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2.75k
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5.51k
AlphaFoldDB
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10
Q8EU02
SYE_OCEIH
Glutamyl-tRNA synthetase
Oceanobacillus
MSKEVRVRYAPSPTGHLHIGNARTALFNYLYAKHFDGKFIIRTEDTDDKRNVEGGEESQLKYLKWLGLQWDEGADIGGEYGPYRQTERLDIYQEYLNELFAKNLAYKCYMTEDELEAEREEQRQNGQVPKYSGAHRDLTPEQIEQFEAEGRQPSIRFRVPENTTYTFNDLVRGKITFESSDFGDWVIVKKNGIPTYNFAVAIDDHLMKISDVLRGEEHISNTPKQMMIFDAFGWEAPRYGHMTLILNEERKKLSKRDEHILQFIEQYRNLGYLPEAMFNFISLLGWSPVGEEEMFTQAQLIEIFDPERLSTSAAIFDQHKLKWMNNEYIKAADLDRVIDLALPHLIKAGKLSEDMDDETRQWAENVISLYREQLRYGAEIVELTELFFQKEISYDEEAKEVLNGEQVPEVLQVFTDKLIHLESFDKDAIKAQFKATQKETGHRGKKLFMPIRVATTGQMHGPELPFAIELLGRDIILNRLDKLLKEMGA
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).
Q8EU02
Q09826
SDS23_SCHPO
Phosphoprotein at stationary phase 1 protein
Schizosaccharomyces
MPLSTQSSDSLSSAGRQSFGVNSVSDFLAQFPIPTNLPSNKWQDIPVTFLHDNEIALIDPETSMEEASSILIDRDLSALPIVAAKGSNEIATTFDYADLNSFLLMVVGFDDFNDGRFKKVAEDIRAGKVITAYEVAKLGKNKDDFITIPHTTSLGRLAEILSSGIRRVAVTNEQGELSFMASQRSIIRFLWNNIRAFPDLEPLMSRTIHSLDIGSTDITCISGDQKVAAALRQMNQTGIGSLAVVDAQFRLLGNISLVDVKYVTRSSSVYLLNKSCAHFLSVIKSEQGIRAGKDSAPAFNIYESSTFAFTLAKLVATQCHRLWLVQSPSCPPSPKNNAHLSPGSMGGVKVNQLLGVVSLTDIISVLYAHMKGTLPPAPHSAPSLRHGRRGSTSSHRSHSKASVDTQRR
Required for normal DNA replication and for proper mitosis. Induces sexual development and ascus formation.
Q09826
Q9YBY0
QUEC_AERPE
PreQ(0) synthase
Aeropyrum
MAVCRAVSIVSGGPDSFTYTLIWLSRGCSVHALSFNYGQKASREVLTARKLLEKADELASERGWGRVLEHRLVDISFMKSLWRGTQLTDEEVEVKEDYAPSVVVPIRNVVMLSIAAAYAYSLLEEEDVDRVVVTYGAQRGDIKPRPDTGEPLYPDCSPECIEALQAAFRLCHFRGMRRLEVWSPSREGLSKSDLLKWAYGTVGKLIYDTWSCYLNGKYHCGRCESCINRHRAFKDAGLPDCTRYEKPPGPEAEFESRGDYYVHRSCREA
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Q9YBY0
A8YU90
RF3_LACH4
Peptide chain release factor 3
Lactobacillus
MDKELAEKVKKRRTFAIISHPDAGKTTITEQMLLFGGVIRKAGTVKARKTGNFATSDWMEIEKKRGISVTSSVMQFEYKGKRINILDTPGHQDFSEDTYRTLMAVDAAVMVIDSAKGIEPQTKKLFKVVKKRGIPIFTFMNKLDRDGRPPLDLIAELEDLLGIEGVAMDWPIGSGQTLKGLYDVANNRVELYRKDGEDRFLPLNEDGTLPDSEPLSQDPQFQDTLDEIELVKEAGNKFDPEKIALGDQTPVFFGSALTNFGVETFLNSFVDLAPAPESHTVNGDEELSPEDPEFSGFVFKIQANMNPHHRDRIAFVRVGSGEFKRGLDVTLARTGKPIRLNNATEFMSSERVQVSDAVAGDIVGLYDTGNFQIGDSIYSGKRKIVYPPLPEFTPELFMRVTAKNVMKQKSFHKGMNQLVQEGAIQLYRNYQTDEYILGAVGQLQFEVFQFRMKNEYNSEVEMNSIGHRVARWIDPEQLDPRMSNSRNLLVKDRYGNPLFLFENEFAERFFHDKYPDVKLTEKL
Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP.
A8YU90
B3TP03
CTR2_CHICK
Solute carrier family 7 member 2
Gallus
MLPCGPALTFVRCLVRKKNIKGEGLEDSLCRCLSTLDLIALGVGSTLGAGVYVLAGEVAKSDSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVAVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLGKQISHFFKTYFKMNYPGLAEYPDFFAVFLILLLSGLLSFGVKESAWVNKIFTAINILVLLFVMISGFVKGDVDNWRISEEYLINLSEIAENFSSYKNVTSIYGSGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVVSLLVCFMAYFGVSAALTLMMPYYLLDEKSPLPVAFAYVGWGPAKYVVAVGSLCALSTSLLGSMFPLPRIVFAMARDGLLFSFLAKVSKRQAPLLATLTAGVISAIMAFLFDLKALVDIMSIGTLLAYSLVATCVLILRYQPSLTYEQPKYSPEKATLAASKRESAVSESQINMIQESHFSLQTLINPSSLPTEQTATTVNCFVGLLAFLVCGLSALTTYGTHFIANLEPWSICLLATLVVSFIVTILLIQRQPQNQQKVAFMVPLLPFLPSLSILVNIYLMVQLSADTWIRFSIWMALGFIIYFTYGIRHSLEGRHSDGDGDSCSENSGLQEKNPVEEVDEPENANESDKFLARERTSEC
Low-affinity, high capacity permease involved in the transport of the cationic amino acids (arginine, lysine and ornithine).
B3TP03
C3KVP2
RS17_CLOB6
30S ribosomal protein S17
Clostridium
MERSNRKTRIGRVVSNKMDKTIVVAVETKVRHPLYGKIMNRTTKFKAHDENNTANINDKVLIMETRPLSKQKRWRLVEVVEKAK
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
C3KVP2
Q8L9H6
CLE17_ARATH
CLE17p
Arabidopsis
MTHVLVRRQGQGKKRRWDVNMTMCFFLFFFVFYVSFQIVLSSSASVGYSRLHLVASPPPPPPRKALRYSTAPFRGPLSRDDIYGDDKRVVHTGPNPLHN
Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2 .
Q8L9H6
O74535
CPSFX_SCHPO
Cleavage and polyadenylation factor complex subunit C74.02c
Schizosaccharomyces
MDNWNSVRNVSSDRQTSKTSENPPHTSNEYSGKPEFINLSPDLEENLDEKLMSAFPGLEPHVFQHSQSPLSHKDASLLATMPSVASSNPSLISSGSSQTGSPSQSLSSNKEPSSPGISPSNDSQSQNTNHTSISANPYVNNPSHTSRNPDSGSSLNTASHEVPSSKSDVNVQMLARLKSKSRQKISSSDPLEDLRLTLTECLNPINIVQAPKECAAILVNLMSNITQDDQKLVFLDLLKSKVGNSIYSQLVDGGRKLFLPKLRNWFVSAIRSKHDELIHLILLVLANLPLTTEKLAEVKFGKPILIVKKKSTNSVIRQLAENLSELAEKSFTIEQNRENEKSSTKNDSTVSSSAVVMAPAGPAMAPSASNKPSASSTTKSSNSKSKKKVTSISGTSFFKNLASSTKPTSASSSTKAPLTKQQTNPSTPLSSIMAGLKGREKEKDKDSGISSENVSNNREELPSFRKRSSSSRQSEEIASLQAENAVFSSDPASNDEKTGNKKRKKKSVSWKPDNDLVQVKFIESLNEEGAASVKTPHIYGNARDMDRQEARVAFGSHVEDDVENEIIWYKPVPIKFEISKDEIHPRGYKCGGNERNLTPEATSEIEREKNESKDISTFNIILDLPVIREFDDSRPPAHIKLVSSDTQATTELGFNGLVQQVSENNTNAYSATSNSQLSSIFSNLSSSISDASSNVLQNPSLSIPNYSNAI
RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation. Involved in poly(A) site recognition. May be involved in coupling transcription termination and mRNA 3'-end formation.
O74535
A1TYI8
RL10_MARN8
50S ribosomal protein L10
Marinobacter
MAIRLEDKKAIVAEVNETAGAALSVVLADYRGVTSGDMTALRAKARAENVRLKVVRNNLAKIAIRGTEFECIDPALVGPTILAFSMEDPGAAARLLKDFAKEKEAFEIKGLAVGGELMGAEQIDRLATLPTLHEALTKLAIVTQAPVTKLARTLNDIPGRITRVVAAVRDQKQDAA
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
A1TYI8
P51778
TAL_TRIV2
Transaldolase
Trichormus
MTKNLLEQLREMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAKMPEYQEIVDQTLLQAKKDAGAGASKGQIVSLAFDRLAVSFGLKILQIIPGRVSTEVDARLSYDTEATITKARELIAQYKAAGIGPERVLIKIASTWEGIKAAEILEKEGIHCNLTLLFGLHQAIACAEAGITLISPFVGRILDWYKKETGRDSYPSAEDPGVISVTTIYNYYKKFGYTTEVMGASFRNIGEITELAGSDLLTISPGLLGELQATIGELPRKLDPAKAATLDIEKISIDKATFDKMHAADRMAYDKLDEGIKGFTKALEELETLLAERLARLEVVASH
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
P51778
A6WXR6
RL21_BRUA4
50S ribosomal protein L21
Brucella
MFAVIKTGGKQYRVAANDLIKVEKVAGEAGDIVEFAEVLMVGSTIGAPTVAGAIVTAEVVEQGRARKVIAFKKRRRQNSKRTRGHRQELTTIRISEILTDGAKPSKKAAEKKAPKAAPKKAAAKAESAE
This protein binds to 23S rRNA in the presence of protein L20.
A6WXR6
O95297
MPZL1_HUMAN
Protein zero-related
Homo
MAASAGAGAVIAAPDSRRWLWSVLAAALGLLTAGVSALEVYTPKEIFVANGTQGKLTCKFKSTSTTGGLTSVSWSFQPEGADTTVSFFHYSQGQVYLGNYPPFKDRISWAGDLDKKDASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYVVEKENLPVFPVWVVVGIVTAVVLGLTLLISMILAVLYRRKNSKRDYTGCSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQLDHSGGHHSDKINKSESVVYADIRKN
Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility.
O95297
A9M5X3
COBQ_BRUC2
Cobyric acid synthase
Brucella
MARAIMFQGTGSDVGKSVLVAGLCRVARNRGLKVRPFKPQNMSNNAAVSDDGGEIGRAQWLQALACGVPSSVHMNPVLLKPQTDMGSQLIVQGQVRGEARGRYYQELKPQLMAAVMESFAKVGDGADLVLVEGAGSPAEINLRAGDIANMGFATHADVPVVLVGDIDRGGVIASLVGTHTILPQEDRAMVRGFLINKFRGDISLFDDGLAAITRFTGWRSFGVVPWLKAVSRLPAEDSVILERAVRGDKKALIVAVPMLPRIANFDDLDPLKAEPAVEVVMVPPGSSLPADAGLVVLPGTKSTIADLLALRENGWDRELVAHVKRGGHVLGICGGFQMLGRRISDPAGIEGNVRDIEGLGLLDIETMMEPEKVVRNVEAVSLLHDEPLEGYEIHIGRTSGPDMARPFARIGDHDDGAVSPDGRIMGTYLHGVFSADRFRHHFLRALGVEGGQMNYRESVEEALDELAEGLEASLDIDGLFALA
Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation.
A9M5X3
Q2LT32
FLIW_SYNAS
Flagellar assembly factor FliW
Syntrophus
MKISTTRFGMIEISESDIILMRRGILGFEESKKYALLYQDVKNPFLWFQSLDDGATAFVVIDPFLLQPYYQPELNDDTLEKLEIDNPEDVALMVIVSIRSNPVLLTANLRAPIVINAAKKKACQVVLEDSRFPIRYDILKNREFLLGGHCYEISATAP
Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum.
Q2LT32
Q6UPR8
ERMP1_RAT
Felix-ina
Rattus
MEWSSESAAVRRHRGTAERREGQAAASHPQREASAQEDARGGGRMRGRTESGGESRGAKTALSEARTALALALYLLALRALVQLSLQRLVLSRTSGLQGEFDARQARVYLEHITAIGPRTTGSAENEILTVQYLLEQITLIEEQSNSLHRISVDVQRPTGSFSIDFLGGFTSYYDNITNVVVKLEPQDGAKYAVLANCHFDSVANSPGASDDAVSCAVMLEVLRVMAASPEPLQHAVVFLFNGAEENVLQASHGFITQHPWASLIRAFINLEAAGVGGKELVFQTGPENPWLVQAYVSAAKHPFASVVAQEVFQSGIIPSDTDFRIYRDFGNIPGIDLAFIENGYIYHTKYDTADRILIDSIQRAGDNILAVLKYLATSDMLASSSEYRHGSMVFFDVLGLLVIAYPSRVGSIINYMVVMAVVLYLGRKLLRPNHSNSNYVRDFLCGLGITFISWFTSLVTVLIIAVFVSLIGQSLSWYNYFYIAVCLYGTATVAKIILIHTLAKRFYYVNASDLYLGELFFDTSLFVHCGFLVALTAQGFCSAFMSAVWVAFPLLTKLCVYKDFKKHGAKGRFIALYLLGMFIPYLYGLYLIWAVFEMFTPILGRSGSEIPPDVVLASILAVCVMILSSYFITFIYLVNSTKKTILTLILVCAVTFLLVCSGAFFPYSSNPDSPKPKRVFLQHVSRTFHNLEGSVVKRDSGIWINGFDYTGMSHVTPHIPEINDTIRAHCEENAPLCGFPWYLPVHFLIRKNWYLPAPEISPRNPAHFRLVSKEKMPWDSIKLTFEATGPSHMSFYVRTHKGSTLSQWSLGNGIPVTSRGGDYFVFYSHGLQASAWQFWIEVQVSEEQPEGMVTVAIAAHYLSGENKRSSQLDALKEKFPDWSFPSAWVSTYSLFVF
Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures.
Q6UPR8
Q0P5A5
CKS1_BOVIN
Cyclin-dependent kinases regulatory subunit 1
Bos
MSHKQIYYSDKYDDEEFEYRHVMLPKDIAKLVPKTHLMSESEWRNLGVQQSQGWVHYMIHEPEPHILLFRRPLPKKPKK
Binds to the catalytic subunit of the cyclin dependent kinases and is essential for their biological function.
Q0P5A5
B7V0Q3
FMT_PSEA8
Methionyl-tRNA formyltransferase
Pseudomonas
MSQALRIVFAGTPEFAAEHLKALLDTPHRIVAVYTQPDRPAGRGQKLMPSAVKNLALEHGLPVMQPQSLRNAEAQAELAALRADLMVVVAYGLILPQAVLDIPRLGCINSHASLLPRWRGAAPIQRAVEAGDAESGVTVMQMEAGLDTGPMLLKVSTPISAADTGGSLHDRLAALGPKAVIEAIAGLAAGTLHGEIQDDALATYAHKLNKDEARLDWSRPAVELERQVRAFTPWPVCHTSLADAPLKVLGASLGQGSGAPGTILEASRDGLLVACGEGALRLTRLQLPGGKPLAFADLYNSRREQFAAGQVLGQ
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
B7V0Q3
Q60CR7
ATPD_METCA
F-type ATPase subunit delta
Methylococcus
MSELTTLARPYAVAVFKAAKEAGNIQEWADMLEFLKQVMADPLMQRAASDPKAGKDRFIAKFLDLCKGHVIPEGENFIRLLASNGRLGLVGTIADMFAEFRAEEEGYVDVDVITAYPLEESETTNLNALVEKWMSRKGRLHVTVDESLIAGVVLRAGGRVVDASVHGQLQRLAKRLSN
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
Q60CR7
Q07NJ2
EFTS_RHOP5
Elongation factor Ts
Rhodopseudomonas
MATITAGMVKELRETTGVGMMDCKQALSENDGNMEAAIDWLRKKGLSKAAKKAGRVAAEGLIGALTDGKKGVVVEVNSETDFVARNEQFQGLVKMIAQVALKVGDDIDAINAAPVGSVTVATAIADAIATIGENMTLRRAKLLSVENGVVASYVHGAVVEGAGKLGVLVALESTGKTDELALLGRQIAMHVAAANPQALDAASLDPELIRREKDVMADKYRQQGKPEAMIEKIVENGLKTFYKEVCLLEQAFIHDTGKSVAQAVKEAEGKVGAPIKVAAFVRYALGEGIEKQTSDFAAEVAAVSGQK
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
Q07NJ2
Q8CMW2
OTCC2_STAES
Ornithine carbamoyltransferase 2, catabolic
Staphylococcus
MKNIKKPFDLKGKSLLKEYDLTGEEFEGLIDFAMTLKKYKQQGTPHRYLEGKNIALLFEKTSTRTRAAFTVASIDLGAHPEFLGKNDIQLGKKESVEDTAKVLGRMFDGIEFRGFSQKTVEQLAEFSGVPVWNGLTDDWHPTQMLADYMTIKENFGYLKGINLTYVGNGRNNVAHSLMVAGAMLGVNVRICTPSSLTPRDVYFNIAKDQASNYGGSVKITDNIHTAVKDADVIYTDVWVSMGEESEFETRIHLLKDYQVNRKMLNLTGKVDTIFLHCLPAFHDTQTEYGQDIFKKYGLTEMEVTDEIFRSEHSRVFDQAENRMHTIKAVMAATLG
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q8CMW2
A8ALC9
MTNN_CITK8
S-adenosylhomocysteine nucleosidase
Citrobacter
MKIGIIGAMEEEVTLLRDKIENRQTITLGGCEIYTGQLNGTEIALLKSGIGKVAAALGATLLLERCKPDVIINTGSAGGLAPTLTVGDIVVSDEARYHDADVTAFGYEFGQLPGCPAGFKADDALIAAAESCIAKLNLNAVRGLIVSGDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVADQQSHLSFDEFLAVAAKQSSLMVETLVQKLAHG
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
A8ALC9
O94778
AQP8_HUMAN
Aquaporin-8
Homo
MSGEIAMCEPEFGNDKAREPSVGGRWRVSWYERFVQPCLVELLGSALFIFIGCLSVIENGTDTGLLQPALAHGLALGLVIATLGNISGGHFNPAVSLAAMLIGGLNLVMLLPYWVSQLLGGMLGAALAKAVSPEERFWNASGAAFVTVQEQGQVAGALVAEIILTTLLALAVCMGAINEKTKGPLAPFSIGFAVTVDILAGGPVSGGCMNPARAFGPAVVANHWNFHWIYWLGPLLAGLLVGLLIRCFIGDGKTRLILKAR
Forms a water-specific channel; mercury-sensitive. Not permeable to glycerol or urea.
O94778
Q925Q8
DACH2_MOUSE
Dachshund homolog 2
Mus
MAVSAPPVISATSSSAGVPGGLFRAEPLYSSPGEPPRLTPNMINSFMANNHNGSVLGGGIGGGSGGSSNTNTNECRMVDMHGVKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFETLFTDCTNARRKRQMTRKQAVNSSRPGRPPKRSLGVLQDNARLLPHAVPGLLSPGLITPTGITAAAMAEAMKLQKMKLMAMNTLQGNGSQNGTESEPDDLNSTTGGSESSWDKDKIQSPLAASGPQHGIAHAALAGQPGLGGAPTLNPLQQNHLLSNRLDLPFMMMPHPLLPVSLPPASVAMAMNQMNHLNTIANMAAAAQIHSPLSRAGASVIKERIPESPSPAPSLEESHRPGSQTSSHPSSSVSSSPSQMDHHSERMVMMPNNREELIVDQDNGQSIKKFQRDNKEEVPAQIPVMKSPLDKIQLAPGQALHPGFPGPFIFADSLSSVETLLTNIQGLLKVALDNARIQEKQIQQEKKELRIELFREREIRENLERQLAVELQSRSTMQKRLKKEKKAKRKLQEALEFESKRREQVEQALKQATSGDSGLRMLKDSGIPDIEIENSGTPHDSAAMQGGNYYCLAMAQQLCSA
Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression. Probably binds to DNA via its DACHbox-N domain.
Q925Q8
O88441
MTX2_MOUSE
Mitochondrial outer membrane import complex protein 2
Mus
MSLVAEAFVSQIAATEPWPENATLYQQLRGEQILLSDNAASLAVQAFLQMCNLPVKVVCRANAEYMSPSGKVPFIHVGNQVVSELGPIVQFVKAKGHSLSDGLDEVQKAEMKAYMELVNNMLLTAELYLQWCDEATVGEITIARYGSPYPWPLNHILAYQKQWEVKRKMKAIGWGNKTLDQVLEDVDQCCQALSQRLGTQPYFFNKQPTELDALVFGHLYTILTTQLTSDELSEKVKNYSNLLAFCRRIEQHYFEDWGKGRLS
Involved in transport of proteins into the mitochondrion.
O88441
E1UV19
BIOW_BACAS
Pimeloyl-CoA synthase
Bacillus amyloliquefaciens group
MEEEIYYSVRMRASRDAPHEQGGKHISGGERLITYSGLQEAVNGLLHKGFSHSRGTPDFMQIQLESINQPIKTIRPLPVAVHQTDTAEKGQAVARKLLQKAGIPPHMIEKAYQNIAEYAEVRGAVLFDIQTGKRIDGRKERGVRVSRMDWPAHDFQKWTLEHKMPENPRIKEAHAIAAKVCAHPGIIAELCWSDDPDYITGYVAAKKLGYQRITKMKNAGDESGCRIFFTDGAIDTESCIHFLEKQPVFIQREGKI
Catalyzes the transformation of pimelate into pimeloyl-CoA with concomitant hydrolysis of ATP to AMP.
E1UV19
P28630
HOLA_ECOLI
DNA polymerase III subunit delta
Escherichia
MIRLYPEQLRAQLNEGLRAAYLLLGNDPLLLQESQDAVRQVAAAQGFEEHHTFSIDPNTDWNAIFSLCQAMSLFASRQTLLLLLPENGPNAAINEQLLTLTGLLHDDLLLIVRGNKLSKAQENAAWFTALANRSVQVTCQTPEQAQLPRWVAARAKQLNLELDDAANQVLCYCYEGNLLALAQALERLSLLWPDGKLTLPRVEQAVNDAAHFTPFHWVDALLMGKSKRALHILQQLRLEGSEPVILLRTLQRELLLLVNLKRQSAHTPLRALFDKHRVWQNRRGMMGEALNRLSQTQLRQAVQLLTRTELTLKQDYGQSVWAELEGLSLLLCHKPLADVFIDG
Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex . DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The delta subunit is the wrench that will open the beta subunit dimer, which has been modeled to leave a gap large enough for ssDNA to pass through . The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA .
P28630
D0L476
MSHA_GORB4
N-acetylglucosamine-inositol-phosphate N-acetylglucosaminyltransferase
Gordonia
MTTGPLPRRVALISVHTSPLAQPGTGDAGGMNVYVWQTATRLARRGVEVEIFTRATSSSDAPRVAAAPRVTVRNVVAGPFEGLDKRDLPAQLCAFTAGVLRAEAAQEPGYYDLIHSHYWLSGQVGWLARDRWGVPLVHTAHTLAAVKNASLAAGDTAEPQLRVIGEQQVVDEADRLIANTETEASELISMYGADPARIDVVTPGADLDCYTPGPREMARTSLGLDQNEAIVTFVGRIQPLKAPDLLIEAAAPLIRRSRTSRRPVRVLIVGGPSGSGLDRPTALIDLAHDLGIADAVTFLPPQAPARLADVYRASNLVAVPSHSESFGLVAIEAQACGTPVLAADVGGLSVAVAGGRTGVLVGSHAVGDWTNALEKALAQPDRLAEMGRNARVHAEQFSWDHTVDAMLSSYSRAMQSFAARNPDAAQSVAAQNVTGSSSRTRRPWRRRRSTLLPMTGRS
Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
D0L476
P0DJQ0
PA2BA_TRIST
Phosphatidylcholine 2-acylhydrolase
Trimeresurus
NLVQLGKMIFQETGKNPATSYGL
Snake venom phospholipase A2 (PLA2) that induces local edema a few hours after injection (5-10 ug) in the hind paw. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
P0DJQ0
Q2N9P5
ATPF_ERYLH
F-type ATPase subunit b
Erythrobacter
MANTPEPLTTEAAQVVSETDLGAAKLLEPSALWLEPYQWVSVAMLVLIAIMLWKKVPSLVTGGLDNKIAEIKAQLDEAKALRAEAEKLRDEYTAKIANAEKDAEAMMENARHEADAILEKAEADSKALVERRKKMAEDKISAAERDAVDEVRATAAAAAAAASRKLIAEKHDAEADRKLADEVIAEL
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
Q2N9P5
Q9KR02
RUVB_VIBCH
Holliday junction ATP-dependent DNA helicase RuvB
Vibrio
MIEADRLIAPISNHFKDEEVIDRAIRPKKLADYQGQDHVRDQMEIFIQAAQMRQEALDHLLIFGPPGLGKTTLANIVANEMGVNIRTTSGPVLEKAGDLAALLTNLEENDVLFIDEIHRLSPMVEEVLYPAMEDYQLDIMIGEGPAARSIKIDLPPFTLIGATTRAGSLTSPLRDRFGIVQRLEYYKVADLQHIVQRSAQCLGLSMDSEGALEVARRARGTPRIANRLLRRVRDYAEVKGDGHICAQTADRALNMLDVDHQGFDYMDRKLLLAIMEKFSGGPVGIDNLAAAIGEEKDTIEDVLEPFLIQQGYLQRTPRGRIATDRAYLHFGIEK
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
Q9KR02
B8IS82
EFG_METNO
Elongation factor G
Methylobacterium
MPRTHAIEDYRNFGIMAHIDAGKTTTTERILYYTGKSHKIGEVHEGAATMDWMEQEQERGITITSAATTCFWRDKRLNIIDTPGHVDFTIEVERSLRVLDGAVCVLDGNQGVEPQTETVWRQADKYDVPRVVFVNKMDKIGADFFKCVADIIDRVAGKPVCLQLPVGAESSFRGVVDLIKMKAIIWSGEALGASFSEEEIPADLAEQAAEYRTKLIEACVELDDDAMAAYLDGVEPDEATLRKLVRVAVQRRAFHPVLCGSAFKNKGVQPLLDAVVDYLPSPADRGEIKGIDYKTEEEVVRKPSDSDPFSMLAFKIMDDPHVGTITFCRIYSGKVESGANLLNSTRDKRERVGRMLLMHANNREDIKEAYAGDIVALAGLKDTRTGDTLCDPNKAVILEKMEFPEPVIEIAVEPKSKADQEKLGIALSKLAAEDPSFRVSTDPESGQTILKGMGELHLDIKVDILKRTYKVEANIGQPQVAYREKLTRRTEVDYTHKKQTGGTGQFARVKLVVEPNEPGAGYSFESKIVGGAVPKEYIPGVEKGLQSVMTAGILAGFPVVDIKVELIDGAYHEVDSSALAFEIASRAALREALQKGGSVLLEPVMKVEVVTPEDYTGSVIGDLNSRRGQIQGQDMRGNATVINAMVPLANMFGYVNQLRSFTQGRANFTMQFDHYEEVPRGEAEKVVAKYA
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
B8IS82
Q68ER2
CBR4_XENTR
Quinone reductase CBR4
Silurana
MTKVCAVFGGSRGIGKAVSKLLAQRDYKVAVISRDLEVAKAAAAEVGAHLALSCDVSKENEIQDTFKEITNNLGNVDYLVNSAGIRRDALLLRTRSEDIRSLLSVNLVGTIQTCKLALRSMIQQQGGAIVNIGSIVGHKGNIGQSIYGASKEGLIGFSKSLAKEVAKRNIRVNVVAPGFIHTDMTLGLEEDSLTKMVPLGRFGDPEEVAQSVLFLLESPYITGHVLVVDGGLQLQM
The heterotetramer with HSD17B8 has NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity, and thereby plays a role in mitochondrial fatty acid biosynthesis. Within the heterotetramer, HSD17B8 binds NADH; CBR4 binds NADPD. The homotetramer has NADPH-dependent quinone reductase activity. Both homotetramer and the heterotetramer have broad in vitro substrate specificity and can reduce 9,10-phenanthrenequinone, 1,4-benzoquinone and various other o-quinones and p-quinones.
Q68ER2
O97878
CCR5_TRAFR
C-C chemokine receptor type 5
Trachypithecus
MDYQVSSPTYDIDYYTSEPCQKVNVKQIAARLLPPLYSLVFIFGFVGNILVVLILINCKRLKSMTDIYLLNLAISDLFFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQREGLHYTCSSHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEAPERASSVYTRSTGEQETSVGL
Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor.
O97878
C4L0S1
LUTB_EXISA
Lactate utilization protein B
unclassified Exiguobacterium
MSMGIRLDEKFQDRRKDGIEDAFMRQAVSSAQNRLRDGRLNAAGELGDWEAFRDHSEEIRQHVLEHLDYYLYQLSENVSKRGGSVFFAETPEEANRYIREVIRSKQAKHVVKSKSMVTEEIGLNEALQEEGCTVVESDLGEWILQLDEDPPSHIVAPALHKDRNAVHETFTAHGYTGSNDPTELGRYARQELRKDFLKAEVGITGCNFAIAESGAVGLVTNEGNGRMVTSLPDTVISVMGMERVVPSYEEFEVLVNMLCRSAVGQRLTSYITTFAGTRAVGEVDGPEEFHLVIVDNKRSNILGTQFQSVLQCIRCAACINVCPVYRHIGGHAYGSIYPGPIGAVLAPLLDGYENYKELPYASSLCGACTEACPVKIPLHELLIEHRRVIVEEKKQSPFVERIAMKGFAVTASSPFLFEAAEHVAPFATSPFATSGQIEKGLPAWTDSKDLPQPNKQTVRDWFKKRGNA
Is involved in L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate.
C4L0S1
Q6F7R2
RL3_ACIAD
50S ribosomal protein L3
Acinetobacter
MAIGLVGRKCGMTRIFTDAGVSVPVTVIEVDPNRITQIKTLETDGYQAVQVTTGERRESRVTNAQKGHFAKAGVAAGRLVKEFRVTEAELEGREIGGTIGVDLFTVGQVVDVTGQSKGKGFQGGVKRWNFRTQDATHGNSVSHRVLGSTGQNQTPGRVFKGKKMAGHLGDERVTVQGLEIVSIDAERSVLVVKGAIPGATGGDVIVRPTIKA
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Q6F7R2
C4LCT8
DAPB_TOLAT
4-hydroxy-tetrahydrodipicolinate reductase
Tolumonas
MTAPIRIALMGCQGRMGKALLEAIRANEQVTLGTALERPGSTVIGLDVGDLNGLGAMNVLIADDLEKVKDQFDVIIDFTRPEVTLKNLAFAVANNKRIVIGTTGFDDAGKAAINEAAKKIGIVFASNFSVGVNLVFKLLEQAAKVMGDYTDIEIIEGHHRHKVDAPSGTALSMGEVVAKTLGRDLKQCAVYGREGITGERDRNTIGFATIRAGDLVGEHTVMFADIGERVEITHKASSRLTFANGAVRAANWLKDQPCGLFDMQDVLNLK
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
C4LCT8
A8G1C6
RS4_SHESH
30S ribosomal protein S4
Shewanella
MARYLGPKLKLSRREGTDLFLKSGVRAIDSKCKLETAPGQHGARKTRLSEYGVQLREKQKVRRTYGVLEKQFRNYYKDAARTKGNTGENLLTLLETRLDNVVYRMGFGATRAEARQLVSHKSIMVNGSVVNIPSFKVSANDVISIREKSKKQARIIAALEVASQREKPTWVEVDNTKMEGAFKRLPERSDLSAEINEQLIVELYSK
With S5 and S12 plays an important role in translational accuracy.
A8G1C6
Q74LS5
DDL_LACJO
D-alanylalanine synthetase
Lactobacillus
MTDKIKVGLIFGGNSSEYEVSIMSAHNIYEEIDTNKFDVYPMWITNDGYLADDADSRKVLDNPKMEVANPHKVANISNIIELKDRPEIDVFFPIVHGNLGEDGCLQGLFRVLDKPFVGDDVLAAAVTMDKEMTKILAQRAGVPVAKWIAVKRFEYNDPDNEKLDYEYVASQLGSDLFVKPSNQGSSVGVSHVTNEKEYKVALAEAFKYDDKVLVEETVHGTEVETAVLGNDKPIVAGVGQIINAKDSFYTYENKYDDDSTSTLEIPAKLPEGIVETVRKNALKVFQATECSGLARIDSMLRSEDNEVVLTEVNALPGFTNISMYPKLFEEIGIPYTDLITKLIDYAMERYDHKKTLLHKHD
Cell wall formation.
Q74LS5
A6W3H7
RNPH_MARMS
tRNA nucleotidyltransferase
Marinomonas
MRPSGREADQLRPLKITRNFTKHAEGSVLIECGDTKVICTATVVSGVPRFLKGKGQGWITAEYGMLPRSTHSRMDREAARGKQGGRTVEIQRLIGRSLRAAVDLKKLGENTITIDCDVIQADGGTRTASITGGFVALADAMRVLVENKKVKENPIVSQIAAISVGVYKGVPVLDLDYPEDSNAETDMNVIMNDKGGFIEIQGTAEGEAFSDEHMMGMLAVARKGIAEIMEAQRAALFDK
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
A6W3H7
A4SRH0
CYSG2_AERS4
Sirohydrochlorin ferrochelatase 2
Aeromonas
MDYLPMFARLEGRPVLLVGGGEVALRKARLLLAAGARLTLVSPEIEPEFAEFAGRFTHLVERFTPAHLAGQLLVVAATDNLEVNALVYQSANQLGLFVNVVDDPKRSSFIFPSIIDRSPLMVAVSSGGKAPVLVRLLRERLESLLPRHLGGLTELSGRVRDKAKQVLSSISDRRRFWERAFASNTLAGLIEKQDWQSAETWLNDGLDKAQSEVGEVVLVGAGPGDPGLLTLKALQQIQQAEVVLYDQLVSPEILDLVRRDATLVSVGKKAGAHSVPQEETNRLLVEYARAGNRVVRLKGGDPFMFGCGGEELEVLAAEGIPFSVVPGITAAAGATAYAGIPLTHRDHAQSAVFITGHCQKEGKEPDWQQLAVTQQTLVIYMGLMRSEHIQQQLVSHGRSCTTPIAIIEWGTTARQRVLTGTLAELAVLAQQAVSPSLIVIGEVVSLRKQLAWFGEKSGEKRDVQAGTDMNGCDLKLVNLA
Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
A4SRH0
A1WVD2
RL1_HALHL
50S ribosomal protein L1
Halorhodospira
MAKLTKRQKQIRERVDGNHAYPVDEALALVKELATARFPESIDVAVNLGVDPRKSDQIVRGSTVLPNGTGKSMRVAVFAQGENADAAQAEGADAVGMDDLAERMQGGELDYDVVIASPDAMGVVGKLGPVLGPRGLMPNPKTGTVSADVAGAVRNAKAGQVRYRTDRGGVIHSAIGRANFDEQALRENLDALLADLNKLKPSTSKGVYIKGITVSSTMGAGVRVDRATLGV
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A1WVD2
Q9HWZ3
AQPZ_PSEAE
Aquaporin Z
Pseudomonas
MKQYGAEFFGTFWLVLGGCGSAVLAAGVPELGIGYLGVALAFGLSVLTMAYAIGPISGAHLNPAVSVGLWVGGRFPASQLLPYVVAQVLGGLAAGGVLYLIASGKAGFDLAAGFASNGYGEHSPGGYSLQAALVSEVVLTGMFLLIILGATSKRAPQGFAPIAIGLTLTLIHLISIPVTNTSVNPARSTAVALYVGDWAVSQLWLFWVAPILGAVLGALAYRLIGDKND
Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.
Q9HWZ3
Q2QD12
RPEL1_HUMAN
Ribulose-5-phosphate-3-epimerase-like protein 1
Homo
MASGCKIGPSILNSDLANLGAKCLQMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQDPFFDMHMMVSKPEQWVKPMAVAEANQYTFHLEATENPGTLIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGEQKFMEDMMPKVHWLRTQFPSLDIEGDGGVGSDTVHKCAEAGANMTVSGSAIMRSEDPRSVINLLRNICSEAAQKRSLDR
Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.
Q2QD12
Q1JB00
QUEA_STRPB
Queuosine biosynthesis protein QueA
Streptococcus
MNTNDFDFELPEELIAQTPLEKRDSSKLLIIDHRQKTMVDSHFDHIIDQLNPGDALVMNNTRVLPARLYGEKPDTHGHVELLLLKNTQGDQWEVLAKPAKRLKVGSQVNFGDGRLKATIIDELEHGGRIVEFSYDGIFLEVLESLGEMPLPPYIHEKLEDAERYQTVYAKENGSAAAPTAGLHFTTDLLKKIEAKGVHLVYLTLHVGLGTFRPVSVDNLDEHDMHSEFYSLSEEAAQTLRDVKQAGGRVVAVGTTSIRTLETIGGKFQGDIQADSGWTNIFIKPGYQFKVVDAFSTNFHLPKSTLVMLVSAFAGRDFVLEAYRHAVDEKYRFFSFGDAMFVN
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
Q1JB00
B9DM19
RL3_STACT
50S ribosomal protein L3
Staphylococcus
MTKGILGRKIGMTQVFGENGDLIPVTVVEAGQNVVLQKKTEEVDGYNAIQVGFEDKQAYKKDSKSNKYANKPAEGHAKKAGTAPKRFIREFKNINVDEYEVGQEVSVDTFEAGDIIDVTGVSKGKGFQGNIKRHGHARGPMAHGSHFHRAPGSVGMASDASKVFKGHKMPGRMGGNTVTVQNLEVVQIDAENNVILVKGNVPGPKKGLVEIKTSIKKGNK
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
B9DM19
Q65UL1
NADK_MANSM
ATP-dependent NAD kinase
Basfia
MSQDSVKSLQSTFKTVGVVGRPRNDSTLQMHKNIFHWLCEQGYQVLVENEIGKALNLSENHLASLDQIGQHAQLAIVIGGDGNMLSHARILCKYNTPLIGINRGNLGFLTDIDPKNAYAQLEACLNGEFFVEERFLLEAVVKRHGETVARGNAINELVIHPAKIAHMIDFHVYIDDKFAFSQRSDGLIVATPTGSTAYSLSAGGPILTPQLNAIALVPMFPHTLSSRPLVVDGNSKISVNFAEYNIPQLEISCDSQLALDICCNDVVHIQKSPYKLRLLHLHNYNYYNVLSSKLGWLKKLF
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.
Q65UL1
Q96F86
EDC3_HUMAN
YjeF domain-containing protein 1
Homo
MATDWLGSIVSINCGDSLGVYQGRVSAVDQVSQTISLTRPFHNGVKCLVPEVTFRAGDITELKILEIPGPGDNQHFGDLHQTELGPSGAGCQVGINQNGTGKFVKKPASSSSAPQNIPKRTDVKSQDVAVSPQQQQCSKSYVDRHMESLSQSKSFRRRHNSWSSSSRHPNQATPKKSGLKNGQMKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKDLPTSPVDLVINCLDCPENVFLRDQPWYKAAVAWANQNRAPVLSIDPPVHEVEQGIDAKWSLALGLPLPLGEHAGRIYLCDIGIPQQVFQEVGINYHSPFGCKFVIPLHSA
Binds single-stranded RNA. Involved in the process of mRNA degradation and in the positive regulation of mRNA decapping. May play a role in spermiogenesis and oogenesis.
Q96F86
Q7VMS6
ARGB_HAEDU
NAG kinase
Haemophilus
MNQTTTFDKLCNYSAACLANWQGKTIVVKYGGNAMISAELKQTVMQNILLLNQYGINVVLVHGGGPEISLGMKLLGKEPQFINGLRVTDQDTIDVVLQMLAGKVNKRLVALLKGKGIGLCGIDGGLIQCEKLEAELDYGLVGNIVQVDITVLQMALAANLIPVIAAVAVDQQGIIYNVNADTVASEIAVALGADKLVLMTDIAGLLADRNDERSLMSRVEVSQVETLIAQGIISDGMIPKVASCTRFINAGGIEAHIIDGRIKHAILLSILSDKQNGTRFYKEK
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
Q7VMS6
P86154
BR2EG_PELRI
Brevinin-2Eg
Pelophylax
GIMDTLKNLAKTAGKGALQSLLNHASCKLSGQC
Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
P86154
Q3AR09
CH60_CHLCH
Chaperonin-60
Chlorobium
MTAKDIFFDTDARAKLKVGVDKLANAVKVTLGPAGRNVLIDKKFGAPTSTKDGVTVAKEIELADAVENMGAQMVREVASKTSDVAGDGTTTATVLAQAIYREGLKNVTAGARPIDLKRGIDRAVKEVVAELKAISRSISSKKEIAQVGTISANNDPEIGELIAEAMEKVGKDGVITVEEAKGMETELKVVEGMQFDRGYLSPYFVTNSDTMEAELDNPLILIYDKKISNMKELLPILEKSAQSGRPLLIIAEDIEGEALATLVVNKLRGTLKVCAVKAPGFGDRRKAMLEDIAILTGGTVISEEKGYKLENATLSYLGQAGSVSLDKDNTTLVEGKGASDAIKARINEIKGQIEKSTSDYDTEKLQERLAKLSGGVAVINIGASTEVEMKEKKARVEDALHATRAAVQEGIVVGGGVALIRAIKGLNNAQADNEDQKIGIEIVRRALEEPLRQIVANTGTQDGAVVLEKVKEGEGDFGFNARTETYENLVEAGVVDPTKVTRSALENAASVAGILLTTEAAITDIKDDKMDMPAMPPGGMGGMGGMY
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.
Q3AR09
O74288
ABFB_EMENI
Alpha-L-arabinofuranosidase B
Aspergillus subgen. Nidulantes
MTMSRSSRSSVLALALATGSLVAAGPCDIYSSGGTPCIAAHSTTRALYSSYNGPLYQVQRASDGTTTTITPLSAGGVADASAQDAFCENTTCLITIIYDQSGNGNDLTQAPPGGFNGPDVGGYDNLAGAIGAPVTLNGKKAYGVFVSPGTGYRNNEAIGTATGDEPEGMYAVLDGTHYNDGCCFDYGNAETSSLDTGNGHMEAIYYGTNTAWGYGAGNGPWIMADLENGLFSGQSSDYNAGDPSISYRFVTAILKGGPNLWALRGGNAASGSLSTYYNGIRPTDASGYNPMSKEGAIILGIGGDNSVSAQGTFYEGAMTDGYPDDATENSVQADIVAAKYATTSLISGPALTVGDTVSLKVTTSGYDTRYIAHTGSTINTQVVSSSSSSTLKQQASWTVRTGLASTAAANGCVSFESVDTPGSYIRHSNFALLLNANDGTKLFSEDATFCPQDSFNDDGTNSIRSWNYPTRYWRHYENVLYVASNGGVNTFDAATAFTDDVSWVVADGFA
Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.
O74288
Q9FGG1
EC15_ARATH
Egg cell-secreted protein 1.5
Arabidopsis
MATKSTSKPLLLSFLMMSYLISTFHVITVAEGRTLQFTKMATDHSGAGNLMDCWNAGLELKSCTDEIVKFFLSQTGTSEPPVKGGIDKDCCGAIGLVVKDCWSVMFTSLGLTTMEGNNLREYCEFQAEKSELSPSPAPETLALSPVEITYPGLDY
Involved in the regulation of gamete interactions during the double fertilization and to prevent multiple-pollen tube attraction; mediates the redistribution of the gamete fusogen HAP2/GCS1 to the cell surface after secretion upon sperm arrival.
Q9FGG1
Q2HXU8
CL12B_HUMAN
Macrophage antigen H
Homo
MSEEVTYATLTFQDSAGARNNRDGNNLRKRGHPAPSPIWRHAALGLVTLCLMLLIGLVTLGMMFLQISNDINSDSEKLSQLQKTIQQQQDNLSQQLGNSNNLSMEEEFLKSQISSVLKRQEQMAIKLCQELIIHTSDHRCNPCPKMWQWYQNSCYYFTTNEEKTWANSRKDCIDKNSTLVKIDSLEEKDFLMSQPLLMFSFFWLGLSWDSSGRSWFWEDGSVPSPSLFSTKELDQINGSKGCAYFQKGNIYISRCSAEIFWICEKTAAPVKTEDLD
Inhibitory receptor postulated to negatively regulate immune and non-immune functions . Upon phosphorylation, recruits SH2 domain-containing PTPN6 and PTPN11 phosphatases to its ITIM motif and antagonizes activation signals . Although it inhibits KLRK1/NKG2D-mediated signaling, it does not bind known ligands of KLRK1/NKG2D and therefore is not its inhibitory counterpart . May limit activation of myeloid cell subsets in response to infection or tissue inflammation . May protect target cells against natural killer cell-mediated lysis . May negatively regulate cell cycle and differentiation of melanocytes via inactivation of STAT3 .
Q2HXU8
B1J268
RIMP_PSEPW
Ribosome maturation factor RimP
Pseudomonas
MGASPIFYLHSMHEGVQVSSKLEQLQALLAPVVEGLGYQCWGIEYVSQGKHSVLRIYIDKEGGILVEDCEAVSRQASAILDVEDPISSEYTLEVSSPGMDRPLFTLEQFASHAGEQVKIKLRTPFEGRRNFQGLLRGVEEQDVVVQVDSHEFLLPIDSIDKANIIPSFD
Required for maturation of 30S ribosomal subunits.
B1J268
Q7ZX51
SYYC_XENLA
Tyrosyl-tRNA synthetase
Xenopus
MGDSLTLEGKAQLITRNLQELLGEDKMKEILKERPLRIYWGTATTGKPHVAYFVPMSKIADFLKAGCEVTILFADLHAYLDNMKAPWDLLELRTRYYEQVIQAMLQSIGVPLERLRFIRGTEFQLSKEYTLDVYRLSSVVTQHDAKKAGAEVVKQVEHPLLSGLLYPGLQALDEEYLKVDAQFGGVDQRKIFTFAEKYLPALGYAKRIHLMNPMVPGLTGAKMSSSEEESKIDLLDSPADVKKKLKKAFCEPGNVENNGVLSFVRHVLFPLKSEFVVLRDEKFGGNKTYTDFETLEKDFAEELVHPGDLKASVEKALNKLLHPIREKFNSPEMKKLSNDAYPDASKQKSVPKGSTKNSGTEEIDPSLLDLRVGKILSVSQHPDADSLYVESVDVGEANPRCVVSGLVQYVPSDQLLGRSVVLLCNLKPQKMRGIESQGMLLCASTEGEQKQVEPLDPPSGSAPGERIYIEGYENGEPEGELKPKKKVFEKLQVDFRISDDLCAQWKGKNFLTKLGSVTCKTLRGGSIG
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Q7ZX51
Q3J1A0
BCHZ_CERS4
Chlorin reductase subunit Z
Cereibacter
MLVQDHDRAGGYWGAVYAFCAVKGLQVVIDGPVGCENLPVTSVLHYTDALPPHELPIVVTGLGESEMSEGTEASMSRAWKVLDPALPAVVVTGSIAEMIGGGVTPQGTNIQRFLPRTIDEDQWEAADRAMTWIFSEFGMTKGRMPPEAKRPEGAKPRVNILGPMYGVFNMASDLHEIRRLVEGIGAEVNMVMPLGAHLAEMRHLVNADANIVMYREFGRGLAEVLGKPYLQAPIGVESTTAFLRRLGEILGLDPEPFIEREKHSTLKPVWDLWRSVTQDFFGTANFGIVATETYARGIRNYLEGDLGLPCAFAVARKRGSKTDNEAVRGLIRQHRPLVLMGSINEKIYLAELKAGHGPQPSFIAASFPGAAIRRATGTPVMGYAGATWLLQEVCNALFDALFHILPLGTEMDSAAATPTTLRRDFPWDADAQAALDRIVEEHPVLTRISAARALRDAAEKAALDAGAERVVRETVEALRGPGFGERKGENQ
Converts chlorophylls (Chl) into bacteriochlorophylls (BChl) by reducing ring B of the tetrapyrrole.
Q3J1A0
Q5PID0
METN1_SALPA
Methionine import ATP-binding protein MetN 1
Salmonella
MIKLSNITKVFQQGARTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVMVGGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQMDYAGGVKFGIMLTEMHGTQEETQAAIAWLQDHHVKVEVLGYV
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
Q5PID0
Q7VQL4
DNAK_BLOFL
Heat shock protein 70
Candidatus Blochmannia
MGKIIGVDLGTTNSCVAIIESNKPRVLENSEGDRTTPSVVAYTQDGEILVGQPAKRQSVTNPKNTLFAIKRLIGRRFQDQEVQRDVKIMPYKIISSNNGDAWLDIKGQKIAPPQISAEILKKMKKTAEDYLGENVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKEAHGNRIIAVYDLGGGTFDISIIEIDNVDGEKTFEVLATNGDTHLGGEDFDSLLINYLVEEFKKDQGIDLYNDPLAMQRLKESAEKSKIELSTSQQTDVNLPYITADSTGPKHMNLRVTRAKLESLVEDLVNRTLDPLKTALKDANLSVSSVNDVILVGGQTRMPLVQKKVSEFFNKEPRKDVNPDEAVAIGAAVQGGVLSGDVKDVLLLDVTPLSLGIETMGGVMTSLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRASDNKSLGQFNLDGIAPAMRGIPQIEVTFDIDADGILHVSAKDKNSGREQKITIKASSGLNEEEIKKMVQEAEANAESDRKFEELVQIRNQADHLLHSTRKQLKEVGDRISLDDKNSIEQSLKELELVMKNENKGDIESKVQELIKVSGKLLEASSQKYKEKVNDSKSDLNKDKSETDASGDVVDAEFEEIKNKK
Acts as a chaperone.
Q7VQL4
Q7MA19
ATPG_WOLSU
F-ATPase gamma subunit
Wolinella
MGSNLKEIRKKITSVKNTQKTTKAMKLVSTSKLKKAEEMAKRSRVYAERITAVFQEIKAKIEQNGFSGLESPYFTAGEDREVKMVDIVFVTADKGLCGGFNSTTIKEVTRLMAEYKSQNVKVRLRAIGKKGISFFGFNEVELLDKVSDLSATPDYERAAEFVNKATTDFINGVTDKVILVHNGFKNMISQELKVQDLLPIKADAIEAKESLGMMEVEPSEQEREILDQLAKKYIEFNMYYALIDSLAAEHSARMQAMDAASNNAGELVKSLTIAYNKARQEAITTELVEINTGVESMK
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Q7MA19
A3LU17
IRC22_PICST
Increased recombination centers protein 22
Scheffersomyces
MKFSAILSAVFASIAAVSAIEPAEGRQHEIAFIVDYKIKQQPELTQADVAEWTNGETITLQYHAQNNEAEEVTIIGVSGTFIEPSTGNVKVNMTAATIGPIVVAPGESHVFEQNIPLNVLPDHYLLVPQVYVAHEEKVKHVAIRGQLATVVEPNVSIFNPQLLFLELVLLATFAGFGYFVYEFWGKQYFKGTAPVAAKVKRAASPSSATASGKAYDESWIPEAHLKQKKTKKAA
Is probably involved in a pathway contributing to genomic integrity.
A3LU17
A0L576
ACSA_MAGMM
Acyl-activating enzyme
Magnetococcus
MSDVKVYPVDPNVAANALINEEQYQEMYKRSIDDPAAFWAEQAEARIDWFKKWDNVLDFDLRKGHIKWFEGAKLNVSYNCIDRHLEKRGDKVAILWEGDNPAADRKITYRELSALVNKFANALKARGVKKGDRVCIYMPMIPEAAVAMLACTRIGAVHSIVFGGFSPDALRDRIIDAECRVVITADGGMRGSKKIPLRKNVETALAQCPNVHTCFVVQDTQLEIEWTEGRDVWYHEAIAAASADCPPEEMDAEDPLFVLYTSGSTGKPKGVLHTTGGYLLYASITHQYIFDYHEDDIYWCTADVGWVTGHTYIVYGPLANGATTLMFEGVPTYPDASRFWQVVDKHQVSIFYTAPTAIRSIMSQGDALVKATSRQSLRILGSVGEPINPEAWEWYYHVVGEGRCPIVDTWWQTETGGILITPLPGATPLKPGSATRPFFGVNPKVLSNEGKEMEGPCEGILVLDHPWPGMMRTVYGDHDRFINTYFANYPGYYFCGDGCRRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVLHDQVAEAAVVGMPHEIKGQGIYAYVTLMSGVEPSDALKTELVKLVRKEIGPIASLDVIQFAPGLPKTRSGKIMRRILRKIAAHEVDTLGDTSTLADPSVVQNLIDNMPK
Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.
A0L576
P14410
SUIS_HUMAN
Isomaltase
Homo
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDSGKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMTTTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEFTGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISTRLPSDYIYGIGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSNAMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRWNYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQKYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNPNCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMYSKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAHWLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSRNHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHEFYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDMYLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDTIQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMNAHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGCVWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRVEVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRSSGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPPGYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGPTPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDIDYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVFVKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVDFYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEAEQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGDNYARWDNMDKSIIGMMEFSLFGMSYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNIANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKPTWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDTINLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLYLSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNEDTTNMILRIDLTTHNVTLEEPIEINWS
Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides.
P14410
Q10UY5
YBEY_TRIEI
Endoribonuclease YbeY
Trichodesmium
MYLKVNIQDYFWSSSSEVKKLKLQEDRDQKCPIFFYRWEYWFQKWLEILQPNIPPAQNYELSLRLTDDSEIQILNNKYRYQNQPTDVLAFANLEVDIPQPEVVDSDLQLYLGDIVISVETAFQQAKQQGHPLITELTWLAAHGFLHLLGWDHLDQESWQKMVKQQLFLLNAVGEVYWITDNSR
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
Q10UY5
Q42882
GLGS_SOLLC
Alpha-D-glucose-1-phosphate adenyl transferase
Solanum subgen. Lycopersicon
MAASIGALKSSPSSHNCINERRNDSTRAISSRNLSFSSSHLAGDKLMPVSSLRSQGVRFNVRRSPLIVSPKAVSDSQNSQTCLDPDASRSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGEYKNEGFVEVLAAQQSPENPDWFQGTADAVRQYLWLFEEHNVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEKRATAFGLMKIDEEGRIIEFAEKPQGEQLQAMKVDTTILGLDDKRAKEMPFIASMGIYVISKDVMLNLLRDKFPGANDFGSEVIPGATSLGMRVQAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGADYYETDAERKLLAAKGSVPIGIGKNCLYKRAIIDKNARIGDNVKIINKDNVQEAARETDGYFIKSGIVTVIKDALIPSGIVI
This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Q42882
Q08050
FOXM1_HUMAN
Winged-helix factor from INS-1 cells
Homo
MKTSPRRPLILKRRRLPLPVQNAPSETSEEEPKRSPAQQESNQAEASKEVAESNSCKFPAGIKIINHPTMPNTQVVAIPNNANIHSIITALTAKGKESGSSGPNKFILISCGGAPTQPPGLRPQTQTSYDAKRTEVTLETLGPKPAARDVNLPRPPGALCEQKRETCADGEAAGCTINNSLSNIQWLRKMSSDGLGSRSIKQEMEEKENCHLEQRQVKVEEPSRPSASWQNSVSERPPYSYMAMIQFAINSTERKRMTLKDIYTWIEDHFPYFKHIAKPGWKNSIRHNLSLHDMFVRETSANGKVSFWTIHPSANRYLTLDQVFKPLDPGSPQLPEHLESQQKRPNPELRRNMTIKTELPLGARRKMKPLLPRVSSYLVPIQFPVNQSLVLQPSVKVPLPLAASLMSSELARHSKRVRIAPKVLLAEEGIAPLSSAGPGKEEKLLFGEGFSPLLPVQTIKEEEIQPGEEMPHLARPIKVESPPLEEWPSPAPSFKEESSHSWEDSSQSPTPRPKKSYSGLRSPTRCVSEMLVIQHRERRERSRSRRKQHLLPPCVDEPELLFSEGPSTSRWAAELPFPADSSDPASQLSYSQEVGGPFKTPIKETLPISSTPSKSVLPRTPESWRLTPPAKVGGLDFSPVQTSQGASDPLPDPLGLMDLSTTPLQSAPPLESPQRLLSSEPLDLISVPFGNSSPSDIDVPKPGSPEPQVSGLAANRSLTEGLVLDTMNDSLSKILLDISFPGLDEDPLGPDNINWSQFIPELQ
Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis . Plays a role in the control of cell proliferation . Also plays a role in DNA break repair, participating in the DNA damage checkpoint response . Promotes transcription of PHB2 .
Q08050
Q2TXF5
ORYJ_ASPOR
Oryzines biosynthesis cluster protein J
Aspergillus subgen. Circumdati
MGSLPEKDFPQVHRFITTHKEDGTPTFETKIPEPIEWERTNIGVDFFLAYTLGSFPAPLSHDADLNQYKDHLVNHPPFMIPGGAVVRYVDYHPGCEPMWHRTVTVDFGVVIEGELELEVEGGEKRLMKRGDVAVQRGTNHCWRNPSKTQFARALYIALDAKPVIVNGQELGESLGEVKH
Part of the gene cluster that mediates the biosynthesis of oryzines, natural products with an unusual maleidride backbone . The two subunits of the fungal fatty acid synthase oryfasA and oryfasB probably form octenoic acid (Probable). This fatty acid is most likely activated by the acyl-CoA ligase oryP to give octenyl-CoA before the citrate synthase-like protein oryE catalyzes condensation with oxaloacetate to form tricarboxylic acid (Probable). The next steps of the pathways are conjectural, but a favorite possible route has been proposed, beginning with decarboxylation and concomitant dehydration by the decarboxylase oryM, followed by tautomerization, which may lead to the production of a diene intermediate (Probable). Reduction of this diene intermediate could give the known metabolite piliformic acid (Probable). On the pathway to oryzine B and oryzine A, however, hydroxylation of the diene by the alpha-ketoglutarate-dependent dioxygenase oryG and lactonisation by the lactonohydrolases oryH or oryL could give oryzine B directly (Probable). Finally, enoyl reduction by the dehydrogenase oryD would then convert oryzine B into oryzine A (Probable).
Q2TXF5
A0A0K0PVL0
UGT12_PANGI
UDP-glucosyltransferase 102
Panax
MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVFISKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAILPSVIETQKTHVRDIISGMTQSESTRVVGLLADLLFINIMDIANEFNVPIYVYSPAGAGYLGLAFHLQTLYDKKQDVTEFRNSDTELLVPGFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGTFQENQVKEIAMGLERSGHRFLWALRPSIPKGETKLQLKYSNLEEILPVGFLDRTSCVGKVIGWAPQVAVLGHEAVAGFMSHCGWNSTLESVWFGVPVATWPMYGEQHLNAFEMVKELGLAVEIEVDYKNEYFNTKNDFIVRAEEIETKIKKLMMDEKNSEIRKKVKEMKEKSRVAMSENGSSYNSLAKLFEEIM
Probable component of the triterpene saponins (e.g. ginsenosides) biosynthetic pathway . No detectable activity toward protopanaxatriol (PPT) .
A0A0K0PVL0
D5HR52
SCX3A_ANDCR
Neurotoxin 3
Androctonus
VESIKDGYIVDDRNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKAPGKCNGR
Alpha toxins bind voltage-independently at site-3 of sodium channels (Nav) and inhibit the inactivation of the activated channels, thereby blocking neuronal transmission.
D5HR52
Q39056
CNX3_ARATH
Molybdopterin biosynthesis protein CNX3
Arabidopsis
MISTLRRAVFLRRFPAVVSPIKRAFSSRIDDEFDPQIMNINELNQEMQSIFGQEPSPDGPGTMDFSELKSSKIEPLRSKNIDFRQQIEYHKSTHSSKNDSQAIEQYAKVASDMSKLTHVGIAGEAQMVDVSSKDNSKRTALACCKVILGKRVFDLVLANQMGKGDVLGVAKIAGINGAKQTSSLIPLCHNIALTHVRVDLRLNPEDFSVDIEGEASCTGKTGVEMEAMTAVSVAGLTVYDMCKAASKDISITDVRLERKTGGKSGSWSRL
Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Q39056
Q9KP03
RL15_VIBCH
50S ribosomal protein L15
Vibrio
MLLNTLSPAAGSKHAPKRLGRGVGSGLGKTGGRGHKGQKSRSGGKVRPGFEGGQMPLKQRLPKFGFTSRKSFVSAEVRLSELAKVTGDVVDLNALKAANLVTKNIEFAKIVLSGEINKAVTVKGLRVTKGAKAAIEAAGGKIEE
Binds to the 23S rRNA.
Q9KP03
A0R665
ETHA_MYCS2
Prodrug activator EtaA
Mycolicibacterium
MTEHFDVVIVGAGISGISTAWHLQDRCPTKSYVILERRANIGGTWDLFKYPGIRSDSDMFTLGFRFKPWTSAKSIADGPSIWNYINEAAQENGIDKHIRTNHRVLGADWSDAENRWTITVEADGEQKQITASFLSVCSGYYNYDQGYSPEFPGADDFAGQIIHPQHWPEDLDYAGKKIVVIGSGATAVTLIPSLVNGGAAHVTMLQRSPTYIGSLPLVDPVAEKTNKYLPKNLAHFVNRWKAIAFSTAQYQLARKFPNYMRKTLMTMAQRRLPEGFDVQKHFGPRYNPWDERLCLAPNGDLFKTIRAGKADVVTDTIAKFTETGIKLTSGEELTADIIITATGLNMQLFGGASLTRNGQEVDLTETMTYKGLMLSGVPNMAITFGYTNASWTLKADLVSEFICRVLNYMDDNGFDRVEPQHPGDAVDALPFMDFNPGYFRRAMDSLPKSGSRAPWRLKQNYFFDLRMIRYDKVDEESLHFTKHRAAVSASSS
Is responsible for the activation of several thiocarbamide-containing pro-drugs, such as ethionamide (ETH), isoxyl (ISO) and thiacetazone (TAC), into reactive species.
A0R665
P00229
FER1_PHYAM
Ferredoxin I
Phytolacca
ATYKVTLVTPSGTQTIDCPDDTYVLDAAEEAGLDLPYSCRAGSCSSCTGKVTAGTVDQEDQSFLDDDQIEAGFVLTCVAFPKGDVTIETHKEEDIV
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
P00229
Q1DDB3
KDSB_MYXXD
CMP-2-keto-3-deoxyoctulosonic acid synthase
Myxococcus
MQSCRTVAVIPARHASTRFPGKPLAIIAGRTMIEHVWRRCQEAQAFDEVWVATDDDRIRAAVEGFGGKAVMTSPACATGTDRVAEVALGRPDIDIWVNVQGDEPLVDPATLQRLAGLFQDASVRMGTLVRPLEADEAASPHVVKAVLALNGDALYFSRSLVPHVREPGTPVQRWGHIGLYGYRREVLLSLAKLAPTPLEDAEKLEQLRALEHGIPIRCAKVTSHTVAVDLPGDVEKVEALMRARGG
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
Q1DDB3
Q9CXV1
DHSD_MOUSE
Succinate-ubiquinone reductase membrane anchor subunit
Mus
MAVLLKLGVLCSGQGARALLLRSRVVRPAYVSAFLQDQPTQGRCGTQHIHLSPSHHSGSKAASLHWTSERVVSVLLLGLIPAGYLNPCSVVDYSLAAALTLHSHWGLGQVVTDYVHGDTLPKAARAGLLALSALTFAGLCYFNYHDVGICRAVAMLWKL
Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Q9CXV1
Q9QZA0
CAH5B_MOUSE
Carbonic anhydrase VB
Mus
MAVMNHLRVILQVSSSTLPWRRCWVPRLVPRRSCSLYTCTYRTRNRALPPLWENLDLVPAGDRQSPINIRWRDSVYDPGLKPLTISYDPATCLHIWNNGYSFLVEFEDSTDKSVVEGGPLEHNYRLKQFHFHWGAIDAWGSEHTVDSKCYPAELHLVHWNAVKFESFEDAALEENGLAVIGVFLKLGKHHKELQKLVDTLPSIKHKDTLVEFGSFDPSCLMPTCPDYWTYSGSLTTPPLSESVTWIIKKQPVEVDRDQLEQFRTLLFTSEGEKEKRMVDNFRPLQPLMNRTVRSSFRHDYVLNIQVKPKPTASEVTP
Reversible hydration of carbon dioxide.
Q9QZA0
O30745
DADA_KLEAE
D-alanine dehydrogenase
Klebsiella
MRVVILGSGVFGVASAWYLSQAGHDVTVIDRQPGPAEETSAANAGQISPGYAAPWAAPGVPLKAIKWMFQRHAPLAIGLDGTSFQLKWMWQMLRNCDTRHYMENKGRMVRLAEYSRDCLKALRDTTGIQYEGRQGGTLQLFRTAKQYENATRDIAVLEDAGVPYQLLEAKRLAEVEPALAEVSHKLTGGLRLPNDETGDCQLFTTRLAAMADQAGVTFRFNTAVDALLHEGDRIAGVKCGMRIIKGDAYVMAFGSYSTAMLKGLVDIPVYPLKGYSLTIPIAQEDGAPVSTILDVTYTIAITRFDQRIRVGGMAEIVGFNKTLLQPRRETLEMVVRDLFPRGGHVEQATFWTGLRPMTPDGTPVVGRTAYKNLWLNTGHGTLGWTMACGSGQLISDLISGRTPAIPYDDLAVARYSPGFTPARPQHLHGAHN
Catalyzes the oxidative deamination of D-amino acids. Participates in the utilization of alanine as the sole source of carbon and nitrogen for growth.
O30745
A8XAF4
UFC1_CAEBR
Ufm1-conjugating enzyme 1
Caenorhabditis
MDETTKSSLKAIPLCKTKAGPRDGDLWMERLKAKYEAIIAAVQNNKTSDRDWFKLEANERGTKWFGKCWYFHNMVKYEFDVEFDIPITYPVTAPEIALPELDGKTAKMYRGGKICLSEHFKPLWARNTPKFGIAHAFALGLGPWMAVEIPDLIEKGIIQPKA
E2-like enzyme which forms an intermediate with ufm-1. The intermediate is formed via a thioester linkage.
A8XAF4
Q9X2H4
THPR_THEMA
RNA 2',3'-cyclic phosphodiesterase
Thermotoga
MRTFIAIDVNEEVKKQASEIIEKLMKRGFGATWVSEENMHLTLFFLGEVDEQKISEIAEHLCRRVRGFPSFSFTVKGFGYFKRKMSPRVFWLGVENTDRLMKLYEELRNELSHHGFSFEEKFVPHITIGRVKYYPDKWEKLIEDIDFPPIEVAVDRFKIYSSTLTPTGPIYKVLYECQFEGGLIRYA
Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'-phosphomonoester.
Q9X2H4
O65571
CDA2_ARATH
Cytidine deaminase 2
Arabidopsis
MAQRPNLLSHLQDLVTKFKNMTMAQDRFKFVFTANEAALEGVTDPIRLPNLIRKAMCLARAPISKYKVGAVGRASSGRVYLGVNVDFPGLPLHHSIHAEQFLVTNLALNYEKDLCKLAVAISTDGLEFGTPCGNCLQFLMEMSNALDMKILSKPKHEAGSFSSLRLLLPNVLPKGSPFLLEKRYNCLTLSGSAGEICSLDCSHLKRRALAAANNSFSPYTESPSGVALLDNDGNWYRGWYIESVASNPSLGPVQAALVDFVARSRGKMFNKIVQAVLVEKNNASVSQERTAKIILDTIAPNCDFKVFHCSVDCAKRLKYLRETLVIDTLGDYTGLHY
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
O65571
O85227
HCNB_PSEPH
Glycine dehydrogenase (cyanide-forming)
Pseudomonas
MSLNPVIVGGGPAGMAAAIELAEHGVRSTLIEEASRLGGVVYRGPLRDGVQLDYLGPRYCEMLAKLHGDFADHEQMIDVRLNSRVVGAEGTQSLVLLDGEEQVQQVSYEQLILAAGCHERSVPFPGWTLPGVKLLGGLQLQIKSGVVKPQSPVVIAGTGPLLPLVACQLHASGVRVAGVYEACALGKIAKQSLAMLNKPQLFLDGLSMLAYLKLHGIALRYGWGVVEAQGQDALSVVTVAPYSSDWQPDMAKAQRIAAQTLAVGYGFIPRTQLSQQMGLEHNFSDDGYLRASANAWQQSSEPHVHLAGDMGGIRGGEAAMLSGRIAALSILMQRGVLSNEAALQRRQGYERKLASILRFRGAVDRYTARGAGQVELPKGDTVICRCEHTTRNDIERALSQGVQDMASLKMRTRVSMGDCQGRMCVGYCSDRLRQATGRKDVGWIRPRFPLDPIPFSAFPPSDQEVSQHD
A three-component membrane-bound flavoenzyme that catalyzes the formation of hydrogen cyanide, a secondary metabolite, by transfer of electrons to a cyanide-resistant branch of the aerobic respiratory chain. Contributes to suppression of black root rot of tobacco.
O85227
Q90XB6
SULF1_COTCO
Extracellular sulfatase Sulf-1
Coturnix
MKTSWFALFLAVLSTELLTSHSSTLKSLRFRGRVQQERKNIRPNIILVLTDDQDVELGSLQVMNKTRRIMENGGASFINAFVTTPMCCPSRSSMLTGKYVHNHNIYTNNENCSSPSWQATHEPRTFAVYLNNTGYRTAFFGKYLNEYNGSYIPPGWREWVGLVKNSRFYNYTISRNGNKEKHGFDYAKDYFTDLITNESINYFRMSKRIYPHRPIMMVISHAAPHGPEDSAPQFSELYPNASQHITPSYNYAPNMDKHWIMQYTGPMLPIHMEFTNVLQRKRLQTLMSVDDSMERLYQMLAEMGELENTYIIYTADHGYHIGQFGLVKGKSMPYDFDIRVPFFIRGPSVEPGSVVPQIVLNIDLAPTILDIAGLDTPPDMDGKSVLKLLDLERPGNRFRTNKKTKIWRDTFLVERGKFLRKKEEANKNTQQSNQLPKYERVKELCQQARYQTACEQPGQKWQCTEDASGKLRIHKCKVSSDILAIRKRTRSIHSRGYSGKDKDCNCGDTDFRNSRTQRKNQRQFLRNPSAQKYKPRFVHTRQTRSLSVEFEGEIYDINLEEEELQVLKTRSITKRHNAENDKKAEETDGAPGDTMVADGTDVIGQPSSVRVTHKCFILPNDTIRCERELYQSARAWKDHKAYIDKEIEALQDKIKNLREVRGHLKRRKPDECDCTKQSYYNKEKGVKTQEKIKSHLHPFKEAAQEVDSKLQLFKENRRRKKERKGKKRQKKGDECSLPGLTCFTHDNNHWQTAPFWNLGSFCACTSSNNNTYWCLRTVNDTHNFLFCEFATGFLEFFDMNTDPYQLTNTVHTVERGILNQLHVQLMELRSCQGYKQCNPRPKGLETGNKDGGSYDPHRGQLWDGWEG
Regulates Wnt signaling through desulfation of cell surface heparan sulfate proteoglycans.
Q90XB6
Q5F9L4
PTH_NEIG1
Peptidyl-tRNA hydrolase
Neisseria
MSNTIKMVVGLGNPGKEYEQTRHNAGFWFLDELAWKWKASFKEEKKFFGEVARAALPDGDVWLLKPATFMNRSGQAVAALAQFYKIKPEEILVVHDELDIPCGRIKFKLGGGNGGHNGLKDIQAKLGTADYYRLRLGIGHPGDRNLVVGYVLNKPSAEHRRQIDDAVAKSLQAVPDIISGKWEEATRFLHSK
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Q5F9L4
Q9H9E3
COG4_HUMAN
Component of oligomeric Golgi complex 4
Homo
MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVAVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL
Required for normal Golgi function . Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 .
Q9H9E3
B0UUD4
G6PI_HISS2
Phosphohexose isomerase
Histophilus
MQNINPTQTNAWKALEQHQKDLEQVTIQQLFEQEPTRFNDYSLKFAEQILVDYSKNNINQQTLSLLRQLAKECALNEATESMFNGEKINRTENRAVLHTALRNCANTPVYVDGKDVMPEVNAVLAKMKSFCQRVISGDWKGYTGKAITDVVNIGIGGSDLGPYMVTEALRPYKNHLTMHFVSNVDGTHIAETLKKVNPETTLFLVASKTFTTQETMTNAISARKWFLAAAQDESQIAKHFAALSTNVKEVEKFGIDTHNMFEFWDWVGGRYSLWSAIGLSIALSIGFDNFEQLLAGAHEMDKHFRTAPMEQNIPITLALIGIWNCNFLGAETEAMLPYDQYLHRFAAYFQQGNMESNGKYVDRSGQVINNYQTGPIIWGEPGTNGQHAFYQLIHQGTKIIPCDFIAPAQTHNVLSDHHNKLLSNFFAQTEALAFGKTQQEVEAEFIQAGKSLDEVKNIVPFKIFTGNKPTNSILVQKITPFTLGALIAMYEHKIFVQGVIFNIYSFDQWGVELGKQLANRILPELVGDEQINSHDSSTNGLINQFKSWR
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
B0UUD4
C1H0K4
SLX1_PARBA
Structure-specific endonuclease subunit SLX1
Paracoccidioides
MAPSIQSLSMIHDSQECIKPIPAFSCCYLLRSCVRHASLYIGSTPDPARRLAQHNGDRYGAAKRTLRENLRPWEMVAIVSGFTSRVAALQFEWAWQNTKVSRHADLDGNATQELGVRICPRTAKEVKRVAKPRTSLTNILANLHLLLRSPYFSKWPIEVRFFSADVHRVWQVWLQRVDGLLNDGIRVVTDFAPDGISEVEGKELLAGAGRVGTLDVGYNSIKEYVEKSQFLLEDGERINCGVCKQRLILQHDIIAVCSHSSCHCAAHLSCLSSHFLKDKDSDSELVPREGTCPTCYSKLEWLTMMKEISLRLRGQAEVNRLFGRRQRAGTPKGQGLKSVRGRGHSEDENESDALQVSTGLDTVNLPPCSDGPWTIDCAIGVLGGIAHRPGGVSSGNDSDATVTPEIETHPQRCRRNQNTRTQRLGLQKSAMINLSDWYDAEVIE
Catalytic subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA.
C1H0K4
A1U392
RS18_MARN8
30S ribosomal protein S18
Marinobacter
MARFFRRRKFCRFTAEGVKEIDYKDLDTLKGYITETGKIVPSRITGTKARYQRQLATAIKRARYLALLPYTDGHDH
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.
A1U392
B8G1W3
EFG_DESHD
Elongation factor G
Desulfitobacterium
MARQFPLEKTRNIGIMAHIDAGKTTTTERILFYTGRVHKIGEVHDGAATMDWMVQEQERGITITSAATTAQWKGHRINIIDTPGHVDFTVEVERSLRVLDGAVAVFCSVGGVEPQSETVWRQADKYGVPRIAYINKMDRMGADFFRGVSMIADRLGANPVPIQIPIGAEDQFKGIIDLVTMKAMIYTDDLGTTSDVADIPGDLVDQANEYREKLLEAVADTDEELMMKYLEGEELTEEEIRNGIRKGTIGLKFIPVVCGSSFKNKGVQPLLDAVVEYMPAPTDVPNIKGVHPETGEADERHSSDKDPFSALAFKIMADPYVGKLAFFRVYSGVLGSGSYVYNSTKGKRERIGRILQMHANHREEIPEVYAGDIAAAVGLKDTTTGDTLCDDKAPIILESMQFPDPVINVAIEPKTKQDQEKMGTALARLAEEDPTFKMHTDQDSGQTIIEGMGELHLEIIVDRLQREFKVECNVGRPQVAYKETIRRAVKSEGKFVRQSGGRGQYGHCWIEIEPLEQGSGFEFVNKIVGGVIPREYIAPIGQGIEEAMQNGIQAGYPVMDIRATVYDGSYHDVDSSEMAFKIAGSMAFKAGAAKADPAIIEPVMKVEVTVPEEYMGEVIGDMNSRRGRIEGMEATGTAQIVRGFVPLSEMFGYATDLRSKTQGRGVYVMMFDHYEEVPKNIAEGIVAKRAGA
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
B8G1W3
Q9C2Z0
PLYA_ASPNG
Pectate lyase A
Aspergillus subgen. Circumdati
MTNFKWIVAAAGLLFGQVLAAPTATSTHAKRATVSDAAFGYASLNGGTTGGAGGTTTTVSSYAAFTSAVSGDDAKVVYVDGTIKQTADQVKIGSNTSIIGKDANAILEGFGVLVKEKENVIIRNLGVSKVLADNGDAIGVQYSNNVWIDHCDVSSDRDHDKDYYDGLIDITHGSDYVTVSNTFIHDHWKASLVGHSDSNEDEDSGHLTVTYANNYWYNVNSRAPSFRFGTGHVYNSYYLDVSDGINTRDGAQLLVESNQFVDSKKALYSTDDGYAVSNDNDFGDSENTAEEGTLTSMPYDYTLLGSANVKAAVVGTAGQTLTF
Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Q9C2Z0
Q48QG6
TRPB_PSE14
Tryptophan synthase beta chain
Pseudomonas
MTQTNFRSGPDVNGLFGSFGGRYVAETLMPLVLDLNREYEAAKADPEFAKEMAYFQRDYVGRPNPLYFAERLTEFCDGAKIYFKREELNHTGAHKINNCIGQVLLAKRMGKKRLIAETGAGMHGVATATVAARFGLPCVIYMGATDIERQQANVFRMKLLGAEIVPVTSGTGTLKDAMNEALRDWVTNVDDTFYLIGTVAGPHPYPAMVRDFQAIIGKETKEQMQEKEGRLPDSLIACVGGGSNAMGLFHPFLDDASVEIIGVEAGGHGVDTDKHAASLNGGVPGVLHGNRTYLLQDGDGQITDAHSISAGLDYPGIGPEHAFLHEVKRVEYVSITDDEALDAFHQCCLLEGIIPALETAHALAEAMKRATNLRDDHLMVVCLSGRGDKDMQTVMNHMAAAEKTQEKLV
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Q48QG6
Q9UZZ3
TRUA_PYRAB
tRNA-uridine isomerase I
Pyrococcus
MRVAFKIAYDGTRFHGFQRQPNLRTVEGEIIKALNNSGIMYSDFKSASRTDRGVSALGNVVAITTEDEKALNPMVLNARLEDVWILSAIEVPQDFHPRFWAKSKVYRYYLPSIGLEVEKVKECSQLFLGVHDFSAFSRVDGRDTVRSIDRIEVFTLGPILIIEIEAKSFLWEMVRRIVKALELCGLGRLSCEEIKEMLEGKFEKSKKVPPAPPEGLLLVDIKYEGIEFPLNDKALKKFKREVEERFRQKIMGAYLLWDMIQLL
Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs.
Q9UZZ3
Q71W25
NPD_LISMF
Regulatory protein SIR2 homolog
Listeria
MNKLNEALKKAEHIVFLTGAGVSVPSGIPDYRSKNGLYAGMSSPEYMLSHTCLVREPEKFYQFVTENMYYPDAEPNAIHTKMAEIEAEKDVTIITQNIDGLHEKAGSKKVVNFHGSLYHCYCQKCGMSVTAEEYLKSDIHSGCGGVIRPDVVLYEEAIPESAIDQSLAAIRQADLIVIVGTSFRVSPFCNLTDYRNKKARIFAVNKEQISLPYPFEMMESDAVKVFAEI
NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Q71W25
Q818W3
OTC_BACCR
Ornithine carbamoyltransferase
Bacillus cereus group
MSTVQVPKLNTKDLLTLEELTKEEIISLIEFAIYLKKNKQEPLLQGKILGLIFDKHSTRTRVSFEAGMVQLGGHGMFLSGKEMQMGRGETVSDTAKVLSQYIDGIMIRTFSHADVEELAKESSIPVINGLTDDHHPCQALADLMTIYEETNTFKGIKLAYVGDGNNVCHSLLLASAKVGMHMTVATPVGYEPNEEIVKKALAIAKETGAEIEVLHDPELAVNEADFIYTDVWMSMGQEGEEEKYSLFQPYQINNELVKHAKQTYRFLHCLPAHREEEVTGKIIDGPQSIVFEQAGNRLHAQKALLVSLFKNVEEPS
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Q818W3
Q4A164
PURA_STAS1
IMP--aspartate ligase
Staphylococcus
MSSIVVVGTQWGDEGKGKITDFLAEQADVIARFSGGNNAGHTIKFGGETYKLHLVPSGIFYKEKLAVIGNGVVVDPVALLKELDALNERGISTDNLRISNRAQVILPYHIKQDEYEEERRGDNKIGTTKKGIGPAYVDKAQRIGIRVADLLDKETFEKLLKDNIEYKGAYFEGMFGKACPTFEEIFETYYAAGQRLAQFVTDTAKVLDDAFVADEKVLFEGAQGVMLDIDHGTYPFVTSSNPVAGNVTVGGGVGPTFVSKVIGVCKAYTSRVGDGPFPTELFDEDGHHIREVGREYGTTTGRPRRVGWFDSVVLRHSRRASGITDLSINSIDVLTGLKEVKICTAYELDGKEITEYPANLKDLQRCKPIFETLPGWTEDVTGCRSLEELPNNARRYLERISELCDVKISIFSVGPDRNQTNLLKSLW
Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Q4A164
O65888
NLTP_STRHE
Non-specific lipid-transfer protein
Striga
ARVSNGALPCGTVDMKAASCISFATGKDKKPSAACCSGLHPLAQTVKTVEDNKAICRCLKTAIKNFSRVQDRFLGQIPTPCKIKGRLPCFHKHRLRKAPLRCIGLETDGFESSPLGMC
Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
O65888
P0A9J4
PANE_ECOLI
Ketopantoate reductase
Escherichia
MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDFLATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTHAARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVNCVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAENISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLPRPW
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
P0A9J4
B4S5B4
RS8_PROA2
30S ribosomal protein S8
Prosthecochloris
MPVTDSIADYLTRLRNAGQAKNKTTDIPYSTQKENISKLLVEKGYIKNYTVITSDRFPFIRVELKYGSNGTFAIKEITRVSKPGRRVYEGKDLRKYLGGLGLLILSTSKGILTDKEAREQGVGGEVLFRIL
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.
B4S5B4
E4RUV9
QUEG_LEAB4
Queuosine biosynthesis protein QueG
Leadbetterella
MRDYSKEIKSWAAELGFDFCGISAADFLEEEAPRLERWLNRNYHGKMAYMANHFDKRLDPRKLVDGAKSVVSLLLNYYPEEPLDASPYKISKYAYGKDYHYVIKDKLKLLFERIQKEIGEVGGRIFVDSAPVMDKIWAKKAGLGWVGKNSNLINRKMGSFFFIAELILDLPLQADGPIRDYCGTCTACIDACPTDAITPYEVDGSKCISYLTIELKDQIPNEFKGKMENWIFGCDICQDVCPWNSFARPHSTEEFYPNENLKTFQDWDEITSEIFSHLFKKSAVERTKLEGLKRNIAFVKEV
Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
E4RUV9
A9M3Q7
HLDD_NEIM0
ADP-L-glycero-beta-D-manno-heptose-6-epimerase
Neisseria
MTIIVTGAAGFIGSNIVKALNQRGITDIVAVDNLSKGEKFKNLAECEIAHYLDKHEFIRQVREHILPYQNIEAVFHQGACSDTMNHDGLYMMDNNYQYTLDLLDWCQDERIPFLYASSAAVYGKGEIFREERELEKPLNVYGYSKFLFDQVLRRRMKEGLTAQVVGFRYFNVYGQHEQHKGRMASVAFHHFHQYREHGYVNLFGSNDGYGNGEQTRDFVSVEDVAKVNLYFFDHPELSGIYNLGTGRSQQFNELAAATVNACRAAEGKPEMSLKELVEEELIRYIPFPDALKGKYQSFTQADITKLREAGYTEEFFDVKSGVERYVKWMLENLA
Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose.
A9M3Q7
Q0H8B9
CL2DB_RAT
Osteoclast inhibitory lectin
Rattus
MSAKKASQPMLNTTGSLQEGEMGKMFHGKCLRIVSPESPAKLYCCYGVIMVLSVAVVALSVALSVKMTPQISTINTYAACPRNWIGVGNKCFYFSEYASNWTFSQTFCKAQEAELARFDTEEELNFLSRYKGSFDYWIGLHRESSEHPWKWTDNTQYNYSLSIRGVERYAYLNDIGISSARVYADKRWSCSKLNSYSLQCKTPFSPM
Receptor for KLRB1B that protects target cells against natural killer cell-mediated lysis.
Q0H8B9
C9JLJ4
U17LD_HUMAN
Ubiquitin carboxyl-terminal hydrolase 17-like protein 13
Homo
MEEDSLYLGGEWQFNHFSKLTSSRLDAAFAEIQRTSLPEKSPLSCETRVDLCDDLVPEARQLAPREKLPLSSRRPAAVGAGLQNMGNTCYVNASLQCLTYTPPLANYMLSREHSQTCHRHKGCMLCTMQAHITRALHNPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHPSKDTTLIHQIFGGYWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVQQALEQLVKPEELNGENAYHCGVCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKIAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHNGHYFSYVKAQEGQWYKMDDAEVTAASITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDEHLVERATQESTLDRWKFLQEQNKTKPEFNVRKVEGTLPPDVLVIHQSKYKCGMKNHHPEQQSSLLNLSSSTPTHQESMNTGTLASLRGRARRSKGKNKHSKRALLVCQ
Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes that may include cell proliferation, progression through the cell cycle, apoptosis, cell migration, and the cellular response to viral infection.
C9JLJ4