accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
B9KR99
|
LPXK_CERSK
|
Lipid A 4'-kinase
|
Cereibacter
|
MRPPAFWFTPPDRPALAARLLAPLGQAYAAATARRLRAPGHRAGVPVICIGNLNAGGTGKTPTAIALMQRLAARGIEAHVVSRGYGGRLEGPVEVDARRHRAADVGDEPLLLAAFGRAWVARDRAAGVRAAEAAGAQAILLDDGFQNPSVVKDLSLIVVDAAVGFGNGRCLPAGPLREPVEAGLARADLLLSIGGPEAQRRFATDWPALPVPRLTGRLATLQMGMYWQGARVLAFAGIGRPEKFFASLRAEGAELLRAEALDDHQPLGEALMKRLEIEAMALGAQLVTTEKDAVRLPPSFRQKVLTLPVRLEFDDGSALDAALDRLNLTARS
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
B9KR99
|
Q971I8
|
SECE_SULTO
|
Protein transport protein Sec61 gamma subunit homolog
|
Sulfurisphaera
|
MSLSQRLKNLREDWKRIISVAKKPEKDTLNQSIKLTLLVMAIVGIIAYIIQLTVALLLH
|
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
|
Q971I8
|
Q8FT51
|
DEF1_COREF
|
Polypeptide deformylase 1
|
Corynebacterium
|
MTVRDVRIFGDPVLTSRADEVVDFDESLATLIDDMFDTMEDAGGVGLAANQVGVLRRVFVFDCSHVDGGLRGHVVNPVWEPIGEETQTGKEGCLSIPDVSAETTRYETVKLSGQDRDGNPIGLVASGLLSRCIQHETDHLDGVLFLKRLDPAERKAAMGVIRASDWFNK
|
Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
|
Q8FT51
|
P0A2F7
|
SSB1_SALTI
|
Single-stranded DNA-binding protein 1
|
Salmonella
|
MASRGVNKVILVGNLGQDPEVRYMPSGGAVANLTLATSESWRDKQTGEMKEQTEWHRVVMFGKLAEVAGEYLRKGSQVYIEGQLRTRKWTDQSGQERYTTEINVPQIGGVMQMLGGRQGGGAPAGGQQQGGWGQPQQPQQPQGGNQFSGGAQSRPQQSAPAPSNEPPMDFDDDIPF
|
Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.
|
P0A2F7
|
P13077
|
FLAB2_HALSA
|
Flagellin B2
|
Halobacterium
|
MFEFITDEDERGQVGIGTLIVFIAMVLVAAIAAGVLINTAGYLQSKGSATGEEASAQVSNRINIVSAYGNVDTSGSTEVVNYANLTVRQAAGADNINLSKSTIQWIGPDTATTLTYDGTTADAENFTTNSIKGDNADVLVDQSDRIEIVMDAAEITTNGLKAGEEVQLTVTTQYGSKTTYWANVPESLKDKNAVTL
|
Flagellin is the subunit protein which polymerizes to form the filaments of archaeal flagella.
|
P13077
|
A8G734
|
RL31_PROM2
|
50S ribosomal protein L31
|
Prochlorococcus
|
MPKSEIHPKWYPDAKVICNGEVVMTTGSTQPELHVDVWSGNHPFFTGTQKILDTEGRVDRFMKKYGMGSANSATSKEQKADKDSQK
|
Binds the 23S rRNA.
|
A8G734
|
Q8HS25
|
PSBT_PEA
|
Photosystem II reaction center protein T
|
Pisum
|
MEALVYTFLLVSTLGIIFFAIFFREPPKVPTKNTK
|
Seems to play a role in the dimerization of PSII.
|
Q8HS25
|
B3EP42
|
RL15_CHLPB
|
50S ribosomal protein L15
|
Chlorobium
|
MDLSSLRPAKGAVKNKKRIGRGPGSGNGTTAGKGNKGQQSRSGYTRPVSEGGQMPIYRRLPKFGFTKPNRKNVIPVNLSQIALWMENGKATSEITVENLKSLCSARRADYFKILGNGELKSPVTITAHFVSKSAQEKILQAGGTITLAERTLLEAERIKDTPVEEGLMKPKARLRKKKKIKS
|
Binds to the 23S rRNA.
|
B3EP42
|
Q2YUP1
|
DNAA_STAAB
|
Chromosomal replication initiator protein DnaA
|
Staphylococcus
|
MSEKEIWEKVLKIAQEKLSAVSYSTFLKDTELYTIKDGEAIVLSSIPFNANWLNQQYAEIIQAILFDVVGYEVKPHFITTEELANYSNNETATPKETTKPSTETTEDNHVLGREQFNAHNTFDTFVIGPGNRFPHAASLAVAEAPAKAYNPLFIYGGVGLGKTHLMHAIGHHVLDNNPDAKVIYTSSEKFTNEFIKSIRDNEGEAFRERYRNIDVLLIDDIQFIQNKVQTQEEFFYTFNELHQNNKQIVISSDRPPKEIAQLEDRLRSRFEWGLIVDITPPDYETRMAILQKKIEEEKLDIPPEALNYIANQIQSNIRELEGALTRLLAYSQLLGKPITTELTAEALKDIIQAPKSKKITIQDIQKIVGQYYNVRIEDFSAKKRTKSIAYPRQIAMYLSRELTDFSLPKIGEEFGGRDHTTVIHAHEKISKDLKEDPIFKQEVENLEKEIRNV
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q2YUP1
|
Q8M9X3
|
CEMA_CHAGL
|
Chloroplast envelope membrane protein
|
Chaetosphaeridium
|
MKLIIYQIIKFLLITYYDCLHKAYNESKKIQKIQNEYISYTQLLTSAQHSSQTVILYIDSEINKCLFFINLNLFKYKIIKLVINFIGEDKISNFLSNHVDIKNEYVNLSIEKIFSSNSDFRKSQSESNSKNLVLKKNLDTNKNFHFDFLKYKIKYERQLAWVEAVLEDLKIWKDFYLYNFDFFNKKINNTRRFFFFNKPSSYTLSLSYESIGLIPRSITRTLSKFQTELLGNSYSYIIQEFRLAKYHTWVSLQYVASLIFLPWLITKLCQNLFLQSWIENWWNTSQSQIFINLSQQTKALQRLQQLEELLWLDMAMSERIEGQPQDLGALIHQRTIQLAEYYNQDSINIILHLFTDFIAIFTLIVLLILGKKRLAILNSWVQEVFYSLTDTMKAFLILLFTDLCIGFHSPHGWEIAIDGLLEHLGFAHNKYIVSCLVSTFPVILDTVLKYWIFRHLNRISPSIVVTYHTMNE
|
May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
|
Q8M9X3
|
B0S9S9
|
QUEC_LEPBA
|
Queuosine biosynthesis protein QueC
|
Leptospira
|
MVSILDSSFKSKTEKKGAIVLLSGGLDSTTCLYLAAKDFGYPKNKKLPLLALSFDYSQKHKIELTKSKKIAKTLGIKHVIQKLDPGFFLGSSLTESKIKVRKNAKSLFSGDETEIPNTYVPGRNILFLSFALSLAEGHGYDSIYIGVNALDYSGYPDCRPEFIDSFQKMANLGTKKGVSGTGDSIQIKTPLLHLGKKEIIELGMSVGAPLGLTHSCYDPVSGKPCGKCDSCILRAKGFLEVGLKDPAL
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
B0S9S9
|
A6L0W6
|
RIMM_PHOV8
|
Ribosome maturation factor RimM
|
Phocaeicola
|
MIKKDEVFKIGIFNKPHGVKGEISFTFTDDIFDRVECEYLVCLLDGIFVPFFIEEYRFRSDTTALVKLEGVDTSEKARMFTNVEVYFPKKYVGEEEDSDDIPTWNYFIGFKVEDVNHGELGEIVAVDDSTMNVLFAIEKGGEELLLPAHEEFITKLDKKKRLLTVEVPDGLI
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
A6L0W6
|
P86015
|
PER3_VITVI
|
Peroxidase 3
|
Vitis
|
QTFVTIPGTLRDHPDNLSLAGDGFDTVIKVSCADILTMATR
|
Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
|
P86015
|
Q62401
|
CCL12_MOUSE
|
Small-inducible cytokine A12
|
Mus
|
MKISTLLCLLLIATTISPQVLAGPDAVSTPVTCCYNVVKQKIHVRKLKSYRRITSSQCPREAVIFRTILDKEICADPKEKWVKNSINHLDKTSQTFILEPSCLG
|
Chemotactic factor that attracts eosinophils, monocytes, and lymphocytes but not neutrophils. Potent monocyte active chemokine that signals through CCR2. Involved in allergic inflammation and the host response to pathogens and may play a pivotal role during early stages of allergic lung inflammation.
|
Q62401
|
B0R2L5
|
MOAA_HALS3
|
Molybdenum cofactor biosynthesis protein A
|
Halobacterium
|
MLEDDFGRDVSGVRVSLTDRCNFDCVYCHNEGLGDTRGPIDPRENELSTDRVVRFLSVAHEFGVDAVKLTGGEPMLRSDLEAIIRRTPDDMAVSMTTNGTFLPGRAADLVDAGLERVNISQDAMDNDAFAELTQSGAYDAVLEGVEAALDAGLAPVKLNMVVFEPTAGYVPEMVDHVAARDGLRLQLIEYMPELAGHPEWAIDIDRVHDWLADRADRIETREMHDRRRYWVSSRDAGSTADDAAQSVTPDGGAHPDQGMVEIVDPVGNPQFCANCHRVRLTHDGYLKGCLNRNDDLRGIGETTQSMRAAFRETVANRVPYYGEYMTRTDDGGWEINDDYLDVEGDRDPYEYAADDSA
|
Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
|
B0R2L5
|
F1SY52
|
CY045_POSPM
|
Cytochrome P450 monooxygenase 45
|
Postia
|
MHSVLAQAASGALSFELRLGQSSVLTICILALLTFVLREIVLYFTRHSMPPGPFRWPLIGNALQLPQDHPWVKYTEWAKMYGPLMQLDVLGQHMLVITSAQTARDLMEKRSSIYSDRPHLVMAGDLAGFGDTLILQNYGEEFRYQRKLVSHSFSPSVIHRYYDLQEAAARRLVLAIIEDPDSLENSTRLHIASIILRMTYGYTVKGVDDPLFTTGIAVINGFSEATRPGAWPVDFVPILQYVPHWVPGFVFTRKAREWRGVLERAMWAPYHWCKENYARDAAHGLCLCGSILAAEGSQLSSDQEWLFVNAAVTVMGGGLDTNISTILSFVLAMLRFPEVQKKAQAEIDAVIGPNRLPLISDRHSLPYVRSVVTEVYRWIPAVPLGIPHALRQDDHYDGLFLSKGSVVVPNVWGMLHDPSIYPAPHEFKPERYGGLDAEMTKVTDIAFGFGRRACPGFYFAEGTIFAIVATVLAICDVVPTVDEHGQEVIPEVSLTSGAIVSPENVKCAFRPRSGRVKDILVEAVETEQE
|
Cytochrome P450 monooxygenase that is able to use trans-stilbene as a substrate for oxidation.
|
F1SY52
|
Q02710
|
ECM23_YEAST
|
SRD1 homolog 2
|
Saccharomyces
|
MLYNKEQGTSGASSSGRRTKFHFDRFVQMVLFIAANPNYCCSVASIPKSGVTPDLKRADILEQKIKSLNSALSPKLKEESRLGGPLHNPSILPAPSFSSLPISSNGKKSLAGYRPKSRKKQTILPNGQPKECATCGDTWTSQWRSGPNGNVELCSRCGIAYRKKMEKKIRSQQSSDDGTKNFIFKNK
|
Involved in morphogenesis. May be involved in cell wall organization and biogenesis.
|
Q02710
|
Q6A8N5
|
LGT_CUTAK
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
|
Cutibacterium
|
MRHRRRPGGRSTAGGTPVSQLSIPSPSIEAFHLGPLTIHIYALCILAGIVVAYISGGRRYQARGGKQEQFEELCALAVIAGIIGGRLYHVITDHQLYFGPGRTWYHCFFIWQGGLGIWGAISLGGLAIWLYCRRKGIRFASVADSLAPGILAAQAIGRLGNWFNQELFGRPTSLPWGLEIDLSHRPAGYLQYATFHPTFLYELVWSLVGAVFLLWVDRRWTLDHGRLFTLYVAIYTFGRFWVERLRIDPAHHVGQWRLNDVTALVVFTGAVVILIVLQRRYGKGDEHSSCPAHKTR
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
Q6A8N5
|
Q8AV97
|
SLAA_PROFL
|
Snaclec flavocetin-A subunit alpha
|
Protobothrops
|
MERLIFVSFGLLVVILSLSGTGADFDCIPGWSAYDRYCYQAFSKPKNWEDAESFCEEGVKTSHLVSIESSGEGDFVAQLVAEKIKTSFQYVWIGLRIQNKEQQCRSEWSDASSVNYENLVKQFSKKCYALKKGTELRTWFNVYCGTENPFVCKYTPEC
|
Strong platelet aggregation inhibitor. Binds specifically to platelet glycoprotein Ibalpha (GP1BA) with high affinity and inhibits vWF-dependent platelet aggregation . Has also been observed to induce small agglutinates in washed platelets by binding to GPIb .
|
Q8AV97
|
Q54E86
|
MND1_DICDI
|
Meiotic nuclear division protein 1 homolog
|
Dictyostelium
|
MATRRKGMSPEEKKEKLKEFFHSNSTIYSSKDVESEASKYTGMTQVQCKETLQMLIDDGVVNTDKMGSSNFYWSFPSFEFDSKKDKIIEQTKLLSETKERIQSETKKIEQLKSERVESETRTKNLEKLQTLKDDNKSFKEELLLYADSSLIDDKKRDIKIAIAAVNRYTDNISSLRQFCDSKYNIRPSDFDTSFGIKPDMDYLEEYNFNDTPQPVNKKKRK
|
Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination.
|
Q54E86
|
C0Q3L1
|
RHAD_SALPC
|
Rhamnulose-1-phosphate aldolase
|
Salmonella
|
MQNITDSWFVQGMIKATSDAWLKGWDERNGGNLTLRLDETDIAPFAANFHEKPRYIALSQPMPLLTNTPFIVTGSGKFFRNVQLDPAANLGVVKIDSDGAGYHILWGLTHDAVPTSELPAHFLSHCERIKATHGKDRVIMHCHATNLIALTYVLENNTALITRKLWEGSTECLVVFPDGVGILPWMVPGTDEIGQATAQEMQKHSLVLWPFHGVFGSGPTLDETFGLIDTAEKSAEVLVKIYSMGGMKQTITREELVALGKRFGVTPLASAVALY
|
Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde.
|
C0Q3L1
|
Q38X91
|
AROD_LATSS
|
Type I dehydroquinase
|
Latilactobacillus
|
MHLEFTTGQTQTAVSLMPRHLDDCLRELILINQKKDAIDILEWRLDYWQAPAQLLTAAEKIAALDLPLILTVRTTNDGGLASAQDYLTYYAPLIKAHIGQAIDLEWSLAAEQRHQLAELAHQQHYQVLLSHHDTVQTPDNDTLRTQLLAMQADPDADLLKLATTAQSPADTTRLLAATQSFTHQFDKPLTTMAMSEFGVASRIFGGQFGSAISFGYLETPSAPGQLPIEQLKGLLTTNQA
|
Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids. Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate.
|
Q38X91
|
A0RMQ7
|
RSMI_CAMFF
|
rRNA (cytidine-2'-O-)-methyltransferase RsmI
|
Campylobacter
|
MLYFLPTPIGNLDDISKRCLDVLELCEIIICEDTRVTKSLITLLNAKFGLQISPKEFYSLHTHNEKDFFDKFDKVRLETKICIYASDAGMPCISDPGISLVKFAQQNSIKYEVLSGANALLLAAAASGIIEKEFTFLGFLPNLGKERAIAIQNALNSLYPVIIYESPKRILSLIKSISEFDPLREVFIIKEATKKFEAKFKNSATNLLTQLENSNLNGEWCVVIDRSANKALERITTKDIMELDLPLKQKAKLISKITGENAKKIYQNLIT
|
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
|
A0RMQ7
|
Q82SI9
|
YBEY_NITEU
|
Endoribonuclease YbeY
|
Nitrosomonas
|
MPTRNMPLTKNPVESPDHEQELVLTVQYVADKTDIPNRRLFRKWVKAALSKPAEVVIRIVDRQEGEILNRDFRGKSSATNVLTFVYDDDVPLLGDIVLCAPVICNEAQQQGKDLTAHYAHLTIHGILHLQGYDHIRDEDAVVMESLETEIITRLGYPDPYVIQH
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q82SI9
|
Q180P4
|
PFKA_CLOD6
|
Phosphohexokinase
|
Clostridioides
|
MKTIGLLTSGGDAPGMNAAIRAVVRSAIYYGCKVYGINRGYKGLLEEDLTEMNLSSVGDIIHRGGTILKSSRCEEFKTEEGRLKAVKILKKYKIDCLVVIGGDGSFAGAQKLSDLGFPAIGIPGTIDNDLAYTDYTIGFDTAMNTIIDAIGKIRDTSSSHERVNIVEVMGRHCGDLALYAGLAGGAETIIVPEVEITVDEVALRLKTTQKRGKRHSIIVLAEGVGSASDLEKELKKESGADLRVTVLGHVQRGGSPTVSDRILASRLGVRAVELLLDGKSARVVGIKENKIIDLEISEALAQKKVFDKEAYEMAKILSI
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
Q180P4
|
A4FWU0
|
BIOB_METM5
|
Biotin synthase
|
Methanococcus
|
MKEIKLNSDSLEIYEKSASKKLNRNDLIDLWNLDLNDLLDISYALKKLFNKDKIDLCSIMNAKSGICPENCIFCSQSKHNSSKIDTYELKSKEEILKNAKSVEKYSNRFSIVVSGKTVTDLEFEKIIESIEEIQNKTKLKVCVSLGLLNKDQLKALNEKNVRIHNNLETSENYFKNICTTHDYNDKIKVILEAKKIGLEMCSGGIFGMGESIDDRINLFLDLKKLGVDSIALNLLNPIYGTKIYDRINSGDISPINSIGALKSLCIARITLPNKVIRLCGGREHVLKDMQKYSLLAIDGLMIGNYLTTNGQNIQSDLKMIEEMGFER
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
A4FWU0
|
Q8RWL5
|
CLT3_ARATH
|
Chloroquine-resistance transporter-like transporter 3
|
Arabidopsis
|
MATTSRRFTTGLFASITSVKSHSANRPQSISLIRRNHIDHRLPLIVPSSRRWIIQAARSWDGFDDGAEAEIKKPGAYGYAIGDNEIEGSSSSTVHVIDGEHVKTAEIVIWAAVTAAFGVGNRVMYKLALVPLKEYPFFLAQLSTFGYVAVYYTILYFRYRAGTVTDAMLSVPKSPFLIVGILEALAAAAGMAAAANLSGPSTTVLSQTFLVWQIFFSIIFLGRRYSVNQILGCTLVALGVIVSVASGSGAAHSLNEAGVLWILLMVLSFLLQGAGTVLKEVIFIDSQRRLKGASLDLFIVNSYGSAFQAICIALLLPFLSKLWGIPFNQLGTYLKDGAVCFLNNGTITKGCDGAPFLPLLFVIMNIGYNIALLRLLKISSAVVSCLASTVSVPIAVFLFTMPLPYLGVASSLPKGFMGGTIILVLGMILYSWTPHGANSSHTDSVIPSPPPT
|
Involved in thiol transport from the plastid to the cytosol. Transports probably both glutathione (GSH) and its precursor, gamma-glutamylcysteine (gamma-EC). Exhibits some functional redundancy with CLT1 in maintaining the root GSH pool.
|
Q8RWL5
|
A1VM56
|
PNP_POLNA
|
Polynucleotide phosphorylase
|
Polaromonas
|
MSIFNKVTKSFQWGQHKVTMETGEMARQAGGAVLLDMDGTVVLATVVAKSDAKPGQDFFPLTVDYLEKTYAAGRIPGSFFKREGRPSEFETLTSRLIDRPIRPLFPEGFFNEVQVVIHVLSLNPEVEGDIPALIASSAALSISGIPFNGPIGAARVAYINGEYVLNPGKTQLQNSTMDLVVAGTEAAVLMVESEAKQLSEEIMLGAIVFGHEQGNIAINAIHELVRDAGKPVWDWKAPAKDEVLIAKVVALAEEKLVAAYQIRNKQARTHATRQVTTWTKMGLKAEGVEFDGVAVEGMLFDIEAKIVRSQILAGDPRIDGRDTRTVRPIEIRNSVLPRTHGSALFTRGETQALVVTTLGTERDAQRIDALSGDYEDRFMLHYNMPPFATGETGRVGSPKRREIGHGRLAKRALIAVLPSKEEFPYTMRVVSEITESNGSSSMASVCGGCLSLMDAGVPMKAHVAGIAMGLIKEDNRFAVLTDILGDEDHLGDMDFKVAGTTFGITALQMDIKIQGITKEIMQVALAQAKEARMHILGKMQEAMGQANAEVSDFAPRLYVMKINPEKIRDVIGKGGAVIRALTEETGTQINIEEDGTITIASNDSAKADEAKRRIAEITAEVEIGKVYEGAITKILDFGALVNLMPGKDGLLHISQIAHERVEKVTDYLSEGQIIKVKVLETDEKGRVKLSMKALLDRPSQHQG
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A1VM56
|
O74988
|
COX5_SCHPO
|
Cytochrome c oxidase polypeptide V
|
Schizosaccharomyces
|
MYLSKIICKKVPMKLLCTRNAATVSAAATNALQKEQPSGEAMIARPRLVDLDKRWGIMSQEEKDGLITDLYARQKQPWTTLSIEEKKAAYWIAFGEHGPRAFSHISQKTVFWGTVAGLTIGVVLFGLIRTQAAPSPRTMTREWQEKSNEYMKENKINPISGEASEGFKGRGQISGGIFSPSEKDKK
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
O74988
|
A6MVW5
|
ATPD_RHDSA
|
F-type ATPase subunit delta
|
Rhodomonas
|
MSSKNVKVAKPYADAFIEIANKGSVINDLNCIATALSESKDLQKAIANPLVSSAAKKDIIKSIFAGNVDENTVKFMMVLCDRGRIEYLDAIAETALILAYKQASIEMAYVASSVKLSSAQTEALVDKLKAMTKADQIKLELKVDESLIGGFKVQIGSRIIDTSVQNQLKQLSSYLGASVA
|
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.
|
A6MVW5
|
O64518
|
MCA5_ARATH
|
Metacaspase-6
|
Arabidopsis
|
MAKKAVLIGINYPGTKAELRGCVNDVRRVHKSLVDRFGFSERNITELIDTDESSTKPTGKNIRRALLNLVESAKPGDVLVVHYSGHGTRLPAETGEDDDTGYDECIVPCDMNLITDDEFRDLVEKVPKEAHITIISDSCHSGGLIDEAKEQIGESTKKKPKKESGGSSGLGIKGFVREAVEEALESKGIAIPHHKDEKDENKTKELKLEDGAKVHVVNKSLPLQTLIDILKQNTGNNDIEVGKIRPTLFNVFGEDASPKVKKFMKVILTKLQEGKTEGGILGMIGKLAQEFLKHKLNDDEEYVKPAMKTHVGNKQEVYAGASNGSLADNGILISGCQTDQTSADASPQGHPEMAYGAFTNAVQIILEETKGMITYKELVLKARKLLKKQGFSQRPGLYCSDSFVNAPFIC
|
Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. May be involved in the modulation of programmed cell death activated by oxidative stress.
|
O64518
|
A2CC49
|
RS13_PROM3
|
30S ribosomal protein S13
|
Prochlorococcus
|
MARIAGVDIPRDKRVEVALTYIYGIGLTRAKTILTKSGVNPDIRVKDLEDGDVQKLRTALEAFTIEGDLRRQEGMALKRLQDIGCLRGRRHRMSLPVRGQRTRTNARTRRGARKTVAGKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
A2CC49
|
P0A132
|
IF3_PSESM
|
Translation initiation factor IF-3
|
Pseudomonas
|
MIIKREMRQDKRAAPKAPINENISAREVRLIGADGEQIGIVSIDEALRIAEEAKLDLVEISADAVPPVCRVMDYGKSIFEKKKQVAAAKKNQKQIQVKEIKFRPGTEEGDYQVKLRNLVRFLSDGDRAKVSLRFRGREMAHQELGMELLKRVEGDLLEYGSVEQHPKMEGRQLIMVIAPKKKK
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
P0A132
|
B5Y963
|
RS13_COPPD
|
30S ribosomal protein S13
|
Coprothermobacter
|
MARIVGVELPDNKRIVFALPRIYGIGKSTAEDICEALGIDPMQKLGELTPEQINTLQDYITAHYKVEGDLRREVAMNIKRLMDIKCYRGIRHQRGLPVRGQRTRHNARTRKGPRKTVGAKKGKR
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
B5Y963
|
A0LQM0
|
HIS3_SYNFM
|
Phosphoribosyl-AMP cyclohydrolase
|
Syntrophobacter
|
MTLDPDFSKNDGLLPVIVQSADDDKVLMLAYMNELAWHRTLETGKAHYWSRSRRKLWQKGEESGNVQTIREILLDCDLDTILLKVVQTGGAACHDGYESCFYRRYADGKLEVVGKRVFDPKEVYKK
|
Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP.
|
A0LQM0
|
P86197
|
ODP2_MESAU
|
Pyruvate dehydrogenase complex component E2
|
Mesocricetus
|
VPLPSLSPTMQAGTIARDVPLGAPLCIIVEKGRVFVSPLAKGIDLTQVKGTGPEGDIDSFVPSKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKEGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPITMLL
|
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle.
|
P86197
|
A1UUD2
|
DAPE_BARBK
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Bartonella
|
MPVLTDPVQLLQALIRCPSITPNEAGALSILEQFLRKMGFSVERPIFSDKNTADVENLYAKMGNKGPHLMFAGHSDVVPPGELDNWMYPPFEGIINQGKIYGRGAVDMKGAIACFIAALARVLEKQPIKGAVSLLITGDEEGPAINGTVKLLKWAAQKGEKWNAAIVGEPTSVKRVGDMIKIGRRGSISGIITVKGRQGHVAFPERAANPLPLAHKLIQALTDTALDQGTKNFQASNLELTTIDTGNSATNIIPAQTVIRFNIRYNDLWTKEALIAEIEKRLALVHSENNSNQYPYYQLEWIQNLGSVFLIKNDHLIEILSNAIEIVTGKRPECSTSGGTSDARFIKDYCPVVEFGLPGNTMHMVDECVTLDAMESLTVIYERFIIDFFA
|
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.
|
A1UUD2
|
Q5SXM2
|
SNPC4_HUMAN
|
snRNA-activating protein complex 190 kDa subunit
|
Homo
|
MDVDAEREKITQEIKELERILDPGSSGSHVEISESSLESDSEADSLPSEDLDPADPPISEEERWGEASNDEDDPKDKTLPEDPETCLQLNMVYQEVIQEKLAEANLLLAQNREQQEELMRDLAGSKGTKVKDGKSLPPSTYMGHFMKPYFKDKVTGVGPPANEDTREKAAQGIKAFEELLVTKWKNWEKALLRKSVVSDRLQRLLQPKLLKLEYLHQKQSKVSSELERQALEKQGREAEKEIQDINQLPEEALLGNRLDSHDWEKISNINFEGSRSAEEIRKFWQNSEHPSINKQEWSREEEERLQAIAAAHGHLEWQKIAEELGTSRSAFQCLQKFQQHNKALKRKEWTEEEDRMLTQLVQEMRVGSHIPYRRIVYYMEGRDSMQLIYRWTKSLDPGLKKGYWAPEEDAKLLQAVAKYGEQDWFKIREEVPGRSDAQCRDRYLRRLHFSLKKGRWNLKEEEQLIELIEKYGVGHWAKIASELPHRSGSQCLSKWKIMMGKKQGLRRRRRRARHSVRWSSTSSSGSSSGSSGGSSSSSSSSSEEDEPEQAQAGEGDRALLSPQYMVPDMDLWVPARQSTSQPWRGGAGAWLGGPAASLSPPKGSSASQGGSKEASTTAAAPGEETSPVQVPARAHGPVPRSAQASHSADTRPAGAEKQALEGGRRLLTVPVETVLRVLRANTAARSCTQKEQLRQPPLPTSSPGVSSGDSVARSHVQWLRHRATQSGQRRWRHALHRRLLNRRLLLAVTPWVGDVVVPCTQASQRPAVVQTQADGLREQLQQARLASTPVFTLFTQLFHIDTAGCLEVVRERKALPPRLPQAGARDPPVHLLQASSSAQSTPGHLFPNVPAQEASKSASHKGSRRLASSRVERTLPQASLLASTGPRPKPKTVSELLQEKRLQEARAREATRGPVVLPSQLLVSSSVILQPPLPHTPHGRPAPGPTVLNVPLSGPGAPAAAKPGTSGSWQEAGTSAKDKRLSTMQALPLAPVFSEAEGTAPAASQAPALGPGQISVSCPESGLGQSQAPAASRKQGLPEAPPFLPAAPSPTPLPVQPLSLTHIGGPHVATSVPLPVTWVLTAQGLLPVPVPAVVSLPRPAGTPGPAGLLATLLPPLTETRAAQGPRAPALSSSWQPPANMNREPEPSCRTDTPAPPTHALSQSPAEADGSVAFVPGEAQVAREIPEPRTSSHADPPEAEPPWSGRLPAFGGVIPATEPRGTPGSPSGTQEPRGPLGLEKLPLRQPGPEKGALDLEKPPLPQPGPEKGALDLGLLSQEGEAATQQWLGGQRGVRVPLLGSRLPYQPPALCSLRALSGLLLHKKALEHKATSLVVGGEAERPAGALQASLGLVRGQLQDNPAYLLLRARFLAAFTLPALLATLAPQGVRTTLSVPSRVGSESEDEDLLSELELADRDGQPGCTTATCPIQGAPDSGKCSASSCLDTSNDPDDLDVLRTRHARHTRKRRRLV
|
Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
|
Q5SXM2
|
Q15UB7
|
PYRD_PSEA6
|
Dihydroorotate oxidase
|
Pseudoalteromonas
|
MYAILQKFLFTQDAEWSHDFTINWLKRTQHNFLNVAYKQHIDDKPVEFLGITFKNPVGLAAGLDKNAECIDAFAAMGFGFIEVGTVTPKAQAGNDKPRMFRLPAGQAIINRMGFNNKGVDYLVEQVKQAKYKGVLGINIGKNKTTPEDEALNDYLICLRKVYAHASYVTVNISSPNTPGLRNLQYGDALTQLLEGLKEEQANLEVKHNKRVPILIKIAPDLEDSELDSMVDSFLTVGIDGVIATNTTLDRDRVKGQEHAEEAGGLSGSVLTDKSQQIVSSLCTKLAGNVPVIGVGGIDSPHAAKARIEAGSPLIQVYSALIYQGPKLIKEIVDSL
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
Q15UB7
|
A1UR46
|
ATPD_BARBK
|
F-type ATPase subunit delta
|
Bartonella
|
MSDSFSLLPLPLVSQRYAHALFDLVQKEGYVGDVEKALASFQVILEQDKALKHLVQSPFLSVKEQVKAVCAVCENLGLAHKKAGQILRNFLCVVAANRRLSALSGILQAFQRRVALSRGEVSAQVISAHPLDADQKKELCVALESVVGGKVTLRLSVDPAILGGLIVRLGLYQIDTSLATQLSSLKLALKKEVS
|
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.
|
A1UR46
|
Q5R109
|
PDXJ_IDILO
|
Pyridoxine 5'-phosphate synthase
|
Idiomarina
|
MKGLRLGVNIDHVATLRNARGVRYPDPVAAAAIAEQAGADGITIHLREDRRHITDRDVAMLKQTLNVPMNLEMAVTEEMLDIAIKTQPTYSCLVPEKRQELTTEGGLNVAGQLETITDATRRLSDAGIQVSLFIDADHEQIDAAKKAGAPIVELHTGQYAEAETEEQRTVELARLMEASEYAHSIGLQVNVGHGLHYHNTLEVAEIPQVCELNIGHSIIARAVLVGLDQAVRDMRNILDKAR
|
Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate.
|
Q5R109
|
Q8IUC8
|
GLT13_HUMAN
|
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
|
Homo
|
MRRFVYCKVVLATSLMWVLVDVFLLLYFSECNKCDDKKERSLLPALRAVISRNQEGPGEMGKAVLIPKDDQEKMKELFKINQFNLMASDLIALNRSLPDVRLEGCKTKVYPDELPNTSVVIVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKIIRMEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRNYFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFRKATPYTFPGGTGHVINKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIYPDSQIPRRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDLCLDVSRLNGPVIMLKCHHMRGNQLWEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCSGSRSQQWLLRNMTLGT
|
Can glycosylate both unmodified peptides and glycopeptides that already contain an O-linked GalNAc sugar. Transfers GalNAc to Thr-/Ser-rich tandem repeats GTTPSPVPTTSTTSAP of MUC5AC, specifically on Thr-3 of non-glycosylated MUC5AC peptide, on Thr-12 and Thr-13 of preglycosylated MUC5AC at Thr-3 (MUC5AC-3), on Thr-3 of preglycosylated MUC5AC at Thr-13 (MUC5AC-13) and on Thr-12 of preglycosylated MUC5AC at Thr-3 and Thr-13 (MUC5AC-3,13).
|
Q8IUC8
|
Q2IWG9
|
SURE_RHOP2
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Rhodopseudomonas
|
MRILCTNDDGIHAPGLKIVEDIARALSDDVWVVAPELDQSGVSHSLSLNDPLRLREVGPRHFAVRGTPTDCVIMGARHILADKAPDLVLSGVNRGRNVAEDVVYSGTIAGALEGTILGLPSFALSQEFTLETRNAPLWDTAKAHGPEILRKAIKAGVPKNTVININFPACAPDEVAGVQVTRQGKRNQGFLRVDERHDGRGNPYFWIGFERVAVVDMPAEGTDLAALAAKYISVTPLRLDRTDEAFSATLAKTLG
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q2IWG9
|
Q043G6
|
ADDA_LACGA
|
ATP-dependent helicase/nuclease AddA
|
Lactobacillus
|
MTNFTKEQDQAINDAGKDILVSASAGSGKTTVLVERVLKKILSGTPVSSLLIITFTKAAAREMKERIKQKISDQLEIEPDNQFLRSQLLDVDTANISTIDSFCLDVIRRFYYVIDLDPQFSVLTDETQAELLKERALREIEADYLEGDNQDFQDFYDNFSGDRDAEGARNLLLQLYNTATTEPNYEKFLDNLPTCYEVGDNLIRSNLWQQQIKPLLLKEISDLKAEVEALLAEPEINSSDLVKVKENYDIFSNRLDSFWESLNTDQPYNEIRANLMNCKFEKAVRKSKKWSDESIEVYQDSQDLKLDLNDQLKKIFASFFVVEEKEQIAVLQKSEKIVKTIVAAEKKLIQKFSQLKREQNLIDYSDMEQFAFSILTTDTSNAHIAQEYYQEKFNEILIDEYQDVNALQENIIKAIKKKGQNTLFMVGDVKQSIYGFRQARPDLFLSKYHTYGKDNDSEKIILADNFRSTKRVTKTVNDLFNPILTTNFGGIDYKKEGQLQFGASYYPSDLPTASEYIFTDKKQTQSAYEDQYGDEMDFSEVQMVIARIKQLKAENFQVWDRRTQLKRPLEYSDIAIITRTRSDNLQVMQEFAKADLPLFVTDAQNYFQTFELIMIMNYLRLIDNPQQDIPLVAVMRSPLFNFKEPELAQIRVKTPAGNFYTALTSFASVNSSLGKKCKEFLQQLETLRSFAATHRISELIWSIYEKTHLLEIVTGLPNGQQRRVNLESLYERATSYESAGFKGLYQFISFIERMRKNQKDLAQPLLSDKADNAVKLMTIHASKGLEFPIVFVMGLGHQYQTRDLSGNFTISQNELGLTIKEKNYRIDSLVKSLADVQKRQQMLEEEARILYVGLTRAQQKLILVASVNEIENKRKKWVSELDQKKDIIPLVKKINAQSPLDFLGPKLEQKHEFDQTIRDMTSALEEQDKLYYLKFNLDLEPEKIKDQNEDSQEVNSNVNKVVKELYNFKYPFEDATKTTAYQSVSEIKKAFNDPIDTELENSRLISSSNRYLQPIDETPTFLEGQKFTGAEIGTAMHLVLQYYNYEGNKDQENLDQEIDQLVELGKLNSLMVPHLSKEALNWFVMSDFAKEFWKQPDKLHRESQFSSLVNASELFNDFSDPSAKVLVHGTVDGYFEAKDGLILFDYKTDFVDKTNEEQAIEKIKQKYTGQLRLYEQALNEMNNDKKVIGKYLILLDARKVVPVD
|
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
|
Q043G6
|
Q8YLJ5
|
RL7_NOSS1
|
50S ribosomal protein L7/L12
|
Nostoc
|
MSAATDQILDQLKSLSLLEAAELVKQIEEAFGVSAAAPAGGMMMMAAPGAAAAAEPVEEQTEFDVVLESVPADKKIAVLKIVREITGLGLKEAKDLVEAAPKAVKEAIAKDAAEDAKKRIEEAGGKVTVK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
Q8YLJ5
|
O73819
|
GNA14_XENLA
|
Guanine nucleotide-binding protein subunit alpha-14
|
Xenopus
|
MAGCCLSAEEKESQRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYTDEDRKGFTKLVYQNIFTSMQSMIRAMDTLRIQYTSEQNMENALVIREVEVDKVSSLERKHVEAIKKLWEDEGIQECYDRRREYQLSDSTKYYLSDIDRISNPGFIPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIIFLVALSEYDQVLAECDNENRMEESKALFKTIITYPWFQNSSVILFLNKKDLLQEKIMYSHLIDYFPEFTGPKQDSQAARDFILKLYQDQNPDKEKVIYSHFTCATDTENIRFVFAAVKDTILQLNLREFNLV
|
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C. Mediates responses to trypsin.
|
O73819
|
P22520
|
CVAB_ECOLX
|
Colicin V secretion/processing ATP-binding protein CvaB
|
Escherichia
|
MTNRNFRQIINLLDLRWQRRVPVIHQTETAECGLACLAMICGHFGKNIDLIYLRRKFNLSARGATLAGINGIAEQLGMATRALSLELDELRVLKTPCILHWDFSHFVVLVSVKRNRYVLHDPARGIRYISREEMSRYFTGVALEVWPGSEFQSETLQTRISLRSLINSIYGIKRTLAKIFCLSVVIEAINLLMPVGTQLVMDHAIPAGDRGLLTLISAALMFFILLKAATSTLRAWSSLVMSTLINVQWQSGLFDHLLRLPLAFFERRKLGDIQSRFDSLDTLRATFTTSVIGFIMDSIMVVGVCVMMLLYGGYLTWIVLCFTTIYIFIRLVTYGNYRQISEECLVREARAASYFMETLYGIATVKIQGMVGIRGAHWLNMKIDAINSGIKLTRMDLLFGGINTFVTACDQIVILWLGAGLVIDNQMTIGMFVAFSSFRGQFSERVASLTSFLLQLRIMSLHNERIADIALHEKEEKKPEIEIVADMGPISLETNGLSYRYDSQSAPIFSALSLSVAPGESVAITGASGAGKTTLMKVLCGLFEPDSGRVLINGIDIRQIGINNYHRMIACVMQDDRLFSGSIRENICGFAEEMDEEWMVECARASHIHDVIMNMPMGYETLIGELGEGLSGGQKQRIFIARALYRKPGILFMDEATSALDSESEHFVNVAIKNMNITRVIIAHRETTLRTVDRVISI
|
Involved, in conjunction with CvaA, in the secretion of colicin V.
|
P22520
|
Q6BV91
|
PRP45_DEBHA
|
Pre-mRNA-processing protein 45
|
Debaryomyces
|
MFSSLLPKPKYSSHEPTSRIKLKKVRAHEKSNQLVKLPENKSDIKVTHNPSNSESTISQLHLNPDGTLNYNLTIASSNSNSRKVQSSYEDTIPLKVKFPNLKHHFPRYTVETCPDDSLKECVEDTKAAINKMINEKMGVDEKTNNKKDDVTYIKYTSNNLVNDPEGSDDERGRERIIQIRNYQEDPMLPPKFKLRKNRHKNPSPPPPLLKSSNNEQTSKLTKEDQAKWQIPSAISNWKNNQGFTISLDKRMVAANGGSELATNDVNLEKFGELSQALENADKQAREEIKIRSEMLKQLAIKEQHEKENKLKELADIARSKKLNNKRPPNGDYDDVKKKTKY
|
Involved in pre-mRNA splicing.
|
Q6BV91
|
Q8D3Z2
|
DEOD2_VIBVU
|
Purine nucleoside phosphorylase DeoD-type 2
|
Vibrio
|
MATPHINAQPGDFAETVLMPGDPLRAKYIAETFLEDVKQVCDVRNMFGFTGTYKGKKVSVMGHGMGIPSACIYVHELIAEYGVKNVIRVGSCGAVRDDVNLMDVVIGMGASTDSKVNRIRFNDHDFAALADYGLLEEAVKQARAQNVPVKVGNVFSADLFYTPEADIFEKMEKLGILGVDMEAAGIYGVAADLKAKALTILTVSDHIIRGEKLSSEDRQKSFNDMMKVALETAINL
|
Catalyzes the reversible phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
|
Q8D3Z2
|
C8WLM1
|
CGR2_EGGLE
|
Cardiac glycoside reductase operon protein 2
|
Eggerthella
|
MEYGKCRGIERGMGRRDFLKAATLLGATAAGAGMLAGCAPKSASEAQAQTAPAATGGLDPADVDWKYETDVVIVGSGSGGTCAAIEAAEAGADVVVFEKDKAMYGGNSALCGGYMLAAGWSTQEEITGYAGDTGEAFANQMLRWSQGLGNQDMIREACLRSGEAVDWMMDTGRTYEGASPLPPVWSCGDTEADVVPRSVYNHNAYGATEGHMATLKKRAESLSNIEIEMGCEVAHILKNAEGSVIGVQLADGSFAKARKGVVMACASVDNNLEMSKDLGLMQNVWGLTLEGAGLLAPGNPDMDSNTGDGVRMLREIGAELCMQQAVCMNDSIYVGGISDWGMSEILGKDVNIHDSSNIDAILVDKTGRRFCQDDAEWGYVMHECAQAAWKQGFTPDDPTTGYIFYVYDATGAPFFEMKGHTPDTCDTTFSADSVDGLAEFIGCDPTALASEVERWNSFCEAGLDADFGRRANMAPIATPPFYCDVVRPGPMGTFAGAKSNVEAEIIGLDGNPIPRLYGAGCIIGGNVSGAFYFGCGWSITNTVVWGREAGRNVAALEPWE
|
Involved in the inactivation of the cardiac medication and plant natural product digoxin, thus decreasing drug efficacy and toxicity. Catalyzes the reduction of the alpha,beta-unsaturated butyrolactone ring of digoxin to the inactive metabolite dihydrodigoxin. Likely uses the cytochrome Cgr1 as the physiological electron donor, encoded by the adjacent gene in the locus. Only reduces digoxin and other cardenolide toxins, such as digitoxin, digoxigenin, ouabain and ouabagenin. Therefore is a specialized enzyme present in some gut bacteria E.lenta that protects their human host against ingested plant toxins.
|
C8WLM1
|
Q30QB8
|
SURE_SULDN
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Sulfurimonas
|
MRYKILVTNDDGYEAKGLRALVKALKELEDVEVMVVAPASEKSACGHSLTLVRPLRFVGVDDNFFKLDDGTPSDCVYLALSTIYVDSKPDLLISGINRGSNMGEDITYSGTAAGAMEGVLHDVPSIAISQVMDFSDPQGDFTLAQKVIKELVIKIKNGSFPLPQREFLNVNIPPDLDSTDNRDAKMVVTYAGYRFYANDSHIHRNPRGEEFYWLGLHPLDFLPREGIKGISDYEAIEAGNISITPIQLDMSAYKSMNKLKEWIE
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q30QB8
|
C1CVN9
|
EFTS_DEIDV
|
Elongation factor Ts
|
Deinococcus
|
MMESIKKLRELTGAGMMDVKKALSDAGNDEDKAVALLRERGIVKAAKKADREAKEGIVRFVVEGNRAAIVEVNSETDFVARNSDFQALVEKLAQTALSAKTNDVEEFRNFSMDGETVGTVVAAAAGKIGENLVLNRVAYIEGDKVAGYVHSNGKIGVLVDVAGGDETKAKDVALHVAAERPQYLSRDEVNQDDIEKEREILTNKALNEGKPQQIVEKIVSGQIGKFYEEKVLPEQRYVKDNSMTVGQYLGDASVKRFVRFEIGA
|
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.
|
C1CVN9
|
Q5GYM5
|
LEXA2_XANOR
|
LexA repressor 2
|
Xanthomonas
|
MDLTDTQQAILALIAERIDADGVPPSQTEIARAFGFKGVRAAQYHLEALEQAGAIRRVPGQARGIRLAGQGGQTRAAAVSEPVRDDVLRLPVLGRVAAGLPIGADIGSDDFVVLDRVFFSPSPDYLLKVQGDSMRDEGIFNGDLIGVHRTRDARSGQIVVARIDEEITVKLLKIGKDRIRLLPRNPDYAPIEVLPDQDFAIEGLYCGLLRPNR
|
Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
|
Q5GYM5
|
Q2ST42
|
UPP_MYCCT
|
UPRTase
|
Mycoplasma
|
MAFTEIKHPLIIDKLTRMRKTETSSKDFRENLSEIAQLMVYEIFRDLKLESVDIETPVSKTTGYTINQPVVLVPILRAGIGMLDGIQKLIPTARIAHIGLYRDEETLETHQYFAKTTKDIDKSYVIVVDPMLATGGSACKAIDIVKQWGAKEIKFVCLVAVEPGIKRLQEQHPDVEIYAASKDEKLNEKGYIVPGLGDAGDRIFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q2ST42
|
P18863
|
HXB8_RAT
|
Homeobox protein R1A
|
Rattus
|
VLSPIPSSRRTQRGRQTYSRYQTLELEKEFLFNPYLTRKRRIEVSHALGLTERQVKIWFQNRRMKWKKENNKDKFPSSKCEQEELEKEKLER
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
P18863
|
A6VJ76
|
DPCKG_METM7
|
Dephospho-coenzyme A kinase
|
Methanococcus
|
MYLLTDEVARELKKPFGKVYKELPSIDGKVVSIGDVTTKHLLSNGIIPNLSILDFKTKRNIPVNIPHKFKTIFEVENPQGCISDEAIERIKYLSTIHDRDMALIIKGEEDLLTIPVIKYFPEDTSVIYGQPDEGMVLLKITDELKQKIEKLLKDMEER
|
Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
|
A6VJ76
|
Q6FTG6
|
FYV10_CANGA
|
Protein FYV10
|
Nakaseomyces/Candida clade
|
MAETTSLINEPDVDFHLKLNQHSFNIPYEQLQRNSRYLNRLIEKEIDELNSHYERLNIALGSGNIEGDKKALQELKDIIRSVEIFEKRLQKRVNEEVPILKRLEVRINFFKELENAKQQVADITPLMEWYLKFTNILIGDYLTRHTTSNSSPELGLPGVTFLEQEGIQDLLDTDILLTGNRISTALVDNHDLRPLLDWINDSKSYLKKNGSRLEFEARFQQYIELLKASEYEEAIKCFQDYLLKFVNTNFNELTHASGLLLSINYCKEIMKAKASERSAILTKDDGNPLENEIRAYKYFFHKKPKIVEQQHVKPVDLSYMNLSQNTDFEKYMLLLDDKRWGLLNELFLKDYYSLYGISQNDPLLIYLSLGISTLKTRECLHHRRVAKSSSPLVDKKVEEEVLQNSCPVCDKTFAPIAESLPFAHHTQSQLFDDPIMLPNGNIYEAKRLKRLAKYLVDIKAIELGETEVIDPIDKQIYNEADFITMYPT
|
Involved in the proteasome-dependent degradation of fructose-1,6-bisphosphatase.
|
Q6FTG6
|
Q0C1A1
|
TRPD_HYPNA
|
Anthranilate phosphoribosyltransferase
|
Hyphomonas
|
MSESALNTAIQAIARGLPLEESVLEGAFDTLLSGEAAPEEVGAFLAGLTVRGETANELIAGARIMRRHGRSVSVEGPLLDTCGTGGLPWKSLNTSTASAIVIAAAGGRVAKHGNRSVPPKTGSADVLEALGLQLELSDTAFKSCLEIAGVGFLFARSYHSAMRHVAPIRHKLGIRTIFNLLGPLSNPAGAEYSVLGVYDKQWVTPMAEALKALGTRCAWVVHGLAGIDEISISGPTDVCEVTPASIRHFQITPSDAGLPSHPLSTLEGGAPEENTAAIRDLLDGREGPFRDIVLINAAAGLHVSGMVADLPAGVQRAAQAIDSGAARETLNTLVRTSRESD
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q0C1A1
|
B8J7G5
|
SSRP_ANAD2
|
Small protein B
|
Anaeromyxobacter
|
MKGKAGGKAADAAEKVAASNRRARFDYDVEDTWEAGLVLTGSEVKSLREGNVNLSDAYAMPRGEELWLLNCRIGEYQQAAHFGHAPLRDRKLLMNRAEIDRVRGKVEQRGYTLVPLRIYFKQGWAKVELGLARGRSHEDRRGAIAERESKREMDRALARGRRR
|
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.
|
B8J7G5
|
Q9EPB8
|
V1R54_MOUSE
|
Vomeronasal type-1 receptor A9
|
Mus
|
MNKMNRLSHNTEIRNAIYSGVGIGISGNSFLLLFHIFKYIRGQRSRHIDLPIGLLSLIHLVMLIAMSLVATDIFMPWGRWGDTTCKCVISLYRFCRSLSLCATSLLSILQAVTLNPRNSCLEKFKRKSPHYMLGCLLFLSVFYTFISSPLATYITAKSNLTSPSFTYITTSCSLAPMSYSFHLTVFILLTSRDVIFVGLMLLSSGYMVTFLGRHKKQSQFLHITSFSLKPSAEKRAMRTILCLMSFFVLMYTLDSIVSYIRSIDDGQIFYCVHIFTAHGYATVSPFLILSTEKYIINIFRSTFGRMVTIILLRNR
|
Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
|
Q9EPB8
|
Q8D3J8
|
ATPL_WIGBR
|
Lipid-binding protein
|
Wigglesworthia
|
MNSINADLLYISAAIIMGFASIGAAIGIGILGGKFLEGAARQPDLIPTLRTQFFIVMGLVDAIPMISVGLGLYLIFAAS
|
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.
|
Q8D3J8
|
B8J8F0
|
MURB_ANAD2
|
UDP-N-acetylmuramate dehydrogenase
|
Anaeromyxobacter
|
MTWRDEIARRVRGEHLRDAPLAPRTAVRVGGPADLLCRPADGDALSALLRAVRELGVPLSVLGGGANTLVADAGVRGVVLRLPQEFPGESTDGDTLVLSAGAPISRLPARAHAHGLVGMEFLGGIPGTLGGAAAMNAGTRLGEMKDVVTRLELATPDGTGFVPASALGYAYRTCRLPPGAVIARVEVRLHPGDVAASEALMREDRERRRATQPLYRPTFGSTFTNPPGEYAGRLVEAVGLKGHRVGNAIWSPVHANFVTNLGGATARDVLALVRLARARVQERFGIALETEVRLLGEFLEEDLEGLDGHAAAGGGPGAASGGVRPPEAT
|
Cell wall formation.
|
B8J8F0
|
Q56336
|
CFPA_TREPA
|
Cytoplasmic filament protein A
|
Treponema
|
MASLDLPKSPNVFHPEKPSAVGSRNSLAQDCRDQQQEVNQLIEEETNKILHHLNTKLPKEVLERLDVMGGLKEKLYNYFNQNYQNMFNRYMVTAEDEMLKKVRGFIDREEMKVLNRYTPKEIAILLDEVAGADKFNTGEIEKSMVNMYGHLQGHIQRGVNELETHTNSLLRQKVDVGAFVRGENAYAVVKCAFKDNLARPKTVTDVKLSINILDSELVSPIFHYQTTVAYLIKDLISNHYIDAIDKEIDRVKDELIDQGKEEMSDSSIIFEKMKMVSDFTDDDCENPDSKRYELISRELMERISNLRAEIDPETFDQLNVRENIKKIVDLENIRNRGFNTAINSITSILDTSRMGYQYIENFKNARELILREYDDTDISNLPDERYQLRLKYLDNAQLIEERKGYEVMLRSFETEVDHLWDVLRTKYDKSKASRFMAKITDFDDLAKVYKKHIKKHYKDKTGEPVYEDIAKVWDEIAFVKPAETEVERMNRTFVYEKDKMRRKLILMRGKLKGMYDYQYPIERRVMEERLAFLESEFNRFDYLVNPFHLQPGLLLDIDITSIKRKKATLDGMANVLNEFLHGISKGFADAAFASFSRRRSTVRADIGQSFASDGSADQKESSGRVAFMDMVNETPALESSVAAEQVDVRSDVGMKTRKAGAVDAGKGRRGRRSAIREL
|
Component of the cytoplasmic filaments that run the length of the organism just underneath the cytoplasmic membrane.
|
Q56336
|
Q9US60
|
KLP3_SCHPO
|
Kinesin-related protein 1
|
Schizosaccharomyces
|
MTSIKVVCRIRPTNQLEQDLGGNNVIYPLNDSTVHIETSDYSGNFVFDRVFHPSSTQNDIFSYSIESTVDDLFLGYNGTVLAYGQTGSGKTYTMMGIENNFEKEGMTPRMLRRIFDKIRDSPSTTEYEVKVSYMEIYMEKIHDLLSEKNDRLTVHEDKLQGVYVQGLKTIYVSSETEALDILNKGMGSRAVASTSMNAQSSRSHSIFVLEVVQTDTESGETRRGRLFLVDLAGSESVGKSGAVGQTLEEAKKINRSLSTLGMVINSLTDSKLSHVPYRDSKLTRILKESLGGNSRTTLIINCSPDSYNATETLSTLRFGHRAKSIKNKAVVNSELSVDEMKRQLYIYKDALSRCVCGARINNNLDYNNCHSNVWSGEHSLTLSNLAEKSNLKEAEIIQGNRTIQESNNDRDESTVASIHRHNFDSDSINRLYAEAQLELKQRDGVLSSTKQQLSDLMTALGDAQERYVELVKNHRVNSNLTANNSLNDKPGFTIEQKDKNFSINNERNNFLQKLSTLDSSLAALVNVQRKLIKALISKERPQNGTVIKKIQGGT
|
Cytoplasmic motor that could play a role in Golgi membrane recycling.
|
Q9US60
|
Q9RME2
|
SERC_ALKAL
|
Phosphohydroxythreonine aminotransferase
|
Alkalihalobacillus
|
MVKQVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQAQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSWSEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNTIYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSGVTVVIVKKDLLNTKVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLDWIKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFNLRNEELNQQFLAKAKEQGFVGLNGHRSVGGCRASIYNAVPIDACIALRELMIQFKENA
|
Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
|
Q9RME2
|
P56831
|
IFNT3_BOVIN
|
Trophoblastin
|
Bos
|
CYLSEDHMLGARENLRLLARMNRLSPHPCLQDRKDFGLPQEMVEGSQLQKDQAISVLHEMLQQCFNLFHIEHSSAAWNTTLLEQLCTGLQQQLEDLDACLGPVMGEKDSDMGRMGPILTVKKYFQDIHVYLKEKEYSDCAWEIIRVEMMRALSSSTTLQKRLRKMGGDLNSL
|
Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the suppression of the pulsatile endometrial release of the luteolytic hormone prostaglandin F2-alpha, hindering the regression of the corpus luteum (luteolysis) and therefore a return to ovarian cyclicity. This, and a possible direct effect of IFN-tau on prostaglandin synthesis, leads in turn to continued ovarian progesterone secretion, which stimulates the secretion by the endometrium of the nutrients required for the growth of the conceptus. In summary, displays particularly high antiviral and antiproliferative potency concurrently with particular weak cytotoxicity, high antiluteolytic activity and immunomodulatory properties. In contrast with other IFNs, IFN-tau is not virally inducible.
|
P56831
|
P59198
|
LPXM1_SHIFL
|
Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase 1
|
Shigella
|
METKKNNSEYIPEFDKSFRHPRYWGAWLGVAAMAGIALTPPKFRDPILARLGRFAGRLGKSSRRRALINLSLCFPERSEAEREAIVDEMFATAPQAMAMMAELAIRGPEKIQPRVGWQGLEIIEEMRRNNEKVIFLVPHGWAVDIPAMLMASQGQKMAAMFHNQGNPVFDYVWNTVRRRFGGRLHARNDGIKPFIQSVRQGYWGYYLPDQDHGPEHSEFVDFFATYKATLPAIGRLMKVCRARVVPLFPIYDGKTHRLTIQVRPPMDDLLEADDHTIERRMNEEVEIFVGPRPEQYTWILKLLKTRKPGEIQPYKRKDLYPIK
|
Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A.
|
P59198
|
Q14558
|
KPRA_HUMAN
|
39 kDa phosphoribosypyrophosphate synthase-associated protein
|
Homo
|
MNAARTGYRVFSANSTAACTELAKRITERLGAELGKSVVYQETNGETRVEIKESVRGQDIFIIQTIPRDVNTAVMELLIMAYALKTACARNIIGVIPYFPYSKQSKMRKRGSIVCKLLASMLAKAGLTHIITMDLHQKEIQGFFSFPVDNLRASPFLLQYIQEEIPNYRNAVIVAKSPDAAKRAQSYAERLRLGLAVIHGEAQCTELDMDDGRHSPPMVKNATVHPGLELPLMMAKEKPPITVVGDVGGRIAIIVDDIIDDVESFVAAAEILKERGAYKIYVMATHGILSAEAPRLIEESSVDEVVVTNTVPHEVQKLQCPKIKTVDISLILSEAIRRIHNGESMAYLFRNITVDD
|
Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.
|
Q14558
|
O02100
|
HOP1_CAEEL
|
Presenilin hop-1
|
Caenorhabditis
|
MPRTKRVYSGKTITGVLYPVAICMLFVAINVKLSQPEQQEQSKVVYGLFHSYDTADSGTITLYLIGFLILTTSLGVFCYQMKFYKAIKVYVLANSIGILLVYSVFHFQRIAEAQSIPVSVPTFFFLILQFGGLGITCLHWKSHRRLHQFYLIMLAGLTAIFILNILPDWTVWMALTAISFWDIVAVLTPCGPLKMLVETANRRGDDKFPAILYNSSSYVNEVDSPDTTRSNSTPLTEFNNSSSSRLLESDSLLRPPVIPRQIREVREVEGTIRLGMGDFVFYSLMLGNTVQTCPLPTVVACFVSNLVGLTITLPIVTLSQTALPALPFPLAIAAIFYFSSHIALTPFTDLCTSQLILI
|
Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function.
|
O02100
|
Q6CMV8
|
H2B2_KLULA
|
Histone H2B.2
|
Kluyveromyces
|
MAPKAEKKPASKAPAEKKPAAKKTSSSVDPSKKRTKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATESSKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
|
Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Q6CMV8
|
Q2INL1
|
CHEB2_ANADE
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 2
|
Anaeromyxobacter
|
MSLAGGDRPIRVLVADDSELFRELLARVVAAEPGFEVAAVAADGDAAAAMARALRPDVVTMDLHMPDADGYSGIARIMAETPTPILVLTANPTEAAGFRALSLGALDILEKPSATADLGEYGRLIRSRLRLLAGVKVIRHLRGLRERRDAAPARAARVEVVVIGASLGGPRALAAVLRGLPPDFPAPIAVVQHIADGFTAGLAGWLAQESRLDVREARHGDPLRAGRVLIAPSGRHLVLGEGVARLSDAPPVDTFRPSVTPLFTSAARQYGRRCCGVLLTGMGRDGAEGLRVIKDAGGPTLAQDEATSAVFGMARAAVELGAVDRVLPVDEIPRALRELTR
|
Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid.
|
Q2INL1
|
B9DZF9
|
HEM1_CLOK1
|
Glutamyl-tRNA reductase
|
Clostridium
|
MIQLIGIKSQCDIGIRQKFSITSEVLEGKLKYINELVGSVLILSTCNRTEIYVDSNLEEKKLIDTVFYGLDWDYDLVSYIFYIKDKYAIKHLMEVSCGFHSKILGEDQILGQIKTAYDAALEAKTIKGKLQRLFQKAITCGKEFKHICESYRIPVSIPSIVAKEILNMDIRKYMIIGFGKIGQLLFKYLNNSQAQIIYIAVRDLNKVHDSYKKCGKIRFISFKDRKSYYNDIDCIVSCTSAPDKIISKGDLPCRKLTIFDLAVPEDIDRNVLDLDNVTLYDIDNISVIDEKNKAIRKKTMGKYRYILENHIDKFIKWEKLHQLSPEIQKVKKYGDEICEKRITTFKNKKHTKDNDILVKTMIESTARFYINRAIEVMKEEKLNGREEECLRLINKIFCK
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
B9DZF9
|
A0T0U9
|
PSBI_THAPS
|
PSII 4.8 kDa protein
|
Thalassiosira
|
MLTLKILVYTTVIFFVSLFIFGFLSSDPSRNPNRRDLE
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
A0T0U9
|
O94992
|
HEXI1_HUMAN
|
Menage a quatre protein 1
|
Homo
|
MAEPFLSEYQHQPQTSNCTGAAAVQEELNPERPPGAEERVPEEDSRWQSRAFPQLGGRPGPEGEGSLESQPPPLQTQACPESSCLREGEKGQNGDDSSAGGDFPPPAEVEPTPEAELLAQPCHDSEASKLGAPAAGGEEEWGQQQRQLGKKKHRRRPSKKKRHWKPYYKLTWEEKKKFDEKQSLRASRIRAEMFAKGQPVAPYNTTQFLMDDHDQEEPDLKTGLYSKRAAAKSDDTSDDDFMEEGGEEDGGSDGMGGDGSEFLQRDFSETYERYHTESLQNMSKQELIKEYLELEKCLSRMEDENNRLRLESKRLGGDDARVRELELELDRLRAENLQLLTENELHRQQERAPLSKFGD
|
Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor . Core component of the 7SK RNP complex: in cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation . May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity . Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway .
|
O94992
|
Q1QP34
|
NUOD1_NITHX
|
NDH-1 subunit D 1
|
Nitrobacter
|
MVEAAPRNFTINFGPQHPAAHGVLRLVLELDGEVVRRVDPHIGLLHRGTEKLIEHKTYLQALPYFDRLDYVAPMNQEHAFCLATEKLLNITIPKRGQLIRVLYCEIGRLLSHLLNVTTQAMDVGALTPPLWGFEEREKLMVFYERASGARMHANYFRVGGVHQDLPSKLLDDIWDFCDPFLKVCDDLEGLLTENRIFKQRNVGIAEVKLADAWGWGFSGVMVRGSGAAWDLRKAQPYECYSELDFDIPIGKHGDCYDRYLVRMEEMRQSVRIMKQCLEKLRLPEGQGPVATRDHKIVPPSRAEMKRSMEAMIEHFKLYTEGHRVPAGEVYVAVEAPKGEFGVYLVSDGTNQPYKCKIRAPSFAHLSAMDFLTRGHMLADVSAIIGSLDIVFGEIDR
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
Q1QP34
|
Q1GHU0
|
RL9_RUEST
|
50S ribosomal protein L9
|
unclassified Ruegeria
|
MQVILLERVAKLGQMGDVVDVKPGFARNYLLPQGKAQTASDANIAAFEAQKAQLEARNLETKKEAEALGEKLGGQQFVVIRSASDGGNLYGSVTTRDAADVATEEGFSVDRKQVIIREPIKTLGLHIAEVHLHPEVMVTIELNVARSPEEAELQASGKSIQELAAEEEAAAEFEISELFDDIGGAASDDEGDAPAAAADEEESK
|
Binds to the 23S rRNA.
|
Q1GHU0
|
Q1I5F9
|
AMPA_PSEE4
|
Leucyl aminopeptidase
|
Pseudomonas
|
MELVVKSVAAVSVKTATLVVPVGEGRKLGATAKAVDLASEGAISAVLKRGDLAGKPGQTLLLHSVPGLKAERVLLVGSGKDEALGDRAWRKLAASVAGVLKGLGGSDAVLALDDIAVTGRDGHYGKYRLLAETLLDSDYVFDRYKSQKAEPRALKKITLLADKAGLAEAERAVKHASAIATGMAFTRDLGNLPPNVCHPSFLAEQAKGLGKAHKGLKVEVLDEKKIKELGMGAFYAVGQGSDQPPRLIVLNYQGGKKSEKPFVLVGKGITFDTGGISLKPGAGMDEMKYDMCGAASVFGTLRAVLELQLPINLVCLLACAENMPSGGATRPGDIVTTMSGQTVEILNTDAEGRLVLCDTLTYAERFKPQAVIDIATLTGACIVALGSHTSGLMGNNDELVGQLLDAGKRADDRAWQLPLFDEYQEQLDSPFADIANIGGPKAGTITAGCFLSRFAKAYNWAHLDIAGTAWISGGKDKGASGRPVPLLTQYLLDRAGA
|
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides.
|
Q1I5F9
|
B4U8T1
|
RSMH_HYDS0
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
unclassified Hydrogenobaculum
|
MHKSVLLKEVTDFLSNPCPKIHIDATLGLGGHAKALLEVCKDTFLIGIDKDENAIEIAKEKLKGFNAVFYHGSFKDFDIVLKEEGLLYFDSILFDFGVSSLQLDEEEGFSFQREDFLDMRMDKRQQKTAYIVINTYKEKELADIFYKYGEERLSKKIARSIVEKRKKKPIETTKELVDIVSSCYPYKYSKINPATKVFQALRIEVNSELEDIKIALSKLLDFAKEGSKFAFISFHSLEDRLVKEFIKNNADKLKVCSKKPITPSDEELLYNKRARSAKLRCAKLCYNEKKDEAFDS
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
B4U8T1
|
Q1H4L2
|
RPOA_METFK
|
Transcriptase subunit alpha
|
Methylobacillus
|
MQNSPTEYLKPRVVDVDVISPVRARVTLEPMERGFGYTLGNALRRVLLSSIPGFAITEVKIDGVVHEYSTLDGVQEDVVDILLNLKGVALKLNSKNEATLTLNKSTEGVVTAGDFDTGHDAEIANPDHVIAHLTKGGKLNLEVKVEMGRGYQPVPQRRKTEDEDRVLGFIQVDASFSPISKVSYQVESARVEQRTDLDKLIMDVETNGIIEPEQAIRDAARILMGQLSVFADLEGAPSEVEVKQAPQVDPILLRPVDDLELTVRSANCLKAENIYYIGDLIQRTENELLKAPNLGRKSLNEIKDVLASKGLTLGMKLENWPPAGLEKV
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q1H4L2
|
Q9PCG4
|
FABH_XYLFA
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
Xylella
|
MSKRIYARIAGTGGYLPEKVLTNDDLAHIVDTSDEWIRTRTGIRERHIAAEGETTSDLAYEAAICALEAAEVRSADLDLIVVGTTTPDLIFPSTACLLQARLGAVGCGAFDVNAACSGFVYALSVAEKFVSSGCSKTVLVVGADTLTRIIDWSDRTTCVLFGDGAGAVVLKADEDTGILSTHLHADGSKKELLWDPVGVSVGFGEGKDCGALLMKGNEVFKYAVKALDRVVDETLEANHLDKHELDWLIPHQANLRIIEATARRLDMSMDQVVVTVDRHGNTSTASVPLALDEAIRSGRVQRGQLLLLEAFGGGFTWGSALLRY
|
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
|
Q9PCG4
|
Q1Q8V3
|
NHAA_PSYCK
|
Sodium/proton antiporter NhaA
|
Psychrobacter
|
MAIHKIRAFFNLEASGGIVLALAAIAAMIIANTSLNTWYESFIHAPVAIQIGSFSIAKDAHHWINDGLMAVFFFLVGLELKREVLIGELSNVKQIILPAGAALGGMIMPAIVYLFFNYNEPEFWRGWAIPAATDIAFALGILSLLGNRVPNSLKVFLVSIAIFDDIGAIIIIALFYTNDLSLGSLAIAGLCLPFLYLLNRRNVTSITPYLLIGVIMWVAVLKSGIHATLAGVVLALFIPLFDRTDPEHSPLEELEHDLQNTVSYGILPLFAFANAGISLKGAGFGELFHSVPLGIAAGLFIGKQVGVMLMCWLIFKLGISTMPKGMNFKQIYGAALLCGVGFTMSLFIGGLAFAGETPLFDERLGIIMGSIVSGIAGYMMLKATLKDEVNVTSVDLTRHS
|
Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
|
Q1Q8V3
|
A6Q9N6
|
ANMK_SULNB
|
AnhMurNAc kinase
|
unclassified Sulfurovum
|
MNKERYIGIMSGTSLDGVDVVLCEIDKKSCLLKASVEYPFPDDLKKEILSMINGKCTLAQVGSVDVRLGILFSDAVNALLEIEKIDPKSIKAIGSHGQTLWHEPVGKYPFSMQLGDPSAIAVRTGIKVVADFRQKDMALGGQGAPFAPAFHAFLFGGTDASVSILNIGGMANITVLGKTLLGYDTGPGNVLMDMWVAEHKDVTYDRNGEWARSGEVIYPLLEAMLEDPYFSQPHPKSTGREKFNEAWLQKHLNAQHSTLNAHDVQRTLLELTAVSISNEVLKFNQDILLLCGGGAKNAFLVERLGTLMPNIQIGIANDADNIEAMTFAWLAYKRLHNEHVDLKDVTGARQNAILGGVYV
|
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
|
A6Q9N6
|
Q53EZ4
|
CEP55_HUMAN
|
Up-regulated in colon cancer 6
|
Homo
|
MSSRSTKDLIKSKWGSKPSNSKSETTLEKLKGEIAHLKTSVDEITSGKGKLTDKERHRLLEKIRVLEAEKEKNAYQLTEKDKEIQRLRDQLKARYSTTTLLEQLEETTREGERREQVLKALSEEKDVLKQQLSAATSRIAELESKTNTLRLSQTVAPNCFNSSINNIHEMEIQLKDALEKNQQWLVYDQQREVYVKGLLAKIFELEKKTETAAHSLPQQTKKPESEGYLQEEKQKCYNDLLASAKKDLEVERQTITQLSFELSEFRRKYEETQKEVHNLNQLLYSQRRADVQHLEDDRHKTEKIQKLREENDIARGKLEEEKKRSEELLSQVQFLYTSLLKQQEEQTRVALLEQQMQACTLDFENEKLDRQHVQHQLHVILKELRKARNQITQLESLKQLHEFAITEPLVTFQGETENREKVAASPKSPTAALNESLVECPKCNIQYPATEHRDLLVHVEYCSK
|
Plays a role in mitotic exit and cytokinesis . Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis . Not required for microtubule nucleation . Plays a role in the development of the brain and kidney .
|
Q53EZ4
|
A5GCW2
|
HEM3_GEOUR
|
Pre-uroporphyrinogen synthase
|
Geotalea
|
MALKTLRIGTRASQLALWQANWVKSELEKRYPGLEVSLLKIKTIGDKILDVPLAQVGGKGLFVKEIEEAMLRGDIDIAVHSMKDVPTEFPEGLGLHCITEREDPRDAVISRGIKFADLPKGAKIGTSALRRQAQLLKIRPDMEMVIIRGNVETRINKLEAENLDAVILAAAGLKRLGFTDKVAEYLPTDLSIPAIGQGALGIECRLDNEEVKSAIDFFNHPATAYAVRAERALLWRCEGGCQVPIAAFGEVEGDQLKLTGFIASVDGKTSVKGSVSGPAEECEKLGITLAEQLLKDGGHEILAEVYQREVSREKEIPV
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A5GCW2
|
A9AIP4
|
GUAA_BURM1
|
Glutamine amidotransferase
|
Burkholderia cepacia complex
|
MHDKILILDFGSQVTQLIARRVREAHVYCEIHPNDVSDEFVREFAPKAVILSGSHASTYEDHQLRAPQAVWDLGVPVLGICYGMQTMAVQLGGKVEWSDHREFGYAEVRAHGHTRLLDGIEDFTTAEGHGMLKVWMSHGDKVAELPPGFKLMASTPSCPIAGMADEARGYYAVQFHPEVTHTVKGRQMLERFVLQIAGAKPDWIMRDHIEEAVAKIREQVGDEEVILGLSGGVDSSVAAALIHRAIGDQLTCVFVDHGLLRLNEGKMVLDMFEGRLHAKVVHIDASEQFLGHLAGVTDPEAKRKIIGREFVEVFQAEAKKLSNAKWLAQGTIYPDVIESGGAKTKKATTIKSHHNVGGLPETLGLKLLEPLRDLFKDEVRELGVALGLPPEMVYRHPFPGPGLGVRILGEVKREYADLLRRADAIFIEELRNTVATAQDAAAGLCGEADVGKSWYDLTSQAFAVFLPVKSVGVMGDGRTYDYVTALRAVQTTDFMTAHWAHLPYSLLGRVSNRIINEVRGINRAVYDISGKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
A9AIP4
|
A9A1K7
|
LYSZ_NITMS
|
Putative [LysW]-aminoadipate/[LysW]-glutamate kinase
|
Nitrosopumilus
|
MITIKIGGSVVDDLHPSTIADIKKIAESEGVILVHGGGKEVTKVCEQLGKEPKFVTSPSGIKSRYTDKETAEIFTMVMSGRINKTIVQMLQKNGINAIGLSGVDAKVIEADRKKKLLIVNEKGRKQAIDGGYTGKIREVNASFIKSLLDQGLTPVISPIAISEESEFLNVDGDRAAAYVAGKVGSDKVLFITNVDGLLMDDKVVPKLTLAEAKEIRPKIGPGMEKKILASTEALDMGVTTALIANGQKENPISSAISHDNCTVIEHE
|
Involved in both the arginine and lysine biosynthetic pathways. Phosphorylates the LysW-bound precursors glutamate (for arginine biosynthesis), respectively alpha-aminoadipate (for lysine biosynthesis).
|
A9A1K7
|
P74618
|
6PGL_SYNY3
|
6-phosphogluconolactonase
|
unclassified Synechocystis
|
MAPQVDVLINKQILIERALVCVTTRITKAIAERGQGTIALSGGNTPKPLYEALARQALPWEKIHVFWGDERYVSVDHPDSNQRMARLAWLDQVDIPEANIHPMPTAAADPEQDAQTYENELATFFQVEAGHFPAFDLILLGLGDDGHTASLFPHTPALTVGDRLITVGNKDGQPRLTFTIPLINRARSVVFLVAGASKQHALGEIFAPEADPQQYPARFIQPQGELIWLLDQQAGENLRP
|
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
|
P74618
|
P25454
|
RAD51_YEAST
|
DNA repair protein RAD51
|
Saccharomyces
|
MSQVQEQHISESQLQYGNGSLMSTVPADLSQSVVDGNGNGSSEDIEATNGSGDGGGLQEQAEAQGEMEDEAYDEAALGSFVPIEKLQVNGITMADVKKLRESGLHTAEAVAYAPRKDLLEIKGISEAKADKLLNEAARLVPMGFVTAADFHMRRSELICLTTGSKNLDTLLGGGVETGSITELFGEFRTGKSQLCHTLAVTCQIPLDIGGGEGKCLYIDTEGTFRPVRLVSIAQRFGLDPDDALNNVAYARAYNADHQLRLLDAAAQMMSESRFSLIVVDSVMALYRTDFSGRGELSARQMHLAKFMRALQRLADQFGVAVVVTNQVVAQVDGGMAFNPDPKKPIGGNIMAHSSTTRLGFKKGKGCQRLCKVVDSPCLPEAECVFAIYEDGVGDPREEDE
|
Required both for recombination and for the repair of DNA damage caused by X-rays. Its function may be modulated by interaction with other repair proteins. RAD52 interacts directly with RAD51, via its C-terminus. Forms a nucleoprotein filament with DNA as an early intermediate in recombination.
|
P25454
|
O31269
|
ISCS_AZOVI
|
Cysteine desulfurase IscS
|
Azotobacter
|
MKLPIYLDYSATTPVDPRVAQKMCECLTMEGNFGNPASRSHVFGWKAEEAVENARRQVAELVNADPREIVWTSGATESDNLAIKGVAHFNASKGKHIITSKIEHKAVLDTTRQLEREGFEVTYLEPGEDGLITPAMVAAALREDTILVSVMHVNNEIGTVNDIAAIGELTRSRGVLYHVDAAQSTGKVAIDLERMKVDLMSFSAHKTYGPKGIGALYVRRKPRVRLEAQMHGGGHERGMRSGTLATHQIVGMGEAFRIAREEMAAESRRIAGLSHRFHEQVSTLEEVYLNGSATARVPHNLNLSFNYVEGESLIMSLRDLAVSSGSACTSASLEPSYVLRALGRNDELAHSSIRFTFGRFTTEEEVDYAARKVCEAVGKLRELSPLWDMYKDGVDLSKIEWQAH
|
Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine via an enzyme-bound persulfide intermediate. Functions as a sulfur delivery protein for Fe-S cluster synthesis. Cluster assembly on IscU homodimers proceeds sequentially from 1 2Fe-2S per dimer, to 2 2Fe-2S per dimer and finally 1 4Fe-4S per dimer.
|
O31269
|
O64503
|
UTR1_ARATH
|
UDP-galactose/UDP-glucose transporter 1
|
Arabidopsis
|
MEVHGSGFRRILLLALCISGIWSAYIYQGVLQETLSTKRFGPDEKRFEHLAFLNLAQSVVCLIWSYIMIKLWSNAGNGGAPWWTYWSAGITNTIGPAMGIEALKYISYPAQVLAKSSKMIPVMLMGTLVYGIRYTFPEYMCTFLVAGGVSIFALLKTSSKTISKLAHPNAPLGYALCSLNLAFDGFTNATQDSIASRYPKTEAWDIMLGMNLWGTIYNMIYMFGLPQGIGFKAIQFCKLHPEAAWDILKYCICGAVGQNFIFMTISNFGSLANTTITTTRKFVSIVVSSVMSGNPLSLKQWGCVSMVFGGLAYQIYLKWKKLQRVEKKKQKS
|
Essential sugar transporter required for the transport of UDP-galactose and UDP-glucose from the cytoplasm into the Golgi and the endoplasmic reticulum, to ensure quality control of protein folding. Essential for pollen development and involved in embryo sac progress.
|
O64503
|
D3ZQE1
|
CEA16_RAT
|
Carcinoembryonic antigen-related cell adhesion molecule 16
|
Rattus
|
MKMPLTWGSWFLLSAWILNAGAEISITPEPAQPAEGDNVTLVVHGLSGELLAYNWYAGPSISLTFLVASYIVSTGDETPGPAHTGREAVRPDGSLDIHGALPGHTGTYILQTLNRQFQTEVGYGHMQVYEILAPPTVMANDTALVERRDTLRLICSSPSPAEVRWFFNGDALPVAVRLGLSPDGRMLTRHGVRREEAGAYQCEVWNPVSVSRSEPLNLTVYFGPERVAILQDSTTRTGCTIKVDFNTSLTLWCVSRSCPEPEYVWAFNGKALKNGQDHLNISSMSADHEGTYTCIAKNSKTLLSGSASVVVKLSAAAVAMMIVPVPTKPMEGQDVTLTVQGYPKDLLVYAWYRGPASEPNRLLSQLPSGNWIAGPAHTGREVGFANCSLLVQKLNLTDAGRYTLKTVTLQGKTDTLEVELQVA
|
Required for proper hearing, plays a role in maintaining the integrity of the tectorial membrane.
|
D3ZQE1
|
Q3B327
|
CHED_CHLL3
|
Probable chemoreceptor glutamine deamidase CheD
|
Pelodictyon
|
MKKTAKTDTEDAFKFRSTFGEHYYDGYGARHETPHIVAYTGEVTAAGPGRVLISSPLGSCIAVCAYDPGTRVGGLAHVMLPGVPPAHAETGKDRYAAHALETLFSVMQNEGADPGNLLICLIGGANVLRREHDTIHIDNLRSLTSLILQRNLPICRTMTGGSERMMARMETKTGRIFQTTGNNPEEMLFDYFTHNIENPDN
|
Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
|
Q3B327
|
Q4R5L2
|
ENOA_MACFA
|
Non-neural enolase
|
Macaca
|
MSILKVHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVANPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKAKFAGRNFRNPLAK
|
Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
|
Q4R5L2
|
A5D2S0
|
IF2_PELTS
|
Translation initiation factor IF-2
|
Pelotomaculum
|
MVKKRVHELAKELKIESKEIINRLNQMGINVKSHMSTLEDGVVERLHQLYRPDQEEVKPAAAKPPAAGQTIKPEEVAPQAQPESRKKDAAMLDSQKPDRDRVQKNGRERAGKATRADHYKGAGLVERVPSRPPDRRFQERPKQSDKARPWGQPRADQGARLKTADFVQERTRSARAGQDYSQPEKVQQERVQDRQQKERPPFEKAQQPRPQHEHKPQDSVKERPHPERASREADNAKRAERLDKGAGKTAEIAYKSGLKALEKAQVGTKPQRAGERGARPGGLHETKPKKNLAPGDAGYAKLWQEQTPVIPQKLLDDRRRQTEEKVKVTEKQKQQAKSQKLVKSREKRNAMAELAEERLRPRPAVAGSRKKGAAKPQEQAQKPAQPLEKKPIVLGESTTVQELALKMHKSPAELIKKLMQLGVMATINQEIDTDTATILAGEFGYEVEVKLPVDIEAMLMQEPEDDPVSLQDRPCVVTVMGHVDHGKTSLLDAIRETNVTATEAGGITQHIGAYQVEHNGKKITFLDTPGHEAFTAMRARGARVTDIAILVVAADDGVMPQTVEAINHAKEAKVPIIVAINKIDKPGANPDRVKQQLTEHGLVAEEWGGDTICVNVSALKKEGLKDLLEMILLVAEMSELKANPNRPARGTVIEAELDKGRGPVANVLVQNGTLNVGDTLIAGAAFGRVRAMMDDKGRRIKKAGPSTPVEVLGFSEVPQAGDIFVVVEDEKLARTIVARRQARKREEELKSTARVSLADLFKHIQEGQIKELGIIIKADVQGSVEALRQALERLSTDEVRVNIIHGGVGAITETDVMLASASNAIIIGFNVRPDVNARKAAENEKVDVRLYRVIYDAIEDVKAAMSGLLEPEYREVTLGRAEIRKIFRSSKIGNIAGCYVLEGKIERDASVRVIRDGIVVHEGKLESLKRFKDDVREVVQGYECGIALEKFNEIQEGDIIEAFTVEAIKRQLT
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A5D2S0
|
P02710
|
ACHA_TETCF
|
Acetylcholine receptor subunit alpha
|
Tetronarce
|
MILCSYWHVGLVLLLFSCCGLVLGSEHETRLVANLLENYNKVIRPVEHHTHFVDITVGLQLIQLISVDEVNQIVETNVRLRQQWIDVRLRWNPADYGGIKKIRLPSDDVWLPDLVLYNNADGDFAIVHMTKLLLDYTGKIMWTPPAIFKSYCEIIVTHFPFDQQNCTMKLGIWTYDGTKVSISPESDRPDLSTFMESGEWVMKDYRGWKHWVYYTCCPDTPYLDITYHFIMQRIPLYFVVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMIFVISSIIITVVVINTHHRSPSTHTMPQWVRKIFIDTIPNVMFFSTMKRASKEKQENKIFADDIDISDISGKQVTGEVIFQTPLIKNPDVKSAIEGVKYIAEHMKSDEESSNAAEEWKYVAMVIDHILLCVFMLICIIGTVSVFAGRLIELSQEG
|
Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
P02710
|
Q9ZW24
|
GSTU7_ARATH
|
Glutathione S-transferase 25
|
Arabidopsis
|
MAERSNSEEVKLLGMWASPFSRRIEIALTLKGVSYEFLEQDITNKSSLLLQLNPVHKMIPVLVHNGKPISESLVILEYIDETWRDNPILPQDPYERTMARFWSKFVDEQIYVTAMKVVGKTGKERDAVVEATRDLLMFLEKELVGKDFLGGKSLGFVDIVATLVAFWLMRTEEIVGVKVVPVEKFPEIHRWVKNLLGNDVIKKCIPPEDEHLKYIRARMEKLNIKSA
|
May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
|
Q9ZW24
|
P08566
|
ARO1_YEAST
|
Shikimate dehydrogenase
|
Saccharomyces
|
MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQVARLSKILVAYGLPVSPDEKWFKELTLHKKTPLDILLKKMSIDKKNEGSKKKVVILESIGKCYGDSAQFVSDEDLRFILTDETLVYPFKDIPADQQKVVIPPGSKSISNRALILAALGEGQCKIKNLLHSDDTKHMLTAVHELKGATISWEDNGETVVVEGHGGSTLSACADPLYLGNAGTASRFLTSLAALVNSTSSQKYIVLTGNARMQQRPIAPLVDSLRANGTKIEYLNNEGSLPIKVYTDSVFKGGRIELAATVSSQYVSSILMCAPYAEEPVTLALVGGKPISKLYVDMTIKMMEKFGINVETSTTEPYTYYIPKGHYINPSEYVIESDASSATYPLAFAAMTGTTVTVPNIGFESLQGDARFARDVLKPMGCKITQTATSTTVSGPPVGTLKPLKHVDMEPMTDAFLTACVVAAISHDSDPNSANTTTIEGIANQRVKECNRILAMATELAKFGVKTTELPDGIQVHGLNSIKDLKVPSDSSGPVGVCTYDDHRVAMSFSLLAGMVNSQNERDEVANPVRILERHCTGKTWPGWWDVLHSELGAKLDGAEPLECTSKKNSKKSVVIIGMRAAGKTTISKWCASALGYKLVDLDELFEQQHNNQSVKQFVVENGWEKFREEETRIFKEVIQNYGDDGYVFSTGGGIVESAESRKALKDFASSGGYVLHLHRDIEETIVFLQSDPSRPAYVEEIREVWNRREGWYKECSNFSFFAPHCSAEAEFQALRRSFSKYIATITGVREIEIPSGRSAFVCLTFDDLTEQTENLTPICYGCEAVEVRVDHLANYSADFVSKQLSILRKATDSIPIIFTVRTMKQGGNFPDEEFKTLRELYDIALKNGVEFLDLELTLPTDIQYEVINKRGNTKIIGSHHDFQGLYSWDDAEWENRFNQALTLDVDVVKFVGTAVNFEDNLRLEHFRDTHKNKPLIAVNMTSKGSISRVLNNVLTPVTSDLLPNSAAPGQLTVAQINKMYTSMGGIEPKELFVVGKPIGHSRSPILHNTGYEILGLPHKFDKFETESAQLVKEKLLDGNKNFGGAAVTIPLKLDIMQYMDELTDAAKVIGAVNTVIPLGNKKFKGDNTDWLGIRNALINNGVPEYVGHTAGLVIGAGGTSRAALYALHSLGCKKIFIINRTTSKLKPLIESLPSEFNIIGIESTKSIEEIKEHVGVAVSCVPADKPLDDELLSKLERFLVKGAHAAFVPTLLEAAYKPSVTPVMTISQDKYQWHVVPGSQMLVHQGVAQFEKWTGFKGPFKAIFDAVTKE
|
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
|
P08566
|
Q47R66
|
RS4_THEFY
|
30S ribosomal protein S4
|
Thermobifida
|
MRYTGPKVRLSRRAGVPLTRKAVKYFEKRPYPPGEHGRRVRRSTSDYAVRQAEKQKLRWYYDLSEKQLARVYENAKKRPGRTGEEMIAELELRLATVLLRAGFAASIYAARQFINHGHITVDGKKVDIPSYQVKPGQIVSVREKSRKLVPFIEAAEGVHADEKIASYLAVSHKDLTIAVVDRPKREQVPVPFDEQLVVEYYAR
|
With S5 and S12 plays an important role in translational accuracy.
|
Q47R66
|
Q6BSQ1
|
HAT1_DEBHA
|
Histone acetyltransferase type B catalytic subunit
|
Debaryomyces
|
MSDNSPITSITAASLQPELWTSSSNDALQIYITDSDGTALNFHPNFTYPIFGDSEQIFGYRDLVIFLCFDHCTFYPFLNVKYSDKLNDDTLEDPREKLLSYLPESTIFKDEVKWVDSINKEKEGFEIPGELVGNIFTHGDDKFGIYKLDLKNAQGLELHKRLQILVLLFIEAGSYIDHQDELWDIYVMYKVTDEKTPSIIGFCTAYNYWKYGGFEKFDSNQQEVRKKISQFIVLPMYQGLKLGGRFYNKLYEYWMQDPRVIEVVVEDPSESFDDLRDRCDLTRLCQNTIKVASVDLPLINTEWATKLRQEQKLEKRQFSRLLEMILIYQLEHNLTNITKKQVRLFIKKRLYEKNKEILDGLDEPTRLDKLQTAYASLESDYKRILSGLSLHKRALDSTEGSSKKSKPNV
|
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
|
Q6BSQ1
|
P71059
|
EPSJ_BACSU
|
Uncharacterized glycosyltransferase EpsJ
|
Bacillus
|
MIPLVSIIVPMYNVEPFIEECIDSLLRQTLSDIEIILVNDGTPDRSGEIAEDYAKRDARIRVIHQANGGLSSARNTGIKAARGTYIGFVDGDDYVSSAMFQRLTEEAEQNQLDIVGCGFYKQSSDRRTYVPPQLEANRVLTKPEMTEQLKHAHETRFIWYVWRYLYRRELFERANLLFDEDIRFAEDSPFNLSAFREAERVKMLDEGLYIYRENPNSLTEIPYKPAMDEHLQKQYQAKIAFYNHYGLAGACKEDLNVYICRHQLPMLLANACASPNSPKDIKKKIRQILSYDMVRQAVRHTPFQHEKLLRGERLVLALCKWRLTFLIKLFFEQRGTMKGSAKQA
|
May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles.
|
P71059
|
Subsets and Splits
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