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
|
|---|---|---|---|---|---|---|
Q02326
|
RL6A_YEAST
|
YL16
|
Saccharomyces
|
MSAQKAPKWYPSEDVAALKKTRKAARPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLISGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQNKEIKAERVEDQKVVDKALIAEIKKTPLLKQYLSASFSLKNGDKPHMLKF
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
|
Q02326
|
Q2J542
|
ISPD_FRACC
|
MEP cytidylyltransferase
|
Frankia
|
MGEGHRLPVASPRVAAIVPAAGRGERLGGGTPKALRALGGRPMLVRTVESLRRSRLVTQIVVAAPPTLVDAVAQLLGGDVYVIAGGAERVDSVRRALRAVDDDVSVVLVHDAARPLTPPELVDAVAAAVLDGHPAVIPVVPLADTVKEVDADGRVVRTPPRDGLRAVQTPQGFRRDVLSAAYALEDIAVTDDAGLVEALGVPVTTIPGAQEAFKVTRPADLVLAEALLARCDPADDARSAEARSAEARSEEPQFAGARSTDARSGG
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q2J542
|
P15325
|
QUTD_EMENI
|
Quinate transporter
|
Aspergillus subgen. Nidulantes
|
MSILALVEDRPTPREVYNWRVYLLAAVASFTSCMIGYDSAFIGTTLSLQSFQNEFNWESLNTDLISANIVSLYQAGAFFGALFAYPIGHFWGRRWGLMFSALIFFLGAGMMLGANGDRGLGLIYGGRVLAGIGVGAGSNICPIYISEMAPPAIRGRLVGVYELGWQIGGVVGFWINYGVDETLAPSHKQWIIPFAVQLIPAGLLIIGALLIRESPRWLFLRGNREKGIETLAWIRNLPADHIYMVEEINMIEQSLEQQRVKIGLGFWKPFKAAWTNKRILYRLFLGSMLFLWQNGSGINAINYYSPRVFKSIGVSGGNTSLLTTGIFGVVKAVITFVWLLYLIDHFGRRNLLLVGAAGGSVCLWIVGGYIKIAKPENNPEGTQLDSGGIAAIFFFYLWTAFYTPSWNGTPWVINSEMFDPTVRSLAQACAAASNWLWNFLISRFTPQMFTSMGYGVYFFFASLMILSIVFVFFLIPETKGVPLESMETLFDKKPVWHAHSQLIRELRENEEAFRADMGASGKGGVTKEYVEEA
|
Integral membrane transporter that imports quinic acid to be catabolized as a carbon source.
|
P15325
|
P60235
|
3SI13_DENAN
|
Muscarinic m1-toxin3
|
Dendroaspis
|
LTCVKSDSIWFPTSEDCPDGQNLCFKKWQYISPRMYDFTR
|
Binds irreversibly and specifically to M1 (CHRM1) muscarinic acetylcholine receptors, blocking further binding of antagonists and preventing the action of agonists.
|
P60235
|
B2TPW4
|
ENO_CLOBB
|
2-phosphoglycerate dehydratase
|
Clostridium
|
MNDYLEIIDVVARQILDSRCFPTVEVEVYLEDGTIGRAAVPSGASTGMYEAVELRDGDKDKYLGKGVLTAVQNVNDTIAEALIGCNVFDQPYIDKMLIELDGTDNKGKLGANAILGVSLAVANAAANALGLSLYKYVGGVNAKVLPVPMMNIINGGSHADNSVDLQEFMIMPVGATSFTEALRMCAEVYHTLKNTLKDKGYATGLGDEGGFAPNLKSNAEAIDVIIEAITKAGYKAGEDMFIAIDAASSEYYKDGKYVLENEGKTLTSAEMVDFFEDWVNKYPIISIEDGMAEEDWDGWKLLNERLGKKVQLVGDDLFVTNTERLEKGIEIGAANSILIKLNQIGTLTETLNAIEMANRAGYTAVISHRSGETEDTTISDLVVAVNAGQIKTGAPARSERVAKYNQLLRIEEELEDVAEYRGKKAFFNIKK
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
B2TPW4
|
B7N237
|
SELA_ECO81
|
Selenocysteinyl-tRNA(Sec) synthase
|
Escherichia
|
MTTETRSLYSQLPAIDRLLRDSSFLSLRDTYGHTRVVELLRQMLDEAREVIRDSQTLPAWCENWAQEVDARLTKEAQSALRPVINLTGTVLHTNLGRALQAEAAVEAVMKAMRSPVTLEYDLDDAGRGHRDRALAQLLCRITGAEDACIVNNNAAAVLLMLAATASGKEVVVSRGELVEIGGAFRIPDVMRQAGCTLHEVGTTNRTHANDYRQAVNENTALLMKVHTSNYSIQGFTKAIDEAELVALGKELDVPVVTDLGSGSLVDLSQYGLPKEPMPQELIAAGVSLVSFSGDKLLGGPQAGIIVGKKEMIARLQSHPLKRALRADKMTLAALEATLRLYLHPEALSEKLPTLRLLTRSAEVIQIQAQRLQAPLAAHYGAEFAVQVMPCLSQIGSGSLPVDRLPSAALTFTPHDGRGSHLESLAARWRELPVPVIGRIYDGRLWLDLRCLEDEQRFLEMLLK
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
B7N237
|
A7MIM0
|
ISPH_CROS8
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Cronobacter
|
MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAVRNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSNPEGGMYLVESPEDVWKITVKDENNLSFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKTAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSDAHELTGREENIVFEVPKELRIDAREVQ
|
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
|
A7MIM0
|
P38162
|
MIX23_YEAST
|
Mitochondrial intermembrane space CX(n)C motif protein of 23 kDa
|
Saccharomyces
|
MVDNRRTFTAPQSLLETNLTFPNDEPSLTTITVTRERCVDPSLIDSFLRFLRHGSDDIIRQKLNNYRKGSINGKNKCKEFLKQELYPNWQIRNNIISFCEKEAAEMKNETDQQCGNNKKTTAEPLIDARIDPYAARERAEKQEAQYKDWTKVTEWVANNRKIEQILTSTTEGILRQNCEQNNDYLKEFTQFCKDNS
|
Regulator of the mitochondrial protein import machinery that is localized in the mitochondrial intermembrane space (IMS) and facilitates the transport of proteins from the cytosol into the mitochondrial matrix . Not essential for mitochondrial protein import but induced and required when mitochondrial import is compromised . Stimulates or stabilizes the translocation into the mitochondria of proteins such as OXA1, ATP1 and COX12 .
|
P38162
|
Q211G4
|
RL18_RHOPB
|
50S ribosomal protein L18
|
Rhodopseudomonas
|
MSKLKITNARRKQRVRLSLRRIANGRPRLSVFRSSKHIYAQVIDDLKGETLASASSLEKAMRDTGNTGANIDAAKAVGKLLAERAVKNGVTEVVFDRGGYLYHGRIKALADAARESGLSF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
Q211G4
|
O54459
|
AROH_ENTAG
|
Phospho-2-keto-3-deoxyheptonate aldolase
|
Pantoea agglomerans group
|
MNKTDELRTARIGSLITPPSLAAEHPVSPAIADNVTAARKRIACILTGEDHRLLVVIGPCSLHDPKAALEYAERLNALRRRYEDRLEIVMRAYFEKPRTVVGWKGLISDPDLDGSYDVNRGIGIARQLLIDINALGLPTATEFLDMVIGQFIADLISWGAIGARTTESQIHREMASALSCPVGFKNGTDGNVQIAVDAIRAARASHMFLSPDKLGQMTIYQTSGNPHGHVILRGGKQPNYHASDVAAAAESLSAFNLPQQLVIDFSHGNCLKQHRRQMDVAAEVAEQIKAGSQAVAGVMIESFLEEGNQKVVSGEPLVYGKSITDPCLGWQESEKVLALLAEAVSHRL
|
Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP).
|
O54459
|
Q14HG2
|
CYSN_FRAT1
|
Sulfate adenylate transferase
|
Francisella
|
MSHKSDLIATNIQKYLQQHQQKELLRFITCGSVDDGKSTLIGRLLHDSKLIFEDQLASIVADSKKVGTQGDRLDLALLVDGLQSEREQGITIDVAYRYFSTDKRKFIIADTPGHEQYTRNMATGASNCDLAIILIDARKGLQTQTRRHNFICSLLGIKHVIVAVNKMDTVGYSQQIYKSIQDEYLKLAGSLQIPDIRFVPISALDGDNVVSKSPKMPWFRGSPLMHYLETIKIDYAYTDEFRFPVQLVCRPNSEFRGFQGTVVSGSAKIGDTIRVMPSGKITTIKSILSFDGKLNEAEAGQSITITTYDEIDISRGDMIVHKDAISHVSSMLRANIVWMSEQPLIEYKDYYIKFLTKQVIGSVNKFNYKTDINTLKEVACGTLELNEIATIELKLSEPVCFDSYQKNRTIGAFIIIDRLTNVTAGAGMVIKPLAANDKKDSTNDYSEFELELNALIRKHFPHWDAKNLRE
|
With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD.
|
Q14HG2
|
B0WAM5
|
EIF3E_CULQU
|
Eukaryotic translation initiation factor 3 subunit 6
|
Culex
|
MSKFDLTAKNCQYLDRHLTFPLLEFLLQKNIYDQTSLLKFILETVSKTNMVDYTMDIRERLNMGNELPEELTKRRSNVLVKLKELQTEVAPLMKCMEELKNPDTMKDSKSIVHALQQEFDFKYDIIRSAQKLAKYLYECGNYRDSISYLYICLLVMEPTDKNYLNVLWGKLAAEILTLNWPTALEDLTRLRDFIDNHNFSPIEVLQQRTWLIHWSVLVFFNHAKGRDLIIEMFLYKQLYLNAIQTMCPHILRYLATAVIINRGRRNALKDLIKIIQQESYTYKDPITEFLECLYVNFDFEGARMKLHECQTVIINDFFIIGCLQEFIENARLMIFETFCRIHQCITIGMLADKLNMEPDEAECWIVNLIRNARLDAKIDSKLGHVVMGTQPLSPYQQLVEKIDSLSVRSEALTVLVERKQKAKTQESGEGNWKYY
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
B0WAM5
|
P52961
|
NAR1_HUMAN
|
Mono(ADP-ribosyl)transferase 1
|
Homo
|
MQMPAMMSLLLVSVGLMEALQAQSHPITRRDLFSQEIQLDMALASFDDQYAGCAAAMTAALPDLNHTEFQANQVYADSWTLASSQWQERQARWPEWSLSPTRPSPPPLGFRDEHGVALLAYTANSPLHKEFNAAVREAGRSRAHYLHHFSFKTLHFLLTEALQLLGSGQRPPRCHQVFRGVHGLRFRPAGPRATVRLGGFASASLKHVAAQQFGEDTFFGIWTCLGAPIKGYSFFPGEEEVLIPPFETFQVINASRLAQGPARIYLRALGKHSTYNCEYIKDKKCKSGPCHLDNSAMGQSPLSAVWSLLLLLWFLVVRAFPDGPGLL
|
Has ADP-ribosyltransferase activity toward GLP1R.
|
P52961
|
Q98QN3
|
RS15_MYCPU
|
30S ribosomal protein S15
|
Mycoplasmopsis
|
MTDKKLVKELAIEFGGSEKNVGAIEVQIAILTHDIERLKIHFETNKKDKHSKRGFIAKINKRKKLLAYLKDVNFESYQTTIQKLKIRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
Q98QN3
|
O27765
|
PHOU2_METTH
|
Phosphate-specific transport system accessory protein PhoU homolog 2
|
Methanothermobacter
|
MWKLIGALLESRLSNVLDETVRYGNETSERVGRTVSSYIKGDEETARELIETTAAVNEKSYRIEDECLKILGLHQPVAKDLRLASSIMRSAIELERINILLAYIARYAIDGRDRTPPHIEFMSQTVQDMINDALGALMNRDIQLLKRSTRNYIQLQDLYNQLQESNRDFSESGNLMLVARNLLSMGHHVMGMDDRIAYLIVGKRVIHHKVFYSVLMK
|
Plays a role in the regulation of phosphate uptake.
|
O27765
|
Q1MJ01
|
RSMA_RHIL3
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Rhizobium
|
MAALDGLPPLRDVIQRHGLDARKALGQNFLLDLNLTQKIARTAGALEDATVFEVGPGPGGLTRAILALGARKVIAIERDTRCLPALAEIADHYPGRLEVIEGDALKTDFETLAPQGPIKIIANLPYNVGTQLLVNWLLPKAWPPFWQSLTLMFQKEVGERIVANEDDDHYGRLGVLCGWRTEARMAFDVPPQAFTPPPKVTSTVVQLTPRENPIPCAVSNLEKVTQAAFGQRRKMLRQSLKPLGGERLLVKAGIDPARRAETLSVKEFCLLANSL
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
Q1MJ01
|
Q1LIM4
|
MURD_CUPMC
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Cupriavidus
|
MFGVLQKPHVLVLGLGESGLAMARWCGLNGCRVRVADTREAPANLVFLQAELTTAQFMGGQFTENLLDDIGLVAISPGLSPLEPNTRALLEAAQARSIPVWGEIELFAQAIGYLEATSGYAPRVLAITGTNGKTTTTALTGRLIERAGKTVGVAGNISPSALDKLSACIASATLPDVWVLELSSFQLEYTFSLAPHAATVLNVTQDHLDWHGSMEAYAAAKARIFGPAEKGCLQVLNRQDPLTMNMARRGTTLVTFGTDLPETPGSYGVLREGGMPWLVLAEPDTEADAEQKPRRRKKDDVAADAVVPVRHKRLMPADALHIRGMHNATNAMAALALCRAIDLPLNALLHGLREYRGEPHRVEWVATIDEVEYFDDSKGTNVGATVAALSGLDKHVVLIAGGEGKGQDFSPLVAPVAQYARAVVLIGKDAGALREALGATGKPLIDAGSLEEAVEKSASLAEAGDVVLLSPACASLDMFRNYVHRAQVFRGAVEELALSRGIMP
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q1LIM4
|
Q5BK67
|
TIFAB_RAT
|
TIFA-like protein
|
Rattus
|
MERPLTVLQVSLYHPTQGPVAFAKVPLQLQHDASRLLVGRGQDTHLQLQLPQLSRHHLCLEPYLEKGSNLLAFCLKVLTRQSCVWVNGLPLRYLEQVPLHSVNRISFSGIQMLIRKEGGASLEAFVCYFHLSPSPLIYRPKAQETDE
|
Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA.
|
Q5BK67
|
P60196
|
RNZ_STAAM
|
tRNase Z
|
Staphylococcus
|
MEVTFFGTSAGLPTKERNTQAIALNLEPYSNSIWLFDVGEGTQHQILHHAIKLGKVTHIFITHMHGDHIFGLPGLLSSRSFQGGEQKPLTLVGPKGIKAYVEMSMNLSESHLNYPITYIEIDDHLTYHHDGFTVEAHLLNHGIPSYGYRVMAPETTGTINVEALKNIGLEPGPKYQEVKSHDTFEHNGQVYQSKDFRGESKQGPVVAIFGDTKPCSNERVISRDADVMVHEATYIDGEKHLANNYHHSHIEDVFALIKEANVKRTLITHLSNRYNTEDINEIYQILIQNEDTPNFNFVKDFDSFKV
|
Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
|
P60196
|
O87778
|
DNAJ_LATSK
|
Chaperone protein DnaJ
|
Latilactobacillus
|
MAEKRDYYDVLGVGRDASDDEIKKAYRKLSKKYHPDINKAPDAEAKFKEVTEAYEALSDPQKRAAYDQYGHAGMNGGFGGGAGAGQGFGGFGGGAEGFGGFDDIFSSFFGGGARQQPNGPRQGSDLQYRMDLKFEEAVFGKETKISYSREAECHTCHGSGAKPGTSAETCHKCHGAGQIQVERQTPLGRMMSRETCDVCGGTGKEIKSKCDTCHGTGREEERHTVKVKVPAGVEDGQQMRLQGQGEAGSNGGPYGDLFIVFRVAPSDEFERDGAQIFVEVPISFVQAALGDEIEVNTVHGPVKLKIPAGTQTNTVFRLRGKGAPKLHGTGNGDQKVTVNVVTPKSLNSKQRDALKAFAVASGDSVNPQDNNLFDKILNKKHKK
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
O87778
|
A0JZ92
|
RPOC_ARTS2
|
Transcriptase subunit beta'
|
Arthrobacter
|
MSSESSFGLMQIGLATAEDIRGWSYGEVKKPETINYRTLKPEKDGLFCEKIFGPSRDWECYCGKYKRVRFKGIICERCGVEVTRAKVRRERMGHIELAAPVTHIWYFKGVPSRLGYLLDLAPKDLEKVIYFAAYMITSVDTDSRHEELPNLQVEHDIEKKQLVDNRDSDIATIARDLENELARLEGEGAKAADKKKARDSADRQMANVRKRADADIERLEQVWDRFKNLKVADLEGDEGLYRELRDRYGMYFEGSMGAEAIKKRLENFDMQAESDLLRDIIANGKGQRKTRALKRLKVVNAFLTTNNSPLGMVLDAVPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKRLLDLGAPEIIVNNEKRMLQEAVDSLFDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPQLKLHQCGLPKQMALELFKPFVMKRLVDLNHAQNIKSAKRMVERYRPQVWDVLEEIITEHPVLLNRAPTLHRLGIQAFEPQLVEGKAIQLHPLVCGAFNADFDGDQMAVHLPLSPEAQAEARILMLSSNNILKPSDGRPVTLPSQDMIIGLYHLTTKRVGSAGEGRIFSSVSEAIMAFDLHELHLNSQVKIRLEGFVPYAGWEAPEGWEPGQTALVQTSLGQVIFNQTLPEDYPWVEAVADKGELSRIVNDLAERYPKVVTAATLDNLKDAGFYWATRSGVTVAISDIEVPAEKPVILAGYEERAAKIQGQYDKGLIDDDERRQELIEIWNKATNEIAQVMRDNLSPMNTINRMVSSGARGNWMQVRQIAGIRGLVANPKGEIIPRPIKSSYREGLSVLEYFIATHGARKGLADTALRTANSGYLTRRLVDVSQDVIVREEDCGTERGLVTPIAVADANGELVLDENVENSAYARTLAVDVVDSKGKVLAAGGTDCGDVVIAELFAAGITEVKVRSVLTCESSVGTCALCYGRSLATGKTVDIGEAVGIIAAQSIGEPGTQLTMRTFHTGGAVSASGGDDITQGLPRIQELFEARTPKGVAPIAEAAGRIAIEESERQMRLVITPDDGSEEIAYPVLRRSRLLIEDGQHVAVGQKLINGPVDPKQVLRIMGPRAAQKFLVDEVQGVYRSQGIGIHDKHVEVIVRQMLRRVTVIESGESDLLPGELAERSRFEDANRRVVSEGKTPASGRPELMGITKASLATESWLSAASFQETTRVLTQAAMEGKSDPLLGLKENVIIGKLIPAGTGLPRYTEVTVEPTEEAKANLFTGPSAFSDFSYDTLGGDGAPEFHAIPLDDYDLGSDFR
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A0JZ92
|
P10785
|
HBB1_TRICR
|
Hemoglobin beta-major chain
|
Triturus
|
TFTNDESQHIHDVCGKIPVDQVGAEALGRLILVNPWTRRYFKSFGDLSSAEAIQHNPKVASHGAKVMHSIAEAVKHLDDLKAYYADLSTIHCKKLYVDPANFKLFGGIVSIVTGMHLGTDYTAQKQAAFEKFLHHVEAALATGYH
|
Involved in oxygen transport from the lung to the various peripheral tissues.
|
P10785
|
Q59NX9
|
DPH51_CANAL
|
Diphthamide biosynthesis methyltransferase 1
|
Candida
|
MLYLIGLGLSYESDITVRGLETVKKCKRVYLEAYTSILMAANQESLEKFYGREIILADRELVETGSDDILKDADKEDVAFLVVGDPFGATTHTDLVIRARELGIKVETIHNASVMNAVGACGLQLYQFGQTVSLVFFTDSWKPDSFYGKIMENRKIGLHTLLLLDIKVKEQSIENMARGRLIYEPPRYMDIATAAQQLLEIESIRQEQAYTPNTPCVAISRLGSPTQTFKAGTLQELSEYDSGEPLHSLVMLGRQVHELELEYLYQFVDDKEKFKKFVEQDQEFFKPAPYVPPEDVDSE
|
S-adenosyl-L-methionine-dependent methyltransferase that catalyzes four methylations of the modified target histidine residue in translation elongation factor 2 (EF-2), to form an intermediate called diphthine methyl ester. The four successive methylation reactions represent the second step of diphthamide biosynthesis.
|
Q59NX9
|
P35469
|
CH601_RHIME
|
Chaperonin-60 1
|
Sinorhizobium
|
MAAKEVKFGRSAREKMLRGVDILADAVKVTLGPKGRNVVIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVREGAKAVAAGMNPMDLKRGIDLAVAEVVKDLLAKAKKINTSDEVAQVGTISANGEKQIGLDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAFILLHEKKLSNLQAMLPVLEAVVQTGKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRAKKVSITKENTTIVDGAGQKSDIEGRVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRIDDALNATRAAVQEGIVPGGGVALLRSSVKITVKGENDDQDAGVNIVRRALQSPARQIVENAGDEASIVVGKILEKNTDDFGYNAQTGEYGDMIAMGIIDPVKVVRTALQDAASVASLLITTEAMIAELPKKDAPAMPGGMGGMGGMDMM
|
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.
|
P35469
|
B3LP25
|
MDG1_YEAS1
|
Multicopy suppressor of defective G-protein 1
|
Saccharomyces
|
MQSSLPQFTFKWPKGPEAIILTGTFDDWKGTLPMVKDPSGAFEITLPVTFDSPSSKFYFKFIVDGQWLPSKDYKVNIDEGVENNFITEEDVLKQRENGSSTLVPESAGLAVSKNAPLIEPEAEKRAKKLRKFKIKRVIKTNKQTGERSIFSQEVVELPDSEDETQQVNKTGKNADGLSGTTTIIENNVGVNEEKAIKPYEENHPKVNLVKSEGYVTDGLGKTQSSESRLYELSAEDLEKEEEEEDEDKGGGKDTSTSADAEASEDQNKEPLSKSAKFEKPEEKVPVSSITSHAKETSVKPTGKVATETQTYETKQGAPTAAAKKIEAKKATRPSKPKGTKETPNKGVQKNPAKNGGFFKKLAQLLK
|
Involved in G-protein mediated signal transduction and in the regulation of polarized cell growth in pheromone-induced cells.
|
B3LP25
|
B0RQ26
|
PQQD_XANCB
|
Pyrroloquinoline quinone biosynthesis protein D
|
Xanthomonas
|
MSTISRDSCPALRAGVRLQHDRARDQWVLLAPERVVELDDIALVVAQRYDGTQSLAEIAQTLATEFDADASEIETDVIELTTTLHQKRLLRL
|
Functions as a PqqA binding protein and presents PqqA to PqqE, in the pyrroloquinoline quinone (PQQ) biosynthetic pathway.
|
B0RQ26
|
A4Y931
|
SYA_SHEPC
|
Alanyl-tRNA synthetase
|
Shewanella
|
MYQTTAELRSAFLEFFRSHGHQVVDSSSLVPGNDPTLLFTNAGMNQFKDVFLGMDKRNYTRATTAQRCVRAGGKHNDLDNVGYTARHHTFFEMLGNFSFGDYFKEEAICFGWSFLTETLKLPKERLCVTIYQTDDEAFEIWNKKIGVAAENIIRIGDNKGAPYASDNFWQMGDTGPCGPCTEIFYDHGDHIWGGRPGSPEEDGDRFIEIWNIVFMQYNRHISGEMLPLPKPSVDTGMGIERIAAIMQGVHSNYEIDIFRALIAKAAEIIGVTDLSNKSLRVIADHIRSCAFLVADGVMPSNEGRGYVLRRIIRRAVRHGNKLGATEAFFYKLVPTLIDVMGDAAKGLAETQVIVEKALKAEEEQFARTLERGLGILDAALSELTGDTLDGETVFKLYDTYGFPMDLTADVCRERNIIVDEAGFEAAMAEQRSRAQAAGNFGADYNAALKIDAETAFCGYTELVGQAKVTAIYQNGESVTAIKAGDEAVLVLDVTPFYAESGGQVGDKGQLVANGIEFTVNDTQKYGQATGHQGVLVAGSLSIGQMVEAKVDKKLRHRTQLNHSVTHLLHAALRQVLGTHVTQKGSLVDPERLRFDFSHFEAVKPAELKKVEELVNTQIRRNHELKVAEMAIDEAKEKGAMALFGEKYDAQVRVVTMGDFSIELCGGTHVGRTGDIGLFKITSEGGIAAGVRRIEAVTGAAAMAYVAQQQAELEEAAALLKGDTHSVVAKLKAQLDKMKQLEKDMAQLKDKLAAAASADLVGDAVVVNGVNVLIKKLDGVEAGSLRGLQDELKQKLKSAIIVLGTAQEGKVNLIAGVSNDLVGKVKAGELVAMVAAQVGGKGGGRPDMAQAGGSQPENLDAALAQVLPWITERLA
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
|
A4Y931
|
Q7WJQ9
|
PCKG_BORBR
|
Phosphoenolpyruvate carboxykinase [GTP]
|
Bordetella
|
MNKPSEVKPVALNVPDYVKHSGLIAWVERIAALTKPDRVVWCDGSQEEYDRLCEQMVQGGTMRRLNPAKRANSYLACSDPSDVARVEDRTFICSEREEDAGPTNNWAAPQAMRETLGGLFDGAMRGRTMYVVPFSMGPLGSPIAHIGVELSDSPYVVVNMRIMTRMGRKVFDVLGSDGAFVPCVHSVGMPLAEGQQDVAWPCNPTKYIVHYPETREIWSFGSGYGGNALLGKKCFALRIASTMGRDEGWLAEHMLILGVTSPKGRKYHVAAAFPSACGKTNFAMLIPPHGMDGWKVTTIGDDIAWIKPGPDGRLHAINPEAGYFGVAPGTSEKTNFNAMATLKANVIFTNVALTDDGDVWWEGMTDTPPAHLIDWQGQDWTPAIAAETGRKAAHPNARFTAPAAQCPSIDPEWENPKGVAIDAFIFGGRRSTTVPLVTEARNWVEGVYMAATMGSETTAAAAGQQGVVRRDPFAMLPFCGYNMSDYFDHWLKLGRRLEETGATLPRIYCVNWFRKGPDGKFVWPGFGENMRVLRWMLGRLDGQAGGVDQVFGISPAYGDIDWTGLEFSPDKFEQVISVDLPAWRAELALHDELFTQLAARLPEDLPLTRTAIERRMAA
|
Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle.
|
Q7WJQ9
|
Q71PB7
|
NU6M_BOSIN
|
NADH dehydrogenase subunit 6
|
Bos
|
MMLYIVFILSVIFVMGFVGFSSKPSPIYGGLGLIVSGGVGCGIVLNFGGSFLGLMVFLIYLGGMMVVFGYTTAMATEQYPEIWLSNKAVLGAFVTGLLMEFFMVYYVLKDKEVEVVFEFNGLGDWVIYDTGDSGFFSEEAMGIAALYSYGTWLVIVTGWSLLIGVVVIMEITRGN
|
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
|
Q71PB7
|
Q3AEY1
|
PDRP_CARHZ
|
Putative pyruvate, phosphate dikinase regulatory protein
|
Carboxydothermus
|
MAINLKLEQIPVVYILSDSIGETGEVVAKAAASQFDSGRVDIRRVPYLSSVREVEEALQEAESAGALVVYTLVRPDLKEYLEKRAHELSLPHVDIMGPMLEGLKQITKQNPKYQPGLIRKMDEAYFSKVEAIEFAVKYDDGKEPRGLLRADLVVIGVSRTSKTPLCMYLAHKGIKAANVPLVPEATPPEELFKIPPHKVVGLTIKPSILFEIRKERLKTLGLSQTADYANMERILMELDYALGIMKKIGCAVIDVSNKAVEETAARVLEIYRKGVGR
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
|
Q3AEY1
|
C0Q8N5
|
RSMH_DESAH
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Desulforapulum
|
MKFEHRSVMPREVRDGLDLKPGETCVDCTLGGSGHAVTSLAAVLPNGRLIGIDQDLDAIENAHRVFADDMANVSIFHDNFSHLPAILDSLGIKGVDGILLDLGLSLHQLRKGQRGFSFKGDEPLDMRMDMRTALTAADLVNTLEERALVDIFFKYGEEKMSRKIARAIVRQRASAPITRNCELAEIVRAAIPAKIVHQQKIHPATRVFQALRISVNRELEQLERFLETFVDFLNPGGRICIISFHSLEDRMVKRRFRALEQGCTCPRDFPECVCGFKPRLKSVTKRAVMPTPEEIEINPMARSARLRVAWRV
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
C0Q8N5
|
Q9WTV0
|
PREB_RAT
|
Mammalian guanine nucleotide exchange factor mSec12
|
Rattus
|
MGRRRGVELYRAPFPLYALRIDPKTGLLIAAGGGGAAKTGIKNGVHFLQLEQISGCLSASLLHSHDTETRATMNLALAGDILAAGQDAQCQLLRFQIHQQKGSKAEKSGSKEQGPRQRKGAAPAEKKSGAEVHPEGVELKVKNLEAVQTDFSTEPLQKVVCFNHDNTLLATGGSDGHVRVWKVPSLEKVLEFKAHEGEIGDLALGPDGKLVTVGWDFKASVWQKDQLVTQLQWQENGPTSSNTPYRYQACRFGQVPDQPGGLRLFTVQIPHKRLRQPPPCYLTAWDSSTFLPLQTRSCGHEVISCLTVSESGTFLGLGTVTGSVAIYIAFSLQRLYYVKEAHGIVVTDVTFLPEKGCGPKLLGPHETALFSVAVDSRCQLHLLPSRRSVPVWLLLLLCVGLIIVTILLLQSAFPGFL
|
Was first identified based on its probable role in the regulation of pituitary gene transcription. Binds to the prolactin gene (PRL) promoter and seems to activate transcription.
|
Q9WTV0
|
Q4A881
|
RL19_MESH7
|
50S ribosomal protein L19
|
Mesomycoplasma
|
MQAKLIEILESSQIRLYPQFQPGDNVRVYFKIQEGNKTRIQIFEGLVIKFKKNGLSSNFVVRKISHNVGVERTFLLHSPLVDKVEVIRSNKVRRAKLYYMKKRSGKSARLKEIKRKELKNL
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
Q4A881
|
A6Q3V4
|
RNY_NITSB
|
Ribonuclease Y
|
unclassified Nitratiruptor
|
MWVEILVGSSAAIISGAAGYLLSKKIEKDKLKIYEEQARAKAKAIEHEAEKILQNAQVQVKEAELELKRDFEKKLEELKRDYEERFNELMEKEMSLKQMFKDELKHITLEKQEIKAEREEINRLKNEYEELKKRYQEKYQEVLEALQQQAGLTLEEAKNLILQKAEEESRLEIANIVRKYEEEAKREAKRRANYIIAQATTRFAGEFAAERLINTVSIPSEDIKGRIIGKEGRNIKTLEMLLGVDIIIDDTPNAIILSSFNLYRRAIATKVIELLVEDGRIQPSRIEEIYEKVKEEFDQQLLEEGENIVIDLGIGLIHPEIVKLIGRLKFRASYGQNALGHSLEVAHLAGIMAAEMGGDEVMAKRAGLLHDIGKALTHEYSGSHVDLGAEICKRYKEPDVVINAIYAHHGHEEPRSIEAAAVCAADTLSAARPGARREVLEAFLKRVQAIEEIALSKPGVKKAYAINAGREVRVIVNADLVNDNEAVLLAKEIAKDIETGVQYPGEIKVNVIRENRAIEYAR
|
Endoribonuclease that initiates mRNA decay.
|
A6Q3V4
|
Q5HKN7
|
HIS1_STAEQ
|
ATP phosphoribosyltransferase
|
Staphylococcus
|
MLRVALAKGRLLKSFIEYLQQVNQIDIATVLLNRQRQLLLTVDNIEMILVKGSDVPTYVEQGIADVGIVGSDILNGQKYNINKLLDLPFGKCHFALAAKPETSRYKKVATSYVHTATQFFNKEGMDVEVIHLNGSVELSCVVDMVDAIVDIVQTGSTLTANGLVEKKHISEINAKLITNKESYFKQSSEIERLIKQLGVSINYA
|
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
|
Q5HKN7
|
A4XK06
|
HEM3_CALS8
|
Pre-uroporphyrinogen synthase
|
Caldicellulosiruptor
|
MKKLRIGARDSKLSRIQVDIVARKIKQTLGIECEFVPIKTKGDIDKTKSLKDFKSPGVFVKEIELALLSREIDLAVHSLKDLPCEMDSNFEIVAVVEREDPRDVLVSKDGVGFYQLKPNAKIGTSSLRREVHLKNLRQDIQVVNIRGNIETRLSKIESEGLDGVVLAYAALKRLNLDSHVSYIFDVNEITPCPGQGAICIECLKDSPYKNILSKINDADAYIQTQFERLVLKFLGGGCHSSIGVFCKTDQDKIYAFASILSGDKLIKASIEGDKDDFLSLANKLSNMLKS
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A4XK06
|
Q3EC60
|
SUVHA_ARATH
|
Suppressor of variegation 3-9 homolog protein 10
|
Arabidopsis
|
MGLVGLHSGTIDMEFIGVEDHGDEEGKQIAVSVISSGKNADKTEDPDSLIFTGFGGTDMYHGQPCNQKLERLNIPLEAAFRKKSIVRVVRCMKDEKRTNGNIYIYDGTYMITNRWEEEGQNGFIVFKFKLVREPDQKPAFGIWKSIQNWRNGLSIRPGLILEDLSNGAENLKVCLVNEVDKENGPALFRYVTSLIHEVINNIPSMVDRCACGRRSCGSKHVFREKLSVSSSLVISAKKSGNVARFMNHSCSPNVFWQSIAREQNGLWCLYIGFFAMKHIPPLTELRYDYGKSRGGGKKMCLCRTKKCCGSFG
|
Histone methyltransferase family member that may lack methyltransferase activity. May methylate 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression (Potential).
|
Q3EC60
|
D8IJV0
|
RNM51_LIGS5
|
Ribosomal RNA terminal maturase M5 1
|
Ligilactobacillus
|
MNENDKMKIKEVIVVEGKDDTKRIQMAVNADTLETRGSAISDETLDQIEDLYDKRGVIVFTDPDFSGEKIRKIITEAVPGVKHAFLTKHDAAPSHKGSLGVEHASPEAIREALAHLYTEVPDGEPLISREDLAVAGLTSGPQAKEYRRRLGEYLRIGYTNGKQLYKRLKLFQITPDELKKALEYIKNEDNY
|
Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step.
|
D8IJV0
|
O67104
|
BIOB_AQUAE
|
Biotin synthase
|
Aquifex
|
MDKVERRLYELYEKAINYEPLSKEEALYILEVDDIYVPFLVHLAQKIKKHYFPENEVEFCSIINAKSGACSEDCKFCAQSKYYKTPINVYNLVPVDEMVEGAIRGVEFGANRYCIVLSGKSATKEEVERITEAVKEIKNEGLPINVCVSAGTLDEESLKKLKEAGVKRINHNLETSRNFFKNIVTTHTWEDRYETIKRIKKVGLSTCSGGIFGMGESNEDRVDMALTYRELEVDSIPLNFLMPIEGTPMENAPGVEVMEALKIIAMFRFTNPKAELRLCGGREQNLRDFHGMATLMTNAMMVGGYLTRAGRDIKKDYQLLKDLKAKRKVSVE
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
O67104
|
B6YSL7
|
RS19_THEON
|
30S ribosomal protein S19
|
Thermococcus
|
MARKKEFRYRGYTFEELLNMSLEDFAKLLPARQRRSLKRGLSPEQKKLLRKIRLAKKGKYNKPIRTHSRDMVILPEMVGMTIHVYNGKEFVPVEIKEEMIGHYLGEFALTRKIVQHGSPGVGATRSSMFVAIK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B6YSL7
|
Q12891
|
HYAL2_HUMAN
|
Lung carcinoma protein 2
|
Homo
|
MRAGPGPTVTLALVLAVSWAMELKPTAPPIFTGRPFVVAWDVPTQDCGPRLKVPLDLNAFDVQASPNEGFVNQNITIFYRDRLGLYPRFDSAGRSVHGGVPQNVSLWAHRKMLQKRVEHYIRTQESAGLAVIDWEDWRPVWVRNWQDKDVYRRLSRQLVASRHPDWPPDRIVKQAQYEFEFAAQQFMLETLRYVKAVRPRHLWGFYLFPDCYNHDYVQNWESYTGRCPDVEVARNDQLAWLWAESTALFPSVYLDETLASSRHGRNFVSFRVQEALRVARTHHANHALPVYVFTRPTYSRRLTGLSEMDLISTIGESAALGAAGVILWGDAGYTTSTETCQYLKDYLTRLLVPYVVNVSWATQYCSRAQCHGHGRCVRRNPSASTFLHLSTNSFRLVPGHAPGEPQLRPVGELSWADIDHLQTHFRCQCYLGWSGEQCQWDHRQAAGGASEAWAGSHLTSLLALAALAFTWTL
|
Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product which is further hydrolyzed by sperm hyaluronidase to give small oligosaccharides. Displays very low levels of activity. Associates with and negatively regulates MST1R.
|
Q12891
|
D9PZU4
|
PUS10_ACIS3
|
tRNA pseudouridine 54/55 synthase
|
Acidilobus
|
MNEDPAQQAMKVLAKYPLCDRCLGRLFAGLGRGLSNAERGRALKLSVVMSLHAMSLSGRLPENARDVLANAGGAAAQVYVELFGSPPEHRSCYICNDALDKFLDEMPQRVADAVKEWGGSTFLVGAKVDPGVIAREERIKAEFGLAFGESIKSEIKRELGKRAQQLGPKVSFDRPDVVVMVSFPDGSVSVQPRRLVVKGLYRRLRRDLQLRPREALSHPLVARLINDTRSSRVGIVGLVRDEKEVRALGLGIPVEFHLGGPRVRLVPPDGSIIEAEGASLEVNSSVEASGPEDLSRRVRVYRCVLYVEGGAFESLQLAAASLRGKEVRQKFMGKEVSGVVRGAECVDMGGGLAECIIALDERLHVMELVSGSGTEPSLSGLLGTAAECVVADLLGVIPLR
|
Responsible for synthesis of pseudouridine from uracil-54 and uracil-55 in the psi GC loop of transfer RNAs.
|
D9PZU4
|
Q87MQ1
|
APT_VIBPA
|
Adenine phosphoribosyltransferase
|
Vibrio
|
MTTETISLIKSSIKSIQDYPKPGILFRDVTSLLEDAKAYQATIGLLVERYKDMGFTKVVGTEARGFLFGAPLALELGVGFVPVRKPGKLPRPTIAQSYELEYGIDTLEIHTDAIVEGDKVLVVDDLLATGGTIEATTKLIRQLGGEVEHAAFVINLPEIGGDKRLEALGLNVFSICDFEGH
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
Q87MQ1
|
Q3ICG2
|
MINE_PSET1
|
Cell division topological specificity factor
|
Pseudoalteromonas
|
MSLLDYFRSEKKNSASLAKERLQIIVAHERSQRGTPDYLPQLKQDILDVIRKYVNVSSDAVQVQFDQNEDDLAVLELNVTLPDEEPKI
|
Prevents the cell division inhibition by proteins MinC and MinD at internal division sites while permitting inhibition at polar sites. This ensures cell division at the proper site by restricting the formation of a division septum at the midpoint of the long axis of the cell.
|
Q3ICG2
|
Q0ABG5
|
RL14_ALKEH
|
50S ribosomal protein L14
|
Alkalilimnicola
|
MIQMQTTLGVADNSGARQVQCIKVLGGSRRRYAGIGDIIKVSVKDAIPRGRVKKGEVYNAVVVRTRRGVRRPDGSVIRFDGNAAVLLNNQLQPIGTRVFGPVTRELRSEKFMRIISLAPEVL
|
Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome.
|
Q0ABG5
|
B5YFZ0
|
GLYA_THEYD
|
Serine hydroxymethyltransferase
|
Thermodesulfovibrio
|
MKMKSLREVDAEIYSLILQEKKRETNKILMIASENYASRAVMEAQGSLFTNKYAEGYPGRRYYGGCEYADEVERLAQERAKQLFNVEHVNVQPHSGTQANMAVYFAMLQPGDTIMGMSLTHGGHLSHGSPVNFTGKLYKTVFYGVNKETGYIDMDEVRRLAQEHKPKIIITGASAYPRTIDFKAFSEIAKEVGAYLMADIAHIAGLIATSMHPSPVPYSDFITTTTHKTLRGPRGGVVMCKAQYAKAIDKTVFPGIQGGPLVHVIAAKAVAFKEALSEDFKEYQKKVIKNAKTLAEALKKKGFKLVSDGTDNHLMLVDLTNFNITGKEAEEALDKAGITVNKNTIPFDTKPPTVTSGIRIGTPSVTTRGMGEEEMEKIAEIIERVIKNISNDSVIKDMQKKVQELCKKFPIY
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
B5YFZ0
|
Q50940
|
CAH_NEIGO
|
Carbonate dehydratase
|
Neisseria
|
MPRFPRTLPRLTAVLLLACTAFSAAAHGNHTHWGYTGHDSPESWGNLSEEFRLCSTGKNQSPVNITETVSGKLPAIKVNYKPSMVDVENNGHTIQVNYPEGGNTLTVNGRTYTLKQFHFHVPSENQIKGRTFPMEAHFVHLDENKQPLVLAVLYEAGKTNGRLSSIWNVMPMTAGKVKLNQPFDASTLLPKRLKYYRFAGSLTTPPCTEGVSWLVLKTYDHIDQAQAEKFTRAVGSENNRPVQPLNARVVIE
|
Reversible hydration of carbon dioxide.
|
Q50940
|
A4JBS2
|
DNAJ_BURVG
|
Chaperone protein DnaJ
|
Burkholderia cepacia complex
|
MAKRDYYEVLGVAKNASDDEIKKAYRKLAMKYHPDRNPDNKDAEEHFKEAKEAYEMLSDGQKRAAYDQYGHAGVDPNMAGAGGQGFGGFADAFGDIFGDIFGQAAGGAARGGRGGPQVYRGADLRYSMEITLEQAAHGYDTQIRVPSWVSCEVCHGSGAKPGTKPETCPTCHGQGTVRMSQGFFSIQQTCPKCHGTGTYIPEPCAHCHGSGKVKETKTLEVKIPAGIDDGMRIRSAGNGEPGINGGPPGDLYVEIHIKPHAVFERDGDDLHCQMPIPFTTAALGGEIEVPTLAGRASFPVPEGTQSGKTFRLRGKGIKGLRSSIAGDLYVHVQVETPVKLTDQQRDLLKQFEKSLAEGGARHSPQSKSWFDRMKSFFE
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
A4JBS2
|
Q5WAG3
|
MNME_ALKCK
|
tRNA modification GTPase MnmE
|
Alkalihalobacillus
|
MEMDTIAAISTALGEGAIGIVRLSGDQAIAIGDKLFKGTKRLEDTPSHTIVYGHLMDDASEEAIEEAMVTVMRAPRTYTREDIVEINCHGGLVSVNRVLQAVLAKGARLAEPGEFTKRAFLNGRIDLSQAEGVIDLIRSKTDRAMNVALRQVEGRLSKKIGKLRQALLETIASIEVNIDYPEYDAETMTAKLINEKMTIVLAEIEALLATAKQGKVLREGLATAIIGRPNVGKSSLMNSLVHEAKAIVTDIPGTTRDTLEEYVNVRGVPLRLIDTAGIRETEDIVERIGVERSRQALKEADLILLVLNYAEKLSKEDEALFEAVKGLDVVVIVNKIDQTGRIDMERVRQLAGENPVVATSFLQEEGVDQLEEAISRLFFAGGVEGADLTYVSNARHIGLLNQAKAHAEEAIAASLTDVPVDLIQIDVTRTWELLGEIIGEDVQDSLIDQLFSQFCLGK
|
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q5WAG3
|
A1D4C8
|
PLPL_NEOFI
|
Patatin-like phospholipase domain-containing protein NFIA_019760
|
Aspergillus subgen. Fumigati
|
MTSDEKSATRDIYDPNTLPDYDREFIDPDDLRQFEKALNAPEAAPLVALNDWRPVNQRVRKSRRTKPRRSKDETREGVLYTVLKWPFLFTVFAWITVLGFAYTLTRLYIFLYEQFVTWRGKRERLRKELSMQTNYQDWLKAAQALDTYLGNLKWKETDEYAYYDHLTINKVVAQLKQTRKAAETEMQNGRSGLSDPPAVEELCFLLEACVKNNFAGVENPRLYSETYSGTKDLVQEYIDEVHSCIRLVLDSKQISNEDKYQFFKHLDTNFGRTALCLSGGATFAYYHFGVIRALLDNDVLPEIITGTSGGALVAALVATRTDEELKQLLVPALAHRIRACHEGFTTWVRRWWRTGARFDTLDWARQCSWFCRGSTTFREAYERTGRILNVSCVPSDPHSPTILANYLTSPDCVIWSAVLASAAVPGILNPVVLMTKKRDGTLAPYSFGHKWKDGSLRTDIPIKALNLHFNVNFTIVSQVNPHINLFFFNSRGSVGRPVTHRKGRGWRGGFLGSAIEQYIKLDMNKWLRVLRHLELLPRPLGQDWSEIWLQKFSGTITIWPKSIPSDFYHILSDPSPERLARMLHVGKQSAFPKIQFIKNRLKIENAIMQGLQQCSSGGGRVMSPILSRRRQDRAEEHADRMVERLDQSFPERQSDYKDESHYTEVSDSLSATSSRPHTPDARRSSMFEEMRRQSAVFFDDSDMYADEDAVTT
|
Probable lipid hydrolase.
|
A1D4C8
|
Q87S70
|
NCPP_VIBPA
|
Nucleoside-triphosphate phosphatase
|
Vibrio
|
MSKKIMATQKVVIASLNPAKINAVKSAFQSAFPQQVFEFVGISVPSEVADQPMTNEETHRGALNRVKNAKLEMPTADFYVGLEAGIEGNVTFAWMVIESDTHRGESRSASLMLPPEVLAQLADANELGDVMDKVFGTENIKQKGGAISLLTQNQLTRSSVYHQALILALIPFTNPDHFPANL
|
Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
|
Q87S70
|
P50242
|
ESR1_SALSA
|
Nuclear receptor subfamily 3 group A member 1
|
Salmo
|
SRMLTDPPRIGSMQSLGSSPTGPLVFVSSSPQLSPFLHPPGHHGLPSQSYYLETSSTPLYRSSVVTNQLSASEEKLCITSNRQQSYAAAGSGVRVFEMANETRYCAVCSDFASGYHYGFWSCEGCKAFFKRSIQGHNDYMCPATNQCTMDRNRRKSCQACRLRKCYEVGMVKGGLRKDRGGRVLRKDKRYCGPAGDREKPYGDLEHRTAPPQDGGRNSSSSSLSGGGGWCGPRITMPPEQVLFLLQGAEPPALCSRQKVARPYTEVTMMTLLTSMADKELVHMIAWAKKVPGFQELSLHDQVQLLESSWLEVLMIGLIWRSIHCPGKLIFAQDLILDRSEGDCVEGMAEIFDMLLATVSRFRMLKLKPEEFVCLKAIILLNSGAFSFCSNSVESLHNSSAVESMLDNITDALIHHISHSGASVQQQPRRQVQLLLLLSHIRHMSNKGMEHLYSIKCKNKVPLYDLLLEMLDGHRLQSPGKVAQAGEQTEGPSTTTTTSTGSSIGPMRGSQDTHIRSPGSGVLQYGSPSSDQMPIP
|
The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
|
P50242
|
Q6WGK6
|
CXB1_HORSE
|
Connexin-32
|
Equus
|
MNWTGLYTLLSGVNRHSTAIGRVWLSVIFIFRIMVLVVAAESVWGDEKSSFICNTLQPGCNSVCYDHFFPISHVRLWSLQLILVSTPALLVAMHVAHQQHIEKKMLRLEGHGDPIHLEEVKRHKVHISGTLWWTYVISVVFRLLFEAAFMYVFYLLYPGYAMVRLVKCDAYPCPNTVDCFVSRPTEKTVFTVFMLAASGICIILNVAEVVYLIVRACARRAQRRSNPPSRKGSGFGHRLSPEYKQNEINKLLSEQDGSLKDILRRSPGTGAGLAEKSDRCSAC
|
One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Q6WGK6
|
B3WAM4
|
RS12_LACCB
|
30S ribosomal protein S12
|
Lacticaseibacillus
|
MPTINQLVRQGRKSISTKSDSPALNFGYNSKKKSLTNNPAPQKRGVATRVGTMTPKKPNSALRKYARVRLSNLIEVTAYIPGIGHNLQEHSVVLIRGGRVKDLPGVRYHIVRGALDTAGVDGRMQGRSKYGAKRPKKK
|
Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
|
B3WAM4
|
A6WV17
|
RLMN_BRUA4
|
tRNA m2A37 methyltransferase
|
Brucella
|
MSISFDLTIDDTRDQLARHARASLEAKPSLIGMSREEMAEALIKAGVPERQVKMRISQLWHWLYVRGVSDFADMRNISKDLRAMLAQHFTIARPEVVEEQISQDGTRKWLFRFPPRGAGRPVEIESVYIPEEGRGTLCVSSQVGCTLTCSFCHTGTQKLVRNLTSEEILAQLLTARDRLGDFPDKDTPDGAMVPAEGRKITNIVMMGMGEPLYNFEEVKKALLIASDGDGLSLSKRRITLSTSGVVPEIYRTGDEIGVMLAISLHAVRDELRDILVPINKKYPLEQLIKACREYPGLSNAKRITFEYVMLKDINDSLEDAKLLVKLLQGIPAKINLIPFNPWPGTNYQCSEWEQIEKFADYVNAAGYASPIRTPRGRDILAACGQLKSESERMRKSERLALEAMMIAGHGE
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
|
A6WV17
|
C4LAS5
|
NIFH_TOLAT
|
Nitrogenase reductase
|
Tolumonas
|
MALRQCAIYGKGGIGKSTTTQNLVSALAEMGKKVMIIGCDPKADSTRLILHAKAQNTIMEMAAEVGSVEDLELEDVLQIGYGGVRCAESGGPEPGVGCAGRGVITAINFLEEEGAYEEDLDFVFYDVLGDVVCGGFAMPIRENKAQEIYIVCSGEMMAMYAANNISKGIVKYAKSGSVRLAGLICNSRQTDREDELIIALADKLGTQMIHFVPRDNIVQRAEIRRMTVIEYDPTCKQANEYRTLANKVVNNKLFVVPTPVTMDELEELLMEFGIMDVEDETIIGKTAAEEAAATA
|
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
|
C4LAS5
|
B8E0X9
|
RPOZ_DICTD
|
Transcriptase subunit omega
|
Dictyoglomus
|
MKEVNIDTLISKIPNKYVLTVVISKRARQLFEELKFLKTIARDPLILAMEEIAQEKIAYGEGDDLED
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
B8E0X9
|
Q5QVT4
|
CH60_IDILO
|
Chaperonin-60
|
Idiomarina
|
MAAKEVKFGNTARQKMLKGVNILADSVKVTLGPKGRNVVLDKSYGSPVITKDGVSVAKEIELEDKFENMGAQMVKEVASKANDEAGDGTTTATVLAQAIVNEGLKSVAAGMNPMDLKRGIDKAVIAAVEELKKISQPCADSKAIAQVATISANADHTIGEIIAQAMDKVGQEGVITVEEGQALTDELDVVEGMQFDRGYLSPYFINNQESGSVELDNPFILLIDKKISNIRELLPVLEGVSKAGKPLLIIAEDVEGEALATLVVNNMRGIVKVAAVKAPGFGDRRKAMLQDIAVLTGGTVVSEEIGMELEKTQLEDLGTAKRVVITKDNTTVVDGNGDDTAIDGRVNQIKQQMEDTTSDYDREKLQERLAKLAGGVAVIKVGAATEMEMKEKKARVEDALHATRAAVEEGVVPGGGVALVRAASKLAELRGDNEEQNVGIRLALRAMEAPLRQIAMNAGAEGSVVANNVRAGEGNYGYNAGNDTYGDMLEMGILDPTKVTRSALQFAASVGALMITTEAMIADIPQDDNAGGMPGGDMGGMGGMGGMM
|
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.
|
Q5QVT4
|
Q252V7
|
RS19_CHLFF
|
30S ribosomal protein S19
|
Chlamydia
|
MGRSLRKGPFVDHSLIKKVRAMNLLEKKAPIKTWSRRSMITPEMIGHTFEVHNGKKFLTVFVSETMVGHKLGEFSPTRMFKSHPVKKG
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q252V7
|
A0A0B5AC95
|
INS1A_CONGE
|
Con-Ins G1a A chain
|
Gastridium
|
MTTSSYFLLMALGLLLYVCQSSFGNQHTRTFDTPKHRCGSEITNSYMDLCYRKRNDAGEKRGRASPLWQRRGSLSKLKARAKRNGAFHLPRDGRGVVEHCCHRPCSNAEFKKYCG
|
This venom insulin, from a fish-hunting cone snail, facilitates prey capture by rapidly inducing hypoglycemic shock . It is one of the smallest known insulin found in nature and lacks the C-terminal segment of the B chain that, in human insulin, mediates engagement of the insulin receptor and assembly of the hormone's hexameric storage form . Despite lacking this segment, it both binds and activates human insulin receptor (long isoform (HIR-B)) with a high potency (EC(50)=16.28 nM) . In vivo, intraperitoneal injection of this peptide into zebrafish lowers blood glucose with the same potency than human insulin . In addition, when applied to water, this peptide reduces overall locomotor activity of zebrafish larvae, observed as a significant decrease in the percentage of time spent swimming and movement frequency . When tested on a mouse model of diabetes, this insulin also lowers blood glucose with a 10-fold lower potency than human insulin .
|
A0A0B5AC95
|
B2JDU4
|
MURB_PARP8
|
UDP-N-acetylmuramate dehydrogenase
|
Paraburkholderia
|
MSQPESLPFIADFPLKPHNTFGFDVRARLACRIETDAQLLAALRDPRAAGLRRLVLGGGSNVVLTGDFDGLVLLVALRGRKVVREDDEAWYVEAAAGENWHEFVSWTLAEGMPGLENLALIPGTVGAAPIQNIGAYGLEMCERFASLRAVELATGKLVELGAGACRFGYRDSFFKQEGRERFVIVSVTFRLPKVWAPRAGYTDIARQLAAVGLGDATPTPQAIFDAVVAVRRAKLPDPFVLGNAGSFFKNPVVESAQFDALAAKEPEIVSYRQADGRVKLAAGWLIDRCGWKGRTLGAAGVHERQALVLVNRGGASGTEVLALAKAIQQDVAQRFGVELEAEPVCL
|
Cell wall formation.
|
B2JDU4
|
P42949
|
TIM16_YEAST
|
Presequence translocated-associated motor subunit PAM16
|
Saccharomyces
|
MAHRAFIQVIITGTQVFGKAFAEAYRQAASQSVKQGATNASRRGTGKGEYGGITLDESCKILNIEESKGDLNMDKINNRFNYLFEVNDKEKGGSFYLQSKVYRAAERLKWELAQREKNAKAKAGDASTAKPPPNSTNSSGADNSASSNQ
|
Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to regulate activity of mtHSP70 (SSC1) via its interaction with PAM18/TIM14. May act by positioning PAM18/TIM14 in juxtaposition to mtHSP70 at the translocon to maximize ATPase stimulation.
|
P42949
|
Q6GDB4
|
PCP_STAAR
|
Pyroglutamyl-peptidase I
|
Staphylococcus
|
MHILVTGFAPFDNQDINPSWEAVTQLENIIGTHTIDKLKLPTSFKKVDTIINKTLASNHYDVVLAIGQAGGRNAITPERVAINIDDARIPDNDDFQPIDQAIHLDGAPAYFSNLPVKAMTQSIINQGLPGALSNSAGTFVCNHVLYHLGYLQDKHYPHLRFGFIHVPYIPEQVVGKPDTPSMPLEKIVAGLTAAIEAISNDEDLHLALGTTQ
|
Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
|
Q6GDB4
|
Q5U2V5
|
CRLS1_RAT
|
Cardiolipin synthase (CMP-forming)
|
Rattus
|
MLAWRVARGAWGSLRVAVRPPGARLGRGGSRRALLPPAACCLGCLAERWRLRPAAFALRLPGTSPRTHCSGAGKAAPEPAAGGDAAAQAPSARWVRASATSSYENPWTIPNLLSMTRIGLAPVLGYLILEEDFNVALGVFALAGLTDLLDGFIARNWANQKSALGSALDPLADKVLISILYISLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCCTAFTTAASAYSYYHYGRKTVQVIKGK
|
Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
|
Q5U2V5
|
Q9NEU5
|
NOP53_CAEEL
|
Ribosome biogenesis protein NOP53
|
Caenorhabditis
|
MVAGKRTGAAKGSRHNKKYWRKGTNIDDIEDSIHIKSRQAATGGVISEMKDEDLFIVDRTATANKPVVPKLTKKQQAALEKITKNITQEHVTLPKPSTTSKILKKPAKLPRGNAILALKKGPKAAAPAAKKKNFDVWTTDLTPKIPKSKLENQEAAEHFLKVVKKKQPKTPGKSITSLLPAVQIAEGGASYNPESAEYQEYVAKIAGEEQKLIDHEAKIKAGIEPQWEKVTTEHERFLEMAEGLRIHPKYGKDDEEEEEAGNSEKSMKTGGEAEPKSQRVECDRMTKEQKKKKAKAQKLDKEEKRRLEEKAKEQDSHNVYRTKQLHKELDEEEKQRHEESEVRKKEKLINKLTKRQQLGKGKFVDAEDPFLLQEELTGNLRQLKPQGHVLDDRMKSLQRRNMLPIGGDKEKRRIKNRLKSKVVEKRSAKNIVKGSRVI
|
May play a role in ribosome biogenesis, being required for integration of the 5S RNP into the ribosomal large subunit.
|
Q9NEU5
|
Q5NZT6
|
LOLD_AROAE
|
Lipoprotein-releasing system ATP-binding protein LolD
|
Aromatoleum
|
MSEATNEPVLACEGLSKTFREGADALQVLDGVTLAVARGERIAIVGASGSGKSTLLHLLGGLDVPSAGAVRLHGRDFSRMSDAERGRVRNEALGFVYQFHHLLPEFSALENVAMPLYIRRMEREAANERAVAMLKEVGLGHRLDHAPGELSGGERQRAAIARALVTQPACVLADEPTGNLDRRTAQSVFDLMLSLNERLATSFIIVTHDEQLAGRAQRTLRLDDGRLA
|
Part of the ABC transporter complex LolCDE involved in the translocation of mature outer membrane-directed lipoproteins, from the inner membrane to the periplasmic chaperone, LolA. Responsible for the formation of the LolA-lipoprotein complex in an ATP-dependent manner.
|
Q5NZT6
|
Q8VZS0
|
PNC2_ARATH
| null |
Arabidopsis
|
MGVDLDLESISEATSGAIGSLLSTTILYPLDTCKSKFQAEIRVRGQQKYRYLSDVFWEAISSGNVLSLYQGLGTKNLQSFISSFIYFYSYSYFKRLHSQRIGSKSIGTKANLLIAAAAGACTSVLTQPLDTASSRMQTSEFGKSKGLWKTLTDGSWGNAFDGLGISLLLTSNPAIQYTVFDQLKQNLLEKGKAKSNKDSSPVVLSAFMAFVLGAVSKSAATVITYPAIRCKVMIQAADDSKENEAKKPRKRIRKTIPGVVYAIWKKEGILGFFKGLQAQILKTVLSSALLLMIKEKITATTWILILAIRTLFVTKARLKSP
|
Peroxisomal adenine nucleotide transporter catalyzing the counterexchange of ATP with AMP. ATP is needed by reactions that generate acyl-CoA for peroxisomal fatty acid beta-oxidation during postgerminative growth. Required for the beta-oxidation reactions involved in auxin biosynthesis and for the conversion of seed-reserved triacylglycerols into sucrose that is necessary for growth before the onset of photosynthesis.
|
Q8VZS0
|
A4XQK5
|
GATB_PSEMY
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Pseudomonas
|
MQWETVIGLEIHAQLSTQSKIFSASATSFGAEPNTQASLIDLGMPGTLPVLNAEAVRMAVKFGLAIDAHIAPQNVFARKNYFYPDLPKGYQTSQMDHPIVGKGHLDITLEDGTVKRIGITRAHLEEDAGKSLHEDFHGMSGIDLNRAGTPLLEIVSEPDIRSAKEAVAYVKAIHALVRYLGICDGNMAEGSLRCDCNVSVRPKGQEAFGTRAEIKNVNSFRFIEKAINHEIQRQIELIEDGGKVIQETRLYDPNKDETRSMRGKEEANDYRYFPCPDLLPVVIEQSFLDEVRSQLPELPTQKRERFQSQYGLSTYDASVLSASREMAEYFEEVAKVCGDAKLAANWVMGELSSLLNKEGLEIEQSPVSAEHLGGMILRIKDNTISGKIAKMVFEAMAAGEGSADAIIESKGLKQVTDSGAIEAMLDEVLAANAEQVEQYRASDEAKRGKMFGFFVGQAMKASKGKANPGQVNELLKKKLEG
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A4XQK5
|
Q9HIH2
|
PURA_THEAC
|
IMP--aspartate ligase
|
Thermoplasma
|
MVVPNGEGDKTAAVVGLQFGDEGKGKITDYLSGSYDVVVRFNGGTNAGHTVVTDEGTFKFHLLPSGSLRTSYVVLGSGMVIDPVALIPEIEIVRKINPALKIIISRNAHVVTKMHRQIDVEEEKIRSSLMIGTTAQGIGPTYEDKYARTGIRMVDISDIDLIKEKIETMYRMHSNLLANTEFSNLAKREEMAKEIYEAGIKLTGYLDYTEVAIDRLYSQGKRILFEGAQGVFLDPDFGFYPFVTSSNTISASVYTGTGFSLRKVNRIIGVAKAYVSKVGEGPFPTEITGDLAKQLRDLGGEYGTTTGRPRRVGWLDLPMLKYAVRIDDVDEIAITKVDTLGMLDTVKVCRQYLIDGKPIDYVPRDMNTIKKIEPVYDEFEGWGAISDSISGRKISIDQLPSKLVKYIKYIEDQVGKPIGIISMGKERNRTVRIIK
|
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.
|
Q9HIH2
|
B9JVV3
|
RS4_AGRVS
|
30S ribosomal protein S4
|
Agrobacterium
|
MSKRASSKYKIDRRMGENIWGRPKSPVNRREYGPGQHGQRRKGKLSDFGVQLRAKQKLKGYYGDLREKQFRATYDEANRRKGDTSENLIGLLESRLDAIVYRAKFVPTVFAARQFVNHGHVSVNGVKVNIGSYRCKAGDVIEVRQKSKQLAIVLEATQLAERDVPDYIEVDHNKMVATFVRVPTLSDVPYAVIMEPQLVVEFYSR
|
With S5 and S12 plays an important role in translational accuracy.
|
B9JVV3
|
Q8FFG3
|
FADI_ECOL6
|
Fatty acid oxidation complex subunit beta
|
Escherichia
|
MGQVLPLVTRQGDRIAIVSGLRTPFARQATAFHGIPAVDLGKMVVGELLARSEIPAEVIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARVLVDVNKARTMSQRLKLFSRLRLRDLMPVPPAVAEYSTGLRMGDTAEQMAKTYGITREQQDALAHRSHQRAAQAWSDGKLKEEVMTAFIPPYKQPLAEDNNIRGNSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLVPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTMSDLTLIDMHEAFAAQTLANIQLLGSERFARDVLGRAHATGEVDDSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAIVVEAE
|
Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed.
|
Q8FFG3
|
A4WMZ0
|
PSB2_PYRAR
|
Proteasome core protein PsmB 2
|
Pyrobaculum
|
MGEEVQIGATAVGIKAKDGVVLAAEKRVSYGFYTLSSAGRKVFVIDDKLAIASAGIIADMQSLARIVKINAKAYELETRKKPTVRSMAKLLSVIMFSRRYMPFFAEVLVGGVDEEGSHLIVMDPLGSLIEDNYAALGTGAKLAISVLDTGYREDITLQDAKKLAVKALKAAIERDPVSGGGIDLVLIDQTGAKEEEVKVQLLI
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
A4WMZ0
|
A8AV30
|
DEF_STRGC
|
Polypeptide deformylase
|
Streptococcus
|
MSVIEKLIKPAHLIDMRDIIREGNPTLRAVAEEVSFPLADEDILLGEKMMQFLHNSQDPVMAEKLGLRGGVGLAAPQLDISRRIIAVLLPNPEDENGNSPQEAYALKEVMYNPKIVAHSVQDAALADGEGCLSVDRDVPGYVVRHARVTVDYFDKNGEKHRVKLKGYKAIVVQHEIDHINGIMFYDRINETDPFAIKEGMLILE
|
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.
|
A8AV30
|
Q57837
|
Y392_METJA
|
Site-2-type intramembrane protease
|
Methanocaldococcus
|
MNYSIRLFKIMGIPIELHITFILFLVVIIGLSIMNNSIFWAVLFILLFVSVVLHELGHSYVAKKYGVKIEKILLLPIGGVAMMDKIPKEGELRIGIAGPLVSFIIGIVLLIVSQFFDININGYPLLYTLSLLNLMLGGFNLIPAFPMDGGRILRAILSKKYGYLKSTKIAANIGKSLALIMLLFGLLSMNIILILVSLFVYFGAEQESRVVEVETIFKNIKAKDIMTPNPVYVTPDMSIEEFLDFMLKHKYFGYPVVENGKLVGCIGIGNIHKKEGTVRDYMEKPVVVSEDTDIKEILRKMANTDRVFVVEGGKLKGIISKTDILRAMSILELKEELKD
|
A site-2 regulated intramembrane protease (S2P) that cleaves type-2 transmembrane proteins within their membrane-spanning domains; its endogenous substrate is unknown. Regulated intramembrane proteolysis (RIP) occurs when an extracytoplasmic signal triggers a concerted proteolytic cascade to transmit information and elicit cellular responses. A membrane-spanning regulatory substrate protein is first cut extracytoplasmically (site-1 protease, S1P), then within the membrane itself (site-2 protease, S2P, this enzyme), while cytoplasmic proteases finish degrading the regulatory protein, liberating the effector protein. Possible signals, S1P and substrates are unknown in this organism.
|
Q57837
|
Q1D0S8
|
MURD_MYXXD
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Myxococcus
|
MTLALSGQKVLVFGLAKSGVAALRLLRQQGADVTALDARGEDALGAVAHEVKALGATRVSGPTPPGLLASQDLVVVSPGVPLALPEIQAARAAGVAVWGEVELAGRMLSGVPLFGITGTNGKSTTTALTGTLFASGDKRTFVGGNLGRPFSEAAMSPGDWDALVVELSSYQLEGIRTLRPRGAAILNLTPDHIDRYPSHAAYGEAKARIFQNQQAGDFVVVNADDADVLGLARAAKAPVYGFSLTGKPVADAPALAGLAVVEPGGFRLAFLGEHYTLTNRALRGAHNAQNAMAAALLARLGGVASGAVQAGLDGYPGLPHRLESVRVLDGVEWVNDSKATNVDSVLVALRAFSQGVWLIAGGKGKGAPYAPMVEAGQGKVKGVLTIGDDADTLARAYAGAAQVHACGTLAHAVARARELAERGDTVLLSPACASFDQFKNFEDRGDSFKRLVEAL
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q1D0S8
|
A0R3C7
|
GLMU_MYCS2
|
Glucosamine-1-phosphate N-acetyltransferase
|
Mycolicibacterium
|
MTASTEAAVVVLAAGAGTRMRSDTPKVLHTLAGRGMLAHVLHTVSEIDARHLVAVLGHDRERIAPEVARLSEELGRAIDVAVQDQQLGTGHAVNCGLTALPHDFAGMVVVTSGDVPLLDTATLTGLITSHGSGDAAATVLTTTLPDPTGYGRILRTQDHEIIGIVEQADATESQRTICEVNTGVYAFDIADLRSALTRLRSDNAQHELYLTDVVEILRQDHRTVRALHVDDSALVTGVNDRVQLSDLGKVLNRRIVAAHQRAGVTIIDPGSTWIDIDVQIGQDTVVHPGTQLLGATRVGSHCVIGPDTTLTHVTVGDGASVVRTHGSESVIGAGATVGPFTYLRPGTNLGADGKLGAFVETKNCTIGTGTKVPHLTYVGDADIGEYSNIGASSVFVNYDGENKSRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVLRDDVPPGALAVSAGPQRNIEGWVAKKRPGSAADKAARKALGDES
|
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
|
A0R3C7
|
Q6NCM6
|
YBEY_RHOPA
|
Endoribonuclease YbeY
|
Rhodopseudomonas
|
MSQPRPGHRPDCNGADPDSNFASMTHSARPFTEVVIEADCWQAEASAEATVLRAIETAADAVDADTGGAELAVMLTDDDHIRQLNASFRGKDKPTNVLSFPAAQPEVQPDGAPRMLGDIAIAYQTVRREADDEGKPFDHHLSHLAVHGFLHLVGYDHETEEEAEEMEDAERAILARLGIPDPYAGQDRVS
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
Q6NCM6
|
P40614
|
MPCP_CAEEL
|
Phosphate carrier protein, mitochondrial
|
Caenorhabditis
|
MSVFSQLAESSKQNPFSLPVRSGNCASAVSAPGQVEFGSGKYYAYCALGGVLSCGITHTAIVPLDLVKCRIQVNPEKYTGIATGFRTTIAEEGARALVKGWAPTLLGYSAQGLGKFGFYEIFKNVYADMLGEENAYLYRTSLYLAASASAEFFADILLAPMEATKVRIQTSPGAPPTLRGCAPMIYKAEGLTGFYKGLPPLWMRQIPYTMMKFACFEKTVEALYQYVVPKPRAECSKAEQLVVTFVAGYIAGVFCAIVSHPADTVVSKLNQDSQATAGGILKKLGFAGVWKGLVPRIIMIGTLTALQWFIYDSVKVALNLPRPPPPEMPASLKAKLAAQQ
|
Transport of phosphate groups from the cytosol to the mitochondrial matrix.
|
P40614
|
Q8LPN5
|
AHL12_ARATH
|
AT-hook motif nuclear-localized protein 12
|
Arabidopsis
|
MDGREAMAFPGSHSQYYLQRGAFTNLAPSQVASGLHAPPPHTGLRPMSNPNIHHPQANNPGPPFSDFGHTIHMGVVSSASDADVQPPPPPPPPEEPMVKRKRGRPRKYGEPMVSNKSRDSSPMSDPNEPKRARGRPPGTGRKQRLANLGEWMNTSAGLAFAPHVISIGAGEDIAAKVLSFSQQRPRALCIMSGTGTISSVTLCKPGSTDRHLTYEGPFEIISFGGSYLVNEEGGSRSRTGGLSVSLSRPDGSIIAGGVDMLIAANLVQVVACSFVYGARAKTHNNNNKTIRQEKEPNEEDNNSEMETTPGSAAEPAASAGQQTPQNFSSQGIRGWPGSGSGSGRSLDICRNPLTDFDLTRG
|
Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
|
Q8LPN5
|
F4ZGF2
|
COMTA_DANRE
|
Catechol O-methyltransferase A
|
Danio
|
MLWVVLAVVVVLASVLVLLRQSSGLLALLWHDVVHQRLLNFFTGLSRPQRILKAVQKNATKGNPESVIAAIDHYCRHSEWAMNVGDEKGLILDSVVTEVNPSTALELGTYCGYSTVRIARLLSPGTKLITLEFNPDYAAIARQIIAYAGLQDKVILVEGPSGDLIPKMKQQHGIKSFDFVFLDHWKDRYVPDTKLLEECGLLRKGSVLLADNVICPGTPEYLKYVRNDPRYESRYFKSNLEYTKVEDGLEKSVFLG
|
Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Shows highest activity towards catecholestrogens and dobutamine. Also has lower activity towards L-DOPA, dopamine and epinephrine. Active towards the xenobiotic compounds methyl-DOPA, carbidopa, isoproterenol, and apomorphine.
|
F4ZGF2
|
P25312
|
COX2_SYMSY
|
Cytochrome c oxidase polypeptide II
|
Symphalangus
|
MAHAAQMGLQDATSPIMEELISFHDHALMIIFLISFLVLYALFLTLTTKLTNTNITDAQEMETVWTILPAIILVLIALPSLRILYLTDEINDPSFTIKAIGHQWYWAYEYTDYGGLIFNSYMLPPLFLEPGDLRLLEVDNRVVLPIEAPVRMMITSQDVLHSWTVPSLGLKTDAIPGRLNQTTFTATRPGVYYGQCSEICGANHSFMPIVLELIPLKIFEMGPVFTL
|
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.
|
P25312
|
Q63H62
|
ECFA1_BACCZ
|
Energy-coupling factor transporter ATP-binding protein EcfA1
|
Bacillus cereus group
|
MKKEKLRTENISFQYPGAATYALKDVSFSLFEGEWVSVIGQNGSGKSTLAKLLNGLFLPEAGTITVNDTMILSEETVWDVRKQIGMVFQNPDNQFVGTTVQDDVVFGLENIGMPREQMVERLNQALRLVRMEDFLNDEPHSLSGGQKQRVAIAGVLALQPSILILDEATSMLDPQGRREVVETVRQLVNEKGITVLSITHDLEEAAQSDRVIILNKGEILEEGIPEQIFKSSHMLQEIGLDVPFSVKIAELLKRNEILLQNTHLTMESLVNELWRLHSKK
|
ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
|
Q63H62
|
C1F638
|
RS19_ACIC5
|
30S ribosomal protein S19
|
Acidobacterium
|
MARSTKKGPFIDGHLMVKIEAMNQANDRKVVRTWSRRSTVHPDMVGHTIAVHNGKKFVPVYVTENMVGHKLGEFAPTRTFKGHAAKTESSSRAR
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
C1F638
|
O03890
|
COX2_CASBE
|
Cytochrome c oxidase polypeptide II
|
Casuarius
|
AICSLVLYLLTLMLMEKLSSNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEIDEPDLTLKAIGHQWYWTYEYTDFKDLSFDSYMVPTSELPSGHFRLLEVDHRVVVPMESPIRVIITAGDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSYMPIVVESTPLTHFENWSSLLSISSSL
|
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.
|
O03890
|
B8ZR59
|
RNPH_MYCLB
|
tRNA nucleotidyltransferase
|
Mycobacterium
|
MSTRADGRLDDELRAVVITRGFTEHPAGSVLIEFGHTKVMCTASPTEGVPRWRKGSGKGWLTAEYAMLPSATHTRSERESVKGRLSGRTQEISRLIGRSLRACIDLAALGENTIAVDCDVLQADGGTRTAAVTGAYVALADAVTYLSAAGRLLDPRPLSCAIAAVSVGVVDGRIRVDLSYEEDSRAEVDMNVIATDTGTLVEIQGTGEGATFPRSTLDKLLDMALGACDKLFVAQRDALALPYQGMSPEGPPPPKAFGS
|
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.
|
B8ZR59
|
A5UZQ2
|
IF2_ROSS1
|
Translation initiation factor IF-2
|
Roseiflexus
|
MSDMQISGYQSAINARHYIQFAGGGRGPGNPGGGRGPGNPGGGRGPGSPGGGRGPGSPGGGRGPGSPGGGRGPGNPGGGRGPGGGRGGGRGGDGRRRDESFVENEGGRGNRSGRTTSTATTARTPGGLARPTTTVRAPVRPKGPIALPVTMTVREFSEATGVGASEILKALLKAGVVANINQQIDYETAAVIAADFGIETVEYVPPQLEGVVENIRDVLAAQDPKDMKPRPPVVTIMGHVDHGKTKLLDAIRSTRVAESEAGGITQHIGAYQVELHGRKITFLDTPGHEAFTAMRARGAQVTDIVVLVVAADDGVMPQTLEAISHVKAAGVPMIVAINKIDAPNANPDRVRQQLANAGVIVEQFGGDVPSVEVSAKLKKNIDGLLEIILLVADLNEYKANPNAPAVGTIIEAEMDRTRGPVATVLVQNGTLRLEDNVLVGSTTGTIRTMFNDAGKRLRFAEPATPVVILGLHDVPQAGDILQVMPDLAVAREIALQRQRKQRLEAMATSRGVSLDGLFSSIQQGKIKELNIILKADVQGSIGAIEHALSQLNTDEVQIRIIHRGTGTITESDVNLAIASHAIIIGFNARPDPAARRQAEQYGVDIRFYNIIYQLTEDIKKAMIGMLEPEYREVTEGFAEVRNTFRLPTREIVAGLYVTEGKISRQYNVRVLRNGVVLHDGKIASLKRFKDDVREVQAGYECGLIVEGFNDITPGDTMEFYRRERVERTV
|
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.
|
A5UZQ2
|
Q1BLQ3
|
CHEB3_BURCA
|
Protein-glutamate methylesterase/protein-glutamine glutaminase 3
|
Burkholderia cepacia complex
|
MNIGIVNDLPLAVEALRRVIALRADHRVLWVATDGDEAVDFCVAHPPDVVLMDLVMPKVDGVAATRRIMARAPCAILIVTASVSANTSSVYEAMGAGALDAVDTPTLALGLSTDASPQALLAKIDQIGRLLESRTTALVPPGPAPTRGQPTLVAIGASAGGPTALTALLRALPADFPAAIVIVQHVDQAFAYGMAEWLDGYTRLPVRVARQGSVPEAGAVLLAATNDHLMLSPRGVLGYTRHPAETPYRPSIDVFFNSVADGWQGDALGVLLTGMGRDGALGLKAMRAKGCYTIAQDQATSAVYGMPKAAAAIGAASAILPLDQIAPQLIARIALTSRD
|
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.
|
Q1BLQ3
|
Q49Z29
|
CSHA_STAS1
|
DEAD-box ATP-dependent RNA helicase CshA
|
Staphylococcus
|
MQNFKELGISDKMAETLQSMGFNEATPIQKESIPLALEGKDVLGQAQTGTGKTGAFGIPLIEKVADQEGVQSLILAPTRELAMQVAESLKAFAKGQNIQVVTVFGGMPIDRQIKALKKGPQIVVGTPGRVIDHLNRRTLKTNDIHTLILDEADEMMNMGFIDDMKFIMDKIPAEQRQTMLFSATMPKAIQTLVQQFMKSPVIVKTMNNEMSDPQIEEYYTIVKELEKFDTFTSFLDVHQPELAIVFGRTKRRVDELTSALISKGYKAEGLHGDITQAKRLEVLKKFKNDQLDILVATDVAARGLDISGVSHVYNFDIPQDTESYTHRIGRTGRAGKKGVAITFVNPIEMDYIRQIEQANKRQMTALRPPHRKEVLKARENDIKGKVQNWMSRDNEPRLQRIATELLGEYNDVDLIASLLQELVESNDEVDVQLTFEKPLSRGKGRQGKGGPKRGGNHKRGGGKFDNKNRRSGKGGFNNKKKNDRPSSDRNNNKKSMKGRTFADHKK
|
DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.
|
Q49Z29
|
C0ZXR9
|
RIMM_RHOE4
|
Ribosome maturation factor RimM
|
Rhodococcus erythropolis group
|
MELVVGRVAKSHGIKGELVVEVRTDEPEDRFAVGSVLRGRKPRESTLKSYTVEAARDHSGRLLLRLEGVSDRGDADALRGTLFVIDSSELEPSDDPDEFYDHELEGLKVVLTDGTEVGSVIEVLHSAAGELLSIRRTGETSGELLIPFVAAIVTSVSIADGVVMIEPPEGLLDPDFGDKSNSDNSNSDND
|
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.
|
C0ZXR9
|
Q40301
|
FCPE_MACPY
|
Fucoxanthin-chlorophyll a-c binding protein E, chloroplastic
|
Macrocystis
|
MAIACAAAPGLRGAEPFNGAALATSAKSSSAMKMSFESEIGAQPPIGFWDPLGLVADADQERFDRLRYVEIKHGRIAMLAVVGHITQQNTRLPGMLSFKENLAFADSPNGVAAFSKIPPLGTLQIILAIGCHELFVVKQVEGSFPGDCTTGGNIFQSAWDNMSEETQASKRAIELNNGRAAQMGILAMMVHEQLSNQPYIINDLAGAAYQFN
|
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power.
|
Q40301
|
Q1GTA2
|
PYRE_SPHAL
|
Orotate phosphoribosyltransferase
|
Sphingopyxis
|
MTDDQILAEFRAADALLQGHFLLSSGRHSEYYLQCARVLMDTERAGRLAAALAAKLPRELKQAIDLVVSPAMGGVIIGHEMGRALGKPAIFVERPTGTFELRRGFTIDPGAKVLMVEDVVTTGLSSREAMEAVRAAGGEVVAEAALVDRSAGSNIDLGVPFYPLVAINFPTYAADELPPELAGTEAIKPGSRSVAA
|
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
|
Q1GTA2
|
A7GW12
|
RF1_CAMC5
|
Peptide chain release factor 1
|
Campylobacter
|
MFADKLRPFLDRYNEISALLGDPNIINDIEKMTKLSKEQSSIEPIKNAASQYLQTLDDIEENKALLDDAELGELAREELKSAQIRKEELENEIKILLLPKDPNDDKNIFLEIRAGTGGDEAALFVGDLFNAYIRYADLRGYKFEIVSQSEGSAGGFKEIILLIKGKGAYSRLKFEGGTHRVQRVPETESQGRVHTSAVTVAIMPEVEDSEIEINPNDLRIDVMRSSGHGGQSVNTTDSAVRITHIPTGLVVTNQDGKSQHKNKEAAMKVLKARLYEMQEAERIAKETSERKSQVGTGDRSGRIRTYNFPQNRISDHRINLTLYRLDAIMAGGLFDEIIEPLIAHHQAEAITDAGL
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
A7GW12
|
A1RWR7
|
RL18_THEPD
|
50S ribosomal protein L18
|
Thermofilum
|
MARGARYRVPLKRRREGKTNYYKRRKLIISGKPRLVVRVLSRTAIVQIAKATPKGDVVIASAHSNELKKYGWKGYRRNTPALYLLGFLAAKKALKQGVTEAIVDIGLHRPVKASRVFAAVKGALDAGLKIPVGDGVLPEDDRVRGEHIANYAKMLKESNPELFKLRFSGYLSAGLDPESLPEHFDSVKQKIEEALQ
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
A1RWR7
|
A6VKC5
|
RPOB_ACTSZ
|
Transcriptase subunit beta
|
Actinobacillus
|
MGYSYTEKKRIRKDFGKRSQVLNVPYLLTIQLDSFDKFIQRDPDGQQGLEAAFRSVFPIVSNNGSTELQYVSYKLGEPVFDVRECQIRGTTFAAPLRVKLRLVSYDKDAAPGTVKDIKEQDVYMGEIPLMTDNGTFVINGTERVIVSQLHRSPGVFFDSDKGKTHSSGKVLYNARIIPYRGSWLDFEFDPKDNLFARIDRRRKLPATIILRALNYTTEEILDLFFDKVVFEIQGDKLLMELVPERLRGETATFDIEAEGKVYVERGRRITARHIKALEKDGVKKVEVPTEYIIGKVAAKDYVDLESGEVICAANTEISLELLAKLAQAGYTAIEALFTNDLDFGPYISETLRVDPSCDRLSALVEIYRMMRPGEPPTKEAAEGLFDNLFFSQERYDLSAVGRMKFNRSLGIDSETGSGVLSKEDIVSVMKKLIDIRNGRGEVDDIDHLGNRRIRSVGEMAENQFRIGLVRVERAVKERLSLGDLDAVTPQDLINAKPISAAVREFFGSSQLSQFMDQNNPLSEVTHKRRISALGPGGLTRERAGFEVRDVHPTHYGRVCPIETPEGPNIGLINSLSVYARTNDYGFLETPYRKVVNGQVTEEIEYLSAIEEGKYIIAQANANLDDDFRFTDTFVTARGEHGESGLYRPEEIHYMDVSTQQVVSVAAALIPFLEHDDANRALMGANMQRQAVPTLRADKPLVGTGMEKPIALDSGVAVVAKRGGTIQYVDASRIVVKVNEDETIPGEAGIDIYNLIKYTRSNQNTCINQIPCVNLGEPVGRGEILADGPSTDLGELALGQNIRVAFMPWNGYNFEDSMLVSERVVQQDRFTTIHIQELSCVARDTKLGAEEITADIPNVGEAALSKLDESGIVYVGAEVKGGDILVGKVTPKGETQLTPEEKLLRAIFGEKASDVKDSSLRVPNGTSGTVIDVQVFTRDGVEKDKRALEIEEMQLKQAKKDLVEELEILEAGLFSRVRNLLVDGGISEKELDTMERAKWLEQTLSSESKQSRLEQLAEQYEELRKDFEHKLEVKRSKIIQGDDLAPGVQKVVKVYLAVKRQIQPGDKMAGRHGNKGVISKINPVEDMPYDENGRPVEIVLNPLGVPSRMNIGQILETHLGLAAKGIGEQINIMLKQKQDIEKLRGYIQKAYDLGGGSQVVDLNTFTDEEVLRLAENLRKGMPLATPVFDGADESEIKGLLELGGLPTSGQITLYDGRTGEKFERPVTVGYMYMLKLNHLVDDKMHARSTGSYSLVTQQPLGGKAQFGGQRFGEMEVWALEAYGAAYTLQEMLTVKSDDVNGRTKMYKNIVGGTHYMEPGTPESFNVIMKEIRSLGLNIDLDEA
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A6VKC5
|
B2T1N9
|
HSLV_PARPJ
|
ATP-dependent protease subunit HslV
|
Paraburkholderia
|
MEQFHGTTIVSVRRGDKVALGGDGQVTLGNIVMKGGAKKVRRIYNGKVLVGFAGGTADAFSLLDRFEAKLEKHQGNLTRAAVELAKDWRTDRMLRRLEAMLITADATTTLVITGNGDVLDPEGGICAIGSGGAYAQAAATALAHNTELSPREIVEKSLEIAGDMCIYTNHNRVIETIE
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
B2T1N9
|
Q318I8
|
RS19_PROM9
|
30S ribosomal protein S19
|
Prochlorococcus
|
MGRSLKKGPFIADSLLKKVEKQNTDNDKSVIKTWSRASTILPLMIGHTIAVHNGKTHIPVFITEQMIGHKLGEFAPTRTYRGHIRDKKGAKS
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q318I8
|
A5GI59
|
PSAC_SYNPW
|
PsaC
|
unclassified Synechococcus
|
MSHAVKIYDTCIGCTQCVRACPLDVLEMVPWDGCKAGQIASSPRTEDCVGCKRCETACPTDFLSIRVYLGDETSRSMGLSY
|
Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with PsaA/B/D and helps assemble the protein into the PSI complex. Required for binding of PsaD and PsaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn.
|
A5GI59
|
P00468
|
NIFK_NOSS1
|
Nitrogenase component I
|
Nostoc
|
MPQNPERTVDHVDLFKQPEYTELFENKRKNFEGAHPPEEVERVSEWTKSWDYREKNFAREALTVNPAKGCQPVGAMFAALGFEGTLPFVQGSQGCVAYFRTHLSRHYKEPCSAVSSSMTEDAAVFGGLNNMIEGMQVSYQLYKPKMIAVCTTCMAEVIGDDLGAFITNSKNAGSIPQDFPVPFAHTPSFVGSHITGYDNMMKGILSNLTEGKKKATSNGKINFIPGFDTYVGNNRELKRMMGVMGVDYTILSDSSDYFDSPNMGEYEMYPGGTKLEDAADSINAKATVALQAYTTPKTREYIKTQWKQETQVLRPFGVKGTDEFLTAVSELTGKAIPEELEIERGRLVDAITDSYAWIHGKKFAIYGDPDLIISITSFLLEMGAEPVHILCNNGDDTFKKEMEAILAASPFGKEAKVWIQKDLWHFRSLLFTEPVDFFIGNSYGKYLWRDTSIPMVRIGYPLFDRHHLHRYSTLGYQGGLNILNWVVNTLLDEMDRSTNITGKTDISFDLIR
|
This molybdenum-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation.
|
P00468
|
Q5RBD9
|
TBCE_PONAB
|
Tubulin-folding cofactor E
|
Pongo
|
MSDTLTADVIGQRVEVNGEHATVRFAGVVPPVAGPWLGVEWDNPERGKHDGSHEGTVYFQCRHPTGGSFIRPNKVNFGTDFLTAIKNRYVLEDGPEEDRKEQIVTIGNKPVETIGFDSIMKQQSQLSKLQEVSLRNCAVSCAGEKGGVAEGCPNIRKVDLSKNLLSSWDEVIHIADQLRHLEVLNVSENKLKFPSGSVLTGTLSALKVLVLNQTGITWAEVLRCAMGCPGLEELYLESNNIFISERPTDVLQTVKLLDLSSNQLIDENQLYLIAHLPRLEQLILSDIGISSLHFPDAGIGCKTSLFPSLKYLVVNDNQISQWSFFNELDKLPSLRALSCLRNPLTKEDKEAETARLLIIASIGQLKTLNKCEILPEERRRAELDYRKAFGNEWKQAGGHKDPDKNRLSEEFLTAHPRYQFLCLKYGAPEEWELKTQQPLMLKNQLLTLKIKYPHQLDQKVLEKQLPGSMTIQKVKGLLSRLLKVPVSDLLLSYESPQKPGVEIELENDLKSLQFYSVENGDCLLVRW
|
Tubulin-folding protein; involved in the second step of the tubulin folding pathway and in the regulation of tubulin heterodimer dissociation. Required for correct organization of microtubule cytoskeleton and mitotic splindle, and maintenance of the neuronal microtubule network.
|
Q5RBD9
|
A5UBP1
|
UPP_HAEIE
|
UPRTase
|
Haemophilus
|
MKLVEVKHPLVKHKLGVMREAEIDTKKFRELATEIGSLLTYEATSDLETEKVTINGWNGPVEIDRIKGKKVTVVPILRAGLGMMDGVLEHVPSARISVVGIYRNEETLEPVPYFQKLASDLEERLSIVVDPMLATGGSMIATLDLLKAKGCKHIKVLVLVAAPEGIKALEAAHPDIELYCASIDSHLNEQGYIIPGLGDAGDKIFGTK
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
A5UBP1
|
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