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2.75k
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5.51k
AlphaFoldDB
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P56892
CYSD_RHIME
Sulfate adenylate transferase
Sinorhizobium
MPHTLPETELHNPQSTKPPLDPHLKALENEAIHIFREVAAEFERPVMLYSIGKDSSVLLHLARKAFYPGRIPFPLLHVDTGWKFREMIAFRDEMVAKYDLDLVAHTNPRGAAENVTPFTHGSALYTDIMKTEALRQALDAGQYDAAFGGARRDEEASRAKERIYSFRTPDHRWDPRNQRPELWNVYNGMIRKGESVRAFPLSNWTEVDIWRYIQAEDIPIVPLYFAKKRPVVERDGMLILAEDPRLELLPGEVKREEVIRFRTLGCFPLTGAIRSEADTLDDIIAELETATVSERQGRAIDRDQAGSMEKKKREGYF
With CysN 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.
P56892
B7USC8
ASTA_ECO27
AOST
Escherichia
MMVIRPVERSDVSALMQLASKTGGGLTSLPANEATLSVRIERAIKTWQGELPKSEQGYVFVLEDSETGTVAGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPEWRKEGNGYLLSKSRFMFMAAFRDKFNDKVVAEMRGVIDEHGYSPFWQSLGKRFFSMDFSRADFLCGTGQKAFIAELMPKHPIYTHFLSQEAQDVIGQVHPQTAPARAVLEKEGFRYRNYIDIFDGGPTLECDIDRVRAIRKSRLVEVAEGQPAQGDFPACLVANENYHHFRVVLVRTDPATERLILTAAQLDALKCHAGDRVRLVRLCAEEKTA
Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine.
B7USC8
P30516
1B01_SAGOE
Class I histocompatibility antigen, B alpha chain
Saguinus
MTVMAPRTLLLLLSGALVLTETWAGSHSMRYFSTAVSRPGREEPRYIEVGYVDDTQFVRFDSDAASPRMEPRAQWVEKEGREYWEEETQRAKAFAQTFRVNLQTALGYYNQSEAGSHTIQMMSGCDLGPDGRLLRGYDQHAYDGKDYISLNEDLRSWTAADVAAQITQRKWEAANEAERTRAYLEGTCVEWLHRYLENGKETLQRAEPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDMELVETRPTGNGTFQKWAAVVVLSGEEHRYTCHVQHEGLPEPLTLRWEPPSQPTIPIMGIVAILAILGAVVTGAVVTAVMWRKKSSDKKGGSYSQAARSDSAQGSDVSLTACKV
Involved in the presentation of foreign antigens to the immune system.
P30516
Q74IS9
RBFA_LACJO
Ribosome-binding factor A
Lactobacillus
MKHRIGRVEGEILRELTKILRKDIRDPRLNDVTITAVECTNDLSYATVYYSMLTDDPAKEKEVAEGLDKAKGMMRHLLGQTLTVYKVPELIFKRDTSVAYGSKIDKLINQVKKQDQERENKNK
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
Q74IS9
Q7NFA4
ISPG_GLOVI
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Gloeobacter
MQTLDPVTPALLPLRRVTRPVQVGALTIGGNAPVVVQSMINEDTLDTPGAVAAIRALHKAGCELVRVTVPSLAHARALERIRKTLEDTYRPVPLVADVHHDGGPIALEVARHVDKVRINPGLFVFRRARLGDYTAEDVERARAQIREELKPLVDVLGAQDKAMRIGVNHGSLSERMLYIHGDTPEGMVQSAVEFVEICEQLGYHNLVISLKASRVPVMIAVYRLAAKLLDARGMHYPFHLGVTEAGDGEYGRIKSTAGIATLLADGIGDTIRVSLTEDPLKEIPVCYGILQALGLRRTMVEYVACPSCGRTLFNLETVLHRVREATRHLTGLNIAVMGCIVNGPGEMADADYGYVGKTPGTISLYRGREEIKKVPEARGVEALVDLIKSDGRWVDP
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q7NFA4
P46278
CCNB2_MEDSV
CycMs2
Medicago
MVNTSEENNSNAVMPRKFQGGMNQVGHGGGRIVGQNRRALGGINQNFVHGRPYPCVVHKRVLSEKHEICEKKQADLGHRPITRRFAAKIAGSQQSYAEKTKNSNPLNLNEFGNSIAIDDELKSPEDQPEPMTLEHTEPMHSDPLEMEEVEMEDIEGEMILDIDSCDANNSLAVVEYIEDLHAYYRKIEYLGCVSPTYMDEQLDLNERMRAILVDWLIEVHDKFDLMQETLFLTVNLIDRFLAKQNVVRKKLQLVGLVAMLLACKYEEVSVPVVSDLIHIADRAYTRKDILEMEKLMLNTLQYNMSLPTAYVFMRRFLKAAQADKKLELVAFFLVDLSLVEYEMLKFPPSLVAAAAVYTAQCTVSGFKHWNKTCEWHTNYSEDQLLECSMLMVGFHQKAGAGKLTGVHRKYGSAKFSFTAKCEPACFLLENKNQP
Essential for the control of the cell cycle at the G2/M (mitosis) transition.
P46278
P19112
F16P1_RAT
Liver FBPase
Rattus
MVDHAPFETDISTLTRFVLEEGRKAGGTGEMTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQVKKLDILSNDLVINMLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAGYALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTEDVQEFLEIYNKDKAKSRPSLPLPQSRARESPVHSICDELF
Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.
P19112
P52201
PUR8_SPICI
Adenylosuccinase
Spiroplasma
MIERYFVTEIGKIWSDENKYNTWAKVELLVCEGWAQIGLIPPTDIEKIKTNLTVNLPRMLELEAETKHDVVAFTRMLSETLGPEKKWI
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
P52201
A3NX99
HUTI_BURP0
Imidazolone-5-propionate hydrolase
pseudomallei group
MKSILWHNLKLCAHGDPNDTIADAAIAVNGDGTIAWTGRASDVPAGYVHWPREDLRGAWVTPGLVDCHTHLVYGGQRADEFAQRLAGASYEEIAQRGGGIVSTVRATRDASEAALFEQACARLRPLLAEGVTAIEIKSGYGLELASERRMLRVARQLGERFPVSVYTTFLGAHALPPEYAGRADEYIDEVCERMLPALADEGLVDAVDVFCERIGFTLAQSERVFEAAARRGLPVKMHAEQLSNGGGSALAARYRALSADHLEYLDAAGVAAMRASGTTAVLLPGAYYFIRETKLPPIDLLRRHGVPIALATDHNPGTSPLTSLLLTMNMGCTVFKLTVQEALLGVTRHAAAALGASDRHGSLAPGRQADFAVWSVSTLAELAYWFGRPLCERVVKGGVTVFTRDAR
Catalyzes the hydrolytic cleavage of the carbon-nitrogen bond in imidazolone-5-propanoate to yield N-formimidoyl-L-glutamate. It is the third step in the universal histidine degradation pathway.
A3NX99
Q6CZT2
PLY3_PECAS
Pectate lyase III
Pectobacterium
MKYLLPSTAAGLLLLAAQPTMAANTGGYATTDGGNVAGAVNKTARSMQDIIDIIEEAKLDSKGKKVKGGAYPLIITYNGNEDALIKAAENNICGQWSKDARGVEIKEFTKGVTIIGTNGSSANFGIWLTKSSDVIIRNMRFGYMPGGAQDGDAIRIDNTPNVWIDHNEIFAKNFECQGTKDGDTTFESAIDIKKASTNVTVSYNYIHGIKKVGLSGFSSSDTGRDLTYHHNIYDDVNARLPLQRGGQVHAYNNLYTGITSSGLNVRQKGIALIERNWFENAKNPVTSRYDGSNFGTWELRNNNIMSPADFAKYNITWDKDTKAYVNAEDWKSTGTFASVPYSYSPVSPQCVKDKLANYAGVNKNLAVLTAANCN
Involved in maceration and soft-rotting of plant tissue.
Q6CZT2
Q1QUF9
CYSN_CHRSD
Sulfate adenylate transferase
Chromohalobacter
MSHQSSLIAEDIESYLQEHEQKDLLRFITCGSVDDGKSTLIGRLLHDSKMIYEDQLAAITQASRTSGTTGDQVDLALLVDGLQSEREQGITIDVAYRYFSTDKRKFIIADTPGHEQYTRNMATGASTASLAVILIDARHGVQTQTRRHSFIADLLGIQHLVIAVNKMDLVDYSQARFDEIVAEYREFAAKLNAPDIHFVPLSALEGDNVVNKSEAMSWYEGPALLHLLETVEVTHDKNLTDLRLPVQYVNRPHLDFRGYCGTLEAGILRPGQRVKVLPSGKASTVARIVTFDGDLEEAYPGQAITVTLDDEIDISRGDWLVAEDAEVPLADAFEADIVWMHDTALEPGRLYDLKLATRDLAGKITRIDYQTDVNTLEHHAAERLALNAIGRCRVEVAGTLPVDDYRVSPGTGSFIVIDRMTNVTVGAGMVRGAAEGAGNTGEVDWQAFEIEFNALIRKHFPHWEAKDVRSLFGQ
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.
Q1QUF9
C4Z2R3
RL7_LACE2
50S ribosomal protein L7/L12
Lachnospira
MTTQEIIEVIKGLSVLELNDLVKACEEEFGVSAAAGVVVAAAGAGAAAAEEKTEFDVELTEAGDQKVKVIKVVREITGLGLKEAKDVVDGAPKVVKEQASKEEAEEIKKKLEEVGAKVTLK
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
C4Z2R3
Q34653
CYB_ANTRB
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Antigone
MAPNLRKSHPLLKMINNSLIDLPTPSNISAWWNFGSLLGICLATQILTGLLLAAHYTADTTLAFSSVAHTCRNVQHGWLIRNLHANGASFFFICIYLHIGRGLYYGSYLYKETWNTGVILLLTLMATAFVGYVLPWGQMSFWGATVITNLFSAVPYIGQTLVEWAWGGFSVDNPTLTRFFTLHFLLPFMIMGLTLIHLTFLHESGSNNPLGIVSNCDKIPFHPYFSLKDILGFMLMLLPLMTLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAILRSIPNKLGGVLALAASVLILFLAPLLHKSKQCTMTFRPFSQLLFWTLTANLLILTWVGSQPVEHPFIIIGQLASLTYFTILLILFPIIGALENKMLNY
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q34653
Q3JCW1
DER_NITOC
GTP-binding protein EngA
Nitrosococcus
MNALVALVGRPNVGKSTLFNRLTRSRDALVVDQPGVTRDRKYGLAHYGEQSFFVVDTGGVMEQESGIGRLMRAQAQLAIEEADVIFFLVDGREGLSSLDEEIAAWLRCAQKPLKLVINKAEGRDGDLVASEFYRLGLGEPIIISAQQGQGVGRLLEALLTLLPVLEREESEIQAKGLQFAVIGRPNVGKSTLVNRILGEERVLSSEIPGTTRDSISIPFRHHGKDYTLVDTAGIRRRSRILDKVEKFSVIQSLQSIAIAQVVILVIDAHDSVVEQDLHLAGVILESGKGVVIAVNKWDGLPLEQRQRVKTDLDRRLPFLVFARIHFISALHGSGVGDLFPSIDEAYQSANSHLPTGELNRALLAAVEKYPPPVVKGRRIKLRYAHQGGQNPPKIIIHGNQAEAVSANYRRYLINYFRNAFGLMGTPIALEFRTVKNPFKGRANILTQRQQQKRKRLVRFRKGRD
GTPase that plays an essential role in the late steps of ribosome biogenesis.
Q3JCW1
B8E6W2
NRDR_SHEB2
Transcriptional repressor NrdR
Shewanella
MHCPFCSATDTKVIDSRLVAEGHQVRRRRECTECHERFTTFEGAELVMPRVIKRDGSRQPFDEEKLQGGMLRAVEKRPVSMDEIEQALSKIKSTLRATGEREVPSEMVGNLMMEQLMSLDKVAYIRFASVYRAFEDVSEFGEAIAKLQK
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
B8E6W2
Q5E305
SDHE_ALIF1
FAD assembly factor SdhE
Aliivibrio
MYSAEEKARVKWACRRGMLELDVVIMPFFDECFEELTEAEQQAFVSLLECDDPDLFTWVMGHGRSDNLAHASMVDKIVEHNLSKLR
An FAD assembly protein, which accelerates covalent attachment of the cofactor into other proteins. Plays an essential role in the assembly of succinate dehydrogenase (SDH, respiratory complex II), an enzyme complex that is a component of both the tricarboxylic acid cycle and the electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Required for flavinylation (covalent attachment of FAD) of the flavoprotein subunit SdhA of SDH and other flavinylated proteins as well.
Q5E305
A0Q5M5
SYS_FRATN
Seryl-tRNA(Ser/Sec) synthetase
Francisella
MLDAKYIKDNLQQVAEKLATRGYQFDIAEFEAQEQKRRHLQERTQDLQSQRNTISKEIGQKKAKGEDTSDIFAKVNQINEELKIIEKELKDLQDTINQTLLSMPNLPADDVPVGKDENDNVEIRRWGTPREFHPEAPAKDHADIGEILKMIDFKAAAKVTGSRFMVLKNKIAKLHRALSQFMLDLHTEKHGYEELYVPYLVNNDSLYGTGQLPKFAADLFKLEGDFEYSLIPTAEVPITNLVRDEILDTETLPRYYTAHTPCFRSEAGSYGRDTKGMIRQHQFEKVELVHITAADKGEESLELLTSHAEKVLQKLNLPYRVMKLCTGDMSFSAKKTYDLEVWLPSQNTYREISSCSWCGDFQARRMKARHKNPSMKKPELVHTLNGSGLAVGRTLLAIIENYQQEDGSIMVPDALIKYMGGISVIK
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
A0Q5M5
Q8Z327
RSD_SALTI
Regulator of sigma D
Salmonella
MLNQLENLMERVGGSNKLVDRWLDVRKHLLVAYYNLVGIKPGKESYMRLNEKALDDFCQSLVDYLSAGHFSIYERILHKLEGNGQLLHAAKIWPLLEDNTQRIMDYYDTSLETAIDHDNCLEFQQALSDIGEALEARFVLEDKLIMLVFDAMHDGARVKRPA
Binds RpoD and negatively regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with the catalytic core of the RNA polymerase and with promoter DNA. May be involved in replacement of the RNA polymerase sigma subunit from RpoD to RpoS during the transition from exponential growth to the stationary phase.
Q8Z327
A7H2A2
TRMB_CAMJD
tRNA(m7G46)-methyltransferase
Campylobacter
MPNFKSKKIKEINLPYSKDDVEFLWFAKNDNVSLIYTKVQEESFFLQIKKAQNGFVIKGDKHTKPSKIGYLQKALKIFKEGFCEDIINEAFGLKNNALIEKTPFIVDNFDELLSKLQGKIYIEIGFGSGRHLLYQAKENPNVLILGVEIYNPALTQVAKLAKAQNVNNILLIQSDARLLLSVLKSKSVEKIFLHFPVPWGKKPHRRVIGKDFCKECARVLVQNGRFELRTDSFEYFNFTLEQFLTFPAPKFSLRKNENLEISSKYEDRWKKQEKNIYDLWVWNFNQECQNYELNEFNLSSVEFSKEDLKKIEQNFKNITIKKDDFFLHFESIYKQDENLLLKVAFGAFNKSEHCYLHLDKTIDFAFKEPFKIQENIKAINELKEILKVQFKI
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
A7H2A2
P01709
LV208_HUMAN
Ig lambda chain V-II region MGC
Homo
MAWALLLLTLLTQGTGSWAQSALTQPPSASGSPGQSVTISCTGTSSDVGGYNYVSWYQQHPGKAPKLMIYEVSKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYAGSNNF
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition . Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens . The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen .
P01709
Q8KHS0
REBO_LENAE
L-amino acid oxidase protein
Lentzea
MSRGHKKITVLGAGVAGLVAAHELEELGHEVEVLEGSDRLGGRVHTHRFGEGGSVPFVELGAMRIPTKHRHTIDYIGKLGLTPKLKEFKTLFSDDGAYHTTSAGFVRVRDAAKVLVDEFRLLMSGRDLREETILFGAWLTAVGDAIAPADFRAALRTDFTADLLEVVDRIDLDPFLVGAARDQFDLHAFFAAHPEVRTSCTGKLNRFVDDILDETSPRLLRLEGGMDQLVDALVERIRGDIRTGHEVSAIDVREDHVAVTVHNGHGVNTLRSDHVLCTIPFSVLRNLRLTGLSTDKLEIIHDVKYWSATKVAFRCREPFWERDGINGGASFGGGRIRQTYYPPVEGDPTRGAVLLASYTMGDDADVLGGMPEAQRHEVVLDEVGRMHPELHEPGMVVEAVSRAWGEDRWSNGAGVTRWGKDVAACEEERDRAARPEGRLYFAGEHCSSTTAWIDGAVESALAAVRAIEAGDGR
Involved in the biosynthesis of the indolocarbazole antitumor agent rebeccamycin. It generates the imine form of 7-chloroindole 3-pyruvate (7Cl-IPA) from 7-chloro-L-tryptophan (7Cl-Trp), with concomitant two-electron reduction of O(2) to H(2)O(2). The enzyme is also active with L-tryptophan as substrate.
Q8KHS0
Q82FB5
AZOR_STRAW
FMN-dependent NADH-azoreductase
Streptomyces
MATLLHIDSSVFPSAASASRAVAETFRTAWQEQHPDGTVIYRDLSANPVPHITADAHTAGFADPATHTPGQAAAFAEREKLIAELEQADAVLIGAPMYNYAIPSTLKAWLDNVILMGRTAANENSKVTGTPVTVIASRGGSYAPGTPREPYEYVQNYLKAVLSDALGLELEFIVPELTMAAHNPAMSELVPLAEASRAKAHEDAAAKAKELADRFAA
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
Q82FB5
Q7SFC8
ROK1_NEUCR
DEAD box RNA helicase 16
Neurospora
MDIFKVLSRGIKAQPKKNQPGAPQLLPSAGAKVNPQFFHDNVGGANAKRGKKRKRKGAQANNATESGDEDDDASDVDYFAPKPTPEELAAKKDAELKADEPKKQKPKLLEENECRQILKSHRLKFTVLAGRVPQDEAATEEKPPKKQKKQKEDRKKQEEEEKKKKKKDEDKKQIYPQPLNSFGELKYTYGIHPVLADNITRQGFRVPTEVQMGSLPLQLRPEMALEKATDVEDVKVEKGIDFLGVAPTGSGKTISFLIPAIDAIIKRRAEDYTPETDEHVLQAIVVAPTRELASQIVNEGRKLAIGTGVRVVLMKRTLRLVAESNEQEETEQEAKEEVQDSDSDSEAESEPEEVMKIDEEEEEEEESDSDAEKKTESRAKGDQKFKKERPITRVDILVTTPKILLNFLCGGEKEKGKPRIIKKTLPTVQSLILDEADVLLDPIFRKQTMGIWRACTHPNLGMTCWSATMASNIEALLTKHIDKRAKRTPEQTPKPLIRLVVGLKDTAVPNITHKLIYTATEPGKLLALRQLLHPVSSADSGPPLRPPFLVFTQTIERAQALHDELKYDIPLEAGGSARVAVLHSSLPDSVRSKIMARFRSGEVWVLITTDVLARGVDFAGVNGVVNYDVPVSAAAYVHRAGRTGRAGREGGVAVTFYTKDDIPFVKSVANVIAMSEKQAGKDIDEKDTVKAAQGSVQKWLLDALPKVAKEDKRKLKVRGVESRRTGGKATITTKSSWERRRENNRREAIEASKRRKREAQKAQKEGGAAPEKAEEEWTGLD
ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.
Q7SFC8
Q9JK30
ORC3_MOUSE
Origin recognition complex subunit Latheo
Mus
MHTGPRTMATSSVSKGCFVFKPDFKKRKVFVPIEDYFNNEELDSEDSKLRFETYSLLWQRMKSETEQLQEELNENLFDNLVDFLQKSHPEFQKNSRDWGSQMKFREIPTAALILGVNVTDHDVILRSLTETLQNNVTPYVVSLQAKDCPDVKHFLQKFTSQLMDCCVDRHSKEVTSGKALKKTNYSMDSLCSWYSAVTQKADHKVTIKKRTASGHWRSPPVVLILKSMESFTSKVLQDFITISSQHLHEFPLILIFGIATSPVIIHRLLPHSVSSLLCVELFQSLSCEQHLTVVLDKLLLTPQFPFKLSKKALQVLTNIFLYHDFSIQSFIKGIKLSLLEHFYSQPLSVLCCDLSEAKKRVNVFSVSQCENIRRLPSFRRYVENQPLGKQVALLTNETFLKEKTQSLLEDLHVYHINYFLVLRCLHNFTSSLPKYPLGRQIRELYCTCLEKKIWDSEEYKSALQLLRMLAKDELVSILQRCIEVLDSSTEKQLGNTTQKIKDFLTQFQNLDADSKEEEDACGSQPKGLQKTDLYHLQKSLLEMKELRRTKKPTKFEMLRENVMNFIDNLVRDYLLPPESQPLHEVVYFSAANTLREHLNAAPRIALHTALNNPYYYLKNEELEGCIPNTAPDICIAYKLHLECSLLINLVDWAEAFATVVTAAEKMDANSTVSEEMSEVIHARFIRAVSELELLGFIKPTKQKTDHVARLTWGGC
Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication. Binds histone H3 and H4 trimethylation marks H3K9me3, H3K27me3 and H4K20me3.
Q9JK30
B4LUF5
NUBP1_DROVI
Cytosolic Fe-S cluster assembly factor NUBP1 homolog
Drosophila
MQAPPPEHCPGVESEQAGLVSACAGCPNQSICSDPSKKLEDPGKALVAAAMKDVKHKLLILSGKGGVGKSTVTTLLTRYLARSYPDNNFGVLDIDICGPSQPRLLGALGENVHQSGSGWSPVGIDDNVCLMSIGFLLGSVDDAVIWRGPKKNGMIRQFLSEVDWGNLDLLLLDTPPGTSDEHLSVVSYLRDDNAPESLHAIIVTTPQEVALLDVRKEINFCKKQRIPILGVIENMSSFRCGHCGNSSEIFPAKTGGAAAMCIEMDVPLLGSLPLDPLVTRSCDAGEDITAMRNETTEALATICSKIMSSL
Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins.
B4LUF5
C3LPC8
HEM6_VIBCM
Oxygen-dependent coproporphyrinogen-III oxidase
Vibrio
MKSNIDKQAVKNFLLQLQDQICQQLEAADGQAQFIEDAWQREPGEKLGGGGRTRVMRDGAVFEQGGVNFSHVFGEQMPGSATAHRPELAGRRFEAMGVSLVMHPKNPYVPTSHANVRYFIAEKEGEDPIWWFGGGFDLTPFYPFVEDCQLWHQTAKNLCAPFGAEIYNEHKAWCDRYFYLPHRNETRGIGGLFFDDLNEWPFEQCFAYMQAVGEGYTQAYVPIVEKRKNTPFTERERQFQLYRRGRYVEFNLVLDRGTLFGLQTGGRTESILMSMPPLARWEYAYQPESGTPEAQLSEFLVPREW
Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.
C3LPC8
A1JSF8
BIOH_YERE8
Carboxylesterase BioH
Yersinia
MKQLYWNICGEGDCDLVLLHGWGLNAGVWHCIIDRLTPHFRLHLVDLPGYGRSTEFGAMSLSEMAEIVLQQAPQQAIWLGWSMGGLVASQIALSHPERVRGLITVSSSPCFTAHDEWPGIRPEVLAGFQQQLSEDFQRTVERFLALQTLGTESARQDARLLKAVVLQHQMPEVAVLTGGLDILRTADLREELADCSLPFLRIYGYLDGLVPRKVAALLNSQWPHTQSVVMPGSAHAPFVSHPEAFSQLVVDFAQQSNT
The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
A1JSF8
B6HDM7
MMM1_PENRW
Maintenance of mitochondrial morphology protein 1
Penicillium chrysogenum species complex
MALQQHEPAPFAPQSSLSFTQGFLLGQLSVVLLIGAFIKFFIFGEAPPPPSRGMSNRTTHRRYSSVYSPPQDSQKSLREKPSTSNVLRPVPSTSTNTRSILRKTYYSAIPTNPTSKHGRHRMHHSSHQPESLDWFNVLIAQTIAQYRETAYSLKDSPTSSILSSLTAAMNNPEKKPSFIDKIKVTDISLGEEFPIFSNCRIIAVDDPVSDGGRLQALLDVDLSDDNLSIAVETSMLLNYPKPRSAIIPIALSVSVVRFSGTLCISLIPASTEPPEPLQTPAGSPAPPTSDPRDNAGNRPPGPGEHTASQDELPPKSSPKSNVAFSFLPDYRLDLSVRSLIGSRSRLQDVPKIAQLVEARVHAWFEERVVEPRVQVVGLPDLWPRMGRTGVRPGEDSDAGSTAPPRSAGSTESSGPPRFSDDHGREPEGLRFRGALDSRLGLGAGSRTNSFNVDMGGLRSSSMTRQQSGGARSDHFEMPGAMPAGTPVGTPGIPDN
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
B6HDM7
B7NEG2
TREF_ECOLU
Alpha,alpha-trehalose glucohydrolase
Escherichia
MLNQKIQNPNPDELMIEVDLCYELDPYELKLDEMIEAEPEPEMIEGLPASDALTPADRYLELFEHVQSAKIFPDSKTFPDCAPKMDPLDILIRYRKVRRHRDFDLRKFVENHFWLPEVYSSEYVSDPQNSLKEHIDQLWPVLTREPQDHIPWSSLLALPQSYIVPGGRFSETYYWDSYFTMLGLAESGREDLLKCMADNFAWMIENYGHIPNGNRTYYLSRSQPPVFALMVELFEEDGVRGARRYLDHLKMEYAFWMDGAESLIPNQAYRHVVRMPDGSLLNRYWDDRDTPRDESWLEDVETAKHSGRPPNEVYRDLRAGAASGWDYSSRWLRDTGRLASIRTTQFIPIDLNAFLFKLESAIANISALKGEKETEALFRQKASARRDAVNRYLWDDENGIYRDYDWRREQLALFSAAAIVPLYVGMANHEQADRLANAVRSRLLTPGGILASEYETGEQWDKPNGWAPLQWMAIQGFKMYGDDLLGDEIARSWLKTVNQFYLEQHKLIEKYHIADGVPREGGGGEYPLQDGFGWTNGVVRRLIGLYGEP
Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity.
B7NEG2
Q5LIJ0
RSMH_BACFN
rRNA (cytosine-N(4)-)-methyltransferase RsmH
Bacteroides
MKEEETTYHVPVLLKESVDAMNISPDGTYVDVTFGGGGHSREILSRLGDGGRLLGFDQDEDAERNIVNDPHFTFVRSNFRYLHNFLRYHDIGEVDAILADLGVSSHHFDDSERGFSFRFDGKLDMRMNKRAGITAADVVNTYEEERLADIFYLYGELKNSRKLASVIVKARTGQKIETIGEFLEIIKPLFGREREKKELAKIFQALRIEVNQEMEALKEMLMAATEALKPGGRLVVITYHSLEDRMVKNIMKTGNVEGKTTQDFFGNLQTPFRLVNNKVIVPDEDEITRNPRSRSAKLRIAEKK
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Q5LIJ0
Q975D6
CDC62_SULTO
ORC1-type DNA replication protein 2
Sulfurisphaera
MKVLDELRDLVEDAIKGSTVFEKSKVLTPDYIPKNLPHREKQIKELSINFREILSNPGSTSVRVVISGKTGTGKTVTTKKFGELFSEIAKEKGLRVVYTHINCHRQRTLYLMLVEIANQLNLQIPNRGLSSQETFKLIYDYLEKRNIQLIITLDEFDYFVSTSPVEDIYFLVRIYDELNALVKRIHYIFILRELTSLASLDKSIKDHVIKNVIEFPPYTSEELYDILMDRIVNEKAFREGAVLEETVRFISDIYGIDKGGSGNARLALETLELAGKIADTEGSLLVTIDHAKKANSKINPELSIILDTIRDLDLHQLLVVKAIMNLHKKEGDDFFSMGKVEEEYNIVAKDLGEIPRKHTQVFEYIRKLKLMGLITARQSGKGMRGRTTLISLSVPISEELDNLINNEIRDRLLQQKNY
Involved in regulation of DNA replication.
Q975D6
P47932
REL1_MOUSE
Relaxin A chain
Mus
MSSRFLLQLLGFWLLLSQPCRTRVSEEWMDGFIRMCGREYARELIKICGASVGRLALSQEEPALLARQATEVVPSFINKDAEPFDTTLKCLPNLSEELKAVLSEAQASLPELQHAPVLSDSVVSLEGFKKTLHDRLGEAEDGSPPGLKYLQSDTHSRKKRESGGLMSQQCCHVGCSRRSIAKLYC
Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals.
P47932
B0T2C2
RL3_CAUSK
50S ribosomal protein L3
unclassified Caulobacter
MTLPANRTGVIAKKLGMTRFFDETGQHVPVTVLSLDGCQVTAQRTVEKDGYTALQLGAGAKKPKNTPNAMRGHFAKNSVEPKRIVAEFRVDEAALIEVGAEFTADHYVAGQKVDIQGITVGKGFAGAMKRWNFSGLRATHGVSVSHRSHGSTGQRQDPGRTFKGKKMAGHLGQETVTTLNVTVWKVDVERGLILVKGAVPGSEGSYVKVRDAIKKAAPADLPRPGAFRSAGEAPAQAAAETPAEETSAATTEEGEG
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
B0T2C2
Q92A25
LEUD_LISIN
Isopropylmalate isomerase
Listeria
MEAIKVHIGKTVALMNDNIDTDQIIPKSFLKRIERTGFGEFLFDSWRYLPNRKPNPDFPLNAPDRQEATILITGDNFGCGSSREHAAWALLDYRFRVIIAGSYSDIFYMNCTKNGVLPIVLPREAREKLAKITAEEKVTIDLPKQQVISSVGTYPFEIDATWKNKFINGLDDIAITFEHIDAIKAYEQKVDSI
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q92A25
Q72JE9
DEOC_THET2
Phosphodeoxyriboaldolase
Thermus
MDLAAHIDHTLLKPTATPEEVAKAAEEALEYGFYGLCIPPSYVAWVKARYPHAPFRLVTVVGFPLGYQEKEVKALEAALACARGADEVDMVLHLGRAKAGDLDYVEAEVRAVREAVPKAVLKVILETGYFSPEEIARLAEAAIRGGADFLKTSTGFGPRGASLEDVALLVRVAQGRAQVKAAGGIRDRETALRMLKAGASRLGTSSGVALVAGEGGTLGY
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
Q72JE9
C5D4U8
GPR_GEOSW
Spore protease
unclassified Geobacillus
MNRSIDLSMYSVRTDLAIEAHEIAVEERLQQKRESASPIEGVIIHDREIDGIKLSHVEVTEEGAKSIGKKPGNYLTIEAQGIREHNTELQQKVQDIFAKEFNAFLRKLDIRKESSCLVVGLGNSNVTPDALGPLTVENLLITRHLFHLQPESVEEGFRPVSAIAPGVMGTTGIETSDIIHGIVEKTKPDFVIVIDALAARSIERVNATIQISDTGIHPGSGVGNKRKELSKETLGIPVISIGVPTVVDAVSITSDTIDFILKHFGREMREGKRPSSALAPAGWTFGKKKRLTEEDMPSTEQRSTFLGIIGTLEEEEKRRLIYEVLSPLGHNLMVTPKEVDMFIEDMANLLASGLNAALHEQIDQDNTGSYTH
Initiates the rapid degradation of small, acid-soluble proteins during spore germination.
C5D4U8
Q61056
TRPC1_MOUSE
Trp-related protein 1
Mus
MMAALYPSTDLSGVSSSSLPSSPSSSSPNEVMALKDVREVKEENTLNEKLFLLACDKGDYYMVKKILEENSSGDLNINCVDVLGRNAVTITIENESLDILQLLLDYGCQSADALLVAIDSEVVGAVDILLNHRPKRSSRPTIVKLMERIQNPEYSTTMDVAPVILAAHRNNYEILTMLLKQDVSLPKPHAVGCECTLCSAKNKKDSLRHSRFRLDIYRCLASPALIMLTEEDPILRAFELSADLKELSLVEVEFRNDYEELARQCKMFAKDLLAQARNSRELEVILNHTSSDEPLDKRGLLEERMNLSRLKLAIKYNQKEFVSQSNCQQFLNTVWFGQMSGYRRKPTCKKIMTVLTVGIFWPVLSLCYLIAPKSQFGRIIHTPFMKFIIHGASYFTFLLLLNLYSLVYNEDKKNTMGPALERIDYLLILWIIGMIWSDIKRLWYEGLEDFLEESRNQLSFVMNSLYLATFALKVVAHNKFHDFADRKDWDAFHPTLVAEGLFAFANVLSYLRLFFMYTTSSILGPLQISMGQMLQDFGKFLGMFLLVLFSFTIGLTQLYDKGYTSKEQKDCVGIFCEQQSNDTFHSFIGTCFALFWYIFSLAHVAIFVTRFSYGEELQSFVGAVIVGTYNVVVVIVLTKLLVAMLHKSFQLIANHEDKEWKFARAKLWLSYFDDKCTLPPPFNIIPSPKTICYMISSLSKWICSHTSKGKVKRQNSLKEWRNLKQKRDENYQKVMCCLVHRYLTSMRQKMQSTDQATVENLNELRQDLSKFRNEIRDLLGFRTSKYAMFYPRN
Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Seems to be also activated by intracellular calcium store depletion.
Q61056
Q216Q6
RPIA_RHOPB
Phosphoriboisomerase A
Rhodopseudomonas
MSSDELKRQAAAAALEHVRDGMKLGLGTGSTAKHFVELLGERVRGGLNVVGVPTSEVTRADALRCGIALTTLDEVDRLDLTVDGADEINAALNLIKGGGGALLREKIVAAASDRMIVIADESKLVANLGRFPLPIEVNSFGLAATLRAIEEACAECGVFGPLSLRKGSDGHAFVTDGGHWIVDAQLGRIPDAPSLADQLNAIPGVVENGLFIGLASMAVLAGPNGIRIIERP
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Q216Q6
B1YL74
RECO_EXIS2
Recombination protein O
Exiguobacterium
MIDKAEGLVLRTVVYGESNKIITLLTREYGKLAVMARGAKKPGSRFNAASQPFVRAIYVYPRSRGLGQLKSADVITGYSKIRQDVFLMAYAMYLLELADKALDERVPQPALYDLFVDGLEAMDEGLDPDVVSFIVELRLLRHLGIAPHLNGCTVCGSVEAPFAFSLNHGGLLCRRHRQEDEHAVSLTESVAKMLYVFSVYDFSRIGTVDVKPETKRLLRQIMDAYMERYSGLRLRSKRVLDQLLNLGDD
Involved in DNA repair and RecF pathway recombination.
B1YL74
Q812Y1
MURG3_BACCR
Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase 3
Bacillus cereus group
MSKTILFTGGGTAGHVMINIVLIPKFIEKGWRVEYIGSKNGIEKSLVQNVKYNSVSTGKLRRYWDWDNFKDPFKIIRGCLQSYNLIKKTKPDVIFSAGGFVSVPVAIGAWLNRVPIIIREPDSTLGLANKIALPFATKLCTTFPQTGENVSNEKKVYVGPIVRVEIEKGNVLRGRRYCEFQQDKPVLLIMGGSQGAKWINDMVRECLDTILLNFNIIHICGKGKVDPSIGMEGYMQFEYIGDELPHILNMASVVVSRAGSTAISELLFLKKPMLLIPLTNSSSRGDQVLNAEYFSRQGYAEVILQDRVSTNTFIHAVNKLYTNKEKYIQNMNGYKKTNDEGIHQIIDIINEVVK
Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II).
Q812Y1
Q99V46
SSPB_STAAM
Staphylopain B
Staphylococcus
MNSSYKSRVFNIISIIMVSMLILSLGAFANNNKAKADSHSKQLEINVKSDKVPQKVKDLAQQQFAGYAKALDKQSNAKTGKYELGEAFKIYKFNGEEDNSYYYPVIKDGKIVYTLTLSPKNKDDLNKSKEDMNYSVKISNFIAKDLDQIKDKNSNITVLTDEKGFYFEEDGKVRLVKATPLPGNVKEKESAKTVSAKLKQELKNTVTPTKVEENEAIQEDQVQYENTLKNFKIREQQFDNSWCAGFSMAALLNATKNTDTYNAHDIMRTLYPEVSEQDLPNCSTFPNQMIEYGKSQGRDIHYQEGVPSYEQVDQLTKDNVGIMILAQSVSQNPNDPHLGHALAVVGNAKINDQEKLIYWNPWDTELSIQDADSSLLHLSFNRDYNWYGSMIGY
Cysteine protease that plays an important role in the inhibition of host innate immune response. Degrades host elastin, fibrogen, fibronectin and kininogen. Blocks phagocytosis of opsonised S.aureus by neutrophils and monocytes by inducing their death in a proteolytic activity-dependent manner. Decreases surface expression of the 'don't eat me' signal CD31 on neutrophils. Cleaves host galectin-3/LGALS3, thereby inhibiting the neutrophil-activating ability of the lectin.
Q99V46
Q01QM3
DXR_SOLUE
2-C-methyl-D-erythritol 4-phosphate synthase
Candidatus Solibacter
MKTIAVLGSTGSIGTNTLDVVRRNRHLYEVYSLVAGQNIELLTGQILEFRPKLAVVASAAVLDLLTASLQAAGLPKSEWPDLLSGDAARVAAVRAPEVDTVISAIVGVAGLEATYEAVCLGKRVGLANKEVLVSGGSLVMEAVRKFGAELLPVDSEHNGAHQCLRAGNRAQVSRLILTASGGPFRNTPVSELPFVTPGQALNHPTWKMGNRITIDCATLMNKGFEVIEACWLFDFAPRDVGVVIHPQSTVHAMIEYSDGSVLAQISATDMRMPIQYALTYPDRADAPVPKIDWAEARKWEFLPPDLEKFPLLKLAYQCQESGGSATCILNAADEIAVEAFLQGRIGFLSIHEIVQETLSRMPSRTPASVGDILEIDRESRTLARELANCRAAGTVTA
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q01QM3
S3D9F1
GLOL_GLAL2
Pneumocandin biosynthesis cluster protein L
Glarea
MGDISGSVDPSNMAYEPLAIVGMGMRLPGGIHTAEDFWNLLVEKRSSRCKVPSDRFNIEAFYSPSGRVGTVKMEHGHFLGPTDDLQHFDASFFSMSKKEVEILDPQQRMLLEVVYECMQNAGQSNWRGGNIGCYVGVWGEDWVDIHAKDSQDAGMYRISGGQDFAISNRVSYEYDLKGPSFTIKSGCSSSMIALHEAARAIQAGDCDGAIIAGTNLIISPTMSIAMTEQGVLSPDGACKSFDESADGYARGEAINAIYIKRLSDAIRDGDNIRSVIRATASNCDGKTPGITLPSSESHEAMMRRAYKEACLDPTQTAFVEAHGTGTKIGDPLEATAIARVFSSEKGVYIGSVKPNVGHSEGASGVTSIMKAVLALENRTIPPNINFSTPNPQIPFEASNMKVAVEPIPWPKVQAERASVNSFGIGGANAHVILDSPASMGISSTKRNTTNGLSVNGHSINGNSVNGHSVNGHSTNGHSINGNSVNGHSVNGNSVNGHSTNGHSINGHSANGNSINGHSVNGHSKPRPALLVLSATNTESLRANVVKHQQYIETNPEKLVNIEYNLCNRREHLSNRAFCVTDGLSTLQFSPLTKPKKTPTLVMVFTGQGAQWAEMGKELMADFPSFSQDIDLMNNTLSKLDHPPSWNIKEELLKHESVSCLSKAEFAQPLVTAIQVALVNLLRQFGVKPAAVVGHSSGEIAAAYAANAITANEAIIIAYYRGQVTKGFSRRGGMAAVGLGREDVMSFLNPGVSIACENSSSSVTLSGDEDALNATCEIIKTALPDVFLRPLKVEMAYHSHHMKELGEAYEALLRPHLKSTTPVVPFFSSVSGKVVSKSGTLDAAYWRSNLENPVLFNSAIKLILDTLAQDHLFLEIGPHSALAGPIRQILKANSRKNDTYVTALERGKDCGESILKMIGELYLQHISINFKQVAPNGTVLTDLPLYQWCHDQEYWKESRVSKQWRLRKYPNHEILGSRTVEGNELQPEWRNVLHLDNVPWLRDHQIINDVVFPCAGYLSMACEAIRQISASEDFTFRNIVIQTALVMSDSKSVEMITSLRPVRLTNTLNSVWWDFSISSYNGSLWIKHCGGQIRSGTDNPKFKLPRRIEDHPRSVPSPYPAMKKVGLNYGPTFQGLERLSALPKKMTASATLSKSELSESHYAIHPATIDHCLQLFIVSTCEGTLRNINKLCVPTSIDQLYICGGKSTSGIKAEACGAQTSTGTISGDVVAISGDAIILSLIGGQFSPIEEDSSDEDLDTVAGARLDWKPDLDFVQIDNLIRPRQQSTAATKTLEKFTLLSMIDIGRRISGLVTKSEYLEKFRSWINAQVERASEDRYNLVEDAQALTVLNAGERQMLIAELSKEISNSEVATSGELISRVVKNCEDIMVGKIDGIEVLLPENGLTHFYDSLEHRTDCIDFFTAAGHSKPNLRVLEIGSGTGGTSAVVLKGLTSTAQRMYSTYTYTDISSGFFVEAQERFKDYHGLEYKVLDISKDPTEQGFQEGSYDLIIAANVLHATPSLNTTLGHARKLLAEDGRLFLQELSPQVQFANLIMGVLPGWWLGEADGRANEPYISPERWAVELRKAGFSGCDATVYDAEQPYQFNANIISRPAKVDRIARRITLLYEPNLNIQQIKFSLENKGYSVDLCTIQEEPPAGQDIVSLLELETPMFEKISGTDLALFQRLVKNLGTNHLLWVTRSAQIESYDPRFGMVLGLARTLRSELSLSIATLEIDTVDEVAYNAITNVFDKLKNSSSVSDMNPDYEFVLSKGVVNIGRYHPVSVEQELAVSASQSQAVKLEIGRFGLLQTLRWVPDLQNKVGHDQVIVEPRCAGLNFKDVLVSMGIVSGDGLGLEGSGTVVGVGSEVTDFQVGDRVLYIDQNCFSTRTAIPALRCAKIPSTLSWEEAATMPCVYATVIHSLLNLGRIQKGQSVLIHSACGGIGLAAIQICQNIVGAQIYVTVGNEEKVHYLMDTFGISRDHIFNSRDTSFLPAIKAATNGRGVDVVLNSLSGELLHASWECVAEYGSMVEIGKRDFIGKAQLNMDLFESNRSFFGVDLAKFDAARCQLLLVQMMEFYEKGLIKPIAPMKVFEGAKVEDSFRYMQKGSHIGKIVVTIPEQNTDLPLASIVPKLKLNPDAGYLLVGGLGGLGRAVSTWMVERGARHLIFLSRSAGKSDQDQSFFRELESQDCTVQAFTGSVATFQDVQNAVQRASKPIKGVFQMSMVLNDKPFLEMSCSDWETSVLPKVEGTWHLHHALPKDLDFFVATSSLSGSFGNAGQANYAAANTFLDAFVQYRHSLGLPASVVDIGVMGDIGYVSRNAAIQESLRGAGTYFLQEQDFLDSLNWAVAKSAVKPSLPGQNQLLIGVRSSKSLSDPSNRVSFKRDARMGAYLNTGSSTSANTTNATDQLKSFMSSVETDSSILNVPASLDLVTNEIGVRIYTFMLQPIEDLDVSQTLAALGVDSLVTIEIRNWMKRSFGGLEFSTLEILNAGTIEALGLLTIEGLKRKYEMKDGEAKFSEREDTYLLMKAP
Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of pneumocandins, lipohexapeptides of the echinocandin family that prevent fungal cell wall formation by non-competitive inhibition of beta-1,3-glucan synthase . The 10,12-dimethylmyristoyl side chain is synthesized by the reducing polyketide synthase gloL/GLPKS4 . The thioesterase gloN/GLHYD exclusively interacts with gloL/GLPKS4 to maintain turnover of the polyketide side chain . The 10R,12S-dimethylmyristic acid is then transferred to the first thiolation domain of the nonribosomal peptide synthetase gloA/GLNRPS4 by the acyl-AMP ligase gloD/GLligase, followed by its acylation to L-ornithine to trigger elongation of the cyclic hexapeptide . L-ornithine, 4R-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2), 3S-hydroxyl-L-homotyrosine (generated by gloG/GLHtyB, gloH/GLHtyA, gloI/GLHtyC, gloJ/GLHtyD and hydroxylated at C-3 by the dioxygenase gloM/GLOXY1), 3R-hydroxyl-L-glutamine (generated from L-glutamine probably by the dioxygenase gloE/GLOXY3) and 3S-hydroxyl-L-proline (generated from L-proline by the dioxygenase gloF/GLOXY2 to yield pneumocandin B0), or 3S-hydroxyl-4S-methyl-L-proline (generated from L-leucine by the dioxygenase gloC/GLOXY4 to yield pneumocandin A0) are sequentially added to the growing chain . The last C domain of gloA/GLNRPS4 is proposed to be responsible for cyclization by condensation to form the peptide bond between L-ornithine and 3S-hydroxyl-4S-methyl-L-proline (for pneumocandin A0) or 3S-hydroxyl-L-proline (for pneumocandin B0). Finally, the subsequent C-4 hydroxylation of 3S-hydroxyl-L-homotyrosine and L-ornithine dihydroxylation at C-4 and C-5 are performed by the cytochrome P450 monooxygenases gloP/GLP450-1 and gloO/GLP450-2, respectively .
S3D9F1
O83149
RP54_TREPA
RNA polymerase sigma-54 factor
Treponema
MQQLVQQQRLVLNQRLVHGLCLLQLSRGDLKTEVLRAVQRNPLLEIRPSSARRTGKACYLSLGDRRERMRARDRFQQLLENQPDKQVDNIRAVLREQVFYQKHEAIVLDLACAFIQMLDDHGFFSISPAIFQNMCGSMPTALQEKIPQAIALIQRLEPQGCAVFNFKESLAVQARLRFERFSDPLYRCVINLLTHHSELLFCSDNMCDGRVSVHALTTQINSMGLCVQKVSSNDVKDILLLIKELHPFPGKCVSNAQRADTNMLLEPDVLITKTAHGFVTQINCTGIPTVVFRNDYCMHSKAAEKNHALKACMHDALSLVSMLSYRERTLLDIAKTIVHYQCGFFDHGPAKLTPLRMTDVAHRTGLSVSTVSRIVRDKWLQYGSQHFSLRYFFSPRVLSTEEYRDRSSLGQNYPSSPHSKVSVKYRISRLIQEVRTQRISLSDRRIAQLLGEQGIKCARRTVNKYRSELRTCSSS
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
O83149
Q7VGE1
RL2_HELHP
50S ribosomal protein L2
Helicobacter
MAVKTYKPYTPSRRFMSNLSSSDITGKASVKSLLIKLPVSAGRNNNGRITSRHKEGGAKKFYRIIDFKRNKFNIQGKVAAIEYDPYRNCRIALIHYVDGEKRYIIQPSGLKVGDVVFSASSGLDIKTGFAMKLKSMPIGTIVHNIEMHPGAGGALARSAGTSAQIMGREGKYIILRMPSGEMRYILEECMATIGVVGNEDFANISIGKAGRNRHRGIRPQTRGSAMNPVDHPHGGGEGKTGSSGHPVSPWGTPAKGFKTRKKKASDKLIISRKKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
Q7VGE1
Q7N5M6
FLGI_PHOLL
Basal body P-ring protein
Photorhabdus
MIKQFAVSLLLVLLTLVTTTASAERIRDLTTVQGVRENALIGYGLVVGLDGTGDQTTQTPFTTQSLSNMLSQLGITVPPGTNMQLKNVAAVMVTAKLPPFGRAGQNIDVVVSSLGNAKSLRGGTLLMTPLKGVDNQVYALAQGNILVGGAGASAGGSSVKVNQLAGGRISNGAVIERELPTQFGENGVLNLQLNNEDFSLAQQISDTINRTDGTGTATPLDARTVQLRMPRDKSAQVKFLSHVQNLTVRVDVGDAKVIVNSRTGSVVMNRNVMLDSCAVAQGNLSVIVDNQVVVSQPNTPLAGGSTVVTRNPAVAVREQNGALQQVNASASLSQVIQALNALGATPNDLMSILQAMESAGCLRAKLEII
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Q7N5M6
A0B796
RNH2_METTP
Ribonuclease HII
Methanothrix
MMLILGVDEAGKGPVIGSMFVAGVVFSEEDIFDLAACGVKDSKLLSPTRRESMERKILSIARESFVLEVTAQQIDDLRMVMSMNEIMVRAHSRVVSRLQADRAILDAADVNAERFAQRVREVSGKPIDILAEHNADRKHIVVAAASIIAKVARDRSIRDLEAALGRPLGSGYPSDPATVRFLKEWIEENGDLPSFVRKSWSTAQRLKASSV
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
A0B796
Q9BQS7
HEPH_HUMAN
Hephaestin
Homo
MESGHLLWALLFMQSLWPQLTDGATRVYYLGIRDVQWNYAPKGRNVITNQPLDSDIVASSFLKSDKNRIGGTYKKTIYKEYKDDSYTDEVAQPAWLGFLGPVLQAEVGDVILIHLKNFATRPYTIHPHGVFYEKDSEGSLYPDGSSGPLKADDSVPPGGSHIYNWTIPEGHAPTDADPACLTWIYHSHVDAPRDIATGLIGPLITCKRGALDGNSPPQRQDVDHDFFLLFSVVDENLSWHLNENIATYCSDPASVDKEDETFQESNRMHAINGFVFGNLPELNMCAQKRVAWHLFGMGNEIDVHTAFFHGQMLTTRGHHTDVANIFPATFVTAEMVPWEPGTWLISCQVNSHFRDGMQALYKVKSCSMAPPVDLLTGKVRQYFIEAHEIQWDYGPMGHDGSTGKNLREPGSISDKFFQKSSSRIGGTYWKVRYEAFQDETFQEKMHLEEDRHLGILGPVIRAEVGDTIQVVFYNRASQPFSMQPHGVFYEKDYEGTVYNDGSSYPGLVAKPFEKVTYRWTVPPHAGPTAQDPACLTWMYFSAADPIRDTNSGLVGPLLVCRAGALGADGKQKGVDKEFFLLFTVLDENKSWYSNANQAAAMLDFRLLSEDIEGFQDSNRMHAINGFLFSNLPRLDMCKGDTVAWHLLGLGTETDVHGVMFQGNTVQLQGMRKGAAMLFPHTFVMAIMQPDNLGTFEIYCQAGSHREAGMRAIYNVSQCPGHQATPRQRYQAARIYYIMAEEVEWDYCPDRSWEREWHNQSEKDSYGYIFLSNKDGLLGSRYKKAVFREYTDGTFRIPRPRTGPEEHLGILGPLIKGEVGDILTVVFKNNASRPYSVHAHGVLESTTVWPLAAEPGEVVTYQWNIPERSGPGPNDSACVSWIYYSAVDPIKDMYSGLVGPLAICQKGILEPHGGRSDMDREFALLFLIFDENKSWYLEENVATHGSQDPGSINLQDETFLESNKMHAINGKLYANLRGLTMYQGERVAWYMLAMGQDVDLHTIHFHAESFLYRNGENYRADVVDLFPGTFEVVEMVASNPGTWLMHCHVTDHVHAGMETLFTVFSRTEHLSPLTVITKETEKAVPPRDIEEGNVKMLGMQIPIKNVEMLASVLVAISVTLLLVVLALGGVVWYQHRQRKLRRNRRSILDDSFKLLSFKQ
May function as a ferroxidase for ferrous (II) to ferric ion (III) conversion and may be involved in copper transport and homeostasis. Implicated in iron homeostasis and may mediate iron efflux associated to ferroportin 1.
Q9BQS7
A1K991
SYA_AZOSB
Alanyl-tRNA synthetase
Azoarcus
MKSAEIRAKFLKFFESKGHQIVASSSLVPHEDPTLLFTNAGMNQFKDVFLGFDKRPYSRATTSQKCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKRDAITYAWELLTEVFKLPKDKLWVTVYAEDDEAYDIWTKEVGVPAERVIRIGDNKGARYASDNFWMMGDTGPCGPCTEIFYDHGPHIWGGPPGSPEEDGDRYIEIWNNVFMQFNRDEQGVMHPLPKPSVDTGMGLERISAVLQGVHANYEIDLFKSLISSAMRAVGTAEALVERARDSMTNTISPSYKVLADHIRACSFLIADGVIPGNEGRGYVLRRIIRRAIRHGYKLGARAAFFHKMVPDLVAEMGEAYPELKAGERRVADVLRQEEERFFATIENGMAIVEGELAAMATAGNTVFNGDTAFKLHDTYGFPLDLTADICREREVTVDAAAFDAAMARQKEQARAAGKFKMAANLDYDGPATTFHGYDKLEAKGNILALYKDGVAVNELVEGDLGVVVLDHTPFYAESGGQAGDRGELKGAAGIFGVEDTLKIQASVFGHHGVVKTGKLAVGQGVAARVDTAARAATARNHSVTHLMHKALREVLGPHVQQKGSLVDPDKTRFDFAHTAPMSAEEIREVEEIVNREILANAATEAAVMALDDAQKSGAMMLFGEKYGDEVRVLSIGSSKELCGGTHVARTGDIGLFKIVVEGGVAAGVRRVEAVTGENALRYTQEQERRVQGVSALLKVQPDEVAERVAGILDNVRALEKELARLKSKLAASQGEDLVAQAVDVGGAKLLAATLEGADVPTLRETMDKLKDKLKSAAIVLASVADGKVSLIAGVTADLTGKVKAGELVNFVAQQVGGKGGGRPDMAQAGGTEPDKLPAALAAVQAWVSAKL
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.
A1K991
Q5FM92
EFG_LACAC
Elongation factor G
Lactobacillus
MANKREFPLAKTRNIGIMAHIDAGKTTTTERILYYTGKIHKIGETHEGDSQMDWMDEEKERGITITSAATTAQWKDYRINIIDTPGHVDFTIEVERSLRVLDGAVTVLDAQAGVEPQTENVWRQAETYGVPRIVFVNKMDKIGADFDKSVKSLHERLNANAQAVQMPIGSADTFEGVIDLINMVADIYDEDKLGSKWDTVPVPDEYKEEAEKRRAALIEAVADVDDNIMEKYLGGEEISNDELKAAIRKATLNLEFFPVYAGSAFKNKGVQMMLDGVIDYLPSPLDVKPYVAHDPKTGDEVELMADDKKPFAALAFKIATDPFVGRLTFIRVYTGSLESGSYVLNASKNSRERVGRLLQMHANSRTEIPEVFSGDIAGAIGLKNTTTGDSLTDPDHPLILESLQVPDPVIQVSVEPKSKADRDKMDVALQKLTEEDPTFRAETNPETGQTLISGMGELHLDIMVERMRREFNVEAKIGEPQVAYRETFTKEAKAQGKFVRQSGGKGQYGDVWIDFTPNEEGKGYEFEDAIVGGVVPREFIPSVDQGLQEAMKNGVLAGYPLIDVKAKLYDGSYHEVDSSEAAFKVAASLALRNAASKAGAVILEPIMKVQVTTPEEYLGDVMGSITARRGTMEGMEDRAGAKIINSFVPLSEMFGYATTLRSSTQGRGTFTMVFDHYSPTPKSIQADIIKKRGGDAE
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q5FM92
B6EGG8
SYDP_ALISL
Protein Syd
Aliivibrio
MPLSVEQALANFSQRYVEAWKEKHDSLPINEELVGLASPCIDETRNLEVLWQPVARDESIRLVNIENGIELDLHDDFHAFYGAQFSADMTAKFEGMNVELLQIWSDEDLENLQGNMLGHLVMQRRLKLVPTLFIAVTDDEMEVISICNQSGEVILDTVGTKKRKVLAESMAEFLEKLEPVVA
Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
B6EGG8
G2Q4H7
MA26A_MYCTT
GH26 family endo-beta-mannanase
Thermothelomyces
MARTLRYLLCGILALAAGSNAVPAARGSTRAAPAAEPSTSATTYEAEDAILSGTTVDTAQEGYTGSGYVTGFDEASDKITFEVESEATKLYDLSIRIAAIYGDKHTTVVLNGGASSDVSFPAGDTWVDVPAGQVLLNEGANTIEIVSNWGWYLVDSITLTPSAPRPEHQINRSLNNPSADASARALYDYLRSIYGKKILAGQQDLTWADYVTQQTGKTPALVSVDLMDYSPSRVERGTKGTSVEEAITHAERGGIVSALWHWNAPAGLYDTDEHPWWSGFYTDATDFDVAAALSSTDNANYTLLLRDIDAIAVQLKRLRDARVPVLWRPLHEAEGGWFWWGAKGPDPAKQLYALLYDRLVNHHGINNLIWVWNSLSPDWYPGDDTVDILSADVYAQGNGPMSTQYNQLIDLGKDKKMIAAAEVGAAPLPDLLQAYEAHWLWFAVWGDTFINNAEWNSPEVLKTVYTSDYVLTLDEIQGWQDS
Mannan endo-1,4-beta-mannosidase that exhibits high activity against konjac glucomannan and carob galactomannan, as well as a lower activity toward beta-mannan . Shows no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose (CMC) . Has the ability to hydrolyze manno-oligosaccharides such as M4 which is degraded slightly to M3 and M1, M5 which is mainly degraded to M4 and M1, and M6 which is mostly hydrolyzed to M4 and M2 . Shows no activity toward M2 and M3 manno-oligosaccharides .
G2Q4H7
B6I7J5
AIS_ECOSE
Lipopolysaccharide core heptose(II)-phosphate phosphatase
Escherichia
MLAFCRSSLKSKKYFIILLALAAIAGLGTHAAWSSNGLPRIDNKTLARLAQQHPVVVLFRHAERCDRSTNQCLSDKTGITVKGTQDARELGNAFSADIPDFDLYSSNTVRTIQSATWFSAGKKLTVDKRLLQCGNEIYSAIKDLQSKAPDKNIVIFTHNHCLTYIAKNKRDATFKPDYLDGLVMHVEKGKVYLDGEFVNH
Catalyzes the dephosphorylation of heptose(II) of the outer membrane lipopolysaccharide core.
B6I7J5
P34232
MTR2_YEAST
mRNA transport regulator MTR2
Saccharomyces
MNTNSNTMVMNDANQAQITATFTKKILAHLDDPDSNKLAQFVQLFNPNNCRIIFNATPFAQATVFLQMWQNQVVQTQHALTGVDYHAIPGSGTLICNVNCKVRFDESGRDKMGQDATVPIQPNNTGNRNRPNDMNKPRPLWGPYFGISLQLIIDDRIFRNDFNGVISGFNYNMVYKPEDSLLKI
Affects mRNA transport from the nucleus to the cytoplasm.
P34232
A2ANU3
SYNG1_MOUSE
Transmembrane protein 90B
Mus
MDGIIEQKSVLVHSKISDAGKRNGLINTRNFMAESRDGLVSVYPAPQYQSHRLVASAAPGSLEGGRSEPVQQLLDPNTLQQSVESHYRPNIILYSDGVLRSWGDGVATDCCETTFIEDRSPTKDSLEYPDGKFIDLSGDDIKIHTLSYDVEEEEELQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASTSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL
May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation.
A2ANU3
P37068
OLF2_CHICK
Olfactory receptor-like protein COR2
Gallus
MASGNCTTPTTFILSGLTDNPRLQMPLFMVFLVIYTTTLLTNLGLIALIGMDLHLQTPMYIFLQNLSFTDAAYSTVITPKMLATFLEERRTISYVGCILQYFSFVLLTTSEWLLLAVMAYDRYVAICKPLLYPSIMTKAVCWRLVKGLYSLAFLNSLVHTSGLLKLSFCSSNVVNHFFCDNRPLFQISSSSTTLNELLVIISGSLFVMSSIITILISYVFIILTVVMIRSKDGKYKAFSTCTSHLMAVSLFHGTVIFMYLRSVKLFSLDTDKIASLFYTVVIPMLNPLIYSWRNKEVKDALRRLTATSVWLH
Odorant receptor.
P37068
C4WXC1
DRE2_ACYPI
Fe-S cluster assembly protein DRE2 homolog
Acyrthosiphon
MSDRKNVLFVVGKSSAVKELEEFASCNADRANVKIEIVENIGLATDGPLYSAILSGFGADDNVSCDLNLLPTYTTLLTAGGTLIAKTDVGTEDALVKRMKLCGFLNVAKSESVPGVVVGNMPTYKVGSSDKVTLNPEMKENVVSAWKLDDNNSETISEDDLLEADDLIKPDSSSLRVCATTKKAKACKDCSCGLAEELEANRLKDTPKPDTSNAKSSCGSCYLGDAFRCASCPYLGMPAFRPGEKVQLAGNLLQDDF
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
C4WXC1
Q85PQ7
NU2M_CYNPE
NADH dehydrogenase subunit 2
Cynictis
MKPPILITIMLTVVSGTMIVLTSSHWLTVWIGFEMNMLAIIPILMKKSNPRAIEASTKYLLTQATASMILMMGVAIDLLYSGQWTMSKTLCPMASAMMTIALAMKLGLAPFHFWVPEVTQGIHMSSGLILLTWQKIAPLSILYQISPTINPNLLLPMAIASVLIGGWGGLNQTQLRKILAYSSIAHMGWMAAITLYNPTMMILNLTIYIIMTSTTFMLFMYNSSTTTLSLSQTWNKAPLITSLILMLMLSLGGLPPLSGFIPKWMIIQELTKNEMIIVPTLLAMTALLNLYFYMRLTYTTTLTMFPSTNNMMMKWKFNNTKKMTLLSPLIVVSTMLLPITPLLSILD
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.
Q85PQ7
Q2S1I3
PCKA1_SALRD
Phosphoenolpyruvate carboxykinase (ATP) 1
Salinibacter
MPLPNHVTSHLRSLQLAPAAVHYNLKRPRLYEEALDRNEGQLAAGGPLVTRTAPYTGRSPKDRFIVRDASVADQINWGEVNQPTDRATFDHLHERMAEHAEGRDLFVQDLHAGWDESYRLPVRIITEKAWHSLFARNMFVRPDGPVPDSFEPGFTVVDLCEFEADPERDGTHSEAAVFVDIAQNLILIGGTHYGGEIKKSIFSVLNYMLPEEGVLPMHCSANEGEDGDTAVFFGLSGTGKTTLSADASRTLIGDDEHGWSDRGVYNFEGGCYAKMIDITPESEPEIHGTTEEFGTILENVIVDPDTREPDFSDDTITQNTRGSYPLHYIPNTSSDGRGGHPDHVLFLTYDAFGVLPPVSELSPAQAMYHFLSGYTAKVAGTEAGVNEPKATFSTCFGEPFMVRDPSVYAELLGQKIRRHDTDCWLVNTGMTGGPYGVGHRIELDHTRAMVDAILDGTLGTVARTRDPVFGLSIPDRVPGVPDSVLTPRQTWGDPQAYDQHARELVDAFADNFETYVEQVGTEVRAAGPSLETIRG
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
Q2S1I3
A1AML8
RIMP_PELPD
Ribosome maturation factor RimP
Pelobacter
MALHRDDICDRIRTLALPVIDSMNLELVEVEYKRSGREAVLRLFIDKEGGVTLDDCADLSRELSTLLDVEDLIPCEYSLEVSSPGLDRPLKSEADYERFSGRLIKVRTYEPYQDDAGNRRKTFLGRLEGLKDGSVVMSLTEGQTASIPLERIAKAQLEFEF
Required for maturation of 30S ribosomal subunits.
A1AML8
Q9UTR4
ETD1_SCHPO
Septation protein etd1
Schizosaccharomyces
MGVVYGSQQNLSEYFYSSVNMAEVPDTFEENRGHSFEGVTLQRRHVKGMKSYGSDITPRRPKQLGLPKEVNTSECIDQGSWRKPSAFESLRSYSRKFSKRIFSFIGVESKSTVQRNASGADSTSLSHFTANEINKGNCKKTALSNEFNSANKGSKASGVGAELPSVNGFIEGELHDDNETDSFRINELAKQIQETSLGATTQEDESSDGICWDELSTTSPESSKVSEPIIQDNTQTTHINNDSSDIRFSSRCDLFADDADSDWEQDFNVKFDSPLIIPETVNSAGHTVREQLFEVKEFTRSIKDLKDLYEKANSKDIYDKDSEILGEAKAILRLADPANYSDLKDEDAQNILSKYKVKLEGDSSLDFDASMLPGLNDHVHYLMSQLQLLLH
Involved in septation.
Q9UTR4
A8AY74
RL1_STRGC
50S ribosomal protein L1
Streptococcus
MAKKSKQLRAALEKIDSTKAYSVEEAVALAKETNFAKFDATVEVAYNLNIDVKKADQQIRGAMVLPHGTGKTARVLVFARGAKAEEAKAAGADFVGEDDLVAKINDGWLDFDVVIATPDMMALVGRLGRVLGPRNLMPNPKTGTVTMDVAKAVEESKGGKITYRADRAGIVQAIIGKVSFDADKLAENFKAFNEVIQKAKPATAKGTYVTSLTITTTQGPGIKVDVNSL
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
A8AY74
Q4GZK6
ORR5_ORYSI
Type A response regulator 5
Oryza sativa
MATCRSRGVERGGAPHVLAVDDSSVDRAVISGILRSSQFRVTAVDSGKRALELLGSEPNVSMIITDYWMPEMTGYELLKKVKESSRLKEIPVVIMSSENVSTRINRCLEEGAEDFLLKPVQPSDVSRLCSRVLR
Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Q4GZK6
C5C958
FOLD_MICLC
Methenyltetrahydrofolate cyclohydrolase
Micrococcus
MTAKVLDGKATAAAIKEELRGRVAALAERGRTPGLGTLLVGEDAGSQKYVAGKHRDCAEVGIESIQRELPADATEEQILDVVRELNEDPACTGYIVQLPLPKHVDTQKVLEAIDPDKDADGLHPMNLGRLVASVGGELDSPLPCTPAGCVELLRHHGVELAGKHVLVIGRGVTIGRPAGLVLTRREVNATVTLAHTGTTNLDELLASADVVIAAAGSAHMVTPEQVKEGVIVLDVGVSRVTGEDGKSRVLGDVDPAVKEKAAWMAPNPGGVGPMTRVMLLANVVEAAERAADGENWAGERAGA
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
C5C958
Q2RHV8
DTD_MOOTA
Gly-tRNA(Ala) deacylase
Moorella
MRAVVQRVKKARVTVAGEEIATIGPGLLVFLGVGQQDGPADVEYLADKIAGLRIFADEDGKMNLSVRDTGGEVLAVSQFTLYGDCRKGRRPSFTAAAPPEQALNLYRQFVAALAARGLKVATGRFQADMLVALENDGPVTMLLDSQRLF
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Q2RHV8
Q8IU89
CERS3_HUMAN
Very-long-chain ceramide synthase CERS3
Homo
MFWTFKEWFWLERFWLPPTIKWSDLEDHDGLVFVKPSHLYVTIPYAFLLLIIRRVFEKFVASPLAKSFGIKETVRKVTPNTVLENFFKHSTRQPLQTDIYGLAKKCNLTERQVERWFRSRRNQERPSRLKKFQEACWRFAFYLMITVAGIAFLYDKPWLYDLWEVWNGYPKQPLLPSQYWYYILEMSFYWSLLFRLGFDVKRKDFLAHIIHHLAAISLMSFSWCANYIRSGTLVMIVHDVADIWLESAKMFSYAGWTQTCNTLFFIFSTIFFISRLIVFPFWILYCTLILPMYHLEPFFSYIFLNLQLMILQVLHLYWGYYILKMLNRCIFMKSIQDVRSDDEDYEEEEEEEEEEATKGKEMDCLKNGLRAERHLIPNGQHGH
Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very- and ultra-long-chain fatty acyl-CoA (chain length greater than C22) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively . It is crucial for the synthesis of ultra-long-chain ceramides in the epidermis, to maintain epidermal lipid homeostasis and terminal differentiation .
Q8IU89
Q9GPH8
SNMP2_MANSE
Sensory neuron membrane protein 2
Manduca
MLAKHSKLFFTGSVVFLIVAIVLASWGFPKIISTRIQKSIQLENSSMMYDKWVKLPIPLIFKVYFFNVTNAEGINEGERPILQEIGPYVYKQYRERTVLGYGPNDTIKYMLKKNFVFDPEASNGLTEDDDVTVINFPYMAALLTIQQMMPSAVAMVNRALEQFFSNLTDPFMRVKVKDLLFDGVFLNCDGDSPALSLVCAKLKADSPPTMRPAEDGVNGYYFSMFSHLNRTETGPYEMVRGTEDVFALGNIVSYKEKKSVSAWGDEYCNRINGSDASIFPPIDENNVPERLYTFEPEICRSLYASLAGKATLFNISTYYYEISSSALASKSANPDNKCYCKKDWSASHDGCLLMGVFNLMPCQGAPAIASLPHFYLASEELLEYFEDGVKPDKEKHNTYVYIDPVTGVVLKGVKRLQFNIELRNMPRVPQLQAVPTGLFPMLWIEEGAVMTPDLQQELRDAHALLSYAQLARWIILAAAIILAIIATITVARSTSLISWPRNSNSVNFIIGPMVNDKMR
Plays an olfactory role that is not restricted to pheromone sensitivity.
Q9GPH8
Q9K923
COMGC_HALH5
ComG operon protein 3 homolog
Halalkalibacterium (ex Joshi et al. 2022)
MKKPFHHQAGFTLVEMMIVLMIISILLLVALPSMTKNNEVAGDKGCEATVKLLQTQVHAYEIDHDRLPTNLDALKREGYVEHTECPNGKKLTLRNGVVAISE
Required for transformation and DNA binding.
Q9K923
Q57IS3
UGPC_SALCH
sn-glycerol-3-phosphate import ATP-binding protein UgpC
Salmonella
MAGLKLQAVTKSWDGKTQIIQPLTLDVADGEFIVMVGPSGCGKSTLLRMVAGLERVTSGDIWIDRKRVTEMEPKDRGIAMVFQNYALYPHMSVEENMAWGLKIRGMSKAHIEERVREAARILELDGLLKRRPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLELQHLHRRLRTTSLYVTHDQVEAMTLAQRVMVMNKGVAEQIGTPVEVYEKPASRFVASFIGSPAMNLLDGVISASGDRFELPGGLALPIGADYRGHAGRNMTLGIRPEHIALSSQAEGGVPLTVDTLEFLGADNLAHGRWGDQKLVVRLAHQQRPAAGSTLWLHLPEHQRHLFDGETGQRV
Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system.
Q57IS3
Q0I1S1
RBSD_HAES1
D-ribose pyranase
Histophilus
MKKTKLLNASLSHHIATLGHTESLVICDAGLPISNQVERIDLALEAGVPGFLQTVDVVISEMFVEHAVVAKEIREKNPQIHDALLDSLRKLSEQQGNCIAVEYVEHEEFKVLSSESKVAVCTGEFSPYANIILYSGVPF
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Q0I1S1
Q62889
NLGN3_RAT
Gliotactin homolog
Rattus
MWLQLGLPSLSLSPTPTVGRSLCLILWFLSLVLRASTQAPAPTVNTHFGKLRGARVPLPSEILGPVDQYLGVPYAAPPIGEKRFLPPEPPPSWSGIRNATHFPPVCPQNIHTAVPEVMLPVWFTANLDIVATYIQEPNEDCLYLNVYVPTEDVKRISKECARKPNKKICRKGGSGAKKQGEDLADNDGDEDEDIRDSGAKPVMVYIHGGSYMEGTGNMIDGSVLASYGNVIVITLNYRVGVLGFLSTGDQAAKGNYGLLDQIQALRWVSENIAFFGGDPRRITVFGSGIGASCVSLLTLSHHSEGLFQRAIIQSGSALSSWAVNYQPVKYTSLLADKVGCNVLDTVDMVDCLRQKSAKELVEQDIQPARYHVAFGPVIDGDVIPDDPEILMEQGEFLNYDIMLGVNQGEGLKFVEGVVDPEDGVSGTDFDYSVSNFVDNLYGYPEGKDTLRETIKFMYTDWADRDNPETRRKTLVALFTDHQWVEPSVVTADLHARYGSPTYFYAFYHHCQSLMKPAWSDAAHGDEVPYVFGVPMVGPTDLFPCNFSKNDVMLSAVVMTYWTNFAKTGDPNKPVPQDTKFIHTKANRFEEVAWSKYNPRDQLYLHIGLKPRVRDHYRATKVAFWKHLVPHLYNLHDMFHYTSTTTKVPPPDTTHSSHITRRPNGKTWSTKRPAISPAYSNENAPGSWNGDQDAGPLLVENPRDYSTELSVTIAVGASLLFLNVLAFAALYYRKDKRRQEPLRQPSPQRGTGAPELGTAPEEELAALQLGPTHHECEAGPPHDTLRLTALPDYTLTLRRSPDDIPLMTPNTITMIPNSLVGLQTLHPYNTFAAGFNSTGLPNSHSTTRV
Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system.
Q62889
Q5A5M7
RBR3_CANAL
Repressed by RIM101 protein 3
Candida
MIIFRKSFFTFWLLLNSVLALVITQNRVDRGTLDLSVGDITINSGASWSIINNAISTLVGSLTVQPNAGLYITSTSPLLSLQVTLTSLLSTIQNNGIIAFNSSPSLTSSTYNLVGLSLVNTGEMYFSASGVLPSVMALTAASWSNSGLMAFYQNQRSSGVVSLGTPLGSITNNGQICLNNEVYQQTTSINGSGCFTANRDSTIYIANVLLPVSTSQNFYLADSQSSIIVQAILTPQVFNVYGFGNGNMVGVTLPLLGNILNPAYSYNPSTGILRLRNLLVYQDFNIGPGYNPSLFSIVTDNGAGLPSTILGSVSYSGPVPPRALPASCKIACKPVPTAPGTNPTEYTTTITTTNSAGKPLTETGVVDISTDSNGSWFSSTTIFPTSSSSSSSSSTVSSTAPSSSSTKPSSSSQPSSTPPPSSSSKASSTTPSSSSQSSSTTPSSSSKPSSTVPPTGSSQSSSTIPSSSTQPSSTAPSSLSSPSSSTTPSSSSQSSFSAQSSIGQTSSSTVSSSSSQPSSSQPSSSQSSSATTSSSSQFSSSAPPSSTQSSFTAESSNSQLSSTTPSSSTEASSTVPSSSSQLSSSVPLTNSVSLSSVSSSDNGSSSASSPSSSQSSIASTAESSSTFPSSSDQQSSSIQSPSSQESSVSSTPTSSLQSSTNTISSSQDSSSFSPTTSDNSSTNSASSLSTLSSSDTSVSNPSTSNVSSTDNTQSSVASATPTDSAISATSSDITTEFTTTWEVTNSDGSVSTESGIVSESGTSFTTITTFPPPTTSSDITTEFTTTWEVTNSDGSVSTESGIVSESGTSFTTITTFPPPTTSSDITTEFTTTWEVTNSDGSVSTESGIVSESGTSFTTITTFPPPTTSSDITTEFTTTWEVTNSDGSVSTESGIVSESGTSFTTITTFPPPTSSSVAADVTTEFTTTWEVTNSDGSVSTESGIVSESGTSFTTITTFELPVVCKRDDISCGPATSATNSDTAAQDPTSDATAIESEFTTTWTTTNSDGSVETNSGVVSQSGSSLTTITTFAPDATSEYTTSWTTTNSDGSVATNSGVVSQSGTSFTTITTFEPPVVCKRDDISCGPATSAMNSDTAAQQLTSGMTATETEFASTWVVTKSDGSVFTESGIVGQSGTSFTTLTTFAPTTSSGAVQTEYTSTWEVTNTDGSVSTKSGIIDQSGTYFTTLSTFAPTTISGAIETEFTSTWVATDTDGLVSTKSGIVSQSGTSIATLTIFPEPAGTVYPVTTLFTTEYVTTCPNGELSTATGVVVVSTDSKGIEQTVTSVVPSTVYTKETVTSIITHCIKNKCFESTTTLVSSVPCPTQVPGVFTSTDNGHGVPIASIDVTTGAATVSNTIKAQDSTGFTSAGNAITTAITATGAVTTSVGGQGSTDYSNAGNTIAAGSGSDSGSGSGSGSGSGSSSNTVGIVNPKVSSAASGITVAAASASAGQSWPYSSGGSGNGVLPSGANNVGSNQTPTVSGGNSNPSTVTGAAVGAGGVVSGSPSYSGNSLLISFVSSQSGAISSSTGVTIPIATENSGSKFSVGKSAFIAIILTTFIGFI
GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
Q5A5M7
Q829U5
TAL2_STRAW
Transaldolase 2
Streptomyces
MTDALKRLSKEGVAIWLDDLSRKRITSGNLAELIDQQHVVGVTTNPSIFQKAISQGDGYDQQVSDLAARRVTVEEAIRMITTADVRDAADILRPVFDATDGQDGRVSIEVDPRLAHNTKATVAEAKQLAWLVDRPNTLIKIPATKAGIPAITEVIGLGISVNVTLIFSLERYRMVMDAYLAGLEKAKERGLDLSKIHSVASFFVSRVDTEIDKRIDALGTPEAKAARGKAGLANARLAYEAYEAVFSTDRWLALDKAQANKQRPLWASTGVKDPAYKDTMYVEELVAPNTVNTMPEATLEATADHGEIRGNTIAGTYEQARADLDAVEKLGIAYDDVVQLLEEEGVDKFEASWNDLLKSTEAELQRLAPSEG
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q829U5
Q7NCC0
RS18_GLOVI
30S ribosomal protein S18
Gloeobacter
MTSFGYRGKRVSPIPPKDKIDYKEVDLLRKFITERGKILPRRITGLTAKQQRDLTVAIKRARLLALLPFVNQEG
Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit.
Q7NCC0
P83149
OM4VA_VIBAL
Outer membrane protein 40Va
Vibrio
AEVFKSEEGSVDFYGQLRPA
Forms pores that allow passive diffusion of small molecules across the outer membrane.
P83149
Q8ZQ23
TRHO_SALTY
tRNA hydroxylation protein O
Salmonella
MPVLHNRISNDELKAKMLAESEPRTTISFYKYFTIASPQQTRDALYQVFTALDVFGRVYLAHEGINAQISVPQSKLETFRQQLYTFDPALDGVRLNIALEDDGKSFWVLRMKVRDRIVADGIDDPTFDASNVGDYLKAADVNAMLDDPDAVFIDMRNHYEYEVGHFENALEIPADTFREQLPKAVEMLREHADKKIVMYCTGGIRCEKASAWMKHNGFNKVWHIEGGIIEYARRARAQGLPVRFIGKNFVFDERMGERISDEVIAHCHQCGASCDSHTNCKNDGCHLLFIQCPQCASKFNGCCSEQCCEELALPEEEQRRRRAGRENGNKIFNKSRGRLNSKLSIPDPAE
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
Q8ZQ23
Q4ZNZ9
ARGJ_PSEU2
Arginine biosynthesis bifunctional protein ArgJ beta chain
Pseudomonas syringae
MAVGLGPLPALHPVPGFELGISSAGIKRPGRKDVVVMRCAEGSSVAGVFTLNAFCAAPVILAKQRVQGTVRYLLTNTGNANAGTGEPGLAAARRTCEKLAQLTGVDASAVLPYSTGVIGEPLPVEKIEGALQAAIDDLSVDNWAAAATGIMTTDTLPKGTSRQFSHDGVTVTVTGISKGAGMIRPNMATMLGYIATDAKVAQSVLQDLIRDGANKSFNRITIDGDTSTNDCCMLIATGQADLPEITEAKGPLFEALKKAVFDVCMEVAQAIVRDGEGATKFVTVEVNGGGNHQECLDVGYAVAHSPLIKTALFASDPNWGRILAAVGRAGVPDLDVSKIDVFLGGVCIASQGCRATTYTEEQGSAVMAEEEITIRIELGRGDCSETIWTTDLSHEYVKINAEYRT
Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Q4ZNZ9
P15063
MYCB_RAT
Protein B-Myc
Rattus
MPLHVSLANGNRDLDYDSVQPYFMCDDEEEDVHQQPPQPPAPSEDIWKKFELLPTPRPSPGHPGLYSPPCEAVAASFSPRDHDGDSFSTADLPELPGDAVKQSFVCDPDDETFVKNIILQDCMWNGFSASAKLVSKLDPYQAVRKEGASVSPAADVEPATPPDCTCNT
Seems to act as an inhibitor of cellular proliferation.
P15063
O52691
T2S1_STRCS
Type-2 restriction enzyme ScaI
Streptomyces
MINDQLPRWVREARVGTRTGGPAMRPKTSDSPYFGWDSEDWPEVTRQLLSEQPLSGDTLVDAVLASWESIFESRLGSGFHIGTQIRPTPQVMGFLLHALIPLELANGDPSWRADLNSSEKDLVYQPDHKYSIEMKTSSHKDQIFGNRSFGVENPGKGKKAKDGYYVAVNFEKWSDAPGRLPRIRTIRYGWLDHTDWVAQKSQTGQQSSLPAVVSNTQLLAIHTGGQR
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-AGTACT-3' and cleaves after T-3.
O52691
Q72XF3
NUOA_BACC1
NUO1
Bacillus cereus group
MASVYENSYMIVLIFLLLGILLPVVALTLGRMLRPSKPSAAKATTYESGIEPFHDANIRFHARYYIFALLFVIFDVETLFLYPWAVAYDKLGLFALIEMFIFVVMLLVGLAYAWKKKVLQWL
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 a menaquinone. 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.
Q72XF3
Q555X4
GNT15_DICDI
Glycosyltransferase-like protein gnt15
Dictyostelium
MSNFYNNNPRRNTFRLTERIKKKPYQTLIVFILIFLFLYVFGPFGEKKSNNNNNNHPVSKTSSFTESLYTKFQTETFAYRANGDLKKYDISIITQFTVDRFDRIAMMADKWRAPISAAVYITSFKDIDEVFKLVRNSFAVTEFVDLHFLFANKTRYPVNNLRNLALRNARTEWCLLLDVDFISPLGMYDYLHSTLEKLDTSNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNENNDNDNGNNNNNNDNEKNFKKKQEDLKIDPNDFEGDLKAIEKLKRNGEKLYVKNLKKVLDGSENNLGKNINFNNNNNDNNNKDDGGGGGYYLNSDNSNINNNNKIAFVIPSFSSSISRFDFPDNKKDLLDFIKQDLIKEINSGVCPKCHGPTNYSRWYLSSEPYLVQYKWIYEPFLLYNRSQIHDYDERLKGYGFDKNSHTFGMAAAGFDFVVLPDAWIIHMNHVSKPWEGADTFNEQMFDCLSIVCESILPDAKSKNGYDPNAKLFNEPLKNNDNCLTREHW
May have a role in modulating cell adhesion and glycosylation. Essential for development.
Q555X4
A6W841
RECA_KINRD
Recombinase A
Kineococcus
MPAPADREKALDAALAAIDKNFGKGSVMRLGDEVRPPIEVIPTGSISLDVALGIGGLPRGRVVEIYGPESSGKTTVALHAVASAQKAGGIAAFIDAEHALDPDYAAKLGVDTDALLVSQPDTGEQALEIADMLIRSGALDIIVIDSVAALVPKAEIEGEMGDSHVGLQARLMSQALRKITGALNHSGTTAIFINQLREKIGVMFGSPETTTGGKALKFYASVRLDVRRIETLKDGTNPVGNRTRVKVVKNKVSPPFKQAEFDIIYGQGISREGGLIDLGVEHGFVRKSGAWYTYEGDQLGQGKENARAFLRDNPDLGDEIEKRIKEKLGIGARLDAPAEVDVEEKVDF
Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.
A6W841
Q6NHT2
ATPD_CORDI
F-type ATPase subunit delta
Corynebacterium
MHAASREALARVTSDLDKALWEAKENAIATAAHTGAELFDVVEVLDGDRALRVAVADSAKSAEDRAGLVSAVFAGKVSPATLEVLVTSARELWSNPREFRDGLVTLGRRALLRSAEGQGQLGQVEDELFRLSRILDKEPELTLLLDDRSTDGAKKRELLAKVLYGKVTAVTEALALQVIGRRESNAIDDIDALSKEAAALQGHSVAHVVSAGRLNDEQNQALAQKLERIYGRAMSIHSEVDPSLLGGLVIRVGDEVIDGSTSGKLERLRANLA
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.
Q6NHT2
Q54DH8
TAF1_DICDI
Transcription initiation factor TFIID subunit 1
Dictyostelium
MAKDKEKKGNLTGFLFGNVKESGELDVEENDQVFKDLKKDLELFAKSSQHISFKKTIGIDEDDKNAVTDSVIVPDKNALDYEDIDEVAEEIQSTENEINKLNADKLANAAIARLQQQHKEREEQQRLKLLEQQQRQLSKKERRKQRKQVGSKQPLQIKKKPSVDDFDFDEEEEQQQQKSTRSEDEDDDDISSASSLSSSSASSSASSSRSPSMSRSASDIESDSMSDSSRSSGSSISSRSSISSSSSRSDSDSDGGGGGGGGGGGSHRRRHKEKKPKKKVTMKAGSYEVVKSILETPEMFTPEDQEFKVFVSGKSSEGFILKFSQLFAPKFPDKPTRKKSRKTRFSTPQTLNDDSIETDELLLWNQPSKKQPPPSIIKKPITEIDSITKQLLKSNAGITSSTGGGGEEDTLTSSNTTTPTLTSMQLYQAAAEEDEEYVPEPLRETEDEEIMTMFYMVPDSNYHSLQQVNWEDNIIWDEESLIKFKKSDHFNQFYLSSDNQQQNIIIKEAITMPVEINDLTPNLNKNSKQTSSSSTTTSTTTTTSTTTTTTTTTTATTLSSTSTSTTTQRNNKNKNKNNNNNINNSSKLFGLDHISEKEEIMDTDSQNLLQQPLSQEKDKEKEKDKDKAQNEQHIQTIVNNKKNSTTNNNNLTNNNGNNNNTNNNNNNSNNNSNNNNNNNNNNKQNNNKEIDEIMKSNIDKWSLFPISNQELENGDWIDNIIWDESMVPEKIQQVSMLILDLNDREMYFEEHIEKKEHNNGESGSNGDQQAPVKKKSKKKLALEAAQAAQAAALERAQAAARAANGQTMSFEEQLQKDKEEDERKEREEREQSQREIDKFNLSNDKFYRPVRKPPPRPPNGSTKVVIQHSLPGIKLSLVKTHLTKEDLIYAHRPRILFPSNVPFRIIIYNKEGSLSGDLSSSSNNLLLNSSTNSIMGGHNMRGSINGGMMSSSSSSSSSSSKKSLHKSDLSARDGRLVLIEYTEQHPPLVSNVGMGLRIRNYYKKKNTHDTGPKDLNFEDGELVMLDNNEESPFLGDINPGQTIQSVVNNLFKVPIHKHNSANTDFLLVKSRDGKRWYIRDVGPIYAAGQILPEVEVPAPNSRNANMFLKSRLQAYIYRQFLKKSNPQRRLKITDICSAFPSQSETSIRKRLKDCADFQRGGDDSGWWTVKDNFTLPTEEEFQKLVTPEAVVSFESMLIGLQRLQDNGIIHFTAPGTIPTILGNLDDEDPIKKSIKPVEDELSITPWNLTGSFLSAMQGKGRLQIISDDPTGREDEYSYLKMPQKVVNQKQKAIKLALQKNQVTGTDADLRKLSLSASKTVLLELGVDEETINKLARWQRIDLVRKKSSEAALASNSNAAMTKFARGSRYSLDHQNLQYKEQCQLVFDNQIKAIAGKGDDLYDEDLDADLLKDLEDSLFGDSNQSQNQNQNQNQNQNQSNNNNNKSSSKSTGKRSRSLFSRDESDEEEDNEEEEYNKLMGTKNKDEESKAKAKAKAEEEEIKAKAEEAKAKAKAKAEEDDLTQGDRVFVKRTTLFQKPDGSLFKRIEIIRDPKVVQDYQKKKHDQFLQDRKKFGKQNEEDEETKKQRRRIQERLRRLKKNDQREDSFNMNSSNSSIGATIGSSNMINISAGNIPVSNINNNNYNNNNNNNNFSLNTSSSNKPIPPHRSSSSGIGSSGSNNNSNTDRDQTRISIVMPNQQANSDSNSSSSTKIRIGQSSSSSSSSSSSSGHPRSSDREHRSSEHRSGEHRSSEHRSSEHRGSEHRSSEHRSGEHSSHHRSSEHRSGDREHRSSDRGDREHRSSEHRSSEHRSSEHRSSEHRSGDKEHRSDREHRSSEHRSGDREHRSDREHREHRSGDREHRSDREHREHRSERSRNSSSGSSSSSRDHRDSHHRNSTGSSSDSHSSSHHSSSNRDSNHNGGSSSNNNNNNSNNNHNNNNNSNNNNNNNNNNNNNNNINNNNNNNNNINNINNNNNNNINNINNNYNNNNNNNNNNNNNNNNNNNNNNINNNENNNTNNLSNSTNQSPTLSQSGIIIRYNGSNSGNSNNTNGGNNRTEDQSVLNTPLSASSSGSNRKKRTLDQSNSESPSLSSTTLDGSDKSSRRNRVRKDGSGADVELSNIFERILDKLRTNDEFIAFRHKVTPKLAPDYHKVIKNPIDLTTMRDRNRHWEYKSKNQFIDAIKLMVANCFEYNEKRFSHLLPIAEKLLTSTLQLLAPFDSQIGDLEKSIEQTNLKQSSSSLLLSVDHTNGSTPSTPITLNTPITPNLPSNSPFFPPVDPPSKAHHSAEDEEIDIVSLYESGVSPSVKNNFN
May be a component of the TFIID basal transcription factor complex.
Q54DH8
A8Z655
RSMG_SULMW
16S rRNA 7-methylguanosine methyltransferase
Candidatus Sulcia
MKERIFNKYFPDLDKSIIKKFIKLYKIHKFFNKKINIISNNSLNFFYERHILHSLCVYKICYFLNKSIIIDVGTGGGFPGIPLALLFNKTKFILIDSIEKKIKIINLIIKELHLKNVYVKCTRIENFHNKCNFIIGRAVTKLPNFIRLVKKNFLFKKKNKINNGILYLKGGEFENEKNNQYLYIKYNIYNFLKKFFFKKKLFIFLLFNIKII
Specifically methylates the N7 position of a guanine in 16S rRNA.
A8Z655
A2C5M1
Y024_PROM3
Nucleoid-associated protein P9303_00241
Prochlorococcus
MAGFGLPNFGQLTEAFRKAQQIQQNAQKLQEELDAMEIEGSSPDGRASIWLSGNQQPLRVRLEPSLLAEGQDASETAILAALQSAYEHSTTTMKEQMEELTGGLNLNLPGMSD
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
A2C5M1
P60403
RL2_RHOPA
RRP-L2
Rhodopseudomonas
MALKTFNPTTPGQRQLVMVDRSALYKGKPVKRLTEGKNSNGGRNNTGRITVRFRGGGHKQAYRLVDFKRTKVDVPAKVERLEYDPNRTAFIALIKYEDGEQAYILAPQRLAVGDTVIAGAYVDVKPGNVMPLGNMPIGTIVHNVELKIGKGGQLARSAGTYAQIVGRDHDYVILRMNSGEQRLIHGRCIAAIGAVSNPDHMNISIGKAGRKRWLGRRPHNRGVVMNPIDHPHGGGEGRTSGGRHPVTPWGKPTKGKKTRSNKSTDKFILISRHKRKKK
One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome.
P60403
B2J918
SELO_NOSP7
Protein adenylyltransferase SelO
Nostoc
MTLAETPNYKNSSNPLLSLNYESALESLGDDYYDEVAAAEFPQHILRWRNDALLPRLGLDPQVVKDEDFITAFGQFQGRKPLLALRYHGYQFGEYNGQLGDGRGFLYGQVRATDGELYDFGTKGSGRTPYSRGGDGMLTLKGGVREVLAAEALHHLGVRTSRCLTMIETGLPLWRGDEPSPTRSSVMIRMSSSHIRFGTFERLHYFQRPDLTKKLLDHVIEQYYRHLSSEQDKYVLFYAELVKRVAELVAQWMAAGFCHAVLNTDNMSITGESFDYGPYAFIPTYNPSFIAAYFDYYGRYCYGNQPSICKLNLQMLQEPLKAILDKDEMEAALERFDEYYQAEYSSLMLKRLGFVELSYPQAAELLNLTVEFLKDSQVGYHQFFYEMARTFSSKWRDEPGFVMNNSDIVPVPGASGIFDDWCILYHKILNDFDSDRIDVIAQTLAVHNPKTALLRPVIESTWKAIAQEDNWQPFYELIQAIQSRK
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
B2J918
Q9JKM5
S1PR5_RAT
Sphingosine 1-phosphate receptor Edg-8
Rattus
MESGLLRPAPVSEVIVLHYNYTGKLRGARYQPGAGLRADAAVCLAVCAFIVLENLAVLLVLGRHPRFHAPMFLLLGSLTLSDLLAGAAYATNILLSGPLTLRLSPALWFAREGGVFVALAASVLSLLAIALERHLTMARRGPAPAASRARTLAMAVAAWGLSLLLGLLPALGWNCLGRLEACSTVLPLYAKAYVLFCVLAFLGILAAICALYARIYCQVRANARRLRAGPGSRRATSSSRSRHTPRSLALLRTLSVVLLAFVACWGPLFLLLLLDVACPARACPVLLQADPFLGLAMANSLLNPIIYTFTNRDLRHALLRLLCCGRGPCNQDSSNSLQRSPSAVGPSGGGLRRCLPPTLDRSSSPSEHSCPQRDGMDTSCSTGSPGAATANRTLVPDATD
Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. Is coupled to both the G(i/O)alpha and G(12) subclass of heteromeric G-proteins. Displays antiproliferative effects in transfected CHO-K1 and HEK293 cells.
Q9JKM5
Q9D5H4
FTMT_MOUSE
Ferritin, mitochondrial
Mus
MLSCFWFFSKHISSALMSLPRVLHRFTAPQCLASRYPLGPLLASPRRLLASVASSQDSTRPSRVRQNFHPDSEAAINRQINLELYASYVYLSMAYYFSRDDVALYNFSKYFLRQSLEEREHAEKLMKLQNQRGGRICLQDIKKPDKDDWECGLRAMECALLLEKNVNQSLLDLHTLASEKGDPHLCDFLETHYLHEQVKSIKELGDHVHNLVTMGAPAAGLAEYLFDKHTLGSESKH
Catalyzes the oxidation of ferrous iron(II) to ferric iron(III) and stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
Q9D5H4
Q5WLZ3
RECR_ALKCK
Recombination protein RecR
Alkalihalobacillus
MQYPRPIAKLIEGFTRLPGIGPKTASRLAFHVLDMKEDDVLEFAKALVHAKRDLTYCSQCHNITDTDPCQICEDKHRDRTTICVVQESRDLIAMEKMREYTGLYHVLHGAISPMDGIGPEDIKIAELIKRLQDDESVKEVIVATNPTIEGEATAMYISRLIKPTGIKVTRLAHGLPVGGDLEYADEVTLSKAIEGRREL
May play a role in DNA repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecO.
Q5WLZ3
Q3JCC5
LEUD_NITOC
Isopropylmalate isomerase
Nitrosococcus
MEPLTVVEGLVVPLDRANVDTDAIIPKQFLKSIKRTGFGPNLFDEWRYLDHGEPGKDCRHRPLNPEFVLNQPRYQGANILLARDNFGCGSSREHAVWALVDDGFRVVIAPSFADIFHSNAFKNGLLPIILDEDSVTTLFKDTEATLGYRLRIDLPAQEVTTPEGKVMPFTIDEFRKHCLMEGLDEIGLTLQYRDEIRAYEERRQVEAPWLFEKG
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Q3JCC5
P40687
TOP3_SALTY
DNA topoisomerase III
Salmonella
MRLFIAEKPSLGRAIADVLPKPHRKGDGFIECGNGQVVTWCIGHLLEQAQPDAYDSRYARWNLADLPIVPEKWQLQPRPSVTKQLNVIKRFLHQAGEIIHAGDPDREGQLLVDEVLDYLQLPAEKRQQVRRCLINDLNPQAVERAIDRLRANSDFVPLCVSALARARADWLYGINMTRAYTILGRNAGYQGVLSVGRVQTPVLGLVVRRDEEIENFVAKDFFEVKAHIVTPADERFTAIWQPSEACEPYQDEEGRLLHRPLAEHVVNRINGQPALVTSYNDKRESESAPLPFSLSTLQIEAAKRFGLSAQNVLDICQKLYETHKLITYPRSDCRYLPEEHFAGRQAVMNAISVHAPDLLPQPVVNPDTRNRCWDDKKVDAHHAIIPTARSSSVHLTENEAKVYTLIARQYLMQFCPDAVFRKCVIELEIAKGKFVAKARFLAEAGWRTLLGSKERDEENDGTPLPVVAKGDELLCEKGEVVERQTQPPRHFTDATLLSAMTGIARFVQDKDLKKILRATDGLGTEATRAGIIELLFKRSFLTKKGRYIHSTDAGKALIHSLPEMAARPDMTAHWESVLTQISEKQCRYQDFMQPLVGTLYQLIEQAKRTPVKRFRGIVAPGGGDKKKSAPRKRAGKKSPPAAETGRQTE
Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
P40687
Q668Z7
5DNU_YERPS
Nucleoside 5'-monophosphate phosphohydrolase
Yersinia
MSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAFVAHALAIIKNRKFNGNLNAERIALLAMYHDASEVITGDLPTPIKYHNPKIAHEYKKIEKVAQQKLIEMLPKELQHDFRCLLDEHYYSEEEKALVKQADALCAYLKCLEELSAGNNEFIQAKARLENTLAIRQSPEMDYFMAVFVPSFSLSLDEISLDSLD
Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates.
Q668Z7
Q4FR92
SYS_PSYA2
Seryl-tRNA(Ser/Sec) synthetase
Psychrobacter
MIDPKLLRGDLTDLQQQLATRGYTLDMAFWQSIENERKSLQVQTEELQSRRNAGAKQVGALKKSGEDTSELLADMQSVSGEIKTAEDELRTLQERINQAALQIPNIPAADVPVGASEDDNVEVRKWGTPREFDFEIKDHAHIGETLGMLDFEAAAKLTGSRFNVLKGQLAQMHRALIQFMLNTHTIKYGYTETYVPYIVNSESLKGTGQLPKFEGDLFKLINHTNNDDMDFYLIPTAEVPMTNLVRGERLDIKELPLKFTAHTPCFRSEAGSHGRDTRGLIRQHQFEKVEMVNIATAEQSDELLEAMTGQAEFILQQLNLPYRTVKLCTGDMGFAAQKTYDIEVWLPSQDTYREISSCSNCGDFQARRMGTRVKDGKQTSLVHTLNGSGLAVGRTLLAVMENYQNADGSITIPEVLRPFMGGADSIL
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Q4FR92
P55114
NAS33_CAEEL
Nematode astacin 33
Caenorhabditis
MLFVSILISQFVTCLTQPDFFERPPPPDWFFPGPLRPWGPPPPWHRNRGPPPFGPPPPWDRPPPPWRRPPWHRRPPWGLPPPPPPPEPEPQQDQPQVMFSQDIDKVVNSVNQNTAAFQRPGESYDKVIQIMSSYFNRKSGSQYDINTVIPSSGIYNNEMAANSKIAAVMFESDMALTVSQMNKVAQNGFRVKRKMNLNGTTWSRNIPYRFLDTDGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVEPVDPAFINTIGNRVEPSFLDLKLLNTAFCSNICTNRINCQHGGYADPNNCGQCTCPTGLEGTYCERLQTSNCGVELPRADYSWRNISYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCEEFVEMKAEYSHEATGYRQCCKAVLGERISKGNSVLIISKATQNSQFVLRYREDGTAPTQRPPPVRVAAPRSYSLLWSGWTRCSENCGSCGTQYRERCTSTTNCLRSAKQTRVCNTQPCAQGTTRGKRSVLQTQISHRVKRLNGWCCARFVLSRGVCVPVRTGVTHPN
Metalloprotease.
P55114
P0CAR5
3S1E3_MICPY
Weak neurotoxin E3
Micrurus
LICFNDFSPTARTLEYCQIGITTYNPS
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
P0CAR5
Q8FS34
RS4_COREF
30S ribosomal protein S4
Corynebacterium
MARYTGPATRKSRRLRVDLVGGDMAFERRPYPPGQAGRARIKESEYLLQLQEKQKARFIYGVMEKQFRRYYAEANRRPGKTGENLVVMLESRLDNVVYRAGLARTRRQARQLVSHGHFVVNGKAVDVPSFRVSQYDIIDVREKSQKMNWFEEAQDNLVDAIVPAWLQVVPSTLRILVHQLPERAQIDIPLQEQLIVEFYSK
With S5 and S12 plays an important role in translational accuracy.
Q8FS34
Q5F3V3
PDS5A_CHICK
Sister chromatid cohesion protein PDS5 homolog A
Gallus
MDFPAAQPKPAADGKIIYYPPGVKETTDKITNDEVVKRLKMVVKTFMDMDQDSEDEKQQYLPLALHLASEFFLRNPNKDVRLLVACCLADIFRIYAPEAPYTSHDKLKDIFLFITRQLKGLEDTKSPQFNRYFYLLENLAWVKSYNICFELEDCNEIFIQLFRTLFSVINNSHNQKVQMHMLDLMSSIIMEGDGVTQELLDSILINLIPAHKNLNKQAFDLAKVLLKRTVQTIEPCIANFFNQVLVLGKSSVSDLSEHVFDLILELFAIDPHLLLSVMPQLEFKLKSNDGEERLAVVRLLAKLFGSKDSDLATQNRPLWQCFLGRFNDIHVPVRLESVKFASHCLMNHPDLAKDLTEYLKVRSHDPEEAIRHDVIVTIITAGKRDLSLVNDQLLGFVRERTLDKRWRVRKEAMMGLAQLYKKYCLHAEAGKDAAEKVSWIKDKLLHIYYQNSIDDKLLVEKIFAQYLVPHNLETEERMKCLYYLYASLDPNAVKALNEMWKCQNMLRSHVRELLDLHKQPTSEANSAAMFGKLMTIAKNLPDPGKAQDFVKKFNQVLGDDEKLRSQLELLISPTCSCKQADVCVREIARKLANPKQPTNPFLEMVKFLLERIAPVHIDSEAISALVKLMNKSIEGTADDEEEGVSPDTAIRAGLELLKVLSFTHPTSFHSAETYESLLQCLRMEDDKVAEAAIQIFRNTGHKIETDLPQIRSTLIPILHQKAKRGTPHQAKQAVHCIHAIFSNKEVQLAQIFEPLSRSLNADVPEQLITPLVSLGHISMLAPDQFASPMKSVVANFVVKDLLMNDRSTGEKNGKLWSPDEEVSPEVLAKVQAIKLLVRWLLGMKNNQSKSANSTLRLLSAMLVSEGDLTEQKRISKSDMSRLRLAAGSAIMKLAQEPCYHEIITPEQFQLCALVINDECYQVRQIFAQKLHKALVKLLLPLEYMAIFALCAKDPVKERRAHARQCLLKNISIRREYIKQNPMANEKLLSLLPEYVVPYMIHLLAHDPDFTKPQDVDQLRDVKECLWFMLEVLMTKNENNSHAFMKKMAENIKLTRDAQSPDEPKANEKLYTVCDVALCVINSKSALCNADSPKDPVLPTKFFTQPEKDFSNDRNYISEETRVLLLTGKPKPTGVLDTVNKPLSATGRRPYIRTTGSETGSNISVNSELSSSAGNRSREQSSDISETGVSENDENPVRIISVTPAKTEPVKNKEINSDQATQGNSTERGKKRTATASGTENIHQKAEENNADETGPSLAAKTRRGRPPKPEPQGTTAKNEETNKPPVRGRKRAAASQESPGSLEAGNAKAPKQQDTAKKPAAAQRQIDLQR
May regulate sister chromatid cohesion during mitosis and couple it to DNA replication.
Q5F3V3
Q7UN32
RS12_RHOBA
30S ribosomal protein S12
Rhodopirellula
MPTINQLVRKNRKQKKSQSKSPVLEKCPQKQGVCLQVRTMTPKKPNSALRKITRVRLSNGKEVTVYIPGEGHNLQEHSIVLVRGGRVRDLPGVRYQVVRGSRDALGVDGRKQSRSRYGAKK
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.
Q7UN32