPVTNRPADKRSFIPSLVEKEKVSRLVHAIKMGWIKPRRPPDSTPSFYDLWAQEDPNAVLGRHKMHVPAPKLALPGHAESYNPPPEYLPTEEERLAWMQQEPIERKLNFLPQKFPSLRTVPAYGRFIQERFERCLDLYLCPRQRKMRVNVDPEDLIPKLPRPRDLQPFPVCQALVYRGHSDLVRCLSVSPGGQWLASGSDDGTLRLWEVATARCMKTVRVGGVIRSIAWNPNPTICLVAAAMDDAVVLLNPALGDRLLVGSTDQLLETFTPPEEPTLQPAHWLEVSEEERQRGLRLRICHSKPVTQVTWHGRGDYLAVVLSSQGHTQVLIHQLSRRRSQSPFRRSHGQVQCVAFHPTRPFLLVASQRSIRIYHLLRQELTKKLMPNCKWVSSMAVHPAGDNIICGSYDSKLVWFDLDLSTKPYKVLRHHKKALRAVAFHPRYPLFASGSDDGSVIVCHGMVYNDLLQNPLLVPVKVLKGHSLTRDLGVLDVAFHPTQPWVFSSGADGTIRLFS
|
Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
|
Q562C2
|
Q5HQC3
|
MENB_STAEQ
|
1,4-dihydroxy-2-naphthoyl-CoA synthase
|
Staphylococcus
|
MTRQWETLREYDEIKYEFFEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDKAFCSGGDQKKRGHGGYVGEDDIPRLNVLDLQRLIRVIPKPVIAMVRGYAIGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQVEDETVKWCKDIMQHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRNPDFDQFPKFP
|
Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA).
|
Q5HQC3
|
D0N4Y1
|
RD18_PHYIT
|
RxLR effector protein PexRD18
|
Phytophthora
|
MSHQRILLLLMAAFFAWVSAQTPPGQADKSKLIAHDVLMKTTSLSETTIATSSKRFLRLYDAEVRDTVRGDNDVDREERGTTPLLSKVDDLIHKVFKSNPEQAQIKAWMKSRVHPQAIFDTLRLAKSTTKLNDDPNLLLWLKLVAAFRAKNGNQAFSDLDLYYLLLKRSSGEELKILIESFRKTGALKELGKSMQKSLSGSWVSKTLQHETDPKIVYDTLRLQEAGTKLVDSPIFHQWLAYAQQYRAQKGNHWFGDDDMLDLFRKTMPEKDVVTLLHLLRNVPGMKDHGDTMQRFLFLSSKTSRKMMHDVWLNYDVTPEQVFKILRLVKVNMDAVDTNAMFIHWLRYVNLYRSHTKKNVLSSVQMVHFLADTKPLRSEWQFATFFESLKDVPDLKRLAENMQTYLFQNWLHTEWDPKAVSSMLAIPFPTSAVYLPKNDPIYKTWVAYTLYYTERKGGVSLLNKVKTLLDNDNPIGALTAAMKAQ
|
Effector that enhances P.infestans colonization of Nicotiana benthamiana leaves.
|
D0N4Y1
|
Q30UF8
|
RL13_SULDN
|
50S ribosomal protein L13
|
Sulfurimonas
|
MKFTKIATPEQIDQKWVLIDAEGKTFGRIITEVATLLRGKNKPCFTPNIDCGDYVVVVNASKAKFNGLGKIANKEYFSYSGYFGSVKSTKMTELLEKNPEKLYKLATRGMLPKTKLGAKMIKKLKIYASAEHPHSAQLAK
|
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.
|
Q30UF8
|
Q99TA0
|
RIBBA_STAAM
|
GTP cyclohydrolase II
|
Staphylococcus
|
MQFDNIDSALMALKNGETIIVVDDENRENEGDLVAVTEWMNDNTINFMAKEARGLICAPVSKDIAQRLDLVQMVDDNSDIFGTQFTVSIDHVDTTTGISAYERTLTAKKLIDPSSEAKDFNRPGHLFPLVAQDKGVLARNGHTEAAVDLAKLTGAKPAGVICEIMNDDGTMAKGQDLQNFKEKHQLKMITIDDLIEYRKKLEPEIEFKAKVKMPTDFGTFDMYGFKATYTDEEIVVLTKGAIRQHENVRLHSACLTGDIFHSQRCDCGAQLESSMKYINEHGGMIIYLPQEGRGIGLLNKLRAYELIEQGYDTVTANLALGFDEDLRDYHIAAQILKYFNIEHINLLSNNPSKFEGLKQYGIDIAERIEVIVPETVHNHDYMVTKKIKMGHLI
|
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.
|
Q99TA0
|
Q6GWX0
|
DDX4_PIG
|
Vasa-like protein
|
Sus
|
MGDEDWEAEINPHVSSYVPIFEKDGYSGENGDKFNRTTASSSEMDDGPSGRDHFMKSGFTSGRSYGKRDAGESNKRENTSTTGGFGVGKSFGNRGFSNNRFEDGDSSGFWRESTNDCEDNTTRNRGFSKRGGSRDGNKSEASGPFRRGGRGSFRGCRGGFGLGSQNSELDPDQGMQRGGGLFGSGRPAASDTGNGDTYQSRSGRGRGGYKGLNEEVVTGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQADLQVGQYSKREKLLEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD
|
ATP-dependent RNA helicase required during spermatogenesis to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle. Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs.
|
Q6GWX0
|
Q5PL21
|
KEFB_SALPA
|
K(+)/H(+) antiporter
|
Salmonella
|
MEGADLLTAGVLFLFAAVAAVPLAARLGIGAVLGYLLAGIAIGPWGLGFISDVDEILHFSELGVVFLMFIIGLELNPSRLWQLRRSIFGVGAAQVLLSAAVLAGLLMLADFLWQAAVVGGIGLAMSSTAMALQLMREKGMNRSESGQLGFSVLLFQDLAVIPALALVPLLAGSADEHFDWFKVAMKVLAFAVMLIGGRYLLRPVFRFIAASGVREVFTAATLLLVLSAALFMDALGLSMALGTFIAGVLLAESEYRHELENAIDPFKGLLLGLFFISVGMSLNLGVLYTHLLWVAASVVILVVIKMLTLYLLARLYGIRSSERMQFASVLSQGGEFAFVLFSTASSQRLFQGDQMALLLVTVTLSMMTTPLLMKGIDKWLSRRLNGPEENDEKPWVEDDKPQVIVVGFGRFGQVIARLLMANKMRITVLERDIGAVNLMRKYGYKVYYGDATQVELLRSAGAEAAESIVITCNEPEDTMKLVALCQQHFPHLHILARARGRVEAHELLQAGVTQFSRETFSSALELGRKTLVSLGMHPHQAQRAQLHFRRLDMRMLRGLIPEHSDMVQISRAREARRELEEIFQREMQQERRQLDGWDEFE
|
Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
|
Q5PL21
|
Q5HVY8
|
RPOC_CAMJR
|
Transcriptase subunit beta'
|
Campylobacter
|
MSKFKVIEIKEDARPRDFEAFQLRLASPEKIKSWSYGEVKKPETINYRTLKPERDGLFCAKIFGPIRDYECLCGKYKKMRFKGVKCEKCGVEVANSKVRRSRMGHIELVTPVAHIWYVNSLPSRIGTLLGVKMKDLERVLYYEAYIVENPGDAFYDNESTKKVEYCDVLNEEQYQNLMQRYENSGFKARMGGEVVRDLLANLDLVALLNQLKEEMGATNSEAKKKTIIKRLKVVENFLNSNLNANTDSDEAVPNRPEWMMITNLPVLPPDLRPLVALDGGKFAVSDVNDLYRRVINRNTRLKKLMELDAPEIIIRNEKRMLQEAVDALFDNGRRANAVKGANKRPLKSLSEIIKGKQGRFRQNLLGKRVDFSGRSVIVVGPKLRMDQCGLPKKMALELFKPHLLAKLEEKGYATTVKQAKKMIENKTNEVWECLEEVVKGHPVMLNRAPTLHKLSIQAFHPVLVEGKAIQLHPLVCAAFNADFDGDQMAVHVPLSQEAIAECKVLMLSSMNILLPASGKSVTVPSQDMVLGIYYLSLEKAGAKGSHKICTGIDEVMMALESKCLDIHASIQTMVDGRKITTTAGRLIIKSILPDFVPENSWNKVLKKKDIAALVDYVYKQGGLEITASFLDRLKNLGFEYATKAGISISIADIIVPNDKQKAIDEAKKQVREIQNSYNLGLITSGERYNKIIDIWKSTNNVLSKEMMKLVEKDKEGFNSIYMMADSGARGSAAQISQLAAMRGLMTKPDGSIIETPIISNFREGLNVLEYFISTHGARKGLADTALKTANAGYLTRKLIDVAQNVKITIEDCGTHEGVEINEITADSSIIETLEERILGRVLAEDVIDPITNSVLFAEGTLMDEEKAKILGESGIKSVNIRTPITCKAKKGICAKCYGINLGEGKLVKPGEAVGIISAQSIGEPGTQLTLRTFHSGGTASTDLQDRQVSAQKEGFIRFYNLKTYKNKEGKNIVANRRNAAVLLVEPKIKTPFKGVINIENIHEDVIVSIKDKKQEVKYILRKYDLAKPNELAGVSGSIDGKLYLPYQSGMQVEENESIVEVIKEGWNVPNRIPFASEILVEDGEPVVQNIKAGEKGTLKFYILKGDGLDRVKNVKKGDIVKEKGFFVVIADENDREAKRHYIPRESKIEFNDSEKIDDANTIIASAPKKERKVIAEWDAYNNTIIAEIDGVVSFEDIEAGYSADEQIDEATGKRSLVINEYLPSGVRPTLVIAGKGDKAVRYHLEPKTVIFVHDGDKIAQADILAKTPKAAAKSKDITGGLPRVSELFEARKPKNAAVIAEIDGVVRFDKPLRSKERIIIQAEDGTSAEYLIDKSKHIQVRDGEFIHAGEKLTDGVVSSHDVLKILGEKALHYYLISEIQQVYRGQGVVISDKHIEVIVSQMLRQVKVVDSGHTKFIEGDLVSRRKFREENERIIRMGGEPAIAEPVLLGVTRAAIGSDSVISAASFQETTKVLTEASIAGKFDYLEDLKENVILGRMIPVGTGLYGEQNLKLKEQE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q5HVY8
|
Q9SK02
|
RA51B_ARATH
|
DNA repair protein RAD51 homolog 2
|
Arabidopsis
|
MANKLIGEMGLHTKISNIFAARNIITAKDALSMTEFELMELLDVGMKEIRSAISFISEATSPPCQSARSLLEKKVENEHLSGHLPTHLKGLDDTLCGGIPFGVLTELVGPPGIGKSQFCMKLALSASFPVAYGGLDGRVIYIDVESKFSSRRVIEMGLESFPEVFHLKGMAQEMAGRILVLRPTSLANFTESIQELKNSILQNQVKLLVIDSMTALLSGENKPGAQRQPQLGWHISFLKSLAEFSRIPIVVTNQVRSQNRDETSQYSFQAKVKDEFKDNTKTYDSHLVAALGINWAHAVTIRLVLEAKSGQRIIKVAKSPMSPPLAFPFHITSAGISLLSDNGTELKGPGINTIHARGHSDMINFHGDCS
|
May be involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents.
|
Q9SK02
|
A7NAF3
|
GLMU_FRATF
|
Glucosamine-1-phosphate N-acetyltransferase
|
Francisella
|
MGLSVVILAAGKGSRMNSNKPKVLQTLAAKTLIEHVVSSVEKLNPDNIVVVTGHLKEQVEDALQGRNITFVYQQQQLGTGHAVLQALPYLKEQKVLILYGDVPLISTEVLENLVDTTNDDDLGVLTAFVENPQGLGRIVRDKFGAVTEIVEEKDANDIQRQIKEINTGIYCVHKNLLQKWLPEIKANNVQKEYYLTDIITFAKADHVSINVTHPINEFEILGVNDRTQLASLERVWQRNVAEKIMAKGVSIADPNRFDVRGNLDVGKDCWIDINVIIKGNVKLGNNVVIGANCILKNCIIEDNVRIKSNSMVDGSIIREGAIVGPFARVRPECDVKEGAVIGNFVEAKKTILGKGSKASHLTYLGDSEIGANCNIGAGVITCNYDGVNKHKTVIGDYAFIGSDSQLIAPVNIGQGATVGAGSTIVKDVPADNLAISRARQRHIDTWQRSVKKTDK
|
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.
|
A7NAF3
|
Q5E858
|
LEUC_ALIF1
|
Isopropylmalate isomerase
|
Aliivibrio
|
MSNAKTLYEKIYDAHVAVAAEGENPILYIDRHLVHEVTSPQAFDGLREKGRKVRQVGKTFATMDHNVSTQTKDINASGEMARIQMETLSKNCEEFGVTLYDLNHKYQGIVHVMGPELGITLPGMTIVCGDSHTATHGAFGSLAFGIGTSEVEHVLATQTLKQARAKTMKIDVKGKVAEGITAKDIVLAIIGKTTAAGGTGYVVEFCGEAITDLTMEGRMTVCNMAIELGAKAGLIAPDQTTFDYIAGRKFSPQDADLDAAIEYWSSLKTDDDAEFDAVVTLDASEIKPQVTWGTNPGQVIAVDAPIPAPESFADPVEKASAEKALAYMGLEAGKSLSDYNVDKVFVGSCTNSRIEDMRAAAAIAKGRKVASHVQALIVPGSEQVKAQAEKEGLDVIFKEAGFEWRLPGCSMCLAMNNDRLGPHERCASTSNRNFEGRQGRDGRTHLVSPAMAAAAAIAGHFVDIRTITEQA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q5E858
|
Q00VB2
|
METK_OSTTA
|
Methionine adenosyltransferase
|
Ostreococcus
|
MGFLFTSESVNEGHPDKLADQISDGILDACLEQDPDSKVACETATKTNMVMVFGEITTKAKVDYEAVVRQVCRDVGFISNETGLDGNNCRVLVELHDQSPDIGQGVHGMGTKSLEEIGAGDQGHMFGYATDETPELMPLTHVLATKLGHRLTVVRKDGTCPWVLPDGKTQVTIEYENEGGAMIPKRVHTILISTQHIEGVSNEKIAEDLMNEVIKKVVPEKYLDADTIFHLNPSGRFVIGGPDGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIARQVAKSIVAAGLARRALFQISYAIGVAQPLSIHVDTYGSGKIPDSEILEKVKEKFDFRAGMIGKSLDLKRGGNKRYQTTAAYGHFGRDDTDVFTWEKVVPL
|
Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
|
Q00VB2
|
Q39016
|
CDPKB_ARATH
|
Calcium-dependent protein kinase isoform CDPK2
|
Arabidopsis
|
METKPNPRRPSNTVLPYQTPRLRDHYLLGKKLGQGQFGTTYLCTEKSTSANYACKSIPKRKLVCREDYEDVWREIQIMHHLSEHPNVVRIKGTYEDSVFVHIVMEVCEGGELFDRIVSKGHFSEREAVKLIKTILGVVEACHSLGVMHRDLKPENFLFDSPKDDAKLKATDFGLSVFYKPGQYLYDVVGSPYYVAPEVLKKCYGPEIDVWSAGVILYILLSGVPPFWAETESGIFRQILQGKLDFKSDPWPTISEAAKDLIYKMLERSPKKRISAHEALCHPWIVDEQAAPDKPLDPAVLSRLKQFSQMNKIKKMALRVIAERLSEEEIGGLKELFKMIDTDNSGTITFEELKAGLKRVGSELMESEIKSLMDAADIDNSGTIDYGEFLAATLHMNKMEREENLVAAFSYFDKDGSGYITIDELQSACTEFGLCDTPLDDMIKEIDLDNDGKIDFSEFTAMMRKGDGVGRSRTMMKNLNFNIADAFGVDGEKSDD
|
May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-responsive transcription factors ABF1 and ABF4 in vitro.
|
Q39016
|
A5IYE0
|
ATPL_MYCAP
|
Lipid-binding protein
|
Mycoplasmopsis
|
MEKGLIAIGIGISMISGLGVGLGQGLAAGKAAEAVGRNPEAASKIRTMMLVGQAVAESAAIYALVISILLMFAFN
|
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
A5IYE0
|
P24045
|
GBRB4_CHICK
|
GABA(A) receptor subunit beta-4
|
Gallus
|
MWTFQADRLSGIVSALAALCVACCAQSPSTGNISVVKEIVDKLLKGYDVRLRPDFGGNPVTVGMSIHISSIDQISEVNMDYTITMYFQQSWRDKRLAYNDLPLNLTLDNRVADQLWLPDTYFLNDKKSFLHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDQQNCTLEIESYGYTVDDIVFFWQGNDSAVTGMEVLELPQFTIIEQRLVSREVVFTTGSYLRLSLSFRIKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGVTTVLTMTTINTHLRETLPKIPYVKAIDVYLMGCFVFVFLALLEYAFVNYIFFGRGPRQQKKQSERISKANNERHRYEEKRVREQVDPYGNILLSTLDMNNELLATDMMSSVGDSRNSVMSFEGSGIQFRKPLASRDGFGHHPTLDRHVPLTHHAAARNRANCRLRRRSSKLKLKIPDLTDVSTIDKWSRIIFPITFGFFNLVYWLYYVN
|
GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
|
P24045
|
Q54LP7
|
UB2J2_DICDI
|
E2 ubiquitin-conjugating enzyme J2
|
Dictyostelium
|
MSTQVCVTRLKKELLALSKNEDIKDIFIAKPSISNILEWHYVIYGPPDTPYHGGYYHGQIIFPVEYPYKPPSILMTTPSGRFVCNSRICTSMSDFHPDTWSPFWSNCTIILGLISFMTEDENGFGSIVKSKETRKQLASQSMAFNLKNPVFVKLFPELISDYKKKGTFYSSSSTPSSTPPPSSTPSSSSSSSNISKRNVPIPTTKTTPQDTNKKKEQKNNNIPYIILFIALIIILLYLFLK
|
Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum.
|
Q54LP7
|
A6NKD2
|
TSPY2_HUMAN
|
Testis-specific Y-encoded protein Q1
|
Homo
|
MRPEGSLTYRVPERLRQGSCGVGRAAQALVCASAKEGTAFRMEAVQEGAAGVESEQAALGEEAVLLLDDIMAEVEVVAEEEGLVERREEAQRAQQAVPGPGPMTPESALEELLAVQVELEPVNAQARKAFSRQREKMERRRKPHLDRRGAVIQSVPGFWANVIANHPQMSALITDEDEDMLSYMVSLEVEEEKHRVHLCKIMLFFRSNPYFQNKVITKEYLVNITEYRASHSTPIEWYPDYEVEAYRRRHHNSSLNFFNWFSDHNFAGSNKIAEILCKDLWRNPLQYYKRMKPPEEGTETSGDSQLLS
|
May be involved in sperm differentiation and proliferation.
|
A6NKD2
|
Q6DJ55
|
FAKD4_XENTR
|
Transforming growth factor beta regulator 4
|
Silurana
|
MAARLVQRCSRLLAASTAYAPATHTHIHECMKVCHPAQPVLPCSSLHSSSLCRHKDKALTKEQTVSSVPEHGKFESVLESLSSVEELLQLGVDREISGNQAAMIITQVSKVLMESKAQGGSVVQDERFQQLLVQAHNQISTIWNGNLVSLLKRLYILGIREDNKQLQAVENEVRWRLRRLSFKSLVQLSDLYVTFTRSPEQKHLVSDLVKNLELRWTEIEDAKSVVTLMTRVGFISKALMEKLEDKALEYAEQFTPDEMRKVALALAAQNRRTVPLLRALSYHLVQRHIGLSPAVVVDLAFAYGKLNFHQTQVFQKMASDLLPKVPEMSANDIARCVKSFAYLKWSNLPLFEAFAQASIDQSEKFTVPQLCNLVLAFGRLNFQPSKREEFYSMMHQKLHAELDLLDPYLLVDIVWSLCVLRQVDSSYISKVLEPGLYSRFFTDSSPRSANYRLKLAHINATALLEHPEYTGPHLPNESISTTHAVTANRKLSPLQSGLQEVLRELFPVEGTCRCGVNTVYGWYIDGEVVLDSDNKPLSLMDLEAPHLPHSQGKKPLPEGTRRFAFVAWDFPNFNSRSKDLLGRFVLTRRHLQAAGFLVVEVPYYEWLDLKSEWQKSAYLKDKINKVVAEEMAR
|
Plays a role in processing of mitochondrial RNA precursors and in stabilization of a subset of mature mitochondrial RNA species. May play a role in cell cycle progression.
|
Q6DJ55
|
A8AR83
|
RSMJ_CITK8
|
rRNA (guanine-N(2)-)-methyltransferase
|
Citrobacter
|
MKICLVDETGAGDGALSVLAARWGLEHDENNPMALVLTTAHLELRKRDEPKLGGIFVDFVGGAMAHRRKFGGGRGEAVAKAVGIKGDYLPDVVDATAGLGRDAFVLASVGCRVRMLERNPVVAALLDDGLARGYADPEIGPWLQERLQLIHASSLTALTDITPRPQVVYLDPMFPHKQKSALVKKEMRVFQSLVGPDLDADGLLAPARQLATKRVVVKRPDYAPPLADIATPNAVVTKGHRFDIYTGTALVE
|
Specifically methylates the guanosine in position 1516 of 16S rRNA.
|
A8AR83
|
A6W3A2
|
RL1_MARMS
|
50S ribosomal protein L1
|
Marinomonas
|
MAKLTKRARLIAEKVEATKLYSVEEAVALLSELSTVKFKESIDVSVNLGVDPRKSDQVVRGSTVLPHGAGKDVRVAVFAQGANAEAAKEAGADVVGFEDLAEQVKAGNLDFDVVIASPDAMRIVGQLGQVLGPRGLMPNPKVGTVTPDVATAVRNAKAGQARYRTDKNGIIHAAVGSIEFAADAIRGNLEALLTDLRRAKPASSKGVYLRKVTLSSTMGPGLQIDLGALNSTK
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
A6W3A2
|
Q8VCZ7
|
ZBT7C_MOUSE
|
Zinc finger and BTB domain-containing protein 36
|
Mus
|
MANDIDELIGIPFPNHSSEVLCSLNEQRHAGLLCDVLLVVQEQEYRTHRSVLAACSKYFKKLFTAGSLASQPYVYEIDFVQPEALAAILEFAYTSTLTITASNVKHILNAARMLEIQCIVNVCLEIMEPGGSVGEEDDKEEEDEDDDDEDEDDEEEEEEEEEEEEDDPEDFADQENLPDPQDITCPQSPSKTDHLTEKDYSDTPRDFPDSFQPGSPGHLGVIRDFSIESLLRENLYPKANIPDRRPSLSPFAPEFFPHLWPGGFGAFAQLPEQPMDSGPLDLVIKNRKIKEEDKEELAPPPPPPFSSDFFKDMFPDLPGGPLGPIKAENDYGAYLNFLSATHLGSLFPPWPLVEERKLKPKASQQCPICHKVIMGAGKLPRHMRTHTGEKPYMCSICEVRFTRQDKLKIHMRKHTGERPYLCIHCNAKFVHNYDLKNHMRIHTGVRPYQCEFCYKSFTRSDHLHRHIKRQSCRMARPRRGRKPAAWRAASLLFGPGGPSADKAAFVMPPALGDVGGHLGGTAVCLPGPSPAKHFLASPKGTLSLQELERQFEETQMKLFGRAQLEAERNAGGLLALALAENVAATRPYFPLPDPWAAGLAGLPGLTGLNHVASMSEANN
|
May be a tumor suppressor gene.
|
Q8VCZ7
|
Q47AK9
|
MURA_DECAR
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Dechloromonas
|
MDKLLIEGGKVLSGEVAMSGAKNAALPILCASLLTSDPVHFTNVPHLNDISTMLRLLGDMGVGVTMDGIDGIVLNGGGLNNPVASYEMVKTMRASILVLGPLVARCGEARVSLPGGCAIGARPVDQHIKGLQAMGAEVKVEQGYVHAKATRLKGARICTDMVTVTGTENLMMAACLAEGETVIENAAREPEVVDLANCLVSMGARISGAGTDVIRIQGVDKLHGATHAIMPDRIETGTYLCAAAATGGDIRLLKTSAAYLDTVVDKLMDAGCEITVERDAIRLVAPKRLKAVSLRTAPYPAFPTDMQAQFMAINCIADGVATIRETIFENRFMHVNELMRLGANIQIEGNNAIVRGVDRLEGATVMATDLRASASLVIAGLVAQGETVIDRIYHLDRGYERIEEKLAKLGAAVRRVH
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q47AK9
|
Q9FKE9
|
RHD32_ARATH
|
Protein SEY1 homolog 3
|
Arabidopsis
|
MGENDDGCSTQLIDGNGEFNVKGLDNFVKKTKLSDCGLSYAVVAIMGPQSSGKSTLLNHLFKTSFREMDAFAGRSQTTKGIWMARCVGIEPFTIAMDLEGTDGRERGEDDTTFEKQSALFAIAVADIVLINMWCHDIGREQAANKPLLKTVFQVMLRLFSPRKTTLLFVIRDKTKTPIELLERALREDIQKIWDSVRKPEAHKNTPLNEFFNVMIVALSSYEEKEKQFEQEVAELRQRFFHSISPGGLAGDRRGVVPASGFSFSSQQIWKVIKENRDLDLPAHKVMVATVRCEEIANEKLRDLATNESWLELHEAAEGGLVPGFGKKLSSILEKYFSEYDAEAIYFDEGVRKEKRLQLKLNALDFVYPSYATMLGHLRSNALESFKIRLEQSLNQGEGFAKAVRDSQQSCLMVFDKGCEDAAVKQATWDASKIREKLCRDIDAHTFFARSAKLSELTANYEKRLTQALSEPVESLFEAGGKETWPSIRKLLKRETETAVTDFLDVVTGFELDHAKIDAMVQNLKNYSQSLVEKKAREEAAKILIRMKDRFSTVFSHDKDSMPRVWTGKEDIRAITKDARAEALSLLSVMTAIRLDERPDNIESTLFSSLMDGTVSAASSHNRSVGTSTDPLASSSWEEVPPNNILLTPVQCKSLWRQFKSETEYTVTQAISAQEAHKRNNNWLPPAWAIVLMIVLGFNEFMMLLKNPLYLLGFFVAFLLSKALWVQLDIPREFQHGAVAGVLSITSKFLPTVMNLLRKLAEEAQGKTTQEVPDLSASQTYRQQSPSHSISSTISESVASNISSAGDDAEYSSPSPALVRRRNTNNVQESEISQM
|
Probable GTP-binding protein that may be involved in cell development.
|
Q9FKE9
|
Q99PW8
|
KIF17_MOUSE
|
Kinesin-like protein KIF17
|
Mus
|
MASESVKVVVRCRPMNKRERELSCQSVVTVDSARGQCFIQNPGAADEPPKQFTFDGAYYIEHFTEQIYNEIAYPLVEGVTEGYNGTIFAYGQTGSGKSFTMQGLPDPPCQRGIIPRAFEHVFESVQCAENTKFLVRASYLEIYNEDVHDLLGADTKQRLELKEHPEKGVYVKGLSMHTVHNVAQCERVMETGWKNRAVGYTLMNKDSSRSHSIFTINIEIYAVDERGKDHLRAGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGRCKHIPYRDSKLTRLLQDSLGGNTKTLMVACLSPADNNYDETLSTLRYANRAKNIKNKPRINEDPKDALLREYQEEIKRLKAILAQQMGPGNLSALLSTQTPPGPVQSEEKLLSPTTVQQDTEAEKQLIREEYEERLARLKADYEAEQESRVRLQEDITAMRNSYDVKLSTLQENLRKEKETEAILKAEVLCKTEVMSRAELASGPEYSPPLQYETAVKPTILSMPDMPPSGKVTKSQAPLAFEEPHGETSRSEFSFESNECSTLEDSATSEAFPGPEEFSNMEFSMAAALTESRYLPEEYLGGQEAAASPLEAERYVQENEPSLEPLRILASLQDPFAEVEAKLARLSSTVAMSDSSQTVVPQIPKQPSSADLLEPSDTKSEADVAVADNVVLGTEPDVNLRVAEEVVSEAETGVWMESEAQVAHVAQVSEEAQPQPLLAMVSVRRESVGVEVAVLTEEELQPVDQQQVLARLQLLEQQVVGGEQAKNKDLREKHKRRKRYADERKKQLVAALQNSDEDGGDWVLLNVYDSIQEEVRAKSKLLEKMQRKLRAAEVEIKDLQSEFQLEKIDYLATIRRQERDSMLFQQLLEQVQPLIRRDCNYSNLEKIRRESSWDEDNGFWKIPDPIILKTSLPVVPTGTQNKPARKTSAVDSGEPHMQEEDRYKLMLSRSDSENIASNYFRSKRASQILSTDPMKSLTYHNSPPGLNSSLSNNSALPPTQTPEMPQPRPFRLESLDIPFSKAKRKKSKNSFGGEPL
|
Dendrite-specific motor protein which, in association with the Apba1-containing complex (LIN-10-LIN-2-LIN-7 complex), transports vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules.
|
Q99PW8
|
A9VWE8
|
ACCD_METEP
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
|
Methylorubrum
|
MVEPMNWISEVVRPRIKTLFKRETPENLWVKCPDTGQMVFHKEVEQNHWVIPGSEHHLKMSATARLKMMFDEGTWIDVPLPEVPADPLKFRDEKRYVDRLKEARAKTGMPDAFKIGFGRVGSLPMTIAAQEFGFMAGSLGMAGGEAFVRGAETALEKRTPYVLFAASGGARMQEGILSLMQMPRTTVAVRRLRAARLPYIVVLTNPTTGGVTASYAMLGDVHLAEPGALICFAGPRVIEQTIREKLPDGFQRAEYLREHGMVDQVVHRHQLKETISRLCGLLMDVRRTPEPGTAPEPTTPEPLPNAA
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.
|
A9VWE8
|
A9HDM8
|
ATPL_GLUDA
|
Lipid-binding protein
|
Gluconacetobacter
|
MDIAAAREIGAGIAVIALAGVGIGLGNIFSTLVSSIARNPAARPHVFGLGMLGFALTEAVALYALLIAFLILFV
|
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
A9HDM8
|
B9L6Y8
|
LEUC_NAUPA
|
Isopropylmalate isomerase
|
Nautilia
|
MPMTITEKIFAEHIGREVKPGEIIMCDVDMTIGNDITTPISIRAFNESGAEKLAKPDNFAIVLDHFIPPKDIASANQAKINRDFAYKHDLKNFFDEKDMGIEHRLLPEKGLVIPGDVIIGADSHTCTHGALGAFSTGMGSTDIAFCMITGKSWFKIPESIKVVFKGERGEHVYGKDLILELIRRIGVDGALYKALEFTGEVIENLPMDDRMSLCNMAIEAGAKNGIVAYDKITEAFLEEVKKYNPLRSEPKIHYSDPDANYSQVIEIDVNKLEPLVAYPFLPSNGKPISQAVKDDIEIDQVYIGSCTNGTLSDLRIAAEILKGKRVHRRVRLIVTPATQRIYKQAEHEGILDILIDAGAVVANPTCGACLGGYMGILGDGERAVATTNRNFRGRMGSRSSEVYLSNSAVAAASAIAGKIADPRDL
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
B9L6Y8
|
B2HII2
|
LEUD_MYCMM
|
Isopropylmalate isomerase
|
Mycobacterium
|
MEAFDTHTGIGVPLRRSNVDTDQIIPAVFLKRVTRTGFEDGLFASWRSDPSFVLNLSPFDRGSVLVAGPDFGTGSSREHAVWALMDYGFRVVISSRFGDIFRGNAGKAGLLAAEVDQDGVELLWKLIEQSPGLEITVNLQDRNVIAGTVVLPFRIDDHTAWRLLEGLDDIALTLRKLDEIEAYEAAYPAWKPRTLPTS
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
B2HII2
|
Q6KCJ3
|
RECA_ENTMU
|
Recombinase A
|
Enterococcus
|
MADDRKAALDAALKKIEKNYGKGSIMKLGEKIDQQISTIPSGSLALDVALGIGGYPRGRIIEVYGPESSGKTTVALHAIAEVQKNGGTAAFIDAEHALDPQYAQKLGVNIDELLLSQPDTGEQGLEIADALVSSGAVDIVVIDSVAALVPRAEIDGEMGDSHVGLQARLMSQALRKLSGSINKTKTIAIFINQIREKVGVMFGNPEITPGGRALKFYATIRLEVRRAEQLKQGTDIVGNRTKIKVVKNKVAPPFKIAEVDVMYGLGISQEGELLDMAVEKDIVDKSGAWYSYKEDRIGQGRENAKIYMSNHPEMMAEVSTLVRAAYGIGEPVDVPQEAQEELPLDE
|
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
|
Q6KCJ3
|
Q2T4P1
|
THAQ_BURTA
|
Polyketide synthase ThaQ
|
pseudomallei group
|
MRRAMRDGGKPDRIGAAAPLRRAPLTATSGIDMNVQESIFPITPNGFAGHSMDDLMQRWLLAQLQATGILADGRAHAFDALAGRVQPLYRRWLEESLRLLRDAGLVRDDAQGWRAAERAPIDARDAQRHWDASRDAWLADRERAVYVVLIEAVLAQLPAILTGRRRATDVLFPNGSMARVQGVYTGNHVSDHFNRVLVDHAVRYVAGCAARRADAKLRFIEVGAGTGGTTEGLLAALAPHARHVGEYCFTDISKAFLNHAQRRFGEGAPFFGARVLDIEQPIDAQGFEPGAYDALVATNVLHATRDIRTTLRHCKALLKHNGLLFINEMTGSVPYLHLTFGMLEGWWRFTDDALRVAGCPAVAPQTWDRVLREEGFSSVIFPARDAHGQGQQIVIAQNDARRAGSARRDARASNGDAQHGARHEAAHDAQQDASGDTQADAHDSAHDSAHDSAHDSAHDSAHDSAHAAAALRREGRAYLRARAAELLGMPAGAIDPDEGLHAYGLDSILASQFAAQLAEAFDGFDGALLFEHKTINALLDHLLAAHADALARLLPPAGGAPARGVGARAQAAQASGEGRAAPPAAPHADARSDTPSSAPSSAPARPDQPAPSGPPAQPAQPAPRADTPPPAASAGHRGEARASDTRYAPRAPHPDAAAEPVAIIGISGRYPGAYDVPAFWRNLLAGACAITEVPAERWDWRAHYRADAAEAAREGKSYSKWGGFVDDVGRFDPAFFGMTPQDAQHTDPQELLFLEMCWHALQDAGQTPALLPGDVRRRAGVFAAITKHYAFPPTSFASLANRVSHALDFGGKSLAIDTMCSSSLVAVNEAWEYLQRDGRLAVVGGVNLYLDPQQYAHLSRFRFASSGPVCKAFGEGGDGFVPGEGAGAIVLKRLSDAERDGDPIHAVIRGCAVNHNGRSTSFTASDPARQADVVRDALTRAGVDPRTIGYVEAAANGHAMGDAIEMTGLGKVFAACDGVSGTRAIGSVKANIGHCEAASGMSQLTKVVMAMRDGVLAPTLRDGTRNPNIAFERLPFEVQEQAAPWRRLIVDGSEVPRRAGVTSIGGGGVNAHVVLEEYVAPPRAARPGAGTDDEVLFVLSARTREQLGAYAERWAGYLEAHPDCDVDAIAHTVRTAREPMAHRLAVLAHGRGELAALLRGWAAGGAASGAASGAASDQVFYGDVKQHRVVLSDALVQAARREGAASLAKLWVLGNALGAAHGADEPAPRRVGLLPPYPFERRLVWTSAHAPGTRHASAGEATEAAEAAEAAEAGAAAVAESAEAGAPAAAGDARLQPAPASNAEAFYSLSTLNASKDFQEQYLTLCPFPERIPGFSMTRMFIEPQKYPNEFALMQARQIEMRQVLFGREHFERISRVLDIGCGMGTDVIQLAKRFAHLRTTGYTITRAQAELGAGRIAREGLQGRAEIRHGDSAKDPFPGKYDLVIGIEVICHIQDKHGVFGNIARSLDDDGHVLLMDFVANGRGRISSPEIDIDIGTRQDWIDVAAAHGLVVDEVIDVSPQIANFLHDPEHERNIAALPGVAQASFRNFANTCVSLEKGWVSYCLLRLSKASRLSEAERRRLNAERFGASVAYPDALKAMHARGPAPYPRSPDAQPPAARAQAGVDGGVEASAPAGVKADSKAGPKSEVKSDAAARASRADIAASVAASVAASVEDAFEASLGLRRADLERADDLRALGIGSIQAVMLAEAINERLDLALPSRFVLEHATFGALVRAVAEAVAGGRGSSRDAPARELAYLSLLEPGGAMTAELLELPGGARAEILRGGRGPRVVLIPGLGMAGTVFRDLCRALTRRHEVIVYHYPGLGRSDPVAPIDVDAAAAHLYRTLDACGGDGAAALLGWSFGGVIAQRAALMRPRAWRALVLVNTLGAYRPLAPQFLTPGASRDGEPRGLGGLYQTDLDFVFAGDAPPAALARKDACAALMRDSLALDAAQAIDYLDALVRFDATAQLPSLRMPTLVVAGTADHFGDPAHAEQLVSLIPNARLARIAGAGHAVFLTHGEAFEPAVLAFLDETLRAAEAGGAAESVESVEATEAAEAARSPAVARRRATDDAPVGSDA
|
Involved in production of the polyketide antibiotic thailandamide.
|
Q2T4P1
|
Q8R7W1
|
RL16_CALS4
|
50S ribosomal protein L16
|
Caldanaerobacter
|
MLMPKRVKYRKQQRGRIKGNATRGNTLTYGEYGLQALEPGWITATQIEAARVAMTRYIKRGGKVWIKIFPDKPVTKKPAETRMGSGKGSPEFWVAVVKPGRVLFEIGGVSEDVAKEALRLAMHKLPIKTKFLKREELGGESNES
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q8R7W1
|
P35088
|
TXLA_SYNE7
|
Thiol:disulfide interchange protein TxlA
|
Synechococcus
|
MTADNSVPSRLRNILVIAAALVLTILVVLGSRQPSAAASLASLAEQATPYEVAIANDRPMLLEFYADWCTSCQAMAGRIAALKQDYSDRLDFVMLNIDNDKWLPEVLDYNVDGIPQFVYLNGQGQPQGISIGELPRSVLAANLDALVEAQPLPYTNARGNLSEFSADLQPSRSSQTDPRSHSGQVQDGVLD
|
Required for disulfide bond formation in some proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process.
|
P35088
|
Q9D8M7
|
PHF10_MOUSE
|
BRG1-associated factor 45a
|
Mus
|
MTAAGPGAAPSPGRCDSDPASPGAQSPKDDNEDNSNDGTHPCKRRRMGSGDSSRSCETSSQDLSFSYYPAENLIEYKWPPDETGEYYMLQEQVSEYLGVTSFKRKYPDLERRDLSHKEKLYLRELNVITETQCTLGLTALRSDEVIDLMIKEYPAKHAEYSVILQEKERQRITDHYKEYSQMQQQSTQKVEASKVPEYIKKAAKKAAEFNSNLNRERMEERRAYFDLQTHVIQVPQGKYKVLPTDRTKVSSYPVALIPGQFQEYYKRYSPDELRYLPLNTALYEPPLDPELPALDSDGDSDDGEDGGGDEKRKNKGTSDSSSGNVSEGDSPPDSQEDTFHGRQKSKDKMATPRKDGSKRSVLSKSAPGYKPKVIPNALCGICLKGKESNKKGKAESLIHCSQCDNSGHPSCLDMTMELVSMIKTYPWQCMECKTCIICGQPHHEEEMMFCDVCDRGYHTFCVGLGAIPSGRWICDCCQRAPPTPRKVGRRGKNSKEG
|
Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth.
|
Q9D8M7
|
A0QLP6
|
CH602_MYCA1
|
Chaperonin-60 2
|
Mycobacterium avium complex (MAC)
|
MAKTIAYDEEARRGLERGLNALADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQALVREGLRNVAAGANPLGLKRGIEKAVEKVTETLLKSAKEVETKDQIAATAAISAGDQSIGDLIAEAMDKVGNEGVITVEESNTFGLQLELTEGMRFDKGYISGYFVTDAERQEAVLEDPFILLVSSKVSTVKDLLPLLEKVIQAGKPLLIIAEDVEGEALSTLVVNKIRGTFKSVAVKAPGFGDRRKAMLQDMAILTGGQVISEEVGLSLESADISLLGKARKVVVTKDETTIVEGAGDSDAIAGRVAQIRTEIENSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALLHAIPALDELKLEGDEATGANIVRVALEAPLKQIAFNGGLEPGVVAEKVRNSPAGTGLNAATGEYEDLLKAGVADPVKVTRSALQNAASIAGLFLTTEAVVADKPEKAAAPAGDPTGGMGGMDF
|
Together with its co-chaperonin GroES, 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.
|
A0QLP6
|
Q11GC0
|
APT_CHESB
|
Adenine phosphoribosyltransferase
|
unclassified Chelativorans
|
MKQSLEDTLLAAIRTIPDYPRPGILFRDITTLLGDARAFRRAVDELVHPYAGAKIDKIAGIEARGFILGGAIAHQLSSGFIPIRKKGKLPHETVRVAYSLEYGLDEMEMHIDAVSPGEKVILVDDLIATGGTAEAAVRLLRQMGAEIVAACFVIDLPDLGGRAKLEAEGVDVRTLVSFEGH
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
Q11GC0
|
A8EXA8
|
RS18_RICCK
|
30S ribosomal protein S18
|
belli group
|
MLKSNNTSEATTRKVGDKTAKKVFFRRRKGCPLSVPNAPVIDYKNPELLIKFVSEGGRMLPSRITNVCAKKQRKLNNAIKIARILALLPFVFQAK
|
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
|
A8EXA8
|
B8J874
|
RS8_ANAD2
|
30S ribosomal protein S8
|
Anaeromyxobacter
|
MSFTDPIGDMLTRIRNASSARHEKVLVPASRLKVRIAEVLREEGFIKDFVLHEDGVQGAITIVLKYSADREPAISDIKRVSKPGLRRYVATDSIPRVLNGMGVAILSTSKGVMVDREARKQKVGGELICTVW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
B8J874
|
B7IS18
|
RS6_BACC2
|
30S ribosomal protein S6
|
Bacillus cereus group
|
MRKYEIMYIIRPGVEEEAQKALVERFAGVLTNNGAEIINTKEWGKRRLAYEINDLREGFYMILNVNSNAEAINEFDRLAKINEDILRHIVVKEEEK
|
Binds together with S18 to 16S ribosomal RNA.
|
B7IS18
|
Q8IUI8
|
CRLF3_HUMAN
|
Type I cytokine receptor-like factor p48
|
Homo
|
MRGAMELEPELLLQEARENVEAAQSYRRELGHRLEGLREARRQIKESASQTRDVLKQHFNDLKGTLGKLLDERLVTLLQEVDTIEQETIKPLDDCQKLIEHGVNTAEDLVREGEIAMLGGVGEENEKLWSFTKKASHIQLDSLPEVPLLVDVPCLSAQLDDSILNIVKDHIFKHGTVASRPPVQIEELIEKPGGIIVRWCKVDDDFTAQDYRLQFRKCTSNHFEDVYVGSETEFIVLHIDPNVDYQFRVCARGDGRQEWSPWSVPQIGHSTLVPHEWTAGFEGYSLSSRRNIALRNDSESSGVLYSRAPTYFCGQTLTFRVETVGQPDRRDSIGVCAEKQDGYDSLQRDQAVCISTNGAVFVNGKEMTNQLPAVTSGSTVTFDIEAVTLGTTSNNEGGHFKLRVTISSNNREVVFDWLLDQSCGSLYFGCSFFYPGWKVLVF
|
May play a role in the negative regulation of cell cycle progression.
|
Q8IUI8
|
B0SH18
|
IF2_LEPBA
|
Translation initiation factor IF-2
|
Leptospira
|
MEEQKSIKETLQQGASGDKTKKKLVIKKKAAPSDEKKESSPGAQGQTTATEAKQSSPASSDKKKDLNELIREEAKRQGLGSGPQAPSQASPIVSRPDRKPEPLPQPDREKAPMDRKPESILSGDTSSPNFRSGGGQGGGNQGYFRKEDRNPIVSRPTTPRPPRPEGQTGGGYQGNRGPGQGGGYQGNRGPGQGGPGGYQGNRGPGQGGPGGYQGNRGPGQGGPGGYQGNRGPGQGGPGGYQGNRGPGQGGPGGYQGNRGARPIGQGGPGSGRPPGDAPFGAPGGLPGAGGPGGAKKRVFDKEKGGREENENTKFFKQSFRKQKAQAAALAAVPKEISILENIQVGEIAKKLNLKPGEVISKLMKMGMMVTINNVIDAETASILADDYGCKVKIVSLYDETVIEEEKDAPEDYITRPPVVTIMGHVDHGKTKLLDTIRSSRVAEGESGGITQHIGAYQVETERGKIAFLDTPGHEAFTSMRARGASVTDIVVLVVAADDGVMPQTIEAINHAKEAEVPIIVAVNKIDLPAANPEKVRQELSNYGLQPEEWGGTTIFCDISAKSNIGIDKLLEMLIIQAELLDHKANPKRKAKGTIVEAKLDPGRGAVATVLIQNGTLRVGDAFVAGVHAGRVRAMYDDLGRSIKEAGPSFPALVTGLDGVPDAGAPFDVVIDDKEARTISHSRQEYERLGQSKNAATRVTLDNMSEIIKQGALKELKVIIKADVRGSTEAVKEALEKLSTADVRLNVIHAGTGAIVDSDIILASASNAIVIGFHTRANPKTVSLAEKEKVEIKYYSIIYDVVNEVKASMEGMLEPEKVENIIGKVEIRDVFKISKVGNIAGCMVKSGKVTKQAHVRVISSETGEITWEGKIKNLKRMKDDVADVLTGFECGILLDGFNDFSVGDEIEAYEIREIARKL
|
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.
|
B0SH18
|
C3NEU3
|
VATA_SULIY
|
V-ATPase subunit A
|
Sulfolobus
|
MNNGRIVRINGPLVVADNMKNAQMYEVVEVGEPRLIGEITRIEGDRAFIQVYEDTSGIKPNEPVYRTGAPLSIELGPGLIGKIFDGLQRPLDSIKELTKSPFIARGIKVPSVDRKTKWHFIPKVKKGDKIEGGDIIGIVNETPLVEHRILVPPYVHGTLKEIVAEGDYTVEDPIAVVDMNGDEAPIRLMQRWPVRIPRPFREKLEPTEPLLTGTRVLDTIFPIAKGGTAAIPGPFGSGKTVTLQSLAKWSAAKIVIYVGCGERGNEMTDELRQFPSLKDPWTGRPLLERTILVANTSNMPVAAREASIYVGITMAEYFRDQGYDTLLVADSTSRWAEALRDLGGRMEEMPAEEGFPSYLPSRLAEYYERAGRVKTVGKPERFGSVTVASAVSPPGGDFTEPVTSQTLRFVKVFWPLDVSLAQARHYPAINWLQGFSAYVDLVANWWNTNVDPKWREMRDMMVRTLIREDELRQIVRLVGPESLAEKDKLVLETARLIKEAFLKQNAYDDIDAFSSPQKQARVMRLIYLFNTHASRLVERGIPTKKIVDSMGQLLPEIIRSKAAIKNDELNKYDELERKLINVFENLEKEAGT
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal alpha chain is a catalytic subunit.
|
C3NEU3
|
B1H369
|
HDAC8_XENTR
|
Protein decrotonylase HDAC8
|
Silurana
|
MEESLLPVYIHSAEYVELCDNVQSKVPRRASMVHSLIEAYGLLKEMRVVKPKVASMEEMAAFHTDSYLQHLHKVSEEGDNDDPETLEYGLGYDCPITEGIYDYAAAVGGATLTAAEQLMAGKTRIAINWPGGWHHAKKDEASGFCYLNDAVLGILKLREKFDRVLYVDMDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDIGLGKGRYYSVNVPLQDGIQDEKYYQICEGVLKEVFTTFNPEAVVLQLGADTIAGDPMCSFNMTPQGIGKCLKYVLQWQLPTLILGGGGYHLPNTARCWTYLTALIVGRTLSSEIPDHEFFTEYGPDYVLEVTPSCRPDRNDSQKVQEILQSIKGHLKQVV
|
Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of non-histone proteins. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones.
|
B1H369
|
Q863G2
|
COX8A_NYCCO
|
Cytochrome c oxidase subunit 8-2
|
Nycticebus
|
MSVLTPLLLRGLTGSARRLPMPCARVHSKPPREQLGTMDIAIGLTSCFVCFLLPSGWVLSHLENYKKRE
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
Q863G2
|
P84890
|
ITRY_ARCEL
|
Trypsin inhibitor AeTI
|
Archidendron
|
AKELLDSDGIILRNGANYYI
|
Competitively inhibits trypsin stoichiometrically at the molar ratio of 1:1. Also inhibits chymotrypsin.
|
P84890
|
Q5LUD3
|
SYP_RUEPO
|
Prolyl-tRNA synthetase
|
Ruegeria
|
MRLSRYFLPVLKENPAEAQIVSHRLMLRAGMIKQAQAGIYSWLPLGFKVLRKLENIVHEEQIRAGHIPMLMPTLQSADLWRESGRYDDYGQEMLRITDRHGRDMLFGPTNEELITDIFRGHVSSYKDLPLTLYHIQWKFRDEIRPRFGVMRGREFLMKDGYNFDLTKEDALHAYNRHLVSYIRTYERMGLQAIPMRADSGPIGGDDTHEFLVLAETGESEVFYDSKVTDIRLGEREIDYDSVDQCRAVMEEFTSLYARTDETHDEAVFNQIPEERRRSARGIEVGQIFYFGTKYSEPMGATVQGPDGKPVPVHMGSHGIGVSRLIGAIIEASHDDKGIIWPEGVTPFHCGIVNLKQGDGEADAACDQLYAALSAIGLEPLYDDRNERAGGKFATMDLIGLPWRITVGPRGLKNGVVELTSRKTGESVELSPEEAVKKVADIYAPHHPHLSREEPMAGRSFHTWL
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro).
|
Q5LUD3
|
A4YNP1
|
BCHN_BRASO
|
Light-independent protochlorophyllide reductase subunit N
|
unclassified Bradyrhizobium
|
MNAHAQACAVTSSSPDGVLRERGQREVFCGLTGIVWLHRKIQDAFFLVVGSRTCAHLIQSAAGVMIFAEPRFATAIMEERDLAGLVDANDELDRIVAQLLARRPDIKLLFLVGSCPSEVIKLDLSRAALRLSQRFSPGVRVLNYSGSGIETTFTQGEDACLAALVPVLPSADRNARPSLLVVGALADVVEDQFKRTFAALGIDNVAFLPPRRSSELPAIGPETRVLLAQPFLGDTARALEERGCRRISAPFPLGGEGTALWLAAAADAFGVSRAHVERTLAPLKARAEKALARYRAQLAGKRVFLFPDSQIEIPLARFLAREIGMELVEVGTPYLHRDHLAAELPMLPAGTLLSEGQDVERQLDRCREARPDLVVCGLGLANPLEAEGLTTKWSIELIFTPIQGFEQAGDLAELFARPLLRQTRLAV
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
|
A4YNP1
|
B1MVP6
|
LUXS_LEUCK
|
Autoinducer-2 production protein LuxS
|
Leuconostoc
|
MSETVVESFTLDHTKVKAPYVRVIETQSGPNGGTITNYDLRLTQPNETAIETGGLHTLEHLFAGLVRDEIDGIIDMSPFGCRTGFHVISWVNYDSETLAKVFKKVLEKIASDDITEVPAAEIESCGNYKDHSLHSAKEWAKLILAQGISSDAFERHVV
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
B1MVP6
|
Q1H4N2
|
RL22_METFK
|
50S ribosomal protein L22
|
Methylobacillus
|
MEVSAVLRGVHLSPQKARLVADLVRGKKVDQALNILAFTPKKGAEVIKKVVESAIANAEHNEGADIDELKVTSIYVDKGLVLKRIRARAKGRAGRIIKPTCHITVTVGN
|
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.
|
Q1H4N2
|
Q18CB2
|
DISA_CLOD6
|
Diadenylate cyclase
|
Clostridioides
|
MENFLDNKNMLYALKMISPGTPLRLGLNNVLRAKTGGLIVIATNEDVMKIVDGGFAINAEYSPSYLYELAKMDGAIVLSGDVKKILFANAQLIPDYFIETSETGTRHRTAERVAKQTGAIVIGISQRRNVITVYRGNEKYVVEDISKIFTKANQAIQTLEKYKTVLDQAVTNLNALEFNDLVTIYDVALVMQKMEMVMRVTSIIEKYVIELGDEGTLVSMQLEELMGTTRIDQKLIFKDYNKENTEIKELMKKVKNLNSEELIELVNMAKLLGYSGFSESMDMPIKTRGYRILSKIHRLPTAIIENLVNYFENFQQILDASIEELDEVEGIGEIRATYIKNGLIKMKQLVLLDRHI
|
Has also diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) . c-di-AMP acts as a signaling molecule that couples DNA integrity with progression of sporulation. The rise in c-di-AMP level generated by DisA while scanning the chromosome, operates as a positive signal that advances sporulation; upon encountering a lesion, the DisA focus arrests at the damaged site and halts c-di-AMP synthesis.
|
Q18CB2
|
A3PN50
|
PLSY_CERS1
|
Lysophosphatidic acid synthase
|
Cereibacter
|
MPAIESGLWALILTGVLGYLLGSIPFGIVITRALGLGDLRKIGSGNIGATNVLRTGNKPAALATLLLDSGKGAIAVLIARAAVGEDAAQLAAFTSFLGHLFPVWLGFRGGKGVATFLGTLLALAWPVGLACCLTWLATAALGRISSLSALVAAASGVLWMILLGYGQMAALGAVLAVLIFIRHHANIRRILAGTEPRIGKK
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
A3PN50
|
Q9D9K8
|
IQCF1_MOUSE
|
IQ domain-containing protein F1
|
Mus
|
MGEEQQKPEELNAPTDDAPQEKQQPADLSSETEKAKSKKKQELSEKDQVVKIQAWWRGTLVRRSLLHAALSAWIIQCWWRLILPKIMEKRRQSMLDTFQQEQWAVVRLQSWIRMWRIRRRYCRLLKAVRTIQSHWRGHTCSSRGVIKGQYRISTSQMHLELEVLLGSGPCIVTECIPLPIKQ
|
Involved in sperm capacitation and acrosome reaction.
|
Q9D9K8
|
Q9NPA2
|
MMP25_HUMAN
|
Membrane-type-6 matrix metalloproteinase
|
Homo
|
MRLRLRLLALLLLLLAPPARAPKPSAQDVSLGVDWLTRYGYLPPPHPAQAQLQSPEKLRDAIKVMQRFAGLPETGRMDPGTVATMRKPRCSLPDVLGVAGLVRRRRRYALSGSVWKKRTLTWRVRSFPQSSQLSQETVRVLMSYALMAWGMESGLTFHEVDSPQGQEPDILIDFARAFHQDSYPFDGLGGTLAHAFFPGEHPISGDTHFDDEETWTFGSKDGEGTDLFAVAVHEFGHALGLGHSSAPNSIMRPFYQGPVGDPDKYRLSQDDRDGLQQLYGKAPQTPYDKPTRKPLAPPPQPPASPTHSPSFPIPDRCEGNFDAIANIRGETFFFKGPWFWRLQPSGQLVSPRPARLHRFWEGLPAQVRVVQAAYARHRDGRILLFSGPQFWVFQDRQLEGGARPLTELGLPPGEEVDAVFSWPQNGKTYLVRGRQYWRYDEAAARPDPGYPRDLSLWEGAPPSPDDVTVSNAGDTYFFKGAHYWRFPKNSIKTEPDAPQPMGPNWLDCPAPSSGPRAPRPPKATPVSETCDCQCELNQAAGRWPAPIPLLLLPLLVGGVASR
|
May activate progelatinase A.
|
Q9NPA2
|
B8F4W1
|
PCKA_GLAP5
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Glaesserella
|
MLNRVEQELALLGITNVKEIVYNPSYEQLFEEEMKPELEGFEKGRLTTSGAVAVDTGIFTGRSPKDKFIVLDENTKDTVWWTSDEVKNDNKPMSQSTWQSIKELVTNQLSNKRLFVIDAFCGANKDSRVAVRIVTEVAWQAHFVKNMFIRPSEAELANFTPDFVVMNGSKVTNPNWKEQGLNSENFVAFNITEKIQLIGGTWYGGEMKKGLFSLMNYWLPLKGIASMHCSANVGEDGDVAVFFGLSGTGKTTLSTDPKRKLIGDDEHGWDDDGVFNYEGGCYAKTINLSEENEPDIYRAIKRDALLENVVVREDGSIDFADGSKTENTRVSYPIYHIDNIVEPVSKAGHATKVIFLTADAFGVLPPVSKLTPEQTKYYFLSGFTAKLAGTERGVTEPTPTFSACFGKAFLSLHPTQYAEVLVKRMEASGAEAYLVNTGWNGTGKRISIKDTRGIIDAILDGSIEKAEMGSLPIFNLAIPKALPGVDPAILDPRDTYADKAQWQAKAEDLAGRFVKNFEQYATNDEGKALIAAGPKL
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
B8F4W1
|
A1SYX8
|
URED_PSYIN
|
Urease accessory protein UreD
|
Psychromonas
|
MLSTVITKPPITAKPKNQWLAHLMLEFSDTPVGTQLTRTKRKGPLSVQKAFYPEGPDCAHIYLLHPPAGIVSGDELRIGIDVKKNAHLLFTTPGAGRFYRAREDLTIGDSQQTQITQFDLEAQAKCENFPQETIVYEGADGFNSVDINLTSTSVYLGWDITCLGLPNSDQTFIKGKYCQLNRLFCDAKLIYHDRISLSPSNNLLAHPAGLAGNTVFATFLAYAPILHNNPEHSNKPQQHKALVMQIRAKITAESAQEKVSITEINGLLVIRYLGHHAQECKQLFISLWQLLRPLLLNKTAVQPRIWHT
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
A1SYX8
|
A3PB37
|
PSBT_PROM0
|
Photosystem II reaction center protein T
|
Prochlorococcus
|
MEAFAYVLILTLAVVTLFFAVAFRDPPKFDRK
|
Seems to play a role in the dimerization of PSII.
|
A3PB37
|
Q2YWR1
|
NAGD_STAAB
|
Acid sugar phosphatase
|
Staphylococcus
|
MKQYKAYLIDLDGTMYMGTDEIDGAKQFIDYLNVKGIPHLYVTNNSTKTPEQVTEKLREMHIDAKPEEVVTSALATADYISEQSPGASVYMLGGSGLNTALTEAGLVIKNDEHVDYVVIGLDEQVTYEKIAIATLGVRNGATFISTNPDVSIPKERGFLPGNGAITSVVSVSTGVSPQFIGKPEPIIMVKALEILGLDKSEVAMVGDLYDTDIMSGINVGMDTIHVQTGVSTLEDVQNKNVPPTYSFKDLNEAIAELEK
|
Catalyzes the dephosphorylation of 2-6 carbon acid sugars in vitro.
|
Q2YWR1
|
B7M2I0
|
RTCA_ECO8A
|
RNA 3'-terminal phosphate cyclase
|
Escherichia
|
MKRMIALDGAQGEGGGQILRSALSLSMITGQPFTITSIRAGRAKPGLLRQHLTAVKAAAEICRATVEGAELGSQRLVFRPGTVRGGEYRFAIGSAGSCTLVLQTVLPALWFADGPSRVEVSGGTDNPSAPPADFIRRVLEPLLAKIGIHQQTTLLRHGFYPAGGGVVATEVSPVASFNTLQLGERGNIVQMRGEVLLAGVSRHVAEREIATLAGSFSLHEQNIHNLPRDQGPGNTVSLEVESENITERFFVVGEKRVSAEVVAAQLVKEVKRYLASPAAVGEYLADQLVLPMALAGAGEFKVAHPSCHLLTNIAVVERFLPVRFGLIETDGVTRVSIE
|
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
|
B7M2I0
|
A6WWE6
|
RS6_BRUA4
|
30S ribosomal protein S6
|
Brucella
|
MALYEHVLLARQDISQQQVDALVEQYKGVLEANGGKVGKVESWGLRPLTYRIKKNRKAYYTLVNIDAPAAAVAEMERQMRINEDVLRFLTVRVEEHEEGQSAMLTRRDDRRERDGDDRPRRREGGFDRGDRGDRGDRGPRRPRDNEAGEGA
|
Binds together with S18 to 16S ribosomal RNA.
|
A6WWE6
|
A4XUP3
|
GCS2_PSEMY
|
Gamma-glutamylcysteine synthetase 2
|
Pseudomonas
|
MTQSTFGIEEEYFLTDLTSRQVARRNVEAFATACQYELGERVTREMFAAQFEVVTPVLHSLTDARQCLEGARRALARLAREFDCGVLAAGTHPLGQWRRVRATDMPRYRAIFDDYRMVASRSVLAGLHVHVGVAEGVDRIRLMNRLTPWLPLLLGLSASSPFWNGRPSGLMSYRQAVCDEWPRMGIPDHFADEAEYQRYVQVMTDTGCIRSAANLWWNIRPSLRYPTLELRIADACPRLDDALCLAGLFRAMVEHVQLTPHHAWCDDPLTRVLTLENRWRAKRQGLRGLFIEPASQRLLTFATWLEEVLERIAIQVPASDRWILEHARNLALHGGSAEAQLAEYRGARANGLEHGEALHQVVDSLMAQTELHPSQQLA
|
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
|
A4XUP3
|
Q8WVD5
|
RN141_HUMAN
|
Zinc finger protein 230
|
Homo
|
MGQQISDQTQLVINKLPEKVAKHVTLVRESGSLTYEEFLGRVAELNDVTAKVASGQEKHLLFEVQPGSDSSAFWKVVVRVVCTKINKSSGIVEASRIMNLYQFIQLYKDITSQAAGVLAQSSTSEEPDENSSSVTSCQASLWMGRVKQLTDEEECCICMDGRADLILPCAHSFCQKCIDKWSDRHRNCPICRLQMTGANESWVVSDAPTEDDMANYILNMADEAGQPHRP
|
May be involved in spermatogenesis.
|
Q8WVD5
|
B8D680
|
RTCA_DESA1
|
RNA 3'-terminal phosphate cyclase
|
Desulfurococcus
|
MSILEIDGSIGEGGGQILRYALALSALTLKPIRVYNIRAKRDNPGLRPQHLTAVEVLKEVTGAEVENAKVGSMEILFKPTSRRSGEMEIDIGTAGSISLVLQAMLPVLLFAEGDSRARLKGGTNVPWSPPIDYIKHVFLYNISHMGVRANIEVVRRGHYPRGGGLVNVEVKRVEEALKPLMIVRRGRIRGFRIHSHCVKLPAHVAVRQCESARRILSGIFKEKITEEIETYPPDKDPHLGPGSGILIYVEAEPGIRLGSDSLGEKGKPAERVGEEAALILIEELETGMAFDRHMGDMLIPYLFLAKGTSRIGVSMITLHLLTAIEVGKLFFPEAKVEVDGELGKPGIITIQGVGYKP
|
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
|
B8D680
|
Q39JM8
|
DAPB_BURL3
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Burkholderia cepacia complex
|
MKIAIAGASGRMGRMLIEAVLNDSDAQLVGALDRADSPFLGQDAGTFLGKETGVKLTADLDAVFAQADTLIDFTRPEGTMAHIEAALRHDVKLVIGTTGFTAEQKAELQAAAGKIGIVFAANMSVGVNVTLKLLEFAAKHFSHGYDIEIIEAHHRHKVDAPSGTALMMGEAVAGALGRSLDDCAVYGRHGVTGERDPSSIGFAAVRGGDIVGDHTVLFAGIGERIEITHKSSSRVSYAQGALRAVHFLSARGAGLFDMQDVLGLR
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
Q39JM8
|
C6DJC3
|
LIGB_PECCP
|
Polydeoxyribonucleotide synthase [NAD(+)] B
|
Pectobacterium
|
MWLRVCTFLIIIVGGISGFSAVAGVCPDWDNTRSKKEIDALRQQLEQWDDVYYTEGKSPVADDVYDQLREQLNQWLGCFQPQSVASVRLPDHGKQLHPVAHTGLKKLSDREQLVQWIAQREDVWIQPKIDGVAVTLVYQHGKLESAVSRGNGLQGEDWTEKVRLIPEIPHLLTNVPSLLVLQGELFLKMTDHRQHIQGGVNARSVVAGEMRRHQPSPVLSQIGLFIWEWPDGPKTMPERLEKLTEMGFAMTADYTHAIGSFADAEKWHHYWYHNPLPFVTDGVVLRQTKEPQGRYWRNTSADWAIAWKYPPFHQVAEVIDVVFSVGRTGKLAVVLKLNLLKLDDKSVSRVNVGSLSRWKQWDVLPGDRVSVSLAGQGIPRLDNVVWRSTERLPIVSPSEHDFHAFSCFRYSTVCQQQFLARLVWLSGEHGLNLTGVRDGMWLRLMQHGLLEDVLSWLSLTEAQLNAVTGMGDKRARDIYKSLQSARQMPLSRWLLALGLPVPRSAISALNHVNWLALQQWTAQQWRQFSGIGERRAEEIMAFLKHPAVVEFIARLDAEGIHR
|
Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction.
|
C6DJC3
|
Q8EJM8
|
DCUP_SHEON
|
Uroporphyrinogen decarboxylase
|
Shewanella
|
MAELKNDRYLRALLKQPVDMTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNHELACEVTLQPLRRYELDAAILFSDILTVPDAMGLGLYFEAGEGPRFERPTDTIDAIKKLSIPDPEDELGYVMKAVSTIRRELNGQVPLIGFSGSPWTLATYMVEGGSSKTFEKIKKMAYAEPAALHMLLDKLADSVTLYLNAQVANGAQSLMIFDSWGGALSHTAYREFSLRYMQKIVDGLTRFADGRQVPVTLFTKGGGLWLEAMAETGCDALGLDWTVDIADARRRVGHKVALQGNMDPSMLYAPIPRIEEEVGQILAGYGEGTGHVFNLGHGIHQHVDPEHAGAFIKAVHAQSKQYHK
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
Q8EJM8
|
B1LDY6
|
ASTB_ECOSM
|
N-succinylarginine dihydrolase
|
Escherichia
|
MNAWEVNFDGLVGLTHHYAGLSFGNEASTRHRFQISNPRLAAKQGLLKMKNLADAGFPQAVIPPHERPFIPVLRQLGFSGSDEQVLEKVARQAPHWLSSVSSASPMWVANAATIAPSADTLDGKVHLTIANLNNKFHRSLEAPVTESLLKAIFDDEEKFSVHSALPQVALLGDEGAANHNRLGGHYGEPGMQLFVYGREEGNDTRPSRYPARQTREASEAVARLNQVNPQQVIFAQQNPDVIDQGVFHNDVIAVSNRQVLFCHQQAFARQVQLLANLRARVNGFMAIEVPATQVSVSDAVSTYLFNSQLLSRDDGSMMLVLPQECREHAGVWGYLNELLVADNPISELKVFDLRESMANGGGPACLRLRVVLTEEERRAVNPAVMMNDTLFNALNDWVDRYYRDRLTAADLADPQLLREGREALDVLSQLLNLGSVYPFQREGGGNG
|
Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2).
|
B1LDY6
|
Q6HAN7
|
UNG_BACHK
|
Uracil-DNA glycosylase
|
Bacillus cereus group
|
MKHVLKNDWGLLLAPEFEKEYYRELDVFLKEEYSIHVVYPKIEDIFNALEYTSYENTKVVILGQDPYHGPNQAHGLSFSVQPGVKTPPSLLNMYKELRDEYGYDIPNNGYLVKWAEQGVLLLNTVLTVRQGEANSHKGKGWEHFTDRVIELLNEREKPVIFILWGRHAQAKKKLITNSNHHIIESVHPSPLSARRGFFGSKPYSKVNTILANMGEREIDWEIPNL
|
Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
|
Q6HAN7
|
Q72JT0
|
AROE_THET2
|
Shikimate dehydrogenase (NADP(+))
|
Thermus
|
MLRFAVLGHPVAHSLSPAMHAFALESLGLEGSYEAWDTPLEALPGRLKEVRRAFRGVNLTLPLKEAALAHLDWVSPEAQRIGAVNTVLQVEGRLFGFNTDAPGFLEALKAGGIPLKGPALVLGAGGAGRAVAFALREAGLEVWVWNRTPQRALALAEEFGLRAVPLEKAREARLLVNATRVGLEDPSASPLPAELLPEEGAVVDLVYRPLWTRFLREAQERGLKVQTGLPMLAWQGALAFRLWTGLLPDPSGMEEAARRALGV
|
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
|
Q72JT0
|
B5R8Z5
|
NHAB_SALG2
|
Sodium/proton antiporter NhaB
|
Salmonella
|
MEISWGRAMWRNFLGQSPDWYKLALLVFLIVNPFIFLANPFIAGWLLVAEFIFTLAMALKCYPLLPGGLLAIEAVIIGMTSAAHVREEVAANLEVLLLLMFMVAGIYFMKQLLLFIFTRLLLSIRSKMVLSLAFCVAAAFLSAFLDALTVVAVVISVAVGFYGIYHRVASSRGEENDMLDDSHIDPHYKTVLEQFRGFLRSLMMHAGVGTALGGVMTMVGEPQNLIIAKAAGWHFGDFFLRMSPVTVPVLVCGLLTCMLVEKMRWFGYGETLPEKVRDVLQQFDDQSRKKRTRQDKIKLIVQAVIGVWLVTALALHLAEVGLIGLSVIILATALTGVTDEHAIGKAFTESLPFTALLTVFFSIVAVIIDQHLFAPIIQFVLQASEHAQLTLFYLFNGLLSSISDNVFVGTIYINEAKAAMENGAISLKQFELLTVAINTGTNLPSVATPNGQAAFLFLLTSALAPLIRLSYGRMVWMALPYTIVLTLIGLLCVEFTLAPATEWMTQAGWLATLS
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
|
B5R8Z5
|
Q5AZ42
|
DPP4_EMENI
|
Dipeptidyl peptidase IV
|
Aspergillus subgen. Nidulantes
|
MKLSVLSVLLVSVAQAAAAPWRPREPRAAGSKRLTFNETVISAALSPSSISVQWIATENDGDYVYQEEDGSIKIESIVTNRSQTIVPAEKIPADAYSYWISPDLSAVLWATNYTKQYRHSFFADYYIQDVETLETVPLVEDMVGDIQYAEWSPSGDSIAFVRGNNLWTWSDGTVTAITKDGGPDMFHGVPDWIYEEEILGDRFALWFSPDSELLAFLTFNETGVPTFTVQYFMDNQEIAPPYPRELDIRYPKVSETNPTVKLNILQLSDNTVSTIPIDVFDPSELIVGEVAWVTDTHTELAVKAFNRVQDESKVVIVETASGETKIAHERDGTDGWLDNLLSISYVGPLALGSGDASSAYYVDLSDHSGWTHLYLFSTSGGDPIPLTEGEWEVTSIVSIDQERELVYYLSTQHHSTERHLYSVSYRTFEITPLVDDTVEAYWSVSFSAKAGYYILTYAGPSVPYQELYSVNQTAPLRTLTSNAALIEKLEEYALPNISYFELEIPSGEKLNVMQRLPVGFSPDKKYPVLFTPYGGPGAQEVSKRWQSLDFNAYIASDPELEYVTWTVDNRGTGYRGREFRSLVAKQLGKLEAEDQVYAAKQAAKLDWVDSEHIAIWGWSYGGYLTGKVLETDSGAFSLGLLTAPVSDWRLYDSMYTERYMKTLSTNAEGYNTTAIRHTDGFKNVEGGFLIQHGTGDDNVHFQNAAALGDTLIGNGVTPEKMQVQWFTDSDHSIRYNGGNVFLYRQLAQRLYKEKNRAKKEQHQWSKRSQDWVV
|
Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
|
Q5AZ42
|
B9KFM9
|
DCUP_CAMLR
|
Uroporphyrinogen decarboxylase
|
Campylobacter
|
MIFVDACFKKSTPYTPVWMMRQAGRYLPEYMEVRASAGDFLSLCKDYKKASEVTLQPVDILGVDAAIIFSDILVVPLEMGMDLKFEKGEGPVFSNPIKTKEDLERLDVEKSIKNLSYVYDALALTREKLAHDKALIGFCGSPWTIATYMIEGGGSKNYAKCKKLVYQNPEFLHQILSKLTLALKHYIQEQIKAGANAVQIFDSWASALEEEMFFEFSFKYMLEIADFIKEKYPHIPVILFPKGVSGFLDNINGNFDVFGVDWSTPLELAKEKLGAKYTLQGNMEPCRLYDKKAIEVGVDKILNIMQDSAHIFNLGHGILPDIPVENAKYFIKLVQEKSKK
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
B9KFM9
|
B1AIH2
|
ENO_UREP2
|
2-phosphoglycerate dehydratase
|
Ureaplasma
|
MKIINLLAYQILDSRGQPTVAVKLFLENDQSVIAMVPSGASTGAKEALELRDGDVNYFFNKSVKLAIQNINNIIRPHLINKNVLNFFELDNLLINLDGTENKSKLGANALLGVSIAIVKAGAIAASKPLYQYIKEDLMHNYDVNYYAPIPLMNFINGGAHADNDLDIQEFMIVPLNAISFSQAIQIGSEIFHQLDKLLKSNHLSTTKGDEGGFAPMLKNNYVTLELLVHAIKKAHYLPSKTQGVCLALDVAASELYENGKYFFKKSSSHNITLEQTSFSSDEWIKYWSKLVSMFPIISIEDCFEENDWNSFALFLKNNPHIQVVGDDLYCTNLKYLQKGIDFKATNAILIKPNQIGTISETLDVIKFAQKNNINTIISHRSGETEDTFIADLAIGVGAGQIKTGSLSRSERIAKYNRILEIEQELKDKLIYEPSKFFKFR
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
B1AIH2
|
Q47B46
|
KAD_DECAR
|
Adenylate monophosphate kinase
|
Dechloromonas
|
MKLILLGAPGAGKGTQATFISKQFGIPQISTGDMLRAQVKAGTALGLEAKKHMDAGGLVPDAVIIGMVKDRLTQDDCKNGYLFDGFPRTIPQAQAMKDAGVPIEFVLEIDVPDSDIVERMAGRRAHLASGRTYHVKFNPPKVEGIDDVTGEPLVQRDDDKEETVKKRLEIYHSQTKPLVDFYGKWAAEGDAKAPKVRKVAGVGSVDNITKSVFEALK
|
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
|
Q47B46
|
C3PFU5
|
DNLJ_CORA7
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Corynebacterium
|
MSDAVDIQREWSELAQEVRKHRELYYNGEPSIPDADFDELFQRLLALEAEHPELQTPDSPTQQVGAAPEGAVDIEHLERLYSLDNVFSAEELQDWLDRTPAEAYLTELKIDGLSIDLVYRDGKLVTAATRGDGRVGEDITANARVIPDIPHELTGTDEYPVPSLVEVRGEVYMRPDEFEEINAARREDGKPTFANPRNAAAGGLRMKDPEDVKKRRLHMVCHGIGARERFQPTSQHDAYKALEAWGFPVSPYTQRVTTAKEVQERVTYWEEHRHDAYFEMDGLVIKVDDLASQRALGATSRAPRWAIAYKYPPEEVTTKLLNIEVGVGRTGRVTPFAIMEPVFVSGSTVSMATLHNQFEVKNKNVLIGDTIIIRKAGEIIPEVLGPVLDKRDGSETEWVFPENCPACGTKLAPQKEGDQDWRCPNTRSCPAQLAARLEYLASRKALDIGELGEKAAADLISSGVLEDEADLFDLDEQALLKSSVYTTQKGALNASGKKLLENLKTARQAEFWRVLVALSIRHVGPIAARALATRFGSMEVLRAASVEELADTDGVGTIIAESFKQWFEVDWHDNIVQKWTAAGVTMEEESSDKPAQTLEGITVVVTGTLENFTRDSAKEAIITRGGKASSSVSKKTNYVVVGENAGSKEQKARDLGLTILDEEGFTRLLETGEA
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
C3PFU5
|
A3MI97
|
PNP_BURM7
|
Polynucleotide phosphorylase
|
pseudomallei group
|
MSLFNKIVKEFQWGQQKVRLETGEIARQASGAVIVDIEDTVVLATVVGAKSAKPGQDFFPLTVDYIEKTYSAGKIPGGFFRREGRPSEHETLTSRLIDRPLRPLFPEGFYNEVQVVIHVLSVNPEIPADIPALIGASAALAVSGLPFNGPVGAARVAYVNNEYVLNPTREQIKASRLDLVVAGTERAVLMVESEADQLPEDVMLGAVVFGHEQMQTAIDAIHELVREGGKPEWDWQPAPKDEALNARVTELAQPELLAAYQIRDKQARLTKLKEVYAATSAKLEEEAVAAGTVAADKATVGNILFDLEAKIVRGQILNGEPRIDGRDTRTVRPIEIRTGVLPRTHGSALFTRGETQALVVATLGTKGDEQIIDALEGEYRERFMLHYNMPPFATGETGRVGSPKRREIGHGRLAKRALVACLPSADEFGYSIRVVSEITESNGSSSMASVCGGCLALMDAGVPMKAHVAGIAMGLILEGNKFAVLTDILGDEDHLGDMDFKVAGTADGVTALQMDIKIQGITKEIMQVALAQAKEGRMHILGKMKDAVAGANTQLSEFAPRMITIKINPEKIRDVIGKGGSVIRALTEETGTTIDISDDGVVTIASTNSEGMAEAKKRIENITAEIEVGHVYEGTVLKLLDFGAIVNLLPGKDGLLHISEIVNERVKDINDYLKEGQQVKVKVIQTDEKGRVRLSAKALLNEAAAQADTPPQQ
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A3MI97
|
A8YTH8
|
CH60_LACH4
|
Chaperonin-60
|
Lactobacillus
|
MAKDIKFSENARRSLLKGVDKLADTVKTTIGPKGRNVVLEQSYGNPDITNDGVTIAKSIELKDRYENMGAKLVAEAAQKTNDIAGDGTTTATVLTQAIVREGMKNVTAGANPVGIRRGIEKATKAAVDELHKISHKVESKDQIANVAAVSSASKEVGALIADAMEKVGHDGVITIEDSRGINTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQEIVQQGKSLLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLQDIAALTGGTVITEDLGLELKDTKIDQLGQARRITVTKDSTTIVDGAGSKEAIDERVDTIRKQIEDSTSDFDKKKLQERLAKLTGGVAVIHVGAATETELKERRYRIEDALNSTRAAVDEGYVAGGGTALVNVEKAVREVKGETTDEQTGINIVLRALSAPVRQIAENAGKDGSVILDKLEHQENEIGYNAATDKWENMVDAGIIDPTKVTRTALQNAASIAALLLTTEAVVAEIPEPKQSAPQGGAGAPMGM
|
Together with its co-chaperonin GroES, 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.
|
A8YTH8
|
A8FNC2
|
RF2_CAMJ8
|
Peptide chain release factor 2
|
Campylobacter
|
MDNYEFSELLKTLKNKVGNIASIIKPENIQTRLKEIEELENSPSFWSDVKQAGIIGKEKTKITNLLKNYENAFNALNDASELFDLANSENDTETLEALFNDAPKLEDTITSLEISMLLSGENDGKNAIVSIHPGAGGTESNDWASILYRMYLRFCEREGFKVETLDFQEGEEAGLKDVSFLVKGENAYGYLKAENGIHRLVRTSPFDSAGRRHTSFSSVMVSPELDDDIEIEIEEKDIRIDYYRASGAGGQHVNKTESAVRITHFPTGIVVQCQNDRSQHKNKATAFKMLKSRLYELELMKQQDSANAGEKSEIGWGHQIRSYVLFPYQQVKDNRSGEAFSQVDNILDGDIKKMIEGVLIALKAE
|
Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
|
A8FNC2
|
Q7NPT6
|
RNPA_CHRVO
|
Protein C5
|
Chromobacterium
|
MSAYRFRRAHRLLKTDEFSSVFSLRQQRSNAFFQVFARPNGLDHARVGLVVGKKVAKRAVRRNYIKRCVREWFRLNQQGLDGVDYVVRAKTAFTREQRAEAVTALQALFAKLARCRASSSS
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
Q7NPT6
|
Q92837
|
FRAT1_HUMAN
|
Frequently rearranged in advanced T-cell lymphomas 1
|
Homo
|
MPCRREEEEEAGEEAEGEEEEEDSFLLLQQSVALGSSGEVDRLVAQIGETLQLDAAQHSPASPCGPPGAPLRAPGPLAAAVPADKARSPAVPLLLPPALAETVGPAPPGVLRCALGDRGRVRGRAAPYCVAELATGPSALSPLPPQADLDGPPGAGKQGIPQPLSGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLRAKLPQRPLLGPLSAPVHEPPSPRSPRAACSDPGASGRAQLRTGDGVLVPGS
|
Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis.
|
Q92837
|
A0KTG8
|
HLDE_SHESA
|
D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase
|
Shewanella
|
MKVSLPAFEKAKVLVVGDVMLDRYWVGPTGRISPEAPVPVVKINQVEDRPGGAANVALNIATLGGQVQLAGLVGEDDTAKALTLGVQALGVEPQWLNIADKPTITKLRVLSRNQQLIRLDFEESFDKQDSARLLKQSEALLDSVDVVVLSDYAKGAIDKPQDFIALARAKGVKVLVDPKGSDFSRYHGASLITPNMSEFEAVVGAVTSEADLLEKARGLLNKHQFDAILVTRSEKGMTLVTANAPELHIPTVAREVYDVTGAGDTVISALATSLAAGAELPQACAIANTAAGVVVGKLGTSTVSRIELIEALALHHGESGFGVVSEDQLAYALEQAKLRGERVVMTNGCFDILHAGHVSYLKQAKALGDRLIVAVNDDASVKRLKGEGRPVNQVDRRMAVLAGLAAVDWVVPFSEDTPQRIIARLLPDLLVKGGDYKVEDIAGGAEVIAAGGQVQVLGFEDGISTTAIIQNIMAKQ
|
Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.
|
A0KTG8
|
A4QB76
|
DCUP_CORGB
|
Uroporphyrinogen decarboxylase
|
Corynebacterium
|
MSALTIPAARRTLNNAPIIDAANGKTPTRTPVWFMRQAGRSLPEYKKVREGISMLDSCFMPELLAEITLQPVRRHDVDAAILFSDIVVPLRAAGVGVEIVAGRGPVLDAPVRSREDVLNLPILEGNVPEVEQGIGIILDELSDSQALIGFAGAPFTLASYLVEGGPSKNHEKTKAMMHGDPETWHALMARLVPTIVNSLKSQIDAGIDAMQLFDSWAGFLTERDYTEFVLPYSTEILEEVGKYQLPRIHFGVGTGELLGAMSKAGSEVMGVDWRVPLDKAAERIAAVSGPKVLQGNLDPALLFAGRAPLTKEIERIKAEAQTAIDAGHATGHIFNLGHGVLPNTVAEDITEAVSIIHS
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
A4QB76
|
Q6IE64
|
C1RL_RAT
|
Complement C1r subcomponent-like protein
|
Rattus
|
MCWLLLWGILHTCPTQASVLLAQQFPQQLTSPGYPEPYIKGQESHADIEAPEGFAVRLIFQDFDLEPSPGCEGDSVTISTRGTDATRLCGQQGSSLGSPPNQMEFVSSGRSLRLTFRAHSSKNKVTHLHKGFLALYQAAVSQPNGDAEAFTTPGANPPEIQNHCPGPYYKEEQTGTLSCPSSRKWKDRQRGEEVPECVPVCGRPVVPIAENPNTFGSSRAKPGNFPWQAFTSIYGRGGGALLGDRWILTAAHTIFPKDSIYLRKNKTVNVFLGHTDVDELLKLGNHPVRRVVVHPDYRQEESHNFDGDIALLELEHRVPLGPSLLPVCLPDNETLYHSGLWGYISGFGVEMGWLTTKLKYSKLPVAPREACEAWLRQRQRTEVFSDNMFCVGEEMQVNSVCQGDSGSVYVVWDDRALRWVATGIVSWGVGCGKGYGFYTKVLSYVDWIKGVIECKDRCPEA
|
Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum.
|
Q6IE64
|
Q9C0F3
|
ZN436_HUMAN
|
Zinc finger protein 436
|
Homo
|
MAATLLMAGSQAPVTFEDMAMYLTREEWRPLDAAQRDLYRDVMQENYGNVVSLDFEIRSENEVNPKQEISEDVQFGTTSERPAENAEENPESEEGFESGDRSERQWGDLTAEEWVSYPLQPVTDLLVHKEVHTGIRYHICSHCGKAFSQISDLNRHQKTHTGDRPYKCYECGKGFSRSSHLIQHQRTHTGERPYDCNECGKSFGRSSHLIQHQTIHTGEKPHKCNECGKSFCRLSHLIQHQRTHSGEKPYECEECGKSFSRSSHLAQHQRTHTGEKPYECNECGRGFSERSDLIKHYRVHTGERPYKCDECGKNFSQNSDLVRHRRAHTGEKPYHCNECGENFSRISHLVQHQRTHTGEKPYECNACGKSFSRSSHLITHQKIHTGEKPYECNECWRSFGERSDLIKHQRTHTGEKPYECVQCGKGFTQSSNLITHQRVHTGEKPYECTECEKSFSRSSALIKHKRVHTD
|
May be a transcriptional repressor.
|
Q9C0F3
|
Q8K4C5
|
IL17C_MOUSE
|
Cytokine CX2
|
Mus
|
MSLLLLGWLPTGMTHQDPPSWGKPRSHRTLRCYSAEELSHGQAPPHLLTRSARWEQALPVALVASLEATGHRRQHEGPLAGTQCPVLRPEEVLEADTHERSISPWRYRIDTDENRYPQKLAVAECLCRGCINAKTGRETAALNSVQLLQSLLVLRRQPCSRDGTADPTPGSFAFHTEFIRVPVGCTCVLPRSTQ
|
Cytokine that plays a crucial role in innate immunity of the epithelium, including to intestinal bacterial pathogens, in an autocrine manner. Stimulates the production of antibacterial peptides and pro-inflammatory molecules for host defense by signaling through the NFKB and MAPK pathways. Acts synergically with IL22, TNF and IL1B in inducing antibacterial peptides. May have protective function by maintaining epithelial homeostasis after an inflammatory challenge, such as that caused in the intestine by dextran sulfate sodium in a colitis model. May also promote an inflammatory phenotype, such as skin in a psoriasis model. Enhanced IL17C/IL17RE signaling may also lead to greater susceptibility to autoimmune diseases, such as autoimmune encephalitis.
|
Q8K4C5
|
Q8XE10
|
CHBG_ECO57
|
Chitotriose-6P deacetylase
|
Escherichia
|
MERLLIVNADDFGLSKGQNYGIIEACRNGIVTSTTALVNGQAIDHAVQLSRDEPSLAIGMNFVLTMGKPLTAMPGLTRDGVLGKWIWQLAEEDALPLEEITQELASQYLRFIELFGRKPTHLDSHHHVHMFPQIFPIVARFAAEEGIALRIDRQPLSNAGDLPANLRSSHGFSSAFYGEEISEALFLQVLDDSSHRGERSLEVMCHPAFVDNTIRQSAYCFPRLTELEVLTSASLKYAIAERGYRLGSYLDV
|
Involved in the degradation of chitin. ChbG is essential for growth on the acetylated chitooligosaccharides chitobiose and chitotriose but is dispensable for growth on cellobiose and chitosan dimer, the deacetylated form of chitobiose. Deacetylation of chitobiose-6-P and chitotriose-6-P is necessary for both the activation of the chb promoter by the regulatory protein ChbR and the hydrolysis of phosphorylated beta-glucosides by the phospho-beta-glucosidase ChbF. Catalyzes the removal of only one acetyl group from chitobiose-6-P to yield monoacetylchitobiose-6-P, the inducer of ChbR and the substrate of ChbF.
|
Q8XE10
|
O82239
|
RFI2_ARATH
|
Protein RED AND FAR-RED INSENSITIVE 2
|
Arabidopsis
|
MAGAKDSGCDDDLRIAGGCDPGKRGNPEDSSSPVEVSCSICLESVLDDGTRSKAKLQCGHQFHLDCIGSAFNMKGAMQCPNCRNVEKGQWLYANGSTRPFPEFSMEDWIPEEDLYGLSYPEMQYRVHWCPFGELSQAAASFEELEPATTTYHTEFHGHHAAAVNHSYLAYVGPGPAATPRTSDNNSTDDHPWNSHSNDHFHQLPVAPQYHHHSPSFSLPAAHVVDGEVDSSAARGLPYAHPFLFSHRSNQRSSPAINSYQGSSTQMREQHHAYNHQRQQHHANGPTLASPLISMTRRGLPPPPPPPPMPDQNVGFFIYPGGHHEPETDQIHAWERDWFPHFPVPSNHRTIPSLWHRHF
|
Mediates phytochrome (phyA and phyB)-controlled seedling deetiolation responses such as hypocotyl elongation in response to red and far-red light . Required for light-induced expression of LHCB3 and CHALCONE SYNTHASE (CHS) . Regulates negatively CONSTANS (CO) and FLOWERING LOCUS T (FT) expression and photoperiodic flowering .
|
O82239
|
P04211
|
LV743_HUMAN
|
Ig lambda chain V region 4A
|
Homo
|
MAWTPLFLFLLTCCPGSNSQTVVTQEPSLTVSPGGTVTLTCASSTGAVTSGYYPNWFQQKPGQAPRALIYSTSNKHSWTPARFSGSLLGGKAALTLSGVQPEDEAEYYCLLYYGGAQ
|
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
|
P04211
|
Q187T5
|
MIAA_CLOD6
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Clostridioides
|
MKKIPLIILTGPTAVGKTDLSIKLAKDMNAEIISADSMQIYEYMDIGSAKVTEKEMQGVKHYLIDEVKPDYPFSVSEFQQRAKKYIHEINKKEKCVLVTGGTGLYLNSLIYNMDFAQSDANNELREELQKQLAEKGIDYMHNKLKELDEESANRIHKNNTKRVIRALEVCLSGKKMNDFSSDLKFNEEYQPIIIVLNRDREHLYQRINMRVDIMIKNGLVEEVKKLLSMGFKKDMISMQGIGYKEILKYLDGEYTYEEAIEIIKRDSRRYAKRQITWFKRYKTAKWFDLDQYENIDELKNEIILYIKDSIK
|
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).
|
Q187T5
|
O94532
|
FOR3_SCHPO
|
Formin-3
|
Schizosaccharomyces
|
MASKMPEGSPPTSRSIQSRNSSYSTSSNERIGTPSTISLSENSDLSKLQSTNDFESREDLSLTSDDNNDPEYVMCYNTVYHQKTKINDKLLSETEQLRKIYPLESRVFPKPTIVKEITNERTKRYTFYDDDAPLTNQHTVLDEATYNRILKRIDFFIEKVVEVPPTYHFLSLLNVQLRIQPIWWMDEFAERNGIESLLSALRNLGHYPERASKTPLESQIIQSLFHCLNSENCRRRYQSSAKCSVPGFNALGTIAETVLSKSLNSARMATFLLKFLCNKKGLSYFKAVIRAFEWLVEQKLSKTRFSAWMHSFNDVITGVRVCADSSPQAIVHMDEFEDTDCLIDYLVATLALIRDLCAAPPDLQLRCALRHELLSAGLQKAIDSLLKWRNRHVRDALQLLIKEHNADARRFRSGSDVNNVDRKCVKKQMNYREESHTPHGNTTRKTSTPVSNNRPTTPEQQAVWDVFQRIYTRFTGSEGSKESFIKLLEYFVTEPDNGKIQKSMQLLTHTLEALEGFKTAKADTNVGLTILSQRLLDKLGTAEEIAEYKTKYNGAMLENKHLKEQVESMLSQLNVGPRDPMQFLKKQLDELKAELNLRDNLLASMQREFETRYRAQIQAYNKLQSQMEHVQNSNEQHLQPGLLNKVSKSFDSVHRRNLSQDSLDAMTEQFSYHVEPNILSGSGIPVRVHTPSKTEDLDESFSGSEISSSPSPLLPDVSDTVEEQQKLLLKSPPPPPPAVIVPTPAPAPIPVPPPAPIMGGPPPPPPPPGVAGAGPPPPPPPPPAVSAGGSRYYAPAPQAEPEPKIDETSLTEEQKIQLEEARKQRKAADDAARAAIEKYTSIPSLRDLHKPTRPLKRVHWQRVDPLPGPNVFTKFCLNFDITAKVFIDNGLLDFLDEKFDNTPREDFVAVEISDQRSSLLPDTVEQNMAIILRSVSNMPVEDLVQKFLVEPDFLPASILYFDRASLASTNAYTDPFIPYSTDYTKKNPKEPTADVNSLSYFEKFFVLFVVNLRHYFQERMKALKFRSTLFGDLEILEVRMKEVIDTSDSIMEDKNFAEFFQVLLIIGNYFNEPYDRASAFSLYMIYRLETLRDSSSALTLMHYFDEIIRTRFPELLQAESTFKKIQSVSGYNIDAMVAGVDGAYDEFCDFQTSLKDGALSKCDQHHPDDKAYDILSEWLPEAKERIRNIKKLKTDMLTKLENTVKYLCEYDSIDKVRNSFFKNLNSFYEMYSIAKAENEERFEKEKRRIMSEDRDKLIRGRQKTSIVAKYRNKRELPEDSDDKQDTASKDKNSLETIDEKMEDASKIEGDAKTGDDNEMEDLDKMEDLEKPDYAEEKDPYITVMSELRSRIQNVPKRTVTVYSDEGVATLEPGAQGDDVVDKAKMILEKMEGHSQLLTSSANPDEEVLRAKLKAAERLQKPAIPRTRRKGHTEPKSAKSLLAELTNGSNASNLVENDRQKQ
|
Involved in controlling polarized cell growth. Required for interphase actin cable formation and microtubule organization.
|
O94532
|
Q1MRB9
|
ATPA_LAWIP
|
F-ATPase subunit alpha
|
Lawsonia
|
MHIKADEISTIIKEQIQNYSQRIETTEVGTVLSVGDGIARVYGVQDVMSMELLEFPGNLLGMVLNLEQDNVGVALLGDDTGVEEGSTVKRTGRIFSVPVGDAVTGRVLNPLGQPLDGLGPLNATEKKPVEVKAPSIIDRKSIYEPLVTGIKAIDAMTPIGRGQRELIIGDRQTGKTSICIDAILAQKESGVHCFYVAIGQKASTVALVADTLRKHGAMEYTTIIAATASDPAPLQYISPYSGCTMAEYYRDHGQHALIVYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKLSDELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQVYLEPNLFNAGVRPAINVGLSVSRVGGAAQTKAMKQVSGTMRLDLAQYRELAAFAQFSSDLDKETQTKLERGARLVELLKQPQYQPMQLPEQVIVMFAATKGFMDDIPIDHIQNFSKTLIEYIQTMNPKILENISTQQALNEELDQQLTTAITECKKTFLPMNKR
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
Q1MRB9
|
P52200
|
PYRG_SPICI
|
UTP--ammonia ligase
|
Spiroplasma
|
MAKYIFVTGGVVSGLGKGITASSIGVLLKASGLNVFMQKFDPYLNVDPGTMSPYQHGEVFVTTDGAETDLDLGHYERFIDENLTKESNITSGRIYKNVIEKERRGEYDGGTVQVVPHVTNEIKKKVYHAASTSKADIIITEIGGTVGDIESLPFIEAIRQVRMEQGRENVIYMHVSLVPYIAASKESKTKPTQHSVRELLSLGIQPDIVVARTEQALDDNVLEKIALFCNIEKSNVLVATDVASILWSHKMYEQNAQIVISKLLNLKSLKTDMSEWKRFVEKINQSQQVIEIKLVGKYIELPDAYLSVSESLRIAGYENKVKIKIDWIKAEDVNKKNDQQLLKNAKGILVPGGFDERGFEGRGFEGKILACQFARENNIPFFGICFGMQAAVIEFARNVCHIQDANSSELTETKNAIIDIIRGKDKTDALGGTLRLGNYKTTFVPNTLAHKLYGKKWGFRTSRHRYEVNNDYREQLAQAGLVFSGLYVEKNLVEVIEIPKYPFYLAAQYHPEFTSRPNKPNPLFNGFVQAVIKNK
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
P52200
|
Q65JF1
|
RNY_BACLD
|
Ribonuclease Y
|
Bacillus
|
MSPLAILISILLSLFCLVVGYYVRKIIAEAKISGARNAAEQILGDAKRDAEALKKEALLEAKDEIHTLRIEAEQEVRERRNELQKQENRLLQKEENLDRKDESLDKREAMLEKKDHSLNERQQHIEEMESKVDEMIRMQQSELERISSLTRDEAKQIILERVENELSHDIAIMMKESENRAKEEADKKAKNILSLALQRCAADHVAETTVSVVNLPNDEMKGRIIGREGRNIRTLETLTGIDLIIDDTPEAVILSGFDPIRRETARIALDKLVQDGRIHPARIEEMVEKSRREVDDYIREMGEQTTFEVGVHGLHPDLIKILGRLKFRTSYGQNVLKHSMEVAFLTGLMASELGEDVTLAKRAGLLHDIGKAIDHEVEGSHVEIGVELATKYKEHPVVINSIASHHGDQEPTSIIAVLVAAADALSAARPGARSETLENYIRRLEKLEEISESYEGVEKSFAIQAGREVRIMVKPDSINDLEAHRLARDIRKRIEDELDYPGHIKVTVIRETRAVEYAK
|
Endoribonuclease that initiates mRNA decay.
|
Q65JF1
|
Subsets and Splits
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