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2.75k
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AlphaFoldDB
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Q54T57
PONM_DICDI
Ponticulin-like protein M
Dictyostelium
MKFLSTLILLLSVLALVRGEQYNKFTVDLNGVCTNSGSLDTCTNQCGNAGGSFQISQSGGEYQYEQYATKDCDLMASLTSKFACLADEAPVTLGLGNIKITCQDPSNSASSPLTTAVLFVVAFAAAIALLL
Binds F-actin and nucleates actin assembly.
Q54T57
A4WWP0
PNP_CERS5
Polynucleotide phosphorylase
Cereibacter
MFNVTKKSIEWGGETLTLETGKVARQADGSVIATLGETSVMANVTFAKAAKPGQDFFPLTVHYQERYYAAGKVPGGFFKREARPSEKETLTSRLIDRPIRPLFVDGFKNEVLLIVTVLSHDLVNEPDIVAMIAASAALTISGVPFMGPIGAARVGYANGEYVLNPDVDDMQKLRENPEQRLDLVIAGTKDAVMMVESEAYELSEAEMLGAVKFGHEAMQPVIDMIIDFAEEAAKEPFDFSPPDYAALYAKVKSLGEAQMRAAFAIREKQERVNAIDAARAAIKAQLSDAELADENLGTAFKKLESSILRGDIINGGARIDGRDTKTVRPIISETSVLPRTHGSALFTRGETQALVVTTLGTGEDEQIIDALHGNSRSNFLLHYNFPPYSVGEVGRFGPPGRREIGHGKLAWRALQAVLPAATDFPYTIRVVSEITESNGSSSMASVCGGSLSMMDAGVPLKAPVAGVAMGLILEDDGKWAVLTDILGDEDHLGDMDFKVAGTENGITSLQMDIKVAGITPAIMEQALAQAKDGRMHILGEMSKALSSANSFSAYAPKIETLTIPTDKIREVIGSGGKVIREIVETSGAKVDINDDGVIKIASNDQAAIKKAYDMIWSIVAEPEEGQIYTGKVVKLVDFGAFVNFFGKRDGLVHVSQIANKRLTHPNEVLKEGQEVKVKLLGFDERGKVRLGMKMVDQETGQEIAPEKKEEATEA
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
A4WWP0
A9JX75
TOX1_PHANO
Toxin 1
Parastagonospora
MKLTMVLSVAFATLTFANEGILTFEGLGLARRQTICHTPGGSGCRASISGDQCCCTSCTPEDCSDLCKNGKQAAHEAQKQKKCAKCCNAGGESHELCCSIASAGIDCNPCTAGLRMC
Necrotrophic effector that plays a critical role during fungal penetration, via its interaction with the host Snn1 protein . Snn1 is a member of the wall-associated kinase class of receptors, which are known to drive pathways for biotrophic pathogen resistance . Recognition of Tox1 by Snn1 induces mitogen-activated protein kinase genes such as MAPK3 and activates programmed cell death, which allows this necrotroph to gain nutrients and sporulate . Recognition of Tox1 by Snn1 also induces other plant defense responses, including oxidative burst and pathogenesis related (PR) gene expression . The development of necrosis and disease induced by Tox1, and particularly penetration during infection, requires light, which is probably related to the light-dependent expression of host Snn1 . Tox1 plays an additional role in providing significant protection from wheat chitinases by binding chitin in the fungal cell wall .
A9JX75
Q10YP7
PSTB_TRIEI
Phosphate-transporting ATPase
Trichodesmium
MLEHQTNTYQQNSTPALSAENLSIFYGDFKALKDISMRIPKNKVTAFIGPSGCGKSTLLRCFNRLNDLIDIFRLEGRILYHNQNIYDPDIDPVEIRRHIGMVFQKPNPFPKSIYDNIAYGVRVNGLAKSKEEMDEIVERSLRQAVLWDEVKDKLGQSGFALSGGQQQRLCIARAVAISPDVVLMDEPCASLDPISTVKVEELINELRQKYTIIIVTHNMQQATRIADLTAFFNAKAVESGQRFGYLVEFDKTNNIFQNPREKATQDYVSGRFG
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
Q10YP7
B5ZYC6
EX7L_RHILW
Exodeoxyribonuclease VII large subunit
Rhizobium
MSNVFDSDSPTNLAEYSVSELSGSIKRTVETAFDQVRVRGEISGYRGPHSSGHAYFALKDDRARIDAVIWKGTFSRLKFRPEEGMEVIATGKVTTFPGSSKYQIVIETLEPAGAGALMALIEERKRKLGAEGLFDAARKKRLPFMPRVIGVVTSPTGAVIRDILHRISDRFPVHVLVWPVKVQGEGSGEEVANAIRGFNALEPAGLIPRPDVLIVARGGGSLEDLWSFNDEIVVRAAAESRIPLISAVGHETDWTLIDYAADVRAPTPTGAAEMAVPVKAELEAQAAALAARLQGCMNRQMDQRRQSVRALMRALPSLDQLLALPRRRFDEAAAGLGRGLELNTINKRRGFERVGAHLRPDLLSGRIAERRQTLNERIVRAERMVERLIDRSKSRIDRAEAILASLPARFKTQTDRSREALANLSRHGDTAIRHQLARARAELSAQDRVLQSLSYKNVLKRGYAVIRDEDDRPVSQAAALSAGSAVSIEFSDGRIGAVTTEGGAPPASLKKRPAREAGDPPKQGSLF
Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
B5ZYC6
Q8GYC7
PGL1B_ARATH
Ferredoxin-plastoquinone reductase 2
Arabidopsis
MAFTLTIPRFSAISRKPITCSSSRTQCPAPFTHGRSISLRRRLTLLPLKASTDQSGQVGGEEVDSKILPYCSINKNEKRTIGEMEQEFLQAMQSFYYEGKAIMSNEEFDNLKEELMWEGSSVVMLSSDEQRFLEASMAYVSGNPILSDEEYDKLKMKLKMDGSEIVCEGPRCSLRSKKVYSDLAIDYFKMFLLNVPATVVALGLFFFLDDITGFEITYLLELPEPFSFIFTWFAAVPAIVYLALSLTKLILKDFLILKGPCPNCGTENVSFFGTILSIPNDSNTNNVKCSGCGTEMVYDSGSRLITLPEGGKA
Ferredoxin-plastoquinone reductase involved in cyclic electron flow (CEF) around photosystem I. The homodimer is probably not involved in CEF.
Q8GYC7
Q1LLY7
HBOH_CUPMC
D-(-)-3-hydroxybutyrate oligomer hydrolase
Cupriavidus
MQQRHLSQSAHSHGHGTRRAHRRNTIAIAVATLAVAACGGFGTNGSGGNTGPNVKPAFISGPVGVKSYDGNTDDLLTAGLGKDGLAAAAPAFANPNAPTAVELRRNAIWANYRAIVDVQAAGGYGSLYGPNVDAKGNVTTGQGKVPGTEYIAFTDDGSGRQNVTVMAQVPDGFDVKHPCIISATSSGSRGVYGGIAVGEWGLKHNCAVAYTDKGTGAAPHDLGSDTVPLIDGTRQTRAGAGTQAQFAAQPGASETLAGFNSSTPHRLAFKHAHSQQNPEANWGANTLQAIQFTLWAVNDKFGRTNTDGMRQATFTPANVLVIASAISNGGGAAIAAAEQDTGGLIDGVAVGEPNVNLPPTAGVVVKRGGVPVAASGKHLYDYTTIANLYQLCASQDASLGNAPFAKTAGQAALNRCASLAAKKMIAGGSTSAQATSALDALHRAGWEPESDDLFASLSALEVGSSISVTYANAYARASVTDRLCHYSFSSPGSPPQANPVTAPAAALAGLFSTGNGIPPTTAVTLMNDANPSGAMRDFTSISPSTKLADGNVDGALCLRGLLDTRNPALMTGIGQTYRTGNLGGRPSVIVQGRSDGLLPVNHTSRPYLGLNKHVEGASSRLSYIEVTNGQHFDGFIDVIPGYAKRYIPMHVYVNRALDAVYANLRDGTPLPPSQVVRTTPRGGADTDTVGPRIQPSNVPPIAATPAAGDAITVTGSTVDVPN
Participates in the degradation of poly-3-hydroxybutyrate (PHB). It works downstream of poly(3-hydroxybutyrate) depolymerase, hydrolyzing D(-)-3-hydroxybutyrate oligomers of various length (3HB-oligomers) into 3HB-monomers.
Q1LLY7
Q94JS0
UCRI1_ARATH
Ubiquinol-cytochrome c reductase iron-sulfur subunit 1
Arabidopsis
MLRVAGRRLFSVSQRSSTATSFVVSRDHTLSDGGGDSSSAPRSLPSADLSSYHRSLIRGFSSQVLAQGNEIGFGSEVPATVEAVKTPNSKIVYDDHNHERYPPGDPSKRAFAYFVLSGGRFVYASVLRLLVLKLIVSMSASKDVLALASLEVDLGSIEPGTTVTVKWRGKPVFIRRRTEDDIKLANSVDVGSLRDPQEDSVRVKNPEWLVVVGVCTHLGCIPLPNAGDYGGWFCPCHGSHYDISGRIRKGPAPYNLEVPTYSFLEENKLLIG
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of 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. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1.
Q94JS0
P01942
HBA_MOUSE
Hemopressin
Mus
MVLSGEDKSNIKAAWGKIGGHGAEYGAEALERMFASFPTTKTYFPHFDVSHGSAQVKGHGKKVADALASAAGHLDDLPGALSALSDLHAHKLRVDPVNFKLLSHCLLVTLASHHPADFTPAVHASLDKFLASVSTVLTSKYR
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
P01942
P32340
NDI1_YEAST
NADH:ubiquinone reductase (non-electrogenic)
Saccharomyces
MLSKNLYSNKRLLTSTNTLVRFASTRSTGVENSGAGPTSFKTMKVIDPQHSDKPNVLILGSGWGAISFLKHIDTKKYNVSIISPRSYFLFTPLLPSAPVGTVDEKSIIEPIVNFALKKKGNVTYYEAEATSINPDRNTVTIKSLSAVSQLYQPENHLGLHQAEPAEIKYDYLISAVGAEPNTFGIPGVTDYGHFLKEIPNSLEIRRTFAANLEKANLLPKGDPERRRLLSIVVVGGGPTGVEAAGELQDYVHQDLRKFLPALAEEVQIHLVEALPIVLNMFEKKLSSYAQSHLENTSIKVHLRTAVAKVEEKQLLAKTKHEDGKITEETIPYGTLIWATGNKARPVITDLFKKIPEQNSSKRGLAVNDFLQVKGSNNIFAIGDNAFAGLPPTAQVAHQEAEYLAKNFDKMAQIPNFQKNLSSRKDKIDLLFEENNFKPFKYNDLGALAYLGSERAIATIRSGKRTFYTGGGLMTFYLWRILYLSMILSARSRLKVFFDWIKLAFFKRDFFKGL
Catalyzes the oxidation of NADH generated inside the Mitochondrion.
P32340
B2IMY9
SYE_STRPS
Glutamyl-tRNA synthetase
Streptococcus
MSKDIRVRYAPSPTGVVHIGNARTALFNYLYARHHGGTFLIRIEDTDRKRHVEDGERSQLENLRWLGMDWDESPESHENYRQSERLDLYQKYIDQLLAEGKAYKSYVTEEELAAERERQEAAGETPRYINEYLGMSEEEKAAYIAEREAAGIIPTVRLAVNESGIYKWHDMVKGDIEFEGGNIGGDWVIQKKDGYPTYNFAVVIDDHDMQISHVIRGDDHIANTPKQLMVYEALGWEAPEFGHMTLIINSETGKKLSKRDTNTLQFIEDYRKKGYLPEAVFNFIALLGWNPGGEDEIFSREELIKLFDENRLSKSPAAFDQKKLDWMSNDYIKNADLETIFEMAKPFLEEAGRLTDKAEKLVELYKPQMKSVDEIIPLTDLFFSDFPELTEAEREVMTGETVPTVLEAFKAKLEAMTDDEFVTENIFPQIKAVQKETGIKGKNLFMPIRIAVSGEMHGPELPDTIFLLGREKSIQHIENILKEISK
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
B2IMY9
Q6CF69
RLP24_YARLI
Ribosome biogenesis protein RLP24
Yarrowia
MRVYNCHFCSSPVYPGKGIMFVRNDSKEFRFCRSKCHKNFKMKRNPRKLRWTKAFRKAAGKEMVVDSTLAFSARRDVPVRYNRDLVEKTLEAMEKVEEIRLKRERAFYKNRMRGNKAAQLEEDRKLVEAHPELLREREVELRRMQEAGEDDDDEDMSEMEVSEEEESEEEREKVEIALKSKSKRKMRA
Involved in the biogenesis of the 60S ribosomal subunit. Ensures the docking of YALI0_B00990g/NOG1 to pre-60S particles. Activates and recruits ATPase AFG2 to cytoplasmic pre-60S ribosomal particles.
Q6CF69
Q57JA4
AAEB_SALCH
p-hydroxybenzoic acid efflux pump subunit AaeB
Salmonella
MGIFSIANQHIRFAVKLACAIVLALFIGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPYSGAIRYRGMLRIIGTFIGCIAALIIIISMIRAPLLMILVCCVWAGFCTWISSLVRIENSYAWGLSGYTALIIVITIQTEPLLTPQFALERCSEIVIGIGCAILADLLFSPRSIKQEVDRELDSLLVAQYQLMQLCIKHGDSEEVDNAWGDLVRRTAALEGMRSNLNMESSRWVRANRRLKALNTLSLTLITQSCETYLIQNTRPELITDTFRELFETPVETVQDVHRQLKRMRRVIVWTGERETPVTLYSWVGAATRYLLLKRGVISNTKISATEEEILQGEPVVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGNGAMVMIAVVTSLAMRLPNPRMVCIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCLSLAVLGFFIGIEVQKRRLGSMGALASTINIIVLDNPMTFHFSQFLDSALGQIVGCMLAFIVILLVRDKSKDRTGRVLLNQFVSAAVSAMTTNVVRRKENRLPALYQQLFLLMNKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSVFHRQLRRTADHVISAGSDDKRRRYFGQLLDELDIYQEKLRIWEAPPQVTEPVKRLTGMLHKYQNALTDS
Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell.
Q57JA4
Q9S757
CYSC1_ARATH
O-acetylserine (thiol)-lyase 5
Arabidopsis
MASVSRRLLRRETIPCFSHTVRKLFSTVGSPSFAQRLRDLPKDFPSTNAKRDASLLIGKTPLVFLNKVTEGCEAYVAAKQEHFQPTCSIKDRPAIAMIADAEKKKLIIPGKTTLIEPTSGNMGISLAFMAAMKGYRIIMTMPSYTSLERRVTMRSFGAELVLTDPAKGMGGTVKKAYDLLDSTPDAFMCQQFANPANTQIHFDTTGPEIWEDTLGNVDIFVMGIGSGGTVSGVGRYLKSKNPNVKIYGVEPAESNILNGGKPGPHAITGNGVGFKPEILDMDVMESVLEVSSEDAIKMARELALKEGLMVGISSGANTVAAIRLAKMPENKGKLIVTIHASFGERYLSSVLFDELRKEAEEMKPVSVD
Acts as a major beta-cyanoalanine synthase. The cyanoalanine synthesis reaction is more efficient than the cysteine synthase activity. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein. Probably involved in the detoxification of cyanide that arises from ethylene biosynthesis. Maintains a low level of cyanide for proper root hair development.
Q9S757
B0TEJ8
NADK_HELMI
ATP-dependent NAD kinase
Heliomicrobium
MPTVGVVLNDDKPQALEVARRMADWLSQREVPMGIPLTRVAELVHSPSPELRDRLRQLDLIVVLGGDGTLLNTARLAAPHGIPVVGVNLGRLGFLTEVEVSDLFPALERIIAGDYRIEERMMLEARLIRDGLEQPSYFALNDVVVTKGDHPRMIRVEAAVGDEVVWTYSADGLIVSSPTGSTAYSLSAGGPIVSPELHALLLTPISPHALDARPLVIPQDQAVRLTVISSHSHAVVTVDGQPGQPMVCGDSVLVRKASVACRLIRLGERTFFRILREKMQQGR
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
B0TEJ8
P08303
COXZ_PARDE
Cytochrome c oxidase assembly protein CtaG
Paracoccus
MSGGKPRSNTRTVAMLAGVVVLMGALSWAAVPFYSWFCKVTGFAGTTNVAEAASDTVLDEKIRVRFDANADSNLGWTFRPMQREMELKIGENAIAFYEAINNTDEPVTGTASYNVAPDAAGYFFNKIECFCFTEQTLQPGERVEMPVSFFVDADLVNDRDAVIRDITLSYTFHRTDPPAPKQAALDAKTEPTVN
Exerts its effect at some terminal stage of cytochrome c oxidase synthesis, probably by being involved in the insertion of the copper B into subunit I.
P08303
P0A0M0
ETXH_STAAU
SEH
Staphylococcus
MINKIKILFSFLALLLSFTSYAKAEDLHDKSELTDLALANAYGQYNHPFIKENIKSDEISGEKDLIFRNQGDSGNDLRVKFATADLAQKFKNKNVDIYGASFYYKCEKISENISECLYGGTTLNSEKLAQERVIGANVWVDGIQKETELIRTNKKNVTLQELDIKIRKILSDKYKIYYKDSEISKGLIEFDMKTPRDYSFDIYDLKGENDYEIDKIYEDNKTLKSDDISHIDVNLYTKKKV
Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules via their alpha domain, in particular TRAV27 . In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines . Causes also the intoxication staphylococcal food poisoning syndrome. The illness characterized by high fever, hypotension, diarrhea, shock, and in some cases death .
P0A0M0
A6WNV3
DAPE_SHEB8
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Shewanella
MIPADDYPVTELTKALIARPSVTPLDEGCQTLMAERLSAIGFNIEPMVFEDTTNMWARRGNEGPVFCFAGHTDVVPTGDVSRWHTPPFVPTIIDGYLYGRGAADMKGSLAAMVIATERFVAKHPDHNGSIAFLITSDEEGPFINGTTRVIDTLEARNEKITWALVGEPSSTLKLGDVVKNGRRGSLTGNLIVKGIQGHVAYPHLADNPIHKAAPFLAELSQMHWDNGNEFFPPTSFQIANINGGTGASNVIPGALDVMFNFRYSTEVTAEILIERVEALLKAHELGYDISWIFNGLPFLTGDGPLLDATRIAIRQVTGYETDPQTTGGTSDGRFIAPTGAKVLELGPVNATIHKVNECVKVDDLEQLALCYEVILEQLLC
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
A6WNV3
B8EBJ4
RL24_SHEB2
50S ribosomal protein L24
Shewanella
MAAKIRREDEVIVLAGKDKGKRAKVSQVLPTGKLIVEGINLVKKHQKPNPQLGVAGGIVEKEAPIQASNVAIFNSATGKADRVGFRFEDGKKVRFFKSNSELVK
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
B8EBJ4
A9JRZ0
SMUF2_DANRE
SMAD-specific E3 ubiquitin-protein ligase 2
Danio
MSNQGVRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVRNTLDPKWNQHYDLYIGKSDSITISVWNHKKIHKKQGAGFLGCVRLLSNSINRLKDTGYQRLDLNKLGPNDSDTVRGQIVVSLQSRDRIGSGGPVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRSTQWERPTRPASEYSSPGRPLSCLVDENTPIMTPNGAAGVPADDPRVQERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNVNCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNPSPNGSRAAVEAQSSSRPGQLKEQAQSVVSPGNLPEDPECLTVPKYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMVKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKPITLDDMESVDPDLHNSLVWILDNDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVTQDTKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKAFDEKELELIVCGLGKIDINDWKSNTRLKHCTPDSNIVKWFWRAVESYDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDASTNNLPKAHTCFNRIDIPPYESYDKLYDKLLTAIEETCGFAVE
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
A9JRZ0
Q9JYJ8
PYRG_NEIMB
UTP--ammonia ligase
Neisseria
MTKFIFVTGGVVSSLGKGIAAASIAAILESRGLNVTMLKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFIDSTMTRRNSFSTGQVYENVIAKERRGDYLGGTVQVIPHITDEIKRRIHEGAAGYDVAIVEIGGTVGDIESLPFLEAIRQMRSQLGRNNTLFAHLSYVPYIAAAGEIKTKPTQHTVKEMLSIGLQPDILICRMDRTMPADERRKIALFCNVEERAIVGSYDVDSIYECPEMLHDQGIDNIITEQLQLNVQQADLTAWKKIVHAIQNPKHTVKIAMVGKYVDLTESYKSLIEALKHAGIHTETDVQITFVDSENIEKNKGDVSMLKDMDAILVPGGFGSRGVEGKIAAVRYARENNVPYLGICLGMQIALIEYARDVAGLKGANSTEFDLKCAAPVVALIDEWQTADGSVETRDESTDLGGTMRLGAQEVELKAGSLAAKIYGSGHIRERHRHRYEVNNNYVPTLEQAGLVIGGVSAGRERLVETIELPNHPWFFACQFHPEFTSNPRKGHPLFTAFVKAALNNKKA
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.
Q9JYJ8
Q1H1Z8
CRCB_METFK
Putative fluoride ion transporter CrcB
Methylobacillus
MYQVMLVALGGAIGSAARFTLSGLVLRYSLDWRFPLPTFTVNIIGCLVIGMLAGLASKEGFISPDMRVLLFTGLVGGFTTFSAFGLETLVLLREGLVGIAAAYIVSSIVVGLVLMWLGFELVKMTMQA
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q1H1Z8
Q2RLU8
UVRC_MOOTA
Excinuclease ABC subunit C
Moorella
MDLEEKLARLPDHPGVYIMHDANGAIIYVGKAASLRNRVRSYFRGQHQPRTQAMVSHVADFEYILTDNEVEALILECNLIKQHRPRYNVSLKDDKSYPYIKITTQEDFPRIQITRSVTRDGSRYFGPYTSAGSLKETLKLLRGLFPIRTCRDTPLQPRSRPCLNAHIGRCLAPCAGQVDRETYREAVDNVIMFLEGRHTALVKELKEQMEAAAARLEFEKAARLRDQLRAVQEVCEKQKLAAASGEDADAIAFAREGEAALGLIFFSRGGKVIGRDHFFLTGSEGLSRGEVMAALLKEYYSRGVEIPPEILLHDEPEDAATIASWLSRLRGGRVNLRVPKRGTKLKLLRLVHENAVSLLQEHLLTRRRQEEGSRAALLELQEILELPRLPRRMEAYDISNFQGSSQVGAMAVFVDGRPLPSAYRRFQIKTVRGPNDFASLQEVLSRRFRRAAEQDPHFADLPDFVLIDGGLGQLHAARETMEAMGVGYIPTFGLAKEEELLFRVGTSEPIRLPRESKALQILQHLRDEVHRFAITYHRQKREKTAYRSVLDDIPGVGPKRKKALLRHFGSVAAISKATLEDLLAVEGMNRTVAARILAGLGRRSDGEDSTGSP
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
Q2RLU8
P52894
ALA2_HORVU
Glutamic--pyruvic transaminase 2
Hordeum
MAATVAVDNLNPKVLKCEYAVRGEIVIHAQRLQEQLKTQPGSLPFDEILYCNIGNPQSLGQQPVTFFREVLALCDHPDLLQREEIKTLFSADSISRAKQILAMIPGRATGAYSHSQGIKGLRDAIASGIASRDGFPANADDIFLTDGASPGVHLMMQLLIRNEKDGILVPIPQYPLYSASIALHGGALVPYYLNESTGWGLETSDVKKQLEDARSRGINVRALVVINPGNPTGQVLAEENQYDIVKFCKNEGLVLLADEVYQENIYVDNKKFHSFKKIVRSLGYGEEDLPLVSYQSVSKGYYGECGKRGGYFEITGFSAPVREQIYKIASVNLCSNITGQILASLVMNPPKASDESYASYKAEKDGILASLARRAKALEHAFNKLEGITCNEAEGAMYVFPQICLPQKAIEAAKAANKAPDAFYALRLLESTGIVVVPGSGFGQVPGTWHFRCTILPQEDKIPAVISRFTVFHEAFMSEYRD
Transfer of C3 units between the cytosol of mesophyll and bundle sheath cells to maintain a nitrogen-carbon balance in the C4-dicarboxylic pathway.
P52894
A0KSP4
RAPA_SHESA
ATP-dependent helicase HepA
Shewanella
MPFALGQRWISDTESELGLGTVVQVEGRMVTVLFPATGENRMFSRNEAPLTRVIYNPGDTVESHEGWSLSVEELTEKDGLVVYHGIHSETGEKVSLRETLLNHNIRFNKPQDRLFAGQIDRLDRFGIRYQCQLLRHQLATSDLLGLQGPRVGLIPHQMWIAHEVGRRYAPRVLLADEVGLGKTIEAGLIIHQQLLTGRAERVLIIVPDTLRHQWLVEMLRRFNLRFSVFDEDRCVEAFADHDNPFYTEQLVICSLELLRKKKRLDQALDADWDLLVVDEAHHLEWTEEAPSRAYQVVEALSEVVPGVLLLTATPDQLGHESHFARLRLLDPDRFYDYDAFLAEENSYKDVAVAAEALAGDAKLSDAAINSLTELLSEKDIAPSIRLIQAEDIDSELQQAARSELLQELLDRHGTGRVLYRNSRASVKGFPKRIFNAYPHAMPEQYLTAARVNEMMGGRKSLEAQAAQALSPEKLYQEFEDNSASWWKFDPRVDWLIEFLKSHRSKKVLIIASGADTALSLEEALRTREGIQATVFHEGMSIIERDKAGAYFAQEEGGAQALICSEIGSEGRNFQFASHLVLFDLPLNPDLLEQRIGRLDRIGQKNDIQIHLPYLQDTAQERLLNWYHQGLNAFELTCPSGHVLYSEFAEDLLNVLVGGDEDELTNLLNHTQSRYKELKHAMEQGRDKLLEINSHGGDKAKAIVERLAQSDQDTKLIGSVIRLWDIIGVDQEDKGENSIILRPSEHMMFPTYPGLHEDGVTVTFDRDTALSRDDIALITQEHPLVQTGLDLITGSDTGTTSVAILKNKALPAGTLFLELIYMADASAPKSSQLYRYLPPTPIRVLLDKNGNDLSAKVDYTSFDKQLSAVNRHIGSKLVTASQPILHPLFAKGEEYAQTAVNELVAQAREKMTSQLTGELDRLESLKAVNPNIREEELEYLRNQMQELSTYLDASQLQLDAIRMVLVSHV
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
A0KSP4
Q882V6
MOAA_PSESM
Molybdenum cofactor biosynthesis protein A
Pseudomonas
MSEPVLMDRFARKVDYLRMSVTDRCDFRCVYCMAEEMTFLPRQQILSLEEIHQVAERFVALGTRKIRLTGGEPLVRAGVVGLCEKIAALPGLRELCMTTNGSQLDKLAAPLFKAGVTRLNISLDSLDPQRFRELTRTGDLHKVIAGIDAANAAGFVHTKLNCVVMHGRNDHEINDLLAFAIDRNLDVSFIEEMPLGIISEHSRAESFYSSDQVRERIAERYTLIPSTDSTQGPSRYWRLAQAPGIRIGFISPHSHNFCGTCNRVRLTVEGRLLLCLGNEHSVDLKAVLRATPGQPEKLEKAIIDAMQLKPWSHNFTHDDGVQVVRFMNMTGG
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Q882V6
B1IIG7
SYE_CLOBK
Glutamyl-tRNA synthetase
Clostridium
MTNKVRTRFAPSPTGYMHVGNLRTALYAYLIAKHDNGDFILRIEDTDQERLVEGALDVIYNTLKITGLSHDEGPDIGGPVGPYVQSERRNIYIEYAEKLIEKGEAYYCFCSKERLDMLRANSEALKRPFRYDKHCIDLSKEEIDKKIAEGVPYVIRQKNPTTGSTSFHDEIYGDISVDNSELDDMILIKSDGLPTYNFANVVDDHLMGITHVVRGSEYLSSSPKYNRLYEAFGWDVPIYVHCPPIMKDEHHKLSKRNGDASFEDLMAKGYLKEAILNYIALLGWNPGGEKEVFSMEELIEAFNYRNINKAPAVFDTKKLKWMNGEYIRALSLDKFHEMALPYYEEALTRDLDTKKISELLHTRVEVLNEIPEQLDFFNNLLEYSPKMYIHKKMKTTYENSLKSLEEVLPKLEALENWTFENIKEVCMNLVKELEVKNGVVLWPIRTAVSGKQFTPGGAFEIADILGKEETLERIKIGIDKLKALQ
Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).
B1IIG7
A6Q4N8
GUAA_NITSB
Glutamine amidotransferase
unclassified Nitratiruptor
MQEVPIVILDFGSQYTQLIARRLREVGVYCEIYPFFEPIENIRAKKPQGIILSGGPASVYEPDAPRVDKAIYELGIPVLGICYGMQLITVDFGGQVVRALEHEYGKAKLYFDPIHGKVCPLFEGTKDGQIVWMSHGDKVTELPAGFIRIAHTDNSPYAAIANEEKQIYALQFHPEVSHSQEGQKILENFARKICGITSKWDMGHFAKEQIEKIRQRVGEDKVLCALSGGVDSSVVTALLYEAIGDKLIPVFVDNGLLREGEREKVEYVFKNMLKVPLIVVDAKERFLNALQGITDPEQKRKIIGHTFIEVFEEEAKKHTDVKYLAQGTLYPDVIESVSVKGPSETIKSHHNVGGLPDWMKFELIEPLRELFKDEVRKLGLELGLPREMVYRHPFPGPGLAIRILGEVNEEALDLVRKADTILLEEIKAHGLYEKLWQSFAVLLNVKSVGVMGDKRTYENTVALRIVESSDGMTATFAHIPHDLLELISNRIINEVDGINRVVYDITSKPPGTIEWE
Catalyzes the synthesis of GMP from XMP.
A6Q4N8
A0LXV8
NADK_GRAFK
ATP-dependent NAD kinase
Gramella
MKIGIYGQFYHANAAQYIGQLLELLDQRNIEVLIEEDFLKLIHSNNKIEKDYKHFSAFEELDNSFDLFFCIGGDGTILKSINYIRNLDIPIVGINTGRLGFLATIQKEQIESTLEELLEKKFSLSPRSVLTMQTNPRSYDPVFSHIALNEIAVSRKNTTSMITVDTWLDDQYLTSYWADGLIISTPTGSTGYSLSCGGPVITPDADSLVITPIAPHNLNARPLVIKDHTTIKLKVSGRGKEHLVSMDSRIATLQNDTEIIIKKAPYTINFVELQGDSFLNTLRKKLLWGEDKRN
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
A0LXV8
Q9KGJ6
GLMU_HALH5
Glucosamine-1-phosphate N-acetyltransferase
Halalkalibacterium (ex Joshi et al. 2022)
MSNRFAVILAAGQGTRMKSKLYKVLHSVCGKPMVQHVVDQVSALGFDEIVTIIGHGADAVKSQLGERVSYALQEEQLGTGHAVLQAESALGGRRGVTIVLCGDTPLLTAETIDHVMSYHEEEQAKATVLTAELADPTGYGRIVRNDKGLVERIVEHKDATSEEKQITEVNTGTYCFDNEALFQALKEVGNNNAQGEYYLPDVIQILQTKGEKVAAYKTAHVEETLGVNDRVALAQAEQVMKRRINEAWMRKGVTFIDPEQTYVSPDATIGQDTVIYPGTMVLGQTTIGEGCVLGPHTELKDSKIGNKTAVKQSVVHNSEVGERVSIGPFSHIRPASMIHDDVRIGNFVEVKKSTIGKESKASHLSYIGDAEVGERVNFSCGSITVNYDGKNKFLTKIEDDAFIGCNSNLIAPVTIGKGALIAAGSTITEDVPSDALSIARARQTNKEHYVTKKNN
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.
Q9KGJ6
Q1RH25
TGT_RICBR
tRNA-guanine transglycosylase
belli group
MSKFSFNINHQYKKARSGIITTAHGNIRTPAFMPVGTRGTVKAMLPESVAETGADILLGNTYHLMLQPSAERIAKLGGLHKFMNWGKPILTDSGGFQVMSLSKLRKITEEGVSFNSHINGDKYLLTPERSTEIQHLLGSTITMAFDECTPYPATFEEAKTSMQLTTRWAHRSREAFVKRDGYAQFGIIQGSTYEELREQSAKDLIELDFEGYAIGGLAVGEGQELMFKVLAPDFLPQNKPRYLMGVGKPADIIGAVSRGVDMFDCVIPTRSGRNGQAFTKYGTVNIRNSKYAEDNDPLEADCLCPACQNYSKAYLHHLVRIGEILGAMLMTWHNLTYFQNLMSRIREYIALGKDFDFTT
Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Q1RH25
Q9W4C5
NAAT1_DROME
Sodium-dependent nutrient amino acid transporter 1
Sophophora
MELKGVQPSNGSSNGSGNGATNAASTEKTDAEKPTAERTNWGNGLEFLMSCISVSVGLGNVWRFPFTAYENGGGAFLIPYIIVLFLIGKPMYYLEMIMGQFTSQGTVKIWSVVPGFVGVGYGQAFGTICIISYYSSLLALTLYYLFVSFQSELPWSYCRDEWTNCVNSRPQEYVDNLLTGVSLANESARNLSGIVANDETEKLQSSSELYFLNVVIKEKLDISDGVGDPDWKLTLALFVAWVVIFLVIMRGVKSSGKAAYFLALFPYVVLFVLLIRAVTLEGARDGILFFLEPQWGELLNPTVWKEAVVQCFFSLAVGSGPIIMFASYNRFDHGIYRDAMIVTTLDTLTSLLGGITIFAILGNLAHNLQIENIRDVVRSGTGLAFISYPDAISKFQAVPQLFSVLFFFMLFVLGIGSIVALQSTIVTIICDQFKGWKYWKVALTTSVCGFLMGLVYVTPGGQWILTLVDFYGGTYVVFILAIFELAGIVWVYGLQNFCDDIEFMCNRRVSLYWRVCWSFFTPVMMIIIFIYSMVTIEPIKYSELYFPEAANIAGWLLFAIGAAQFPLWGLWYISRHPQGTYWKSLKASLKPSDRWGPANPEIRREWVIFKNQKAAQRATQKDTSKLGFFWRKVANFCGSNK
Unusual broad substrate spectrum amino acid:sodium cotransporter that promotes absorption of the D isomers of essential amino acids. Neutral amino acids are the preferred substrates, especially methionine and phenylalanine.
Q9W4C5
P62452
HIS6_PHOPR
ImGP synthase subunit HisF
Photobacterium
MLAKRIVPCLDVRDGQVVKGVQFRNHEIIGDIVPLAKRYAEEGADELVFYDITASSDGRVVDKSWVARVAEVIDIPFCVAGGIKSVEDASRILQFGADKVSINSPALANPALITELADKFGVQCIVVGIDSYFDAETGKYQVYQFTGDESRTKATQWETRDWVLEVQKRGAGEIVLNMMNQDGVRNGYDLKQLNMVREVCHVPLIASGGAGEMVHFADAYQKANVDGALAASVFHKQIINIGELKQYLKEQNVEIRL
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
P62452
Q3B3Q8
G6PI_CHLL3
Phosphohexose isomerase
Pelodictyon
MDLSRSAAWSALVSHRQEVEQLHMRDMFMSDHDRFKHFSIRWNGLLLDYSKNRINSRTMGLLVELARQANLIEARDGMFAGEKINFTENRAVLHTALRRQPGYTLNVDGLDVPAEVDSVLRQMKAFTDKVVGGEWKGYTGKRITDVVNIGIGGSDLGPCMVTEALRPFADGAIAVHFVSNIDGTHVSEVLKRVDAETTLFVIASKTFTTQETLTNSMTAREWFLSRAIDPAHIALHFAAVSTNRTKVVEFGIDPENMFRFWDWVGGRYSLWSAIGLSIALYLGFEAFQELLRGARAMDEHFQEAPLEENIPVILALLGVWYNNFFDVPSHAVIPYDQYLHRLPAYLQQLDMESNGKRVDRLGNTVEYPTGPIIWGEPGTNSQHAFFQLLHQGTGFIPADFILPLKTQNPIGEHHDILVANCFAQTEALMRGKSASEASEELAAAGVDEETMQMLVAHKVFPGNRPTNTLLLDEINPFTLGSLIAMYEHKVFVQGVIWQVNSFDQWGVELGKQLAKAILPELQSQKESDAHDASTNALINSYRSYREGQKVG
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
Q3B3Q8
A4WIW5
SYT_PYRAR
Threonyl-tRNA synthetase
Pyrobaculum
MRVLYIHAERFSWDPRDPALDIRDEPVSGSASNALVVFVSVERGDSPDEGFLKAVAADVVETAKKVGASSIVVYPYAHLSTDLARPYTAREVVGKLYEVVKAQFKGQVLKAPFGYYKAFELKCLGHPLSELSRVFKPEEAKTEKRAEERRDYYVVLTPDGAEYDPAKFNYAGLDDFKALVEKEVFKRELGGGEPKYLDYLRKFGFEWEPMSDVGHMRYAPEATVMMELVEDYAYMVAKSLGIPVFKIRGTNMFKLSEYAIESHARLFGERLYVVESDTDLILRYAACFQQFAMVKDWVISYRHLPFGLLEIADSYRHEQPGETVLLFRLRRFYMPDLHIFTKDLKEAMEVTFKLHEVIFREIGKLGRTYVSLYNVTEDFYKGHREYLVELARREGKPILVRILPGQKYYWVLNVEFHIVDELGRPREIATFQIDVGNAQRFGIKYVDENNQVRYPVIIHTAILGSVERYLYAVFDTMAKMEKEGKTPRLPTWLSPVQTRVIPVSKENLKYAMAVADLLEAEGIRVDVDDREETLSKKIRDAETAWVPYIIVVGSKEEAEGTVTVRERGGGQYKAKAEELAKKIREEVKGYPQRPLYLPRLLSQRPSRH
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).
A4WIW5
Q1BUV6
MSBA_BURCA
Lipid A export ATP-binding/permease protein MsbA
Burkholderia cepacia complex
METQNTLRKPMDGTGTSPMTVLKRLWPYIRPLIGIVVLAVVTMGVVAATEAGIPALLKPLLDHGFGSHGSDSAKWYVPIAVIGLALVRGVSQYTSNYLLNYVSNRILLQLRLEMFQRMIHTGASFFQRETASTVINAIVFEVNQILSVLTGVMVTLVRDSLTVIFLLGYLFYLNWRLTLIVAVILPGIGWLVSKINRRLRRLNREHQTLTNELSYIVEETVGGYKVVKVHNGEAYEMDRFTTMSKRLRGYAMRMTISGGLAQPLTQFLASIALAVVITIAVVQSSNDQTTVGGFVAFVTSMLLVISPLKHLIDVNQPLQRGMTAAELIFGLIDEPAEPQGGGRPLSQARGEIEFRAVSFDYGAAERPTLDRISFKVAPGEMIALAGPSGSGKTTLVNLLPRFFDPTDGTILVDGVPVSDYDLHALRSQMAMVSQDVVLFNDTIAANVAYGQTPDRARVQAALEAANLADAVAAMPDGLDTLVGGNGMRLSGGQRQRLAIARAIYKDAPILILDEATSALDSESERHVQAALERLMEGRTTLVIAHRLSTIERADRILVLEAGKIVEEGSHDELLRHGGLYAHLHRIQYQQQAA
Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Q1BUV6
P41271
NBL1_HUMAN
Zinc finger protein DAN
Homo
MMLRVLVGAVLPAMLLAAPPPINKLALFPDKSAWCEAKNITQIVGHSGCEAKSIQNRACLGQCFSYSVPNTFPQSTESLVHCDSCMPAQSMWEIVTLECPGHEEVPRVDKLVEKILHCSCQACGKEPSHEGLSVYVQGEDGPGSQPGTHPHPHPHPHPGGQTPEPEDPPGAPHTEEEGAED
Possible candidate as a tumor suppressor gene of neuroblastoma. May play an important role in preventing cells from entering the final stage (G1/S) of the transformation process.
P41271
O77061
MRJP2_APIME
Bee-milk protein
Apis
MTRWLFMVACLGIACQGAIVRENSPRNLEKSLNVIHEWKYFDYDFGSEERRQAAIQSGEYDHTKNYPFDVDQWRDKTFVTILRYDGVPSTLNVISGKTGKGGRLLKPYPDWSFAEFKDCSKIVSAFKIAIDKFDRLWVLDSGLVNRTVPVCAPKLHVFDLKTSNHLKQIEIPHDIAVNATTGKGGLVSLAVQAIDLANTLVYMADHKGDALIVYQNADDSFHRLTSNTFDYDPRYAKMTIDGESFTLKNGICGMALSPVTNNLYYSPLASHGLYYVNTAPFMKSQFGENNVQYQGSEDILNTQSLAKAVSKNGVLFVGLVGNSAVGCWNEHQSLQRQNLEMVAQNDRTLQMIAGMKIKEELPHFVGSNKPVKDEYMLVLSNRMQKIVNDDFNFDDVNFRILGANVKELIRNTHCVNNNQNDNIQNTNNQNDNNQKNNKKNANNQKNNNQNDN
May play an important role in honeybee nutrition. It is found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen.
O77061
Q31Y50
PTYBC_SHIBS
PTS system N-acetylmuramic acid-specific EIIC component
Shigella
MAKEISSELLNTILTRVGGPGNIASCGNCMTRLRLGVHDSSLVDPNIKTLEGVKSVILTSDQVQVVFGPGKAHRAAKAMSELLGEAPVQDAAEIAAQNKRQLKAKQTSGVQQFLAKFATIFTPLIPGFIAAGLLLGIATLIATVMHVPADAQGTLPDALNFMKVFSKGLFTFLVILVGYNAAQAFGGTGVNGAIIAALFLLGYNPAATTGYYAGFHDFFGLPIDPRGNIIGVLIAAWACARIEGMVRRFMPDDLDMLLTSLITLLITATLAYLIIMPLGGWLFEGMSWLFMHLNSNPFGCAVLAGLFLIAVVFGVHQGFIPVYLALMDSQGFNSLFPILSMAGAGQVGAALALYWRSQPHSALRSQVRGAIIPGLLGVGEPLIYGVTLPRMKPFVTACLGGAAGGLFIGLIAWWGLPMGLNSAFGPSGLVALPLMTSAQGILPAMAVYAGGILVAWVCGFIFTTLFGCRNVNLD
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring.
Q31Y50
C6DKV2
OPGH_PECCP
Glucans biosynthesis glucosyltransferase H
Pectobacterium
MNKSTSSLDYIEKLPLPAEQAEVLREKLPQAAWNDQAVLHQALSEGSPSEEHQVNVQSEDDATLQSVQARLEMAWAEGLDNGKQLGTDREGRTALKAMPVITRASMFPDVWRTNPLVRWWESLLGRTVPPRPHYSPEEKISENRWRLVGTIRRYILLVLTLFQTAIATWYMKTILPYQGWALIDPFEMAGQPWTRSLMQLLPYVLQSGILVLFAVLFCWVSAGFWTALMGFLQLLIGRDKYSISSTTVGNEPLNPEHRTALIMPICNEDVERVFAGLRATYESVEATGNLEHFDIYVLSDSNDPDICVAEQKAWMELCRDVGGTGRIFYRRRRRRVKRKSGNIDDFCRRWGNQYSYMVILDADSVMSGECLTSLVRLMEANPNAGIIQSSPKASGMDTLYARCQQFATRVYGPLFTAGLHFWQLGESHYWGHNAIIRVKPFIEHCALAPLPGEGSFAGAILSHDFVEAALMRRAGWGVWIAYDLPGSYEELPPNLLDELKRDRRWCHGNLMNFRLFLVKGMHPVHRAVFLTGVMSYLSAPLWFMFLMLSTALQVVHTLMEPQYFLQPRQLFPVWPQWRPELAIALFSTTLVLLFLPKLLSVILVWAKGAKEYGGALRVFISLLLEMLFSVLLAPVRMLFHTVFVVSAFLGWSVQWNSPQRDDDATPWSEAFVRHGSQLILGLVWAIGMAWLDLRFLWWLAPIVFSLILSPFVSVYSSRASLGLGCKRAKLLMIPEEFNPPRELVATDEYCRLNHQRRLDNGFMQAVFDPSINALASAMATARHRFSQAIEDVREKNVRDALNRKPEEVSNNQRLVLLSDPVTISRLHYHVWQKPETYAAWVESYQKLPAPHIKS
Involved in the biosynthesis of osmoregulated periplasmic glucans (OPGs).
C6DKV2
P61316
LOLA_ECOLI
P20
Escherichia
MKKIAITCALLSSLVASSVWADAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKSQQNGAVDAAKFTFTPPQGVTVDDQRK
May act as a regulator of the RCS-phosphorelay signal transduction pathway.
P61316
P38837
NSG1_YEAST
INSIG homolog 1
Saccharomyces
MGKKKSKNQLNTGGVPNGVHNTKKEAALPPLGNKLGSASFTAINTLTKPALFSFYDDDITKNEGNVYDKALLSNASQLEMVPPSATARHERSLYAKIINTIAAFFILFIAGILFPMISECLFDNDQLAKGDIVSFLKHGIEIKNKIVAEPDMVPDWAVFGTEGVIFGSIVPFIDSFVRYQHQPKTRSSVYKNTLGSFIRCANTLLGLIFGIRKLEWSSSLQAAGAWSLLNIVLWLFFDGTLTVFFPGLVIGALSAFTCSQCFSQLSLALYFIDFYFFGFLMFSKLGRYLFN
Stabilizes the HMG-CoA reductase HMG2 by preventing its HRD1-dependent degradation. Binds directly to the sterol-sensing domain (SSD)-containing transmembrane region of HMG2, promoting its folding to protect it from degradation.
P38837
Q14CS0
UBX2B_HUMAN
p97 cofactor p37
Homo
MAEGGGPEPGEQERRSSGPRPPSARDLQLALAELYEDEVKCKSSKSNRPKATVFKSPRTPPQRFYSSEHEYSGLNIVRPSTGKIVNELFKEAREHGAVPLNEATRASGDDKSKSFTGGGYRLGSSFCKRSEYIYGENQLQDVQILLKLWSNGFSLDDGELRPYNEPTNAQFLESVKRGEIPLELQRLVHGGQVNLDMEDHQDQEYIKPRLRFKAFSGEGQKLGSLTPEIVSTPSSPEEEDKSILNAVVLIDDSVPTTKIQIRLADGSRLIQRFNSTHRILDVRNFIVQSRPEFAALDFILVTSFPNKELTDESLTLLEADILNTVLLQQLK
Adapter protein required for Golgi and endoplasmic reticulum biogenesis . Involved in Golgi and endoplasmic reticulum maintenance during interphase and in their reassembly at the end of mitosis . The complex formed with VCP has membrane fusion activity; membrane fusion activity requires USO1-GOLGA2 tethering and BET1L . VCPIP1 is also required, but not its deubiquitinating activity . Together with NSFL1C/p47, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase . Also, regulates spindle orientation during mitosis .
Q14CS0
Q4JTZ6
RS18_CORJK
30S ribosomal protein S18
Corynebacterium
MKRTNMKKARMEQSRRPKKNPLKAEGIETVDYKNYDLLRKFISERGKIRSRRVTGLTPQQQRQVATAVKNAREMALLPFHSR
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.
Q4JTZ6
Q9PQI5
END4_UREPA
Endonuclease IV
Ureaplasma
MDKYNLIIGSHVSLKAKDFFYGSVKEALSYGSNTFMVYTGAPQNTKRQPIKSFKIEEAHNLLKKHNINLDDLIVHAPYIINPCSSKKNVRELAKEFLIQEIQRTESMGITKLVLHPGSRLEQNEDIALEQVYTMLNDIFSTINTNVIVCLETMAGKGSEIGVNIKQLKTIIDNVHSKKNIGVCLDTCHMNDSGLILDYYNFNQYLKEFDAQIGINYIKVLHINDSKNPCGANKDRHENLGYGTIGFANLINIIYHPLLNNIPKILETPWFNVNDELIPLYKHEIKMIRDCKWYDIKNKLLSKK
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
Q9PQI5
P04969
RS11_BACSU
30S ribosomal protein S11
Bacillus
MAAARKSNTRKRRVKKNIESGIAHIRSTFNNTIVTITDTHGNAISWSSAGALGFRGSRKSTPFAAQMAAETAAKGSIEHGLKTLEVTVKGPGSGREAAIRALQAAGLEVTAIRDVTPVPHNGCRPPKRRRV
Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome.
P04969
C6DIA0
PAGP_PECCP
Lipid A acylation protein
Pectobacterium
MYLKRTLITLSLITLPIVPFLSYAAESINNTSSTENLAPVTVDSSDPVSDKQGESWWQRSKNNLSTTWNAPQSHDIYIPAITWHNRWTYDKEKTDRYNERPWGAGYGVSRLDKDGDWHGLYIMAFKDSFNKWEPIGGYGYEKRWRPTSDQDFQLGLGFTAGVTMRDNWNYIPIPVLLPLASISYSKLSFQATYIPGTYNNGNVFFAWLRWQI
Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors.
C6DIA0
P57776
EF1D_MOUSE
Elongation factor 1-delta
Mus
MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVTSGSRQENGASVILRDIARARENIQKSLAGSSGPGASSGPGGDHSELIVRITSLEVENQNLRGVVQDLQQAISKLEARLSSLEKSSPTPRATAPQTQHVSPMRQVEPPTKKGATPAEDDEDKDIDLFGSDEEEEDKEAARLREERLRQYAEKKAKKPTLVAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFDKI
Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
P57776
A9LYY9
PROA_NEIM0
Glutamyl-gamma-semialdehyde dehydrogenase
Neisseria
MSNTQKQLALAKAAKKSVNTADTEEKNRALLAMADSLEAAAADILAANRQDLEAAAGNIPESMTDRLLLDGKRICAMADGIRAVAALPDPVGEILETSTLPNGLEIVKKRVAMGVIGIIYESRPNVTSDAAALALKSGSAVVLRSGKDAFQSARAIVAALKAGLAQTRIDPDALQLIEDTGREGSYEMMRAKDYLDLLIPRGGAGLIRAVVENAVVPVIETGTGIVHIYIDKDADWDKALRIVYNAKTSRPSVCNSMEVLLVHEDIAADFLPKLERLLVRDRIEAGLPPVRFRLDPQAARHIGGEAAGADDFDTEFLDYILAVKTVASVEEAVWHIETHSTHHSDGIVTENRHAADYFTTHIDSAAVYVNASTRFTDGGEFGLGCEMGISTQKLHARGPMGLKELTSYKYIVQGTGQVRE
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
A9LYY9
A1A1K1
RUVC_BIFAA
Holliday junction resolvase RuvC
Bifidobacterium
MIILGVDPGLTRCGVGVIEAGAYRRLSFIHVDVVRSDPKTSQDLRLLAIYNGLVEKIERFAPDAVSIERVFAQENRNTVLGTAQAAGLAMLAAAQRGIPVALHTPTESKLAITGNGKAEKIQMERMVARILGLNTLPKPADAADALAIAICHALRPAGALQGGEREQHLTAAQRQWAQASQKAARRQGVRRGM
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
A1A1K1
Q93CX7
UPP_LATSK
UPRTase
Latilactobacillus
MAKFTVLNHPLIQHKLTIIRNKNTGTKVFREVANEIAELMVYEITRDLAMEDVEVETPMGPAIEKQLSGKKLAVVPILRAGLGMVDGVLELIPAAKVGHIGMYRDEKTLQPHEYFVKLPTDIDQRQLFIVDPMLATGGSAIMAIDALKKRGATSMRLVVLVAAPEGVKAVQEAHPDVDIYAAGLDDGLNEEGYIYPGLGDAGDRLFGTK
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Q93CX7
C1DI51
PYRE_AZOVD
Orotate phosphoribosyltransferase
Azotobacter
MQAYQREFIRFAIERGVLRFGEFTLKSGRTSPYFFNAGLFDSGLALARLGRFYASALVGSGIAFDVLFGPAYKGIPLAAATAVALAEHHGLDLPWCFNRKEAKDHGEGGSLVGAPLSGRVLIVDDVITAGTAIREVMQIIQGQGARAAGVLIALNRQERGQGALSAIQEVERDFAMPVVSIASLSDVLEYLAEDAQLKRHLSAVEAYRAQYGI
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
C1DI51
Q9H0B6
KLC2_HUMAN
Kinesin light chain 2
Homo
MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGDNKPIWMHAEEREESKDKRRDSAPYGEYGSWYKACKVDSPTVNTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGKLRDALRRSSEMLVKKLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG
Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (Probable). Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends .
Q9H0B6
Q0TRK5
COBT_CLOP1
N(1)-alpha-phosphoribosyltransferase
Clostridium
MLNEVLKGIEGLDNDMILKAKNRVDSLAKPLGSLGKLEDIAIRLSGITGNMFNNIDKKCVIIMSSDNGVEEEGVASAPQCVTLLQTKNFIKGTTGVATLAKSNGTDLMVFDVGINSDEVVEGVINRKISKGTKNIYKEPAMTYEEAKKSLEIGIEAVKIAKEKGYKILGVGEMGIGNTTTSAAVLKALIGCETSQVVGKGGGINNASFEKKKRIVEEVVKKHNINFDDPIDIISKVGGYDIGAMTGVFLGAAFYRIPVVIDGFISVVAALLANRLNPLVKEFCFTSHKSQEIGYELAIKELGLDPMLDLNMRLGEGSGCPIAFSVIDFATAMMNNMATFEEGNIDNSYLEDVKDEECYIVL
Catalyzes the synthesis of alpha-ribazole-5'-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB).
Q0TRK5
B3PW62
RS12_RHIE6
30S ribosomal protein S12
Rhizobium
MPTVNQLIRKPRQANVKRNKVPALQENPQKRGVCTRVYTTTPKKPNSALRKVAKIRLTNGFEVIGYIPGEGHNLQEHSVVMIRGGRVKDLPGVRYHIIRGVLDTQGVKNRKQRRSKYGAKRPK
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
B3PW62
Q9NII6
KAX15_MESMA
Neurotoxin TX1
Mesobuthus
MKISFLLLALVICSIGWSEAQFTDVKCTGSKQCWPVCKQMFGKPNGKCMNGKCRCYS
Potent blocker of both large-conductance calcium-activated potassium channels (KCa1.1/KCNMA1) and voltage-gated potassium channels (Kv1.3/KCNA3) . Has also been shown to moderately inhibit Kv1.2/KCNA2 and weakly inhibit Kv1.1/KCNA1 channels, as well as 5-hydroxytryptamine 3 receptors (HTR3A) .
Q9NII6
P53689
ACT_PHARH
Actin
Phaffia
MDDEVAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNAPAFYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGFALPHAILRLDLAGRDLTGYLVKCLMERGYPFTTTAEREIVRDIKEKLCYVALDFEQEMQTAAQSSQLEKSYELPDGQVITIGNERFRCPEALFQPSFLGLEAAGIHETTYNSIMKCDLDIRKDLYGNVVLSGGTTMYSGIADRMQKEITSLAPSSMKVKIVAPPERKYSVWIGGSILASLSTFQSMWISKQEYDEAGPSIVHRKCF
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
P53689
P23212
MSRA_STAEP
Erythromycin resistance ATP-binding protein MsrA
Staphylococcus
MEQYTIKFNQINHKLTDLRSLNIDHLYAYQFEKIALIGGNGTGKTTLLNMIAQKTKPESGTVETNGEIQYFEQLNMDVENDFNTLDGSLMSELHIPMHTTDSMSGGEKAKYKLANVISNYSPILLLDEPTNHLDKIGKDYLNNILKYYYGTLIIVSHDRALIDQIADTIWDIQEDGTIRVFKGNYTQYQNQYEQEQLEQQRKYEQYISEKQRLSQASKAKRNQAQQMAQASSKQKNKSIAPDRLSASKEKGTVEKAAQKQAKHIEKRMEHLEEVEKPQSYHEFNFPQNKIYDIHNNYPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMRDVSLLQYLMDETDSSESFSRAILNNLGLNEALERSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQSIHDIT
Confers resistance to 14-membered ring macrolides (like erythromycin) and to B streptogramins, by acting as an ATP-dependent efflux pump.
P23212
A7GRN4
DIVIB_BACCN
Cell division protein DivIB
Bacillus cereus group
MKNSKVIKLQDRVPKLKNQKKRNKPPVNHRLILYISILFLLVLFLIYFRSPLSNIKKISVFGNHYMTDEQVMEKSGITYKTSYFRVTARQAEENLKKQIEIKSVDVKKRFPNKIDIHIEEYVTIGYINKNGKLQPLLENGKTLDILPSGKLPVAAPIFEPFKEEKMKELISELEKLTPTILRSISEIRYTPTTSNESHLTLYMNEGYEVSTTIQDFAKRMEAYPLILKQIEPGRKALIDLEVATYFKYLDDEKKK
Cell division protein that may be involved in stabilizing or promoting the assembly of the division complex.
A7GRN4
P33533
OPRD_RAT
Opioid receptor A
Rattus
MEPVPSARAELQFSLLANVSDTFPSAFPSASANASGSPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKLKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTQPRDGAVVCTLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDINRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRAPCGGQEPGSLRRPRQATARERVTACTPSDGPGGGAAA
G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.
P33533
Q9UQ88
CD11A_HUMAN
PITSLRE serine/threonine-protein kinase CDC2L2
Homo
MGDEKDSWKVKTLDEILQEKKRRKEQEEKAEIKRLKNSDDRDSKRDSLEEGELRDHCMEITIRNSPYRREDSMEDRGEEDDSLAIKPPQQMSRKEKVHHRKDEKRKEKWKHARVKEREHERRKRHREEQDKARREWERQKRREMAREHSRRERDRLEQLERKRERERKMREQQKEQREQKERERRAEERRKEREARREVSAHHRTMREDYSDKVKASHWSRSPPRPPRERFELGDGRKPGEARPAPAQKPAQLKEEKMEERDLLSDLQDISDSERKTSSAESSSAESGSGSEEEEEEEEEEEEEGSTSEESEEEEEEEEEEEEETGSNSEEASEQSAEEVSEEEMSEDEERENENHLLVVPESRFDRDSGESEEAEEEVGEGTPQSSALTEGDYVPDSPALLPIELKQELPKYLPALQGCRSVEEFQCLNRIEEGTYGVVYRAKDKKTDEIVALKRLKMEKEKEGFPITSLREINTILKAQHPNIVTVREIVVGSNMDKIYIVMNYVEHDLKSLMETMKQPFLPGEVKTLMIQLLRGVKHLHDNWILHRDLKTSNLLLSHAGILKVGDFGLAREYGSPLKAYTPVVVTQWYRAPELLLGAKEYSTAVDMWSVGCIFGELLTQKPLFPGNSEIDQINKVFKELGTPSEKIWPGYSELPVVKKMTFSEHPYNNLRKRFGALLSDQGFDLMNKFLTYFPGRRISAEDGLKHEYFRETPLPIDPSMFPTWPAKSEQQRVKRGTSPRPPEGGLGYSQLGDDDLKETGFHLTTTNQGASAAGPGFSLKF
Appears to play multiple roles in cell cycle progression, cytokinesis and apoptosis. The p110 isoforms have been suggested to be involved in pre-mRNA splicing, potentially by phosphorylating the splicing protein SFRS7. The p58 isoform may act as a negative regulator of normal cell cycle progression.
Q9UQ88
Q2RVU8
FTSQ_RHORT
Cell division protein FtsQ
Rhodospirillum
MRRVSQPPPRPRHRRRRRRDVLPSLPRASMVFLIAGGVGMAYLAARTPALAGLIGLAPPPALGAPGSSVPPAGARDAGEGWGLGETARVLTRQGLVLRQVTVTGRDLTAGRDILGAIGVPQGGPLLAIDPETVRTRLEALPWVASARVERRLPDQVHVAITEREPMALWQHNGAFAVIDREGRAIAADPGRWRTLPLVVGAGAPGHAAELLNLLTSQPGIAERVKAATLIGERRWTLRLDSIENGLVVRLPEEDPSAALDQLVQIDARDHLLSKNLSVIDMRLPGRLVVRLAEDGPVDPEAEIAGGKPARGAPAGGQKPPPIVRKSEGRDA
Essential cell division protein.
Q2RVU8
Q215X7
YQGF_RHOPB
Putative pre-16S rRNA nuclease
Rhodopseudomonas
MPAPILPLIEAAAQWPARGALIGLDLGTKTIGVAVSDPDRRLATGVETIIHTAFKANAARLLLLAGQRNAVGFVLGLPINMDGSEGPRAQSTRAFARNFARLTDLPIGLWDERLSTSAVERELIANDVSRAKRAKVIDEHAAIFILQGALDRLTVLNAAPRTD
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q215X7
Q6L3A7
RPOB_SACHY
Plastid-encoded RNA polymerase subunit beta
unclassified Saccharum
MLRNGNEGMSTIPGFSQIQFEGFCRFINQGLAEELEKFPTIKDPDHEIAFQLFAKGYQLLEPSIKERNAVYESLTYSSELYVSARLIFGFDVQKQTISIGNIPIMNSLGTFIINGIYRIVINQILLSPGIYYRSELDHKGISICTGTIISDWGGRLELAIDKKERIWARVSRKQKISILVLLSAMGLNLREILDNVSYPEIFLSFLNAKEKKRIESKEKAILEFYQQFACVGGDLVFSESLCEELQKKFFQQKCELGRVGRRNMNRRLNLDIPQNNTFLLPRDVLAATDHLIGMKFGTGILDDDDMNHLKNKRIRSVADLLQDQFGLALGRLQHAVQKTIRRVFIRQSKPTPQTLVTPTSTSILLITTYETFFGTYPLAQVFDQTNPLTQTVHGRKVSCLGPGGLTGRTASFRSRDIHPSHYGRICPIDTSEGINVGLTGSLAIHARIDHWWGSIESPFYEISEKAKEKKERQVVYLSPNRDEYYMIAAGNSLSLNQGIQEEQVVPARYRQEFLTIAWEQIHVRSIFPFQYFSIGGSLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQTALDSRVSVIAEREGKIISSDSHKILLSSSGKTISIPLVAHRRSNKNTCMHQKPRVPRGKSIKKGQILAEGAATVGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTDTTSQGSAEKITKQIPHLEEHLLRNLDRNGVVRLGSWVETGDILVGKLTPQIASESSYIAEAGLLRAIFGLEVSTSKETSLKLPIGGRGRVIDVKWIQRDPFDIMVRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGTPVDMVFNPLGVPSRMNVGQIFESSLGLAGDLLKKHYRIAPFDERYEQEASRKLVFSELYEASKQTKNPWVFEPEYPGKSRIFDGRTGDPFEQPVLIGKSYILKLIHQVDEKIHGRSTGPYSLVTQQPVRGRAKQGGQRIGEMEVWALEGFGVAHILQEILTYKSDHLIARQEILNATIWGKRVPNHEDPPESFRVLVRELRSLALELNHFLVSEKNFRVNREDV
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Q6L3A7
B1V8A0
SH3GH_CAEEL
Uncoordinated protein 57
Caenorhabditis
MSLSGLRKQFNKANQYLSETMGAAEPTKLDDVFNEMEKNVDTTYNLITDLVAGTNEYLQPNPATRAKMATQVALSKVRGTTKTSPYPQTEGMLADVMQKYGQQLGDNSDLGKSLNDAAETYRQMADIKYQMEDNVKQNFLDPLTHLQNNELKDVNHHRTKLKGRRLDYDCKKRQQRRDDEMIQAEEKLEESKRLAEMSMFNVLSNDVEQISQLRALIEAQLDFHRQTAQCLENLQQQLGHRIKDAAARPREEHVPLSVLANESRTPRSSFRSPAPSDMSHNSTAAAAFKMPPQNGGGITQAPPSYQGPPPGGLPPPLSQQQKPQCRALFDFDAQSEGELDFKEGTLIELVSQIDENWYEGRVNGKTGLFPVTYVQVLVPLK
Involved in synaptic vesicle (SV) recycling in neurons probably by regulating clathrin-mediated endocytosis . By controlling SV endocytosis, regulates the rate of excitatory postsynaptic currents (EPSCs) at neuromuscular junctions and thus locomotion . In a similar manner, involved in necrotic neuronal cell death induced by abnormal hyperactivation of ion channels . Plays a minor role in responses to mechanical stimuli . Plays a minor role in unc-26/synaptojanin localization to synapses .
B1V8A0
P83283
IBB2_AMBCE
TcTI2
Amburana
SSKWEACCDRCACTKSIPPQCHCADIRLNSCHSACESCACTHSIPAQCRCFDITDFCYKPCSG
Inhibits trypsin, chymotrypsin, plasmin and factor XIIa. Does not inhibit factor Xa, thrombin, human plasma kallikrein, porcine pancreatic kallikrein and human urinary kallikrein.
P83283
Q64391
CP1A2_CAVPO
Hydroperoxy icosatetraenoate dehydratase
Cavia
MPLSWLLPFSAMELLLTATIFYLVLWVVKAFRLQVPKGLKSPPGPWGWPLIGHVLTLGKNPHLALTRLSARYGDVLQIRIGSTPVVVLSGLDTIRQALVRQSDDFKGRPDLYSSTFISDGQSMIFNPDSGPVWAARRRLAQSALQSFSVASDPASVSSCYLEEHVSREAEHLVTKLLDLMAGPGCFEPSSQIVGSVANVIGAMCFGKNFPQTSEEMLQIVNTSKEFTEFASSGNPVDFFPILRYLPNPMLQQFKDFNKRFLQFLQKTVQEHYQDFDKNHVQDIASALFKHSEESPHVNGDLIPRKKIVNLVNDIFGAGFDTVTTAISWSLLYLVTKPEIQKKIHKELDAVIGRDRKPRLADRPQLPYMEAFILEVFRYSSFLPFTIPHCTTRDTILNGFYIPKDRCVFINQWQVNHDPKQWEDPFEFRPERFLLANNTAVDKTLSDKILLFGLGKRRCIGETLGRWEVFLFLAILLQQLEFSVPPGVKVDLTPVYGLTMKPPHCQHVQARPRFSK
A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis. May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid. Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer. Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA. May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin. Metabolizes caffeine via N3-demethylation.
Q64391
A5GN62
AMPA_SYNPW
Leucyl aminopeptidase
unclassified Synechococcus
MKISLSPATPEAWSGSVLALGIPENDPQGLVAAMEQRFSLQLSDWLKQKPFSGKPGDCVSLPLLRSDCTALVLVGLGEASSVDRDRLRLAAAAAARAAQGQGGTLGLLLPWSSDTPEEDAAAAAEAVRLALYSDERFRSKPEPSPKPDQLELLGSLPGGLSHGLEAVHPVCAGVELARELVAAPPNSVTPAELARTASHLAHEHGLELTILERSDCEERGMGSFLSVCQGSDMDPKFIHLTYRPNDAASKRLVLVGKGLTFDSGGYNLKVGAAQIDMMKFDMGGSAAVFGAMRAIAELRPAGVEVHMLVASCENMINGSAVHPGDIVTASNGTTIEINNTDAEGRLTLADALVYACKLKPDAIVDLATLTGACVIALGDEIAGLWSGDDSLSSQLEMAAQAAGEGLWRMPLHSPYRKGLKSLLADMKNTGPRPGGSITAALFLKEFVDAGIPWAHIDIAGTVWSDKGRGLDPSGATGYGVRTLVNWITNQANT
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
A5GN62
A3CP56
SYT_STRSV
Threonyl-tRNA synthetase
Streptococcus
MIKITFPDGAVREFESGVTTFEIAQSISNSLAKKALAGKFNGKLIDTTRAITEDGAIEIVTPDHEDALDILRHSAAHLFAQAARRLFPDIHLGVGPAIQDGFYYDTDNEAGQISNEDLPRIEEEMKKIVKENFPSIREEVTKDEAREIFKNDPYKLELIEEHSEDEGGLTIYRQSEYVDLCRGPHVPSTGRIQIFHLLNVAGAYWRGNSDNAMMQRVYGTAWFDKKDLKKYLQMREEAKERDHRKLGKELDLFMISQEVGQGLPFWLPNGATVRRELERYIVDKELASGYQHVYTPPLASVELYKTSGHWEHYQEDMFPTMDMGDGEEFVLRPMNCPHHIQVYKHHVHSYRELPIRIAEIGMMHRYEKSGALTGLQRVREMSLNDGHLFVTPEQIQEEFQRALQLIIDVYADFNLTEYRFRLSLRDPQDTHKYFDNDEMWENAQTMLRAALDEMGVDFFEAEGEAAFYGPKLDIQVKTALGNEETLSTIQLDFLLPERFDLKYVGADGEEHRPVMIHRGVISTMERFTAILIENYKGAFPTWLAPHQVTLIPVSNEAHIDYAWQVAKKLRDKGVRADVDERNEKMQYKIRASQTSKIPYQLIVGDKEVEDGTVNVRRYGQKETHTVAVDEFVEQILADIASKSRLEK
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).
A3CP56
Q8DBE8
LPXB_VIBVU
Lipid-A-disaccharide synthase
Vibrio
MSNKPLRIGIVAGELSGDTLGEGFIKAIKAVHPDAEFVGIGGPKMIALGCQSLFDMEELAVMGLVEVLGRLPRLLKVKAELVRYFTENPPDVFVGIDAPDFNLRLELDLKNAGIKTVHYVSPSVWAWRQKRIFKIAKATHLVLAFLPFEKAFYDKFNVPCEFIGHTLADAIPLESDKAPARELLGLEQDKQWLAVLPGSRGSELKMLSQPFIETCKKLQQAFPELGFVVALVNQKRREQFEQAWKEYAPELDFKLVDDTARNVITASDAVMLASGTVALECMLLKRPMVVGYRVNAVTAFLAKRLLKTQYVSLPNILADTELVKEYLQDDCTPDNLFGEVSRLLEGDNHQMLDKFTEMHHWIRKDADQQAANAVLKLIEK
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q8DBE8
A2RAW3
CLP1_ASPNC
mRNA cleavage and polyadenylation factor clp1
Aspergillus subgen. Circumdati
MSLPGLDLTQPSADREFAPAPPSQISLPKGSEWRFEVAFGTTVRVKLLAGTAELFGTELAPSQTYTFSGTKAAIYTWHGCTLESEYVAEETPMVEYANVHFALETLRQEAKATGKDGPRVLILGPEDAGKTSLSKILTAYATKVGRQPLVVNLDPTEGMLSVPGTLTATAFRTMIDVEEGWGSSPMSGPSAVPVKLPLVYFYPMQNPLEADGSVYKAIVSRLALSVTGRMAEDEDARETGIIVDTPGILSQSKAGNVEMINHIVTEFAITTILVIGSERLYSIMMKNFDNKPTASASAAASDERISVVKLSKSGGCVDRDAAFMKAVSESQIRTYFFGNPIPSTASAALSLSASSTTNVTLSPHAQQLDFNALAVYNYTIASAEEDEDEYDPSQLGTGDAFLPGGSNDVDLALANSLLAITHASSTASPADVRDASIMGFLYVADVDAEKGKIRVLAPVGGRVPPRAIKKYIDSSKV
Required for endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation.
A2RAW3
Q7VJX1
SSRP_HELHP
Small protein B
Helicobacter
MPIRVIAKNKKAYFDYEILQSLESGIVLQGSEVKSIRAGRVNLKDSFIKIIRGEAFLFNAHISFLQTTYTHFKPNERRERKLLLHKKEIDKLFGSVSKESLSIVPLNIYFNQKNKIKLCIALVRGKKLHDKRESIKKKMLEREARAHMKSYGKKL
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Q7VJX1
A3GH78
MPH1_PICST
FANCM-like protein 1
Scheffersomyces
MPIDSDDNVFDDDDDFIELLQDSSNQTSNVTNEIATDSTNSTNTRLVVPNNRLLEEIPVPKRILLGPTHHKIDYGNLDKYVYPSNFEVRDYQFNIVQRAFYHNLLVALPTGLGKTFIASTVMLNFLRWFPESKMIFVAPTKPLVAQQIKACCSITGIPSSKVAILLDKTRKNRGEIWDEKQVFFTTPQVVENDLASGLVDPKTIALLVIDEAHRAKGNYAYNNIVKFMDRFTNSYRILALTATPASDVDGVQEIIDNLNISKVEVRSEESIDIIKYMKRKRIIRRNIYQSDEIKECIDLLCTAIAPVLKVANGKGILEITDPSRINFFQCMDASRKIVANPTIPEGTKWSNFFTLQLLGVVGQCFRRLNVYGLRSFFSYFNEKYTEFMAKHSKKKSSNKLNADFYFSEPIKQLMKRIRTMIDDPKVFSHPKIEAMMEELDEFFTINNATDSKVIIFTEFRESALEIVRFIEKVGKNLKPHIFIGQAKERDKFDESNFGKKSKGKRVGKKQQDDSKSSSENAQINGMNQKLQKEIIKNFKQGTYNILVATSIGEEGLDIGEVDLIICYDSTSSPIKNIQRMGRTGRKRDGKVVLLFSSNEESKFDKAMNGYEYIQQHIMKGQLIDLKEQNRMIPKDWEPKVEMRFIEIPEENHELQVVDDEDEIIRIATQYMMGGKSKKKKAAASKKGKTKEKRAKQFFMPDNVEIGFRSVTSMVRAVGSSKSLEEEKKEEKVRDVLDRIVDSDSDEEIPLGSIPIPRSEVIAHKQSTTDEQLLERDCQSGSNISDRTLDQHHSASEERGINSNFSHESNLPTPPENSPPKRKSIVLEEARIAKKKHKKSLGIRKPTIRPPSIIDQLKKQKSKIIRPDSANETICLDEDDILLPEYTNITEKEVTVQEDRREIEHDDDSEIFDDGLDEQLAMIDDMNTTKSFVEPTRIDFKDEVFKNDFDEHEGFLNNDELMELHTSYFTAIDPMDKVFYYDPSSSVHVDGANREYAFYGKIGHSKRSQVLIGLQKRAHEMAAKSKQSKTATPSEPETFQNYLDSDFIALQ
ATP-dependent DNA helicase involved in DNA damage repair by homologous recombination and in genome maintenance. Capable of unwinding D-loops. Plays a role in limiting crossover recombinants during mitotic DNA double-strand break (DSB) repair. Component of a FANCM-MHF complex which promotes gene conversion at blocked replication forks, probably by reversal of the stalled fork.
A3GH78
Q6CG56
DHYS_YARLI
Deoxyhypusine synthase
Yarrowia
MSETPNLATEAVLVHSAPVPEDAVPVSGIDFDKPENKNTRAADLVGAMNGMGFQATSLGQACNIIDEMRTWEGVDKEGNPAKTTIFLGYTSNLISSGLRSTLKYLVKNKMVSAIVSSAGGIEEDLIKCLAETYLGDFALKGSVLRETGMNRIGNLLVPNDNYCKFEEWVVPILDTMLEEQEKQGVSWTPSTVIDRLGKEIDNEDSVLYWAHKNQIPVFCPALTDGSLGDMLFFHTFKASPLQLKIDIVADIRKINSMSMAATRAGMIILGGGLVKHHIANACLMRNGADYAVYINTGQEFDGSDAGARPDEAISWGKIKAGAKHVKVYADATLVFPLVVAATFAKE
Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Q6CG56
Q6NHR6
GLGB_CORDI
Glycogen branching enzyme
Corynebacterium
MVSPTQITPVHPDVLHALKICQYHDPHGVYGWHEVDAERAVIRTRHIGAERVETLLSDSTVVELAAVGDDIFEAIVDHDASCDYRLRIHWQGGQVTEQADAYHFLPTLGDLDLHLINEGRHERLWEVLGANPTTITTAMGDVEGTAFAVWAPNASGVAVIGDFCGWNPSQYPMRSLGSTGIWELFIPNIGVGTVYKFAIHTHEGHRLDKADPMAKRAEVAPATGSIIASSSYTWNDDTWMTNRAHTDHDNTAMSVYEVHLGSWSQGQNYEELATNLVDYVKEMGYTHVEFLPVAEHPFGGSWGYQVSGYYAPTSRWGTPDQLRLLIDAFHQAGIGVIVDWVPAHFPKDAFALGRFDGQALYEHPDWRRGEQKDWGTYVFDFGRNEVRNFLVANALYWLEEFHVDGLRVDAVASMLYLDYSREPGEWLPNIYGGRENLEAVQFLQEMNATVHKSHPGVMTIAEESTSWPGVTSPTWEGGLGFSMKWNMGWMNDTLEYFSHEPIHRMYHHNDITFSMVYAYSEKFVLPFSHDEVVHGKGSLWTRMPGDAWNKAAGLRTLYAYMYAHPGKNLLFQGQEFGQVKEWSEERSLDWGDMDGWEGEYHRGIRTLVQDLNALYKDSPALYSQDNNPAGFSWTKSDDAANNILSFVRYGADGSKILAVFNFGGADHPSYKLGVPEGGNWKCILNTDAGIYEGEDNYLDSDVMAWDTDWDGYQHSLTVHIPAMSGQLYRWEA
Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position.
Q6NHR6
P58749
TM6S1_MOUSE
Transmembrane 6 superfamily member 1
Mus
MSASAATGVFVLSLSAIPVTYIFNHLAAQHDSWTIVGVAALILLLVALLARVLVRRKPPRDPLFYVYAVFGFTSVVNLIIGLEQDGIIDGFMTHYLREGEPYLNTAYGHMICYWDGSVHYLMYLVMVAAIAWEESYRTIGLYWVGSIIMSIVVFVPGNIVGKYGTRICPAFFLSIPYTCLPVWAGFRIYNQPSENYNYPSKVLQEAQAKALLRRPFDLVLVLCLFLATGFCLFRGLIALDCPAELCRLYTQFQEPYLKDPAAYPKIQMLAYMFYSVPYFVIALYGLVVPGCSWMPDITLVHAGGLAQAQFSHIGASLHARTAYVYRVPEEAKIFFLALNIAYGVLPQLLAYRCTYNPEFFLRTKADEKLE
May function as sterol isomerase.
P58749
B4I9X1
EI3G1_DROSE
Eukaryotic translation initiation factor 3 subunit 4-1
Sophophora
MPGVETIKSSWADEVELDYGGLPPTTETVENGQKYVTEYKYNKDDKKTKVVRTYKISKQVVPKTVAKRRTWTKFGESKNDKPGPNSQTTMVSEEIFMQFLNSKEDEKANDPLLDPTKNIAKCRICNGEHWSVNCPYKGTAMDTNMMEKKASAAAAAAVDAPKSGKYVPPFLKDSQKGALGMRGRDDTAAIRISNLSESMTEADLEELVKKIGPQSKMYLARDKNTGLCKGFAYVHFKQRKDAAAAIEILNGHGYDHLILSVEWSKPQNN
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
B4I9X1
Q3K0E8
PYRR_STRA1
Uracil phosphoribosyltransferase
Streptococcus
MKRKEIIDDVTMKRAITRITYEIIERNKNLDNIVLAGIKTRGVFLAKRIQERLKQLENLDIPVGELDTKPFRDDMKVEVDTTTMPVDITDKDIILIDDVLYTGRTIRAAIDNLVSLGRPSRVSLAVLIDRGHRELPIRADYVGKNIPTSQFEEILVEVMEHDGYDRVSIIDPS
Also displays a weak uracil phosphoribosyltransferase activity which is not physiologically significant.
Q3K0E8
A3PAT7
OBG_PROM0
GTP-binding protein Obg
Prochlorococcus
MQFIDQANIILKAGKGGNGIVSFRREKFVPAGGPSGGNGGRGGSVILMADNNLQTLLDFKFKREIIAEDGCKGGPNKRSGASGQDTILKVPCGTEIRDIKTGIILGDLTKDKQSLTIAIGGRGGHGNAYYLSNQNRAPESFTEGKDGEIWEVQLELKLLAEVGIIGLPNAGKSTLISVVSSARPKIANYPFTTLIPNLGVVRKMDGNGCLFADIPGLISGAADGVGLGHDFLRHIQRTKILVHLIDAIAENPLHDFEIIEQELKKYGKGLLDKERIIVLNKMELVDDDYLQIITKKLEDLSKKKVLVISSSLKKGLSSLLSEVWKRI
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.
A3PAT7
P01461
3SA4_NAJHA
Toxin CM-11
Naja
LKCNKLIPPFWKTCPKGKNLCYKMYMVSTLTVPVKRGCIDVCPKNSALVKYVCCNTNKCN
Shows cytolytic activity on many different cells by forming pore in lipid membranes. In vivo, increases heart rate or kills the animal by cardiac arrest. In addition, it binds to heparin with high affinity, interacts with Kv channel-interacting protein 1 (KCNIP1) in a calcium-independent manner, and binds to integrin alpha-V/beta-3 (ITGAV/ITGB3) with moderate affinity.
P01461
Q82W26
HISX_NITEU
Histidinol dehydrogenase
Nitrosomonas
MIKIRRLSSVDDHFQAELDQLLSFEVSVDSEIERTVTQILHQIRTHGDRALLELTRQFDNPDIDRIEEIELPRDEWQSALMSLDKVQREALEQAASRIRAYHEKQLAQSWDYVELDGTRLGQKITALDRVGLYVPGGKAAYPSSVLMNAIPARVAGVRELIMVTPTPKGEKNPLVLAAAAICEVDRVFTIGGAQAVAALAYGTTTVPKVDKIVGPGNAYVAAAKRHVFGTVGIDMLAGPSEILVICDGKTNPDWIAMDLFSQAEHDEQAQSILLCPDKAFLDRVADSISRLIDTLPRRDVIRSSLENRGALIHVRDLEEACMIANRIAPEHLELSVDEPEQWVDSIRHAGAIFLGRYTCEALGDYCAGPNHVLPTSGTARFSSPLGVYDFQKRTSLIQVSAAGASRLGETASILAKGEGLDAHARSAESRYQ
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Q82W26
Q3IZ13
ATPL_CERS4
Lipid-binding protein
Cereibacter
MEGDIAEMGKFIGAGLATIGLGGAGIGVGHVAGNFLAGALRNPSAAPGQMANLFVGIAFAEALGIFSFLIALLLMFAV
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.
Q3IZ13
A4SLX9
RECR_AERS4
Recombination protein RecR
Aeromonas
MKFSPLLDEMMKALQVLPGVGPKSAQRMAFTLLERERSGGLRLAQLLNRALTEIGHCSHCRTFTENALCEICANPKREESGLLCVVESPADVAAIEHTGQFSGRYFVLMGHLSPLDGIGPEELGLEILEQRLKAESISELILATNPTIEGDATAWYIADMARAAGVKVSRIAHGVPVGGELELVDGTTLSHSLMGRQPLN
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.
A4SLX9
D5VGV1
RUTB_CAUST
Ureidoacrylate amidohydrolase RutB
Caulobacter
MSSPITPLSPGCVMLPARPEPVPVDPKTTAVIVIDMQNAYASPGGYLDLAGFDISGAAKVIHEIKGVLEVARSAGMQVIYFQNGWDDQYVEAGGPGSPNWWKSNALKTMRAKPELQGKLLARGQWDYELVDELKPQPGDIQLHKTRYSGFFNSQLDSVLRARGIRHLVFVGIATNVCVESTLRDGFFLEYFGTVLEDATHQAGPEFVQKAALFNIESFFGWVSTTADFKGTFGQLAPRT
Hydrolyzes ureidoacrylate to form aminoacrylate and carbamate. The carbamate hydrolyzes spontaneously, thereby releasing one of the nitrogen atoms of the pyrimidine ring as ammonia and one of its carbon atoms as CO2.
D5VGV1
Q2JL88
MURC_SYNJB
UDP-N-acetylmuramoyl-L-alanine synthetase
unclassified Synechococcus
MPVPSQPLPLHLDPLDPLLSTYHFVGIGGVGMSALAYILAKQGFRVSGSDIVANGRTRRLEALGVRFFQGHSSEGLVGDPQVVYSSAIRPTNPELAAALGKGLTVWHRADLLAALFNRRSGIGVAGTHGKTTTSSMIGYVLLSAGWDPTLIIGGEVDAWDGNARLGKGEYWVAEVDESDGSLVRLYPKIGVITNIELDHPDHYADLGQVIRAFQQYGQQSQTLVACLDCPNVAAHLRVDVGYSLTGHPQAQYQARQILYTASFTCAEIWEKGSLLGQLRLQVLGSHNLSNALAAVAVGRQLGLEFAVIASALAQFRGAHRRFEHKGEVGGVTFIDDYAHHPSEIRATLQAARLQQRRVVAVFQPHRHSRLAALFQDFARCFGEADVVVIVPTYGAGEPAPEGSDSLRLAVAVAEHHPHVRYVSSLPQLPEVLPSVLQPGDLAVFLGAGDLNQQIIATMRAYAAQVREQPGQAKNPNFS
Cell wall formation.
Q2JL88
Q0I3R3
ACKA_HAES1
Acetokinase
Histophilus
MSQKLVLILNCGSSSLKFAILDPVSGAEKLSGLAEAFYLPDARIKWKLNGEKGNADLGAGAAHSEALNFIVSTILTEDLKNSIAAIGHRVVHGGEKYTKSVVITDEVIQGIKDAAEFAPLHNPAHLIGIEEAFKAFPHLKDNNVAIFDTAFHQTMPEEAFLYALPYSLYKEHGVRRYGMHGTSHYFVSREAAKRLNIAEDKINVITCHLGNGASVAAIRQGKCIDTSMGFTPLEGLVMGTRSGDLDPAIIFYMHNTLGMSVAQIEETLVKKSGLLGLTEVTSDCRYSEDNYEKESAAKRALDVFCYRLAKYIGSYMAIIGENLDAIVFTGGIGENAALVRQITLNHLKLFGYKIDDEKNSAARFGNEGVITADNTPIAIVIPTNEELVIAQDTARLSF
Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Q0I3R3
P17305
STP1_BOVIN
Spermatid nuclear transition protein 1
Bos
MSTSRKLKSQGMRRGKNRTPHKGVKRSGSKRKYRKSSLKSRKRCDDANRNLRSHL
Plays a key role in the replacement of histones to protamine in the elongating spermatids of mammals. In condensing spermatids, loaded onto the nucleosomes, where it promotes the recruitment and processing of protamines, which are responsible for histone eviction.
P17305
A7M916
PETG_CUSGR
Cytochrome b6-f complex subunit V
Cuscuta sect. Oxycarpae
MIEAFLLGIILGLIPITLIGLFVTAYLQYRRGDQLDF
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetG is required for either the stability or assembly of the cytochrome b6-f complex.
A7M916
A7I058
SYDND_CAMHC
Non-discriminating aspartyl-tRNA synthetase
Campylobacter
MRSNYCTELDSGDIGKIVDVCGWVNSYRDHGGVIFIDLRDRSGLIQLVCDPKHSQEAYTIANSVRDEFVLRAHGKIRARGKDLINPKLKTGEIEVVVENLIVENPSKPLPFVIGDKNVSEETRLKYRFLDLRTNENFNKFFTRSKAAIAARNALDRLGFVEVETPILTRATPEGARDYLVPSRVYNGQFYALPQSPQLFKQLLMCSCFDKYFQIARCFRDEDLRADRQPEFTQIDIEMSFCDQKDVMKVGEAVLKDIFKSCGKDIKTPFRVMQYKDAMENYGSDKPDLRFGMKFIDVADIFEKSSNEIFANIAKDKKKNRVKAIKVEGGDLKFSKRQMQRFEEYVRKFGAQGLAFIQVKEEGLKGPLVKFFEKSEIDELVKRCELKVGDVVFFGAGKKKIVLDYMGRFRIFLANELELINPDALEFLWVVDFPMFEQNEDGTYSAMHHPFTMPNNVDEPDIEEITSIAYDVVLNGIELGGGSIRIHKEDIQEKVFKLLKIEPAEQREKFGFLLDALSFGAPPHGGIAIGFDRLMMLVTRSSSIRDVIAFPKTQRAQCLLTKAPSGISNEQLRELGLKINKKEQK
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
A7I058
Q3JD12
GLGA2_NITOC
Starch [bacterial glycogen] synthase 2
Nitrosococcus
MYKILFATSEAHPLIKTGGLGDVAGILPIELARLGLEAGIILPAYPACKTHLKNLKEVARLRLPAALEPVRILKGQLLEGPNPVWLVDSPAHFDRPGNPYLNEQGQDWPDNAARFTTFCRAVATLANSPEFDWQPDLIHCNDWQTGLIPPFLAPLRSRPATLFTIHNLAYQGVFSRQQFDALELPSAWWSPAALEFYNQISFIKGGLVFADWLTTVSPTYAKEILTPEFGCGLDGVLRGRSKRLTGILNGADYQRWDPRHDPFIEKRYDQTCWSHKASNKLALQRRYGLPEDDTLPVLGFVGRLVEQKGIDLILGALPKLLAEKIQVVFLGEGEERHQNALQQLASRYPNQIGVSISYDERLAHGVQAGADIFLMPSRFEPCGLTQLYALRYGTVPIARRTGGLSDTIVDATEKNLRQELATGFTFTESSPSALLTAIQRALACYAQSRQWRRLALTGMAQNFSWQTSAKAYFDLYQQLVSQEFSCKNNVL
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
Q3JD12
Q8FMT9
CLPS_COREF
ATP-dependent Clp protease adapter protein ClpS
Corynebacterium
MCSSPSAPTAEPDVEMDVHTVSSENLPWLCIVWDDPVNLMSYVTYVFQTVLGYSRKRANELMMQVHTEGKAVVSSGEKDKVEGDVKKLHVAGLWATMQQAG
Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
Q8FMT9
A5V8U1
PYRG_RHIWR
UTP--ammonia ligase
Rhizorhabdus
MARFIFITGGVVSSLGKGLMAASLAALLQARGYKVRIRKFDPYLNVDPGTMSPYQHGEVYVTDDGAETDLDLGHYERFTGVPGRQSDNITSGRIYQTIIQKERRGDYLGATVQVIPHVTDAIKEFARADTEGLDFVLCEIGGTVGDIESLPFMEAIRQLRNDLGRGNSIFVHLTLVPYIAAAGELKTKPTQHSVRDLTSLGIQPDVLVCRCDRPLPEGERAKIALFCNVPTEAVIPALDASSIYGVPLQYHEEGLDEAVLSAFGIEAKDEPDLTRWTEIMDRLENPEGEVTIGVVGKYVGLLDAYKSLHEALVHGGIANRVKVNIRWIDAELFEQEEGGIAAQLEPMHAILVPGGFGERGSEGKIAAVRFARERKVPYFGICLGMQMACIEGARNTAGIAAASTTEFGPTDEPVVGMITEWMSEDGLQKREAGGDLGGTMRLGAYDARLSGNSHAATIYGATDISERHRHRYEVNVHYRESLERGGLVFSGMSPDGELPEVVERPDHPWFVGVQFHPELKSKPFDPHPLFASFIAAALQQSRLV
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.
A5V8U1
A1WX12
FABZ_HALHL
Beta-hydroxyacyl-ACP dehydratase
Halorhodospira
MSERDAQGATDIEGIMNLLPHRYPLLLIDRVLDFQPHEHLASIKNVTINEPFFVGHFPQKPVMPGVLILESLAQACGMLAFKSVQDTLTDNDVLYLVGIDKARFKRPVQPGDQLRHDVSVRRVTRGIWIFEARGSVDGELAAECEIRCTVRTV
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
A1WX12
Q58605
METK_METJA
Methionine adenosyltransferase
Methanocaldococcus
MRNIIVKKLDVEPIEERPTEIVERKGLGHPDSICDGIAESVSRALCKMYMEKFGTILHHNTDQVELVGGHAYPKFGGGVMVSPIYILLSGRATMEILDKEKNEVIKLPVGTTAVKAAKEYLKKVLRNVDVDKDVIIDCRIGQGSMDLVDVFERQKNEVPLANDTSFGVGYAPLSTTERLVLETERFLNSDELKNEIPAVGEDIKVMGLREGKKITLTIAMAVVDRYVKNIEEYKEVIEKVRKKVEDLAKKIADGYEVEIHINTADDYERESVYLTVTGTSAEMGDDGSVGRGNRVNGLITPFRPMSMEAASGKNPVNHVGKIYNILANLIANDIAKLEGVKECYVRILSQIGKPINEPKALDIEIITEDSYDIKDIEPKAKEIANKWLDNIMEVQKMIVEGKVTTF
Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
Q58605
Q9Z8I4
LEPA_CHLPN
Ribosomal back-translocase LepA
Chlamydia
MKEYKIENIRNFSIIAHIDHGKSTIADRLLESTSTVEEREMREQLLDSMDLERERGITIKAHPVTMTYLYEGEVYQLNLIDTPGHVDFSYEVSRSLSACEGALLIVDAAQGVQAQSLANVYLALERDLEIIPVLNKIDLPAADPVRIAQQIEDYIGLDTTNIIACSAKTGQGIPAILKAIIDLVPPPKAPAETELKALVFDSHYDPYVGIMVYVRIISGELKKGDRITFMAAKGSSFEVLGIGAFLPKATFIEGSLRPGQVGFFIANLKKVKDVKIGDTVTKTKHPAKTPLEGFKEINPVVFAGIYPIDSSDFDTLKDALGRLQLNDSALTIEQESSHSLGFGFRCGFLGLLHLEIIFERIIREFDLDIIATAPSVIYKVVLKNGKVLDIDNPSGYPDPAIIEHVEEPWVHVNIITPQEYLSNIMNLCLDKRGICVKTEMLDQHRLVLAYELPLNEIVSDFNDKLKSVTKGYGSFDYRLGDYRKGSIIKLEVLINEEPIDAFSCLVHRDKAESRGRSICEKLVDVIPQQLFKIPIQAAINKKVIARETIRALSKNVTAKCYGGDITRKRKLWEKQKKGKKRMKEFGKVSIPNTAFIEVLKLD
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
Q9Z8I4
A6TF99
ARNC_KLEP7
Undecaprenyl-phosphate Ara4FN transferase
Klebsiella
MLTYPPVKKVSVVIPVYNEQDSLPELLRRTDAACATLGRQYEILLIDDGSSDDSARMLTEAAEAEGSHVVAVLLNRNYGQHSAIMAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSIFRKTASKMINRLIQRTTGKAMGDYGCMLRAYRRHIIDAMLNCHERSTFIPILANTFARRAVEIPVMHAEREFGDSKYSFMRLINLMYDLVTCLTTTPLRLLSIFGSVIALLGFAFGLLLVVLRLAFGPQWAAEGVFMLFAVLFMFIGAQFVGMGLLGEYIGRIYNDVRARPRYFIQRVVRQPETASKEEDRS
Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
A6TF99
A5GHN9
MURC_SYNPW
UDP-N-acetylmuramoyl-L-alanine synthetase
unclassified Synechococcus
MRSLVCTLDIQSPVHFIGAGGIGMSALARILLSRGHRVSGSDRRLSPAMESLKTAGMVAFESQAAANFQALDRLDRSSPIVVISSAIPDHNPELVAARERQLEVWHRSDLLAALIDQQPSIAIAGSHGKTTTSTVVTTLLHGAGEDPTAVIGGIVPCYDSNGHAGQGRLLVAEADESDGSLVKFRASLGVITNLELDHTDHYRDLDDLIATLQRFGDGCKRLLANQDDPILSEHFQADAWWSVQRSDNVDFAGLPVALEGDRTIADLYEQGTFVGQITLPMPGLHNLSNTIGALAACRMEGVPLEHLISHLSELKTPGRRFDYRGDWQGRQIVDDYAHHPSEVAATLNMANLMVSSGRSPLPRSPQRLVAVFQPHRYSRTQEFQTEFARALLSAELVLLAPIFAAGEAEMPGVNSEALASVMQELSTQQSVLVASTMDELVSLVKEHSLPDDLVLAMGAGDVNSLWSRLSQSSSEGQASCPPALAA
Cell wall formation.
A5GHN9
P26772
CH10_RAT
Chaperonin 10
Rattus
MAGQAFRKFLPLFDRVLVERSAAETVTKGGIMLPEKSQGKVLQATVVAVGSGGKGKGGEIQPVSVKVGDKVLLPEYGGTKVVLDDKDYFLFRDGDILGKYVD
Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein.
P26772
Q8SXL2
CCHA2_DROME
Neuropeptide CCHamide-2
Sophophora
MKSTISLLLVVICTVVLAAQQSQAKKGCQAYGHVCYGGHGKRSLSPGSGSGTGVGGGMGEAASGGQEPDYVRPNGLLPMMAPNEQVPLEGDFNDYPARQVLYKIMKSWFNRPRRPASRLGELDYPLANSAELNGVN
Ligand for the CCHamide-2 receptor CCHa2-R . In one study, shown to be an orexigenic peptide which induces appetite and stimulates food intake, leading to the release of insulin-like peptides which stimulate growth . In another study, shown to be a nutrient-sensitive peptide derived from peripheral tissues which controls growth by directly regulating the production and release of insulin-like peptides .
Q8SXL2
A5IJR7
CH10_THEP1
Chaperonin-10
Thermotoga
MMKVIPLGERLLIKPIKEEKKTEGGIVLPDSAKEKPMKAEVVAVGKIDDEEKFDIKVGDKVIYSKYAGTEIKIDDEDYIIIDVNDILAKIEE
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.
A5IJR7