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
|
|---|---|---|---|---|---|---|
B5EB44
|
COAD_CITBB
|
Pantetheine-phosphate adenylyltransferase
|
Citrifermentans
|
MPLKLAVYPGSFDPVTYGHLDIIDRGLKIFDGVIVAVARNSEKNALFTVQERIELLTEILKDRPEARVETFDGLLVDYVRRVGASVVIRGLRAVSDFEFEFQLAQMNRNITRDVETLFMMTSVPYSYLSSSIVKEVSCLNGPVDKLVPPLVKSALDAKFRG
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
B5EB44
|
Q47EL1
|
ISPF_DECAR
|
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
|
Dechloromonas
|
MNFRVGQGYDVHKLVDGRKLILGGVEIPHPTGLLGHSDADALLHAITDALLGAVALGDIGRHFPDTDPRYKGADSRVLLRAAVALLAERGWRPVNVDATLIAQQPKLAPHAVAMVANVAADLGISPDCVNIKGKTNERLGYLGREEAIEAQAVALVERVG
|
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
|
Q47EL1
|
Q2S6X5
|
NAGB_HAHCH
|
Glucosamine-6-phosphate isomerase
|
Hahella
|
MRVIIADSPEAVARMGAEQCIRLLQDKPAAVLGLATGSTPIALYAHLIQRRQQGEVSFHQVRTFNLDEYIGIAPQHPQSYRSFMQKQLFDHIDVLPENTHIPNGMGDPIAESRAYEDKIHSAGGIDLQILGLGRNGHIGFNEPTSSLSSRTRAKTLTQETIRDNSRFFSADEEQPHLAITMGIGTILDARKIMLLAAGAAKADAVKAMVEGPISAMHPASALQMHPSALVIVDTDAASKLELIDYYRWVQSETLRVQGAYL
|
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
|
Q2S6X5
|
A0A2H5RJD4
|
CRN1_RHIID
|
Crinkler effector protein 1
|
Rhizophagus
|
MSITLLCLIKGNTLANAFPVDIDKDQLVGHLKKVIKAEQPQTFANVDAKDLKLWRVPISDDHDDQLRNLSLEDSDELLAIRKISKYFPDSPPEECIHVLVEPPESTATSEVLKLREEVASLQALLNKSVAFDVVVSPKRTKGFKWTVNIEQATLDGLKEHIRKMEKPPALENDGAVLNIVNESGKYSPLNDQDLREMLQLFVSNKNLKFTVFIETPSKAFSDWTFSSVCQLYGLNGETEDPTMTVFPNFSCGNVKPSQESLEGLMAELKSRLDNTPISLLSVEATKSLYVYSYLLAGANNFKGKFEIRPQKVISGPNGHGPLDFAIDLCQTAKTVGVTEVKKDDFVKGVAQCAVQLESSLSYRKRKADEMEERTFGRVFGIVTDAEKFYFMECSMDDQDRPSFKLSKPVTVVYEDNDLQTKVEKVLEHIVWLLEEAQKPDSALDVKEREIKRVRSGELPKVTDLEGKTN
|
Effector that participates in the arbuscule development step of the symbiosis. Arbuscular mycorrhizal (AM) symbiosis is one of the most prominent and beneficial plant-microbe interactions that facilitates mineral nutrition and confers tolerance to biotic and abiotic stresses . Is not involved in cell death processes .
|
A0A2H5RJD4
|
O79881
|
NU4M_PIG
|
NADH dehydrogenase subunit 4
|
Sus
|
MLKIIIPTTMLLPMTWMSKHNMIWINATVHSLLISLISLSLLNQLGENSLNFSLTFFSDSLSAPLLVLTTWLLPLMLMASQSHLSKETTTRKKLYITMLILLQLFLIMTFTATELILFYILFEATLVPTLIIITRWGNQTERLNAGLYFLFYTLAGSLPLLVALVYIQNTTGSLNFLIIHYWSHPLSNSWSNIFMWLACIMAFMVKMPLYGLHLWLPKAHVEAPIAGSMVLAAVLLKLGGYGMMRITTILNPLTNYMAYPFLMLSMWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIVAIMIQTPWSFMGATALMIAHGLTSSMLFCLANTNYERVHSRTMILARGLQTLLPLMATWWLMASLTNLALPPSINLIGELFIITASFSWSNITIILMGMNMMITALYSLYMLITTQRGKYTHHINNIKASFTRENALMALHILPLLLLTLNPKMILGPLY
|
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.
|
O79881
|
Q8KQN8
|
CPHE_PSEAG
|
Extracellular cyanophycinase
|
Pseudomonas
|
MIRSFIRSSALLLALLPVTGYSAGPLILVGGGLKDDNTAIYQRLIQLAGGNGQARIGVITAASIPESDDPDAGTADAANSKANGEFYAQLLETYGAADAQWIPIDLDQISNNSNPQVVAQINSMTGFFFGGGDQSRLTQTLQTATRADSPALAAIRARHNAGAVLAGTSAGTAIMVQGPMVTGGESYDGLRYGVYTTPSGDDLSYDMQGGFGFFNYGLLDTHFSERGRQGRIVRLADHTQVPFAFGVDENTALLVQNNATLGQVEMEVIGENGVFIFDLRNKERGTGSTYALYDVLGSYLTAGDRYRPVTGQFVIASGKTSLRGRERYSAAMTVTTDIFSSPNNSGANGRRKPREFVKVSADLFDSRVTSTLGRTYETNPLSRRSVQKHAVRQPWLPGHRWRQEHAVLPAFADGFPS
|
Exopeptidase that catalyzes the hydrolytic cleavage of multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer) into aspartate-arginine dipeptides.
|
Q8KQN8
|
Q8EEW2
|
NAGZ_SHEON
|
N-acetyl-beta-glucosaminidase
|
Shewanella
|
MSYLMLDLLSLDVSEAEAEMLRHPQVGGLILFSRNFTSREQLIALVQQIRQIRPEILIAVDHEGGRVQRFREGFTLIPAMGDILPAAKGDMALAKRWACELGFLMAIELLACDIDLSFAPVLDLNGISQVIGKRSFSANPDEVIALARSFIEGMAQAGMGAVGKHFPGHGSVAADSHIAQPIDEREGEVIFNQDILPFKELIFNGKLSGIMPAHVIYPKVDPNPAGFSSYWLKQILRKELGFNGVIFSDDLGMKGASFAGDYVGRAKAALDAGCDMILVCNDNPGVMTLLNGFVWPEAAPQHPASLLKPNMAQTALALENSARWENAKQLAEQIQLAQQAKV
|
Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
|
Q8EEW2
|
Q8UD04
|
ALLA_AGRFC
|
Ureidoglycolatase
|
Agrobacterium tumefaciens complex
|
MTDFLEIRPLTKEAFTPFGDVIETTPSSMRHINGGQTERHHALSAPEAAGEGARIILNIFRGQPRVFPHKIDMMERHPLGSQSFSPLSGRPFLVVVAQDDGGRPARPQVFLARGDQGVNYRRNVWHYPLMPLQAVSDFLVADREGPGNNLEEYFFDEPFMIAEPSL
|
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.
|
Q8UD04
|
Q7NMQ7
|
RSMG_GLOVI
|
16S rRNA 7-methylguanosine methyltransferase
|
Gloeobacter
|
MDSGALWQDLGWQPDTLQARSFERLYALVLAGNTRLNLTRITGREEFWEKHLFDSLRGLAAFQDQKEPSLIDIGTGAGFPGLPIAIAHPDWYVVLVDSVRKKIAFVLSTIQALGLTNAQALTGRAEDLAHRREHRESYDLAVLRAVAQANVCAEYALPFVKLGGAAVLYRGNWEVQEEVELARACRALGGEIVEVDAFELPVSRAVRHCVVIRKTGPGLRVFPRPAGLPTQHPLGAIEGAPRVESEEPEEP
|
Specifically methylates the N7 position of a guanine in 16S rRNA.
|
Q7NMQ7
|
Q8Q0J1
|
OTC_METMA
|
Ornithine carbamoyltransferase
|
Methanosarcina
|
MKRDVLSITDLSREEIYELLESAADLKKKRKAGEPTEYLKHKSLGMIFEKSSTRTRVSFEVAMSDFGGHALYLNSRDIQVGRGETIEDTARTLSGYLHGIMARVMSHDTVEKLARFSTIPVINALSDREHPCQILGDFMTIMEYKNRFEGLKFAWIGDGNNVCNSALLGSAIMGMEFVIACPEGYEPGAEFLEKAKALGGKFSITDDPKTAAKDADIIYTDVWVSMGDEAEQEKRLKDFGSFQVNTELLGVAKPDVIVMHCLPARRGLEITDEVMDGPNSVIFEEAENRLHAQKALILKLMR
|
Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
|
Q8Q0J1
|
Q1RKD1
|
NUOH_RICBR
|
NDH-1 subunit H
|
belli group
|
MIELFFEYIFPLIIIALKVVAITIPLILCVAYLTYAERRVIGLMQLRRGPNVVGPFGLLQPIADAVKLLFKEPIIPTNADKILFVLAPMITFILSLIGWAVIPFAKGVVLADINVGVLYILAISSLSVYGIIIAGWASNSKYAFLGAIRSSAQMISYEVSMGLVIITVLLTTGTLNLSQIVEAQRTMPWWIDLMLMPMGVVFFISVLAETNRLPFDLPEAESELVAGYNVEYSSMGFALFFLGEYANMILVSAMTTTFFLGGYLPPFNISWLDCIPGFFWFVFKVGFLLFCFLWIRATLPRYRYDQLMRLGWKVFLPLTLFWVVLVSSVLIYTDHLPNV
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone.
|
Q1RKD1
|
Q88FY6
|
NICT_PSEPK
|
Nicotinate degradation protein T
|
Pseudomonas
|
MPIANATTVHSDIDHGTKALYSKITWRLIPFLCFCYLAAYLDRINVGFAKLQMLEDLQFSTAAYGLGAGLFFVGYIIFEVPSNLILQRVGAKLWIARIMITWGLLSACTMFVTSTTQFYILRFLLGAAEAGFLPGVLYYLTMWYPTYRRGRIIALFMIGLPLSSVIGGPISGWIMGHFDQVQGLHGWQWLFLLEAIPSVLLGILTFWALPNHFQQAKWLSADDKAQLAADLAADDAEGKDSKHSFRDGFFNLKVWMLGGIDFSILLSAYAMGFWMPTFIRDAGVSDTFHIGLLTAIPSLAALAGMLMIGASSDRHRERRWHIIVPFIIGAIAMASSTLFSQNLVMTVVLFAIASAAIIGAVPVFFSLPATFLKGTAAATGFALACSVANIAGLVSNSLMGVVTDLTGTSHAALWVFAGCLILSCFLVIALPAKLVNR
|
Probable transporter, possibly involved in the aerobic nicotinate degradation pathway.
|
Q88FY6
|
Q7VQP7
|
ORN_BLOFL
|
Oligoribonuclease
|
Candidatus Blochmannia
|
MNEDNLIWIDLEMTGLNPERDRILEIATLITDNELSILSEGPVLTIYQPESQLLLMDEWNTYTHSSNGLLKEVRSSKLNECDASILVLKFLKNWVPCKSSPMCGSSVAQDRRFLLKYMSELESYFSYRYLDVSTIKELMFRWRPDLKTGLQLHKSHRALADIQESVLELKYYRKYFINCN
|
3'-to-5' exoribonuclease specific for small oligoribonucleotides.
|
Q7VQP7
|
B1KQ37
|
ATPD_SHEWM
|
F-type ATPase subunit delta
|
Shewanella
|
MAEITTIARPYAKAAFDFAIEKNAVDSWAEMLNFAAMVSENETMKPLLSGSLASHQLAELFIGVCGEQVNEQGQNLLKVMAENGRLETLPAVSQLFVEMKHEWAKEIEANVVSATELSSEQQQEISVSLEKRLTRKVKLNCSIDASLIAGLIITAGDLVIDGSVRGKVSRLSDSLQS
|
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.
|
B1KQ37
|
C5BES7
|
DER_EDWI9
|
GTP-binding protein EngA
|
Edwardsiella
|
MIPVVALVGRPNVGKSTLFNRLTRTRDALVADFPGLTRDRKYGRAEVNGHEFIIIDTGGIDGTENGVETHMAEQSLMAIEEADIVLFLVDARDGLLPADEAIARHLRSRDKATFLVANKTDGIDAEVAVGDFYSLGMGEVHPIAASHGRGVTQLIEDALVPFIPQEAPAPVLSEEEENAAYWAELEAEADGEAQEEEEAFDPINQPIKIAIVGRPNVGKSTLTNRILGEDRVVVYDMPGTTRDSIYIPMERDEREYVLIDTAGVRKRGKVTDTVEKFSVIKTLQAIEDANVVLLVIDARQGISDQDLSLLGFILNSGRSLVVVVNKWDGLSLEVKEQVKDMLDLRLGFVDFARIHFISALHGSGVGNLFESIQEAYESATRRVSTAMLTRIMTMAQDDHQPPMVRGRRVKLKYAHAGGYNPPIVVIHGNQVKDLPDSYKRYLMNYFRRSLNVMGTPIRIQFKEGDNPFANKRNTLTPNQMRKRKRLLSHLKKTK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
C5BES7
|
Q09X16
|
YCF3_MORIN
|
Photosystem I assembly protein Ycf3
|
Morus
|
MSRSRINGNFIDKTFSIVANILLRIIPTTSGEKEAFAYYRDGMSAQSEGNYAEALQNYYEAMRLEIDPYDRSYILYNIGLIHTRNGEHTKALEYYFRALERNPFLPQAFNNMAVICHYRGEQAIRQGDSEIAEAWFDQAAEYWKQALALTPGNYIEAQNWLKITGRFE
|
Essential for the assembly of the photosystem I (PSI) complex. May act as a chaperone-like factor to guide the assembly of the PSI subunits.
|
Q09X16
|
P50939
|
NUOL_RHOCA
|
NDH-1 subunit L
|
Rhodobacter
|
MTTIILLAPLLGALIGGFGWRLITEKGALVVTTGLLFLSCILSWVVFLTLPAETQHIHLLDWIRSGALDTSWGIRLDRLTAIMLIVVTTVSALVHLYSWGYMAHDENWTHHEAYKARFFAYLSFFTFAMLMLVTSDNLVQMFFGWEGVGVASYLLIGFYYKKPSANAAAIKAFVVNRVGDFGFALGIMGLFFLTDSIDMDVIFASAPELAKTELHFLAWEFNAANLLAVLLFIGAMGKSAQLFLHTWLPDAMEGPTPVSALIHAATMVTAGVFLVCRMSPLFEYAPEAKMMVVYVGAVTAFFAATVGLVQNDIKRVIAYSTCSQLGYMFVAAGSGVYSVAMFHLLTHAFFKAMLFLGAGSVIHAMHHEQDMRNYGGLRKKIPFTFAIMMIGTLAITGVGIPFFSIGGVPVGFAGYLSKDAIIESAFASGNGFAFYVLVAAAGMTSFYSWRLIFLTFYGEARGDHHKHDHAHESPAVMLAPLALLAVGSVLAGMVWYHSFFGDKVASFFNLPAAAHGEAHGTEHATEGHVPEAAMTAEAAHEAAMAGTMAMAEPAAEHAVAKAPQGAIFMAETNHVIHDAHGVPDWVKLSPFGAMVTGFFFAWLYYIGDKPLPGRTARALPGLYRFLLNKWYFDELFDLLFVNPAKSLGRKLWKGGDGAVIDGAINGLALGWIPFFTRVAGRIQSGYLFHYAFAMVLGIVALMFWVVRTGGMN
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
P50939
|
A6LEM6
|
MIAB_PARD8
|
tRNA-i(6)A37 methylthiotransferase
|
Parabacteroides
|
MVNQENGVDLKSATQSDERKLFIETYGCQMNVADSEVVASIMKMDGYSMTENIEEADAIFVNTCSVRDNAEQKIYGRLQYFQSLKRKKKSLIVGVLGCMAERVKEDLIHVHHADLVVGPDSYLDLPNLVGAVEHGEKAINVELSTQETYKDVIPLKLPGVHISGFVSIMRGCNNFCTYCIVPYTRGRERSRDIESILNEIRDMHEKGFKEVTLLGQNVNSYSFEKEGETITFPILLDRVAKEVPDMRIRFTTSHPKDMSDDTLRVIAANDNICKFIHLPAQSGSSRILKVMNRKYTREWYLDRIAAIRRIVPDCAISTDLFCGFHSETEEDYQETLSLMREVGYDSAFLFKYSERPGTYAASHLEDNVPEEEKVRRLQGMIDLQNKLSEESNLRDIGKTFEVLIEGFSKRSREQLFGRTSQNKVVIFDKKNYHVGQFIKVKIHKASSATLFGEPVEE
|
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
|
A6LEM6
|
A3PH14
|
ILVC_CERS1
|
Ketol-acid reductoisomerase type I
|
Cereibacter
|
MRVYYDRDCDINLIKDKKVAILGYGSQGHAHALNLRDSGAKNVVVALREGSPSAKKAEAEGLKVMGIAEAAAWCDLIMFTMPDELQAETYKKYVHDNLREGSAIAFAHGLNVHFGLIEPKPGVDVIMMAPKGPGHTVRGEYVKGGGVPCLVAVHNDATGKAMEIGLSYCSAIGGGRSGIIETNFRQECETDLFGEQAVLCGGLVELIRMGFETLVEAGYEPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVSGPRILPYEETKARMKAVLTDIQTGKFVRDFMQENAVGQPFFKATRRINDEHQIEQVGEKLRGMMPWISKGKMVDRARN
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
A3PH14
|
Q9GZM5
|
YIPF3_HUMAN
|
Protein YIPF3, 36 kDa form III
|
Homo
|
MATTAAPAGGARNGAGPEWGGFEENIQGGGSAVIDMENMDDTSGSSFEDMGELHQRLREEEVDADAADAAAAEEEDGEFLGMKGFKGQLSRQVADQMWQAGKRQASRAFSLYANIDILRPYFDVEPAQVRSRLLESMIPIKMVNFPQKIAGELYGPLMLVFTLVAILLHGMKTSDTIIREGTLMGTAIGTCFGYWLGVSSFIYFLAYLCNAQITMLQMLALLGYGLFGHCIVLFITYNIHLHALFYLFWLLVGGLSTLRMVAVLVSRTVGPTQRLLLCGTLAALHMLFLLYLHFAYHKVVEGILDTLEGPNIPPIQRVPRDIPAMLPAARLPTTVLNATAKAVAVTLQSH
|
Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis.
|
Q9GZM5
|
Q8AA14
|
THIG_BACTN
|
Thiazole synthase
|
Bacteroides
|
MEKLVIAGREFDSRLFLGTGKFNSNEVMEQAILASGTEMVTVAMKRIDMDDKEDDMLKHIIHPNIQLLPNTSGVRDAEEAVFAAQMAREAFGTNWLKLEIHPDPRYLLPDSIETLKATEQLVKLGFIVLPYCQADPVLCKRLEEAGAATVMPLGAPIGTNKGLQTKEFLQIIIEQAGIPVVVDAGIGAPSHAAEAMELGASAVLVNTAIAVAGNPVEMALAFKAATEAGRRAYEAGLGLQADNFIAEASSPLTAFLE
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
Q8AA14
|
Q47745
|
VANS_ENTFA
|
Vancomycin histidine protein kinase
|
Enterococcus
|
MERKGIFIKVFSYTIIVLLLLVGVTATLFAQQFVSYFRAMEAQQTVKSYQPLVELIQNSDRLDMQEVAGLFHYNNQSFEFYIEDKEGSVLYATPNADTSNSVRPDFLYVVHRDDNISIVAQSKAGVGLLYQGLTIRGIVMIAIMVVFSLLCAYIFARQMTTPIKALADSANKMANLKEVPPPLERKDELGALAHDMHSMYIRLKETIARLEDEIAREHELEETQRYFFAAASHELKTPIAAVSVLLEGMLENIGDYKDHSKYLRECIKMMDRQGKTISEILELVSLNDGRIVPIAEPLDIGRTVAELLPDFQTLAEANNQRFVTDIPAGQIVLSDPKLIQKALSNVILNAVQNTPQGGEVRIWSEPGAEKYRLSVLNMGVHIDDTALSKLFIPFYRIDQARSRKSGRSGLGLAIVQKTLDAMSLQYALENTSDGVLFWLDLPPTSTL
|
Member of the two-component regulatory system VanS/VanR. Activates the transcription of vanH, vanA and vanX in response to vancomycin which results in vancomycin resistance. VanS activates VanR by phosphorylation.
|
Q47745
|
B7VMZ9
|
ATPD1_VIBA3
|
F-type ATPase subunit delta 1
|
Vibrio
|
MSDLTTIARPYAKAAFDFAVDKGELDQWGQMLTFAAEVAQNDDVHNLLSGSMTAEKLAEVFIVICGEQFDEFGQNLIKVMAENGRLMAFPDVCKEFFILKKEYEKEIDVEVTSAVELSEEQRAEISSKLEQRLARKVQLNCSIDETLLSGVIIRAGDLVIDNSARSRLDRLSDALQS
|
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.
|
B7VMZ9
|
B5XL15
|
PYRF_STRPZ
|
OMP decarboxylase
|
Streptococcus
|
MKEERPIIALDFSSFEETKAFLDLFPAEEKLYVKIGMELYYAQGPDIVRYIKSLGHNVFLDLKLHDIPNTVRAAMAVLKELDIDMATVHAAGGVEMLKAAREGLGQGPTLIAVTQLTSTSEDQMRGDQNIQTSLLESVLHYSKGAAKAQLDGVVCSAQEVEAIKAVTPTGFNCLTPGIRPKGSNIGDQKRVMTPNQARRIGSDYIVVGRPITQAKDPVATYQAIKAEWAG
|
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
|
B5XL15
|
P41543
|
OST1_YEAST
|
Oligosaccharyl transferase subunit alpha
|
Saccharomyces
|
MRQVWFSWIVGLFLCFFNVSSAAQYEPPATWENVDYKRTIDVSNAYISETIEITIKNIASEPATEYFTAFESGIFSKVSFFSAYFTNEATFLNSQLLANSTTAPGDDGESEIRYGIIQFPNAISPQEEVSLVIKSFYNTVGIPYPEHVGMSEEQHLLWETNRLPLSAYDTKKASFTLIGSSSFEEYHPPNDESLLGKANGNSFEFGPWEDIPRFSSNETLAIVYSHNAPLNQVVNLRRDIWLSHWASTIQFEEYYELTNKAAKLSKGFSRLELMKQIQTQNMRQTHFVTVLDMLLPEGATDHYFTDLVGLVSTSHAERDHFFIRPRFPIFGGWNYNFTVGWTNKLSDFLHVSSGSDEKFVASIPILNGPPDTVYDNVELSVFLPEGAEIFDIDSPVPFTNVSIETQKSYFDLNKGHVKLTFSYRNLISQVANGQVLIKYDYPKSSFFKKPLSIACYIFTALMGVFVLKTLNMNVTN
|
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
|
P41543
|
Q4K4E4
|
YQGF_PSEF5
|
Putative pre-16S rRNA nuclease
|
Pseudomonas
|
MALRLILGFDYGTKQIGVAVGQAITGQARELCTLKAQNGVPDWNQVEALIKEWKPDAVVVGLPLNMDGSPSDMCVRAEKFARRLNGRFNVPFYTHDERLTTFEAKGERLARGGQKGSYRDNPVDAIAAALLLQGWLDENAGLLNT
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q4K4E4
|
Q5E7N0
|
DAPB_ALIF1
|
4-hydroxy-tetrahydrodipicolinate reductase
|
Aliivibrio
|
MVRVAIAGAAGRMGRNLIKAVNGSQFAVLAAASERPESSLIGVDVGEMAGLGKSGILIVDDLAKVTDDFDVIIDFTLPISTLKNIELCQEHNKAIVIGTTGFSEPGKEIIDQASKEIPVVMAPNYSVGVNLVFKLLEKAAKVMGDYCDIEIVEAHHRYKVDAPSGTAIGMGEAIAGAMGNKLEDVAVYAREGITGERSKDEIGFATIRAGDIVGEHTAMFADIGERVEITHKATDRMTFANGAVRASHWLHKKEPGFYTMHDVLNLDQI
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
Q5E7N0
|
A8S6A4
|
3S11_AUSSU
|
Short neurotoxin 1
|
Austrelaps
|
MKTLLLTLVVVTIVCLDLGYTMTCCNQQSSQPKTTTTCAESSCYKKTWRDHRGTIIERGCGCPNVKPGIQLVCCETNECNN
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
A8S6A4
|
Q8NGU4
|
OR2I1_HUMAN
|
Putative olfactory receptor 2I4
|
Homo
|
MLANQASAEERFLLLGFSDWPSLQPVLFALVLLCYLLTLTGNSALVLLAVRDPRLHTPMYYFLCHLALVDAGFTTSVVPPLLANLRGPALWLPRSHCTAQLCASLALGSAECVLLAVMALDRAAAVCRPLRYAGLVSPRLCRTLASASWLSGLTNSVAQTALLAERPLCAPRLLDHFICELPALLKLACGGDGDTTENQMFAARVVILLLPFAVILASYGAVARAVCCMRFSGGRRRAVGTCGSHLTAVCLFYGSAIYTYLQPAQRYNQARGKFVSLFYTVVTPALNPLIYTLRNKKVKGAARRLLRSLGRGQAGQ
|
Odorant receptor.
|
Q8NGU4
|
P19963
|
ALL1_OLEEU
|
Allergen Ole e I
|
Olea
|
EDIPQPPVSQFHIQGQVYCDTCRAGFITELSEFIPGASLRLQCKDKENGDVTFTEVGYTRAEGLYSMLVERDHKNEFCEITLISSGRKDCNEIPTEGWAKPSLKFKLNTVNGTTRTVNPLGFFKKEALPKCAQVYNKLGMYPPNM
|
May be involved in recognition between pollen-stigma and pollen tube-style cells.
|
P19963
|
Q10PI9
|
PUB75_ORYSJ
|
RING-type E3 ubiquitin transferase PUB75
|
Oryza sativa
|
MPQYQELPCGGQVLDIDTALKDGILGGGPELGDAAAGDGGKQPVELRKMMDELDAAGDGGGDEAVPAVFICPISLEPMVDPVTLCTGQTYESANISRWLALGHRTCPTTMQELWDVTPIPNTTLRQLIAAWFSRRYTRFKKRSADFHGRAAELVHALRGTAVPKRQPLKGQARVAALRELRSLAAAHQSVTKAIAEAGGVGLLTSLLGPFTSHAVGSEAVAILVSGVPLDADAKAALMQPAKVSLLVDMLNEGAVDTKINCVRLIRILMEEKGFRPDTVASLSLLVGVMRLVRDKRHPDGVAAGLELLNSICAVHKPARSLIVSIGAVPQLVELLPELPTECVEPALDILDALAAVPEGRIALKDCPRTITNAVRLLMRVSEACTRRALSMLWVVCRMAPEECAPAALDAGLGAKLLLVIQSGCGPELKQQASELLKLCTMNCTSTVFISKCKLTKTIQ
|
E3 ubiquitin ligase that may function as positive regulator of brassinosteroid (BR) signaling. Possesses E3 ubiquitin ligase in vitro . Acts together with the heterotrimeric G alpha subunit GPA1 at the plasma membrane to mediate a BR signaling pathway that affects plant growth and development. Does not seem to be involved in gibberellin or cytokinin responses .
|
Q10PI9
|
Q29478
|
CP2CV_CAPHE
|
CYPIIC31
|
Capra
|
LVSTPWIELFNAFPSLLRHFPGSHNTIFKNMTEQRKFILEEIKKHQESLDLNNPQDFIDYFLIKMEKEKHNKHSEFTMDNLITTVWDVFSAGTETTSLTLRYGLLLLLKHPEVTAKVQEEIDRVVGRNRSPCMQDRSRMPYTDAVLHEIQRYIDLVPSNLPHVATQDVKFREYLIPKGTAILTSLTSVLHDGKEFPNPGQFDPAHFLDESGNFKKTDHFMAFSAGKRVCVGEGLARMELFLLLVSILQHFTLKPVVDPKHIDIAPSFKGMLSIPPFCEMCFIPV
|
Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
|
Q29478
|
Q6Y4S4
|
KISS1_MOUSE
|
Metastin45-54
|
Mus
|
MISMASWQLLLLLCVATYGEPLAKVAPLVKPGSTGQQSGPQELVNAWEKESRYAESKPGSAGLRARRSSPCPPVEGPAGRQRPLCASRSRLIPAPRGAVLVQREKDLSTYNWNSFGLRYGRRQAARAARG
|
Metastasis suppressor protein. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Intracerebroventricular administration induces an increase in serum LH and FSH levels in prepubertal male and female as well as in adult animals.
|
Q6Y4S4
|
A5WHD5
|
SYT_PSYWF
|
Threonyl-tRNA synthetase
|
Psychrobacter
|
MVAITLPDGNVKEFDGATTVMEVAQSIGPGLAKATIAGRVDGKLVDASDPITQDASVEIVTAKDKDGVDIIRHSTAHLLGHAVKQLYPNVKMVIGPVIEDGFYYDIFSEKPFTPEDMAAIEKRMAELIKQNYDVIKKMTPREEAIKIFEERGEDYKLKLIADMPEEKELGLYHHQEYVDMCRGPHVPNTRFLKVFKLMKMSGAYWRGDAKNEQLQRIYGTAWADKKDLQAYIQRIEEAEKRDHRKIGKALNLFHMQEQSPGMVFWHPNGWTIYQVLEQYMRKVQKDNGYQEIKTPQIVDRSLWEKSGHWGNYATNMFTTSSESRDYAVKPMNCPCHVQVFNQGLKSYRELPIRLAEFGSCHRNEPSGSLHGLMRVRGFTQDDAHIFCTQAQIQEEVANFIKLTLDVYKDFGFDQIEMKLSTRPEKRVGTDESWDIAEKALADALDSSGLEWEYLPGEGAFYGPKIEFSLKDSLGRVWQCGTIQVDPNMPERLEAEFVNENNERETPIMLHRAILGSFERFLGMLIEHYAGWMPVWLAPQQVVVMNITDKQADACQNVASELQNAGLRAITDLRNEKIGFKIRERTLERIPYMLVLGDKEVESGQVNVRTREGENLGVMSVADFIELVQKAVAQKGRLTTKTDEE
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged L-seryl-tRNA(Thr).
|
A5WHD5
|
A6LLN6
|
IF1_THEM4
|
Translation initiation factor IF-1
|
Thermosipho
|
MSNKEDIIKMEGTIVEALPNAMFRVELENGHKILAHISGKMRKNFIRLVPGDKVVVELTIYDLTKGRIVYRKKS
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
A6LLN6
|
Q9GRC4
|
CEM20_MEGRO
|
20 kDa cement protein
|
Megabalanus
|
MKWFLFLLTTAVLAAVVSAHEEDGVCNSNAPCYHCDANGENCSCNCELFDCEAKKPDGSYAHPCRRCDANNICKCSCTAIPCNEDHPCHHCHEEDDGDTHCHCSCEHSHDHHDDDTHGECTKKAPCWRCEYNADLKHDVCGCECSKLPCNDEHPCYRKEGGVVSCDCKTITCNEDHPCYHSYEEDGVTKSDCDCEHSPGPSE
|
Component of the insoluble proteinaceous cement which allows underwater adhesion to rocks and other surfaces . Shows specific adsorption on calcite substrates .
|
Q9GRC4
|
Q28MJ1
|
COXX_JANSC
|
Heme O synthase
|
unclassified Jannaschia
|
MSDFTAQTTTEPREYDAGFGDYFALLKPRVMSLVVFTALVGILVAPGGVSPMIGFTAILFIALGAGASGALNMWYDADIDAVMKRTAKRPVPAGKVPAGEALTLGLWLSAISVAMLGLATNWVAAGLLAFTIFFYAVVYSMWLKRATPWNIVIGGAAGSFPPMIGWAAVTGDVSLASVLMFGIIFMWTPPHFWALALFLKKDYNNAGVPMLTVTHGRTETRRQILIYTILLVPVALGLVLTEVAGPVYLITALVCNAIFLKGAYDIWKRDEAMAEADGYAVEKKVFKFSLLYLFLHFGALLLDAIWRLI
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
Q28MJ1
|
Q17YG0
|
HEMH_HELAH
|
Protoheme ferro-lyase
|
Helicobacter
|
MNLAQENLNSPNNLGNNATKSPKETVILLNMGGPNSLYEVGVFLKNMFDDPFILTIKNNFMRKMVGKMIVNSRIEKSKKIYEKLGGKSPLTPITFALTERLNELDPSRFYTYAMRYTPPYASMVLQDLALKEVESLVFFSMYPQYSSTTTLSSFNDAFNALKSLETFRPKVRVIERFYASEKLNEIILNTILSTLNNHKSQDFVLIFSVHGLPKSIIDAGDTYQQECEHHVDLLKDLMRQKNIHFKQVLLSYQSKLGPMKWLEPSTEGLIEKHRKSNIIIYPLAFTIDNSETLYELEIQYRLMAARLAIKEYLVCPCLNDSIEFAKFIIELVKNLKDE
|
Catalyzes the ferrous insertion into protoporphyrin IX.
|
Q17YG0
|
P22302
|
SODF_NICPL
|
Superoxide dismutase [Fe], chloroplastic
|
Nicotiana
|
KFELQPPPYPMDALEPHMSSRTFEFHWGKHHRAYVDNLNKQIDGTELDGKTLEDIILVTYNKGAPLPAFNNAAQAWNHQFFWESMKPNGGGEPSGELLELINRDFGSYDAFVKEFKAAAATQFGSGWAWLAYKPEEKKLALVKTPNAENPLVLGYTPLLTIDVWEHAYYLDFQNRRPDYISIFMEKLVSWEAVSSRLKAATA
|
Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
|
P22302
|
A7HSA5
|
RLME_PARL1
|
rRNA (uridine-2'-O-)-methyltransferase
|
Parvibaculum
|
MTNSGKTGGKSGKGGTGGARALKVRVKTARKRSNSSTRWLQRQLNDPYVHAAKREGYRSRAAFKLAEIDDKYRFLKPGGRVVDLGCAPGGWCQVAVARVKAEGGDAGAEGRHGRVIGLDYLEMDPVPGATILQLDFLSEGADDQVKELLAGEADVVLSDMAAPTTGHKQTDHMRIMSLCEIAAHFATEVLAPGGTFLAKVLRGGTENELLVLLKQHFKTVRHVKPKASRADSAEMYVLAQGFKGRSESPLDDAE
|
Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
|
A7HSA5
|
P40985
|
HUL4_YEAST
|
HECT-type E3 ubiquitin transferase HUL4
|
Saccharomyces
|
MVSLFDKLNAKKDGRDGSVSKELLSHSVAHTKNRLPKSGRRTSERSLAASVKDGSCSNSKSNKRNSSASVSGEEDKSCLISLNCLCCGVPLRFPASITKFRCSACQVTVIVKEPEINSNLESSTHISCTLEGLQMVVRRCHDDLQRLKKTGILDKERKGLIFQPVITYLLDRFHDVSILNRSFLVHDGGKNIKMLNYEVLQRFYSILSNLPTRKPYYSMLCCCNDLLKRITINKGENLQILQYRWLLIILNIPTIRTCLIRDRKSKNVFETQQIRAVSYELAKRCIGYLSNLSTKTSQQLIQSLRRTPTDNFSYQVEILNLYINFQFSRLLSNELSNRTAKNNVKPEDEMRSRLRRHHTTGHEFLSTRPISAQSNDKQGSGFTHPVNNKMKFKFFQYEEDWHIHSAAKLTFIYYVANTRRNGRGALSIQSFYNITLDFIDYKQDFDHWRGVAQKTKMNQLIEEWGNSTTKKCFSFCKYPFILSLGIKISIMEYEIRRIMEHEAEQAFLISLDKGKSVDVYFKIKVRRDVISHDSLRCIKEHQGDLLKSLRIEFVNEPGIDAGGLRKEWFFLLTKSLFNPMNGLFIYIKESSRSWFAIDPPNFDKSKGKNSQLELYYLFGVVMGLAIFNSTILDLQFPKALYKKLCSEPLSFEDYSELFPETSRNLIKMLNYTEDNFEDVFSLTFETTYRNNNWILNDSKSSKEYVTVELCENGRNVPITQSNKHEFVMKWVEFYLEKSIEPQYNKFVSGFKRVFAECNSIKLFNSEELERLVCGDEEQTKFDFKSLRSVTKYVGGFSDDSRAVCWFWEIIESWDYPLQKKLLQFVTASDRIPATGISTIPFKISLLGSHDSDDLPLAHTCFNEICLWNYSSKKKLELKLLWAINESEGYGFR
|
Probable E3 ubiquitin-protein ligase, component of the TRAMP (TRF4) complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates.
|
P40985
|
Q1LTU7
|
MNMG_BAUCH
|
Glucose-inhibited division protein A
|
Candidatus Baumannia
|
MLKNYFFDVIIIGGGHAGTEAAVASAKIGCNTLLLTHNIKTIGEMSCNPAIGGIGKGHLAKEVDAMGGIMAKAIDAAGIQFRILNASKGPAVRATRAQADRYLYRKAVYNMLKNTNNLLVLQQFVENLIIKNNNVIGVISKAKDKFYANSVILTVGTFLDGKIHIGLNSYPGGRTGDLSSISLSSNLRKLPFRVKRLKTGTPPRIHASTVNFNILTKQESDNPLPVFSFTGSVSEHPRQIPCYITYTNKNTHDIIYNNLHYSPIYTKNIEGIGPRYCPSIEDKIIHFAHRDSHQIFLEPEGLMSNIIYPNGISTSLPVDIQLKIVQSIEGLEKASIIQPGYAIEYDFFDPRDLKNTLESKIINGLFFAGQINGTTGYEEAAAQGLIAGINAAKKVLEQDSWYPNRSQAYIGVLIDDLCLQGIEEPYRMFTSRAEYRLSLREDNADLRLTEIARKLGLVNENHWHKFCIKLDYIERERQRLRNLWVQPNTIGIQDLNQLLKKPIMCKINGEELLRRPEINYKTLTNLSFFQPTLKNIQAAEQIEIQIKYEGYIAQQQEQILRQLNYEQTLLPKNMDFSLVTGLSNEAISQLNNHQPYSIGQALRISGITPIAISLLLLWLKKNNLLANKINK
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
Q1LTU7
|
Q4PSR7
|
ATB22_ARATH
|
Homeodomain transcription factor ATHB-22
|
Arabidopsis
|
MEYWSSSFIDGASSSSFISPFYNFDHFSGNQDNRCLGTMMGAQQDILHVPLAMVESGYGEESNSFNGQEKKKKKMTSEQLKFLERSFQEEIKLNPDRKMKLNPDRKMKLSKELGLQPRQIAVWFQNRKARWKNKQLEHLYESLRQEFDIVSREKELLQEELIQLKSMIREDSSCKKKQTWEKACS
|
Probable transcription factor.
|
Q4PSR7
|
Q2HXI5
|
PCS2_CAMPL
|
Theobromine synthase PCS2
|
Camellia
|
MKEVKEALFMNKGEGESSYAQNSSFTETVTSMTMPVLENAVETLFSKDFHLLQALNAVDLGCAAGPTTFTVISTIKKMMEKKCRELNCQTLELQVYLNDLPGNDFNTLFKGLSSKVVGNNCEEVSCYVVGVPGSFHGRLFPRNSLHLVHSCYSVHWLTQAPKGLTSKEGLALNKGKIYISKTSPPVVREAYLSQFHEDFTMFLNSRSQEVVPNGCMVLILRGRLSSDPSDMESCFTWELLAAAIAELVSQGLIDEDKLDTFNVPSYFPSLEEVKDIVERNGSFTIDHMEGFELDSPQMQENDKWVRGEKFATVARASTEPIISNQFGHEIMDKLYEKFTHIVISDLEAKIPKVTSIILVLSKIVG
|
No detectable N-methyltransferase activity.
|
Q2HXI5
|
Q6BKA3
|
3DHQ_DEBHA
|
3-dehydroquinate dehydratase
|
Debaryomyces
|
MVKKILLINGPNLNSLGTREPEKYGTTTLKDIEQAAIEQAKAKGSEMAVYQNNTEGFIVDRIHEAKKQGVEYILINAGAYTHTSVAIRDALSAVAIPFIEIHITNVHSREEFRHKSYLSDTAVAVICGLGVYGYTAAIDFALNK
|
Is involved in the catabolism of quinate. Allows the utilization of quinate as carbon source via the beta-ketoadipate pathway.
|
Q6BKA3
|
Q9HDQ1
|
LEU3_WICAN
|
Beta-IPM dehydrogenase
|
Wickerhamomyces
|
MSEKTIVVLPGDHVGTEITNEAIKVLKAIEEVRPNVKFNFQHHLIGGAAIDATGVPLPDEALEAAKKADAVLLGAVGGPKWGTGAVRPEQGLLKIRKELNLYANLRPCNFASESLLELSPIKAEFAKGTDFTVVRELVGGIYFGERKEDDGSGVASDTETYSVPEVQRITRMAAFMALQHNPPLPIWSLDKANVLASSRLWRKTVTETIEKEFPQLTVQHQLIDSAAMILIKSPTTLNGIVITSNMFGDIISDEASVIPGSLGLLPSASLASLPDTNKAFGLYEPCHGSAPDLPANKVNPIATILSAAMMLKLSLDLFEEGVALEKAVKEVLDAGVRTGDLRGSNSTKEVGDAAVEAAKRILKN
|
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
|
Q9HDQ1
|
B6YSQ2
|
RS11_THEON
|
30S ribosomal protein S11
|
Thermococcus
|
MSEEQQVVNLKKKEKWGVAHIYSSYNNTIIHITDLTGAETVSRWSGGMVVKADRDEPSPYAAMIAAKRAAEEAMEKGFVGVHIKVRAPGGSKSKTPGPGAQAAIRALARAGLRIGRVEDVTPIPHDGTRPKGGRRGRRV
|
Located on the platform of the 30S subunit.
|
B6YSQ2
|
Q5F7G6
|
PYRG_NEIG1
|
UTP--ammonia ligase
|
Neisseria
|
MTKFIFVTGGVVSSLGKGIAAASIAAILESRGLNVTMLKLDPYINVDPGTMSPFQHGEVFVTDDGAETDLDLGHYERFIDSTMTRRNSFSTGQVYENVIAKERRGDYLGGTVQVIPHITDEIKRRIHEGAAGYDVAIVEIGGTVGDIESLPFLEAIRQMRSQLGRNNTLFAHLSYVPYIAAAGEIKTKPTQHTVKEMLSIGLQPDILICRMDRKMPADERRKIALFCNVEERAIVGSYDVDSIYECPEMLHDQGIDNIITEQLQLNVQQADLTAWKKIVHAVKNPKHTVKIAMVGKYVDLTESYKSLIEALKHAGIHTETDVQITFVDSESIEKNKGDVSVLKDMDAILVPGGFGSRGVEGKIAAVRYARENNVPYLGICLGMQIALIEYARDVAGLKGANSTEFDLKCAAPVVALIDEWQTADGSVETRDESADLGGTMRLGAQEVELKAGSLAVKIYGSGHIRERHRHRYEVNNNYVSALEQAGLVIGGVSAGRERLVETIELPNHPWFFACQFHPEFTSNPRKGHPLFTAFVKAALNNKKA
|
Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
|
Q5F7G6
|
Q5GRT9
|
RUVC_WOLTR
|
Holliday junction resolvase RuvC
|
unclassified Wolbachia
|
MTRIIGLDPGMSKTGWAIIDMDERSNIEFLGSGTISTGNKLGMGERLHVIFEQLKKVISLYSPSEAAIEKIFVNKNPKSSLTLGYARGIVILVLEITELTMNEYDTNYVKKSITGNGHADKDQVIFMVKQIIKNLNIKCHHAADALAVAICHVYTKSSYFVR
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
Q5GRT9
|
Q8KA64
|
SECE_BUCAP
|
Protein translocase subunit SecE
|
Buchnera
|
MKIRIPDQKKAKNLEKIKWFFITAIFITSFFINNFFDKIGYFTRISIITLLVVFAISIALYTKKVKNVFVYINASKNEMKKITWPQYKETLYTTFIIISVTILISLLLWGLDSIIFRLIAFIISVRF
|
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
|
Q8KA64
|
C1DPH8
|
ISPH_AZOVD
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
|
Azotobacter
|
MHIKLANPRGFCAGVDRAIEIVNRALEVFGPPIYVRHEVVHNKFVVDDLRSRGAIFVEELDQVPDNVIVIFSAHGVSQAVRQEAARRGLKVFDATCPLVTKVHMEVARYSREGRECILIGHQGHPEVVGTMGQYDTANGGAIYLVEDEEDVARLQVRNPVSLAFVTQTTLSMDDAARMIDALRARFPGIGGPRRDDICYATQNRQDAVRQLAGECQLVLVVGSSSSSNSNRLRELAESIGVPAYLVDGAQDLRREWFDGIRRVGVTAGASAPEVLVRDVIDRLRQWGVVNVEELTGREENITFSIPKELRVVSSD
|
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.
|
C1DPH8
|
B5Z069
|
TRMA_ECO5E
|
tmRNA (uracil(341)-C(5))-methyltransferase
|
Escherichia
|
MTPEHLPTEQYEAQLAEKVVRLQSMMAPFSDLVPEVFRSPVSHYRMRAEFRIWHDGDDLYHIIFDQQTKSRIRVDSFPAASELINQLMTAMIAGVRNNPVLRHKLFQIDYLTTLSNQAVVSLLYHKKLDDEWRQEAEALRDALRAQNLNVHLIGRATKTKIALDQDYIDERLPVAGKEMIYRQVENSFTQPNAAMNIQMLEWALDVTKGSKGDLLELYCGNGNFSLALARNFDRVLATEIAKPSVAAAQYNIAANHIDNVQIIRMAAEEFTQAMNGVREFNRLQGIDLKSYQCETIFVDPPRSGLDSETEKMVQAYPRILYISCNPETLCKNLETLSQTHKVERLALFDQFPYTHHMECSVLLTAK
|
Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
|
B5Z069
|
P15647
|
BACH_NATPH
|
NpHR
|
Natronomonas
|
MTETLPPVTESAVALQAEVTQRELFEFVLNDPLLASSLYINIALAGLSILLFVFMTRGLDDPRAKLIAVSTILVPVVSIASYTGLASGLTISVLEMPAGHFAEGSSVMLGGEEVDGVVTMWGRYLTWALSTPMILLALGLLAGSNATKLFTAITFDIAMCVTGLAAALTTSSHLMRWFWYAISCACFLVVLYILLVEWAQDAKAAGTADMFNTLKLLTVVMWLGYPIVWALGVEGIAVLPVGVTSWGYSFLDIVAKYIFAFLLLNYLTSNESVVSGSILDVPSASGTPADD
|
Light-driven anion pump. Binding affinity for the anions is in the order, bromide > chloride > nitrate > azide > bromate and binding is pH dependent.
|
P15647
|
Q38XV5
|
RL21_LATSS
|
50S ribosomal protein L21
|
Latilactobacillus
|
MYAIIKTGGKQYKVEAGQAIYVEKLTAEAGEKVTFDQVILVGGETTKVGTPNIDGVTVDGTVEKQGREKKVVTFKYKPKKHSHQKKGHRQPYTKVMIDAINA
|
This protein binds to 23S rRNA in the presence of protein L20.
|
Q38XV5
|
Q8RXT4
|
NEK4_ARATH
|
NimA-related protein kinase 4
|
Arabidopsis
|
MERYEVLEQIGKGSFGSALLVRHKQERKKYVLKKIRLARQSDRARRSAHQEMELISTVRNPFVVEYKDSWVEKGCYVCIVIGYCQGGDMTDTIKRACGVHFPEEKLCQWLVQLLMALDYLHSNHILHRDVKCSNIFLTKEQDIRLGDFGLAKILTSDDLTSSVVGTPSYMCPELLADIPYGSKSDIWSLGCCMYEMAAHKPPFKASDVQTLITKIHKLIMDPIPAMYSGSFRGLIKSMLRKNPELRPSANELLNHPHLQPYISMVYMKLESPRRSTFPLQFSERDATLKERRRSSFSNDRRLNPSVSDTEAGSVSSSGKASPTPMFNGRKVSEVTVGVVREEIVPQRQEEAKKQSGAARTPRVAGTSAKASTQRTVFKHELMKVSNPTERRRRVSLPLVVENPYTYESDITALCSLNSPDVSVNTPRFDKIAEFPEDIFQNQNRETASRREVARHSFSSPPCPPHGEDNSNGSITKDKCTVQKRSVSEVKQRRFDTSSYQQRAEALEGLLEFSAKLLQQERYDELGVLLKPFGAERVSSRETAIWLTKSFKEASV
|
May be involved in plant development processes.
|
Q8RXT4
|
Q1GT68
|
RL1_SPHAL
|
50S ribosomal protein L1
|
Sphingopyxis
|
MAKLTKKQKALEGKVDAQKLHGVDEAIKLVRELATAKFDETLEIAMNLGVDPRHADQMVRGVVTLPAGTGKDVKVAVFARGDNAEKALAAGADKVGAEDLMEDMLAGNLDYGRVIATPDMMGIVGRLGKTLGPKGLMPNPKLGTVTPNVAEAVKAAKGGQIEFRVEKVGIIHAGLGKLSFGEEKLRQNFDAFVDAIVKAKPAGAKGKYVRKVALSSSMGPGVKVDTAELTGA
|
Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA.
|
Q1GT68
|
Q291K8
|
SIN1_DROPS
|
Stress-activated map kinase-interacting protein 1
|
Sophophora
|
MATYSNQHWLLSHIRNSFISTDDTGMCETVMLSDDMPKHYLRKFNSSAGVESHRRRPLKPPLASALPDRNTRHPDAPMQEVDFMCYPGLDLSDDEEDMSTHSFDIQMYPEVGAHRFRSNTAQKLEKLDIAKRRAARIKSINYNEEVQPPEDKDFFMRKEIPNIKPTIPKEKKANDDELSDEGVQSMLTEQLAKSPKQTQNKFIEFARFDGTSQVGMQTKRINVYLNMLPEPDRNYPLKVCVLSTAKIQEVIGFVCYKTSLQYPDVPLKSLQHYGLYMTEDNDDMEDFPPLDNREPCSKFGFSHLTLAERRPLAPVTRVDYPGQLGNKSMTSEDDKATLADAALRALKNITLNGGAADPGGGAVGGGEGDGDGDDSPHDNVKEYEKRLLNHNDMLEAPMHRSFRLNIIDKRFFKSDVTLGISGERIEIDQYKNAKFWPQKKPVSTPIDLVAHCEIVERRHLKALLRIWLKSNSSSSSLPSGCTSAPINASVTTLNTGTGSSSAGIAHSPSSPGNSFGFFMTSNIRFKHYDFDTDTHTAEQINSKLNCILEMRSSELRREFLQQRERKQERQQVKKQLKL
|
Component of a multiprotein complex that phosphorylates Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes.
|
Q291K8
|
Q6G336
|
PURQ_BARHE
|
Phosphoribosylformylglycinamidine synthase subunit I
|
Bartonella
|
MKTAIIQLPGLNRDRDMVAALHHITGVEPLKIWQTESTIPDVDVIVIPGGFSYGDYLRCGAIGARTPVLQAVREKAQKGVTVIGICNGFQILLEAGLLPGTLMRNTSLKFVCREIKLEVVNVNTKFSRYYSKGQIICCPVAHHDGNYFVDSETLKQMEENEQIIFRYAENTNPNGSVNDIAGIINKAGNILGMMPHPENFIEPAHGGTDGRLFFQSALELAKG
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
Q6G336
|
Q28HN9
|
CENPL_XENTR
|
Centromere protein L
|
Silurana
|
MQSPTNGVSTPKDFSSARRSIQFQNTGFPQIGLASARRHTPFHHAPSKRRIPQTSPLSETVDPLKIALLLSKQWTLYSVTPMHKFSYTNLKEYARLLSAHICAEKQKGLAVEVGTELNVKATFSPLPGLKGREQDPGSILIQVLAKPQFSAAGAQDRIVWSGCFCCTFADEDTLDLLTSETLLCLPLFLVNGAEALTAMVGTWFQKAFDCSFSNLPISSRDLAWMAAMWTGYEAHEHITATEFIFSVPIEPHMDISYAIHPEDIKALWSNIHKGQDEVLAEEVDLLFQCLYTHFFRHFKIHLSATHLVKVSTSVASAHCDGKVKFLSKEYLLQVLGYLTELAINNIQY
|
Probable component of a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation.
|
Q28HN9
|
P85883
|
PLS3_PITAZ
|
Phylloseptin-8
|
Pithecopus
|
MAFLKKSLFLVLFLGLVSLSICEEEKRETEEEEYNQEDDDKSEEKRFLSLIPTAINAVSALAKHFG
|
Has antimicrobial activity.
|
P85883
|
Q2KDZ5
|
IF2_RHIEC
|
Translation initiation factor IF-2
|
Rhizobium
|
MTDSNDDKTLSVTGKKTLTLKPSGMSQGTVRQDMGRGRTKAVVVETRKRRPMRPEDEKPITPATPAAPVRAAEPAPAPAQARPQQSTPAPRIHQPGGQANQRPQQSYQPPRANDRPRPVVLNHLSPEEMDARRRALAESQARDAQDAIRRAEEEKRRAAEEAVRKAAEAEEAARRAVEEAARQAEAAAAAAAEPAVTAPAPAPVTAEARPNTSPRPAAPAPAARRPDADGAAARPAPGAPAAVRGRRNDGDDDDRGASRGGPARGRVVRPEPAKPVTTRPKTDEERRRGKLTITTADVDGEDAGRSRSLSAMRRRQEKFRRSQVQETREKISREVVLPETITIQELSQRMSERAVDVIKYLMKEGQMMKPGDVIDADLAELIAGEFGHTVKRVSESDVELGIFNIADVEGDRVSRPPVVTIMGHVDHGKTSLLDAIRHANVVAGEAGGITQHIGAYQVEQNGQKITFIDTPGHAAFTAMRARGAQATDIAILVVAADDSVMPQTIESINHAKAAGVPIIVAINKIDKHEADPQKVRNQLLQHEVFVESMGGETLDVEVSAKTGKNLDKLLEAVLLQAEILDLKANPNRTAEGTVIEAQLDRGRGAVATVLVQNGTLKPGQIIVAGDVWGRVRALVNDKGEHMKEAPPAMPVEVLGLSGTPQAGDKFAVVESESRAREISEYRQRLARDKAAARQSGQRGSLEQMMTQMQSTGIKEFPLVIKGDVQGSIEAIAGALEKLGTDEVRARIVHLGAGGITESDISLAEASNAAIIGFNVRANAQARQFAERQGIEIRYYNIIYDLVDDVKAAMSGLLSPERRETFIGNAEILEVFNITKVGKVAGCRVVEGKVERGAGVRLIRNDVVVHEGKLKTLKRFKDEVSEVPMGQECGMAFENYEDMRVGDVIECFRVEHITRTL
|
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.
|
Q2KDZ5
|
Q13X51
|
MUTS_PARXL
|
DNA mismatch repair protein MutS
|
Paraburkholderia
|
MGIQTATASDVAQHTPMMQQYLRIKAEHPGTLVFYRMGDFYELFFEDAEKAARLLDLTLTQRGASAGNPIKMAGVPHHAVEQYLAKLVKLGESVAICEQIGDPATSKGPVERKVVRVVTPGTLTDAALLSDKNDVYLLAMCVAHNRRGVATSVGLAWLNLASGALRLAELAPDQVAAALERIRPAEVLVADTPGDAASWTPPVNAGALTRVPVWHFDIASGTQRLCDQLEVAGLDGFGAHSLTCAWGAAGALLLYAAATQGQQLRHVRSLKVEYESEYIGLDPATRRNLELTETLRGTESPTLCSLLDTCCTTMGSRLLRHWLHHPPRESAVAQARQQAIGALLEAPPGAGVDSLRGALRQISDIERITGRLALLSARPRDLSSLRDTFIALPELRAQLAAVSPNADSLARIDASLEPPQACVELLRRAVAEEPSAMVRDGGVIARGYDAELDELRDISENCGQFLIDLETRERARTGIGNLRVEYNKVHGFYIEVTRGQTDKVPDDYRRRQTLKNAERYITPELKTFEDKALSAQERALARERSLYDALLQALLPFIPDCQRVASALAELDLLAAFGERARALDWVAPTFSPDAGIEIEQGRHPVVEAQVEQFIANDCSLTPERKLLLITGPNMGGKSTFMRQTALIALLAYVGSYVPARRAAFGPIDRIFTRIGAADDLAGGRSTFMVEMTEAAAILNDATPQSLVLMDEIGRGTSTFDGLALAWAIARHLLAHNGCHTLFATHYFELTQLPAEFPQAANVHLSAVEHGHGIVFLHAVSEGPANQSYGLQVAQLAGVPNAVIRAARKHLAYLEQQSAAQPAPQLDLFAAPMPMLLEDADDERDSKAEALVPPAMQALVERLRGIDPNDLRPREALDLLYELHELAAAPDADH
|
This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
|
Q13X51
|
B1Z5M2
|
KATG2_BURA4
|
Peroxidase/catalase 2
|
Burkholderia cepacia complex
|
MQKKRIGKSVVAALAIIAMSAGTVAAWADGAPRTNDFWWPERLDLSPLRQHDVESNPYGKDFDYAQAFNKLDIEAVKKDIRATLTTSQDWWPADYGNYGPFFIRMAWHGAGTYRTYDGRGGAGGAQQRFEPLNSWPDNANLDKARRLLWPIKKKYGQNISWGDLMVLTGNVALESMGFQTFGFGGGREDDWQSDLVYWGAGTKFMSDNRDKNGKLEKPLAATQMGLIYVNPEGPNGNPDPVAAAKDIREAFGRMAMNDEETLALIAGGHTFGKAHGAASPDKCVGAAPAGAGVEAQGLGWANKCGTGKGADTITSGLEGAWSVDPVHFTMQYLDNLLEHDWVLTKSPAGAHQWMPKDAQDIVPDAHDPSKRHPLMMFTTDIALKVDPAYSAIAKRFQAHPEEFKLAFAKAWFKLTHRDLGPKARYLGKDVPKVDLIWQDPLPVAGYQMIGDADIAELKRRILASGVPKSELIKTAWASAASFRATDYRGGANGARIRLAPENAWAVNDPASLSKVLKSLEDIQSGFNRNRTDGKQVSLADLIVLGGSAAVEDAARKAGYDVKVPFSPGRVDATQAQTDVASFAVLEPTSDGFRNYYRKSNERSPAELMVDRASKLDLSVPEMTVLVGGLRALDANAGHSRLGVLTNRPGTLSNDFFVNLLDMSTQWTKSSSADGTYEGRDRKTGALKWTASPVDLVFGSSSELRAVAEVYASDDAHEKFVRDFVHAWTKVMNLDRFDLKRS
|
Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.
|
B1Z5M2
|
Q2J302
|
PIMT1_RHOP2
|
Protein-beta-aspartate methyltransferase 1
|
Rhodopseudomonas
|
MAASGSRHPPISDDATSFAAQRERMVAQQISARGVRDPLVLAAMRQVPREAFLPERMRDLAYDDSPLPIGHGQTISQPYIVAAMIEALQLNGGERVLEIGAGSGYAAAVLAQIAGEVTTIERIGALADKAAAALAALGIGNVQVRQGDGSRGWPPGAPYDAIVVAAGGPHLPQSLKTQLAIGGRLVMPVGADQSAQRLVRLTRTSVDDVRCEQLADVRFVPLIGDEGWASVAPEPRADRPATVRK
|
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
|
Q2J302
|
P14848
|
LGB2_SESRO
|
Srglb2
|
Sesbania
|
MGFTEKQEALVNASYEAFKQNLPGNSVLFYSFILEKAPAAKGMFSFLKDSDGVPQNNPSLQAHAEKVFGLVRDSAAQLRATGVVVLADASLGSVHVQKGVLDPHFVVVKEALLKTLKEAAGATWSDEVSNAWEVAYDGLSAAIKKAMS
|
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
|
P14848
|
B2D2C0
|
DEFI_ORNCO
|
Defensin
|
Ornithodoros
|
MVRARRGCGCPLNQGACHRHCKSIGRRGGYCAGFLKQTCTCYRN
|
Antibacterial peptide mostly active against Gram-positive bacteria.
|
B2D2C0
|
P11482
|
TBB1_VOLCA
|
Beta-tubulin
|
Volvox
|
MREIVHIQGGQCGNQIGAKFWEVVSDEHGIDPTGTYHGDSDLQLERINVYFNEATGGRYVPRAILMDLEPGTMDSVRSGPYGQIFRPDNFVFGQTGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVVPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPTFGDLNHLISAVMSGITCCLRFPGQLNADLRKLAVNLIPFPRLHFFMVGFTPLTSRGSQQYRALTVPELTQQMWDAKNMMCAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMSATFIGNSTAIQEMFKRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDASAEEEGEFEGEEEEN
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
P11482
|
Q61885
|
MOG_MOUSE
|
Myelin-oligodendrocyte glycoprotein
|
Mus
|
MACLWSFSWPSCFLSLLLLLLQLSCSYAGQFRVIGPGYPIRALVGDEAELPCRISPGKNATGMEVGWYRSPFSRVVHLYRNGKDQDAEQAPEYRGRTELLKETISEGKVTLRIQNVRFSDEGGYTCFFRDHSYQEEAAMELKVEDPFYWVNPGVLTLIALVPTILLQVPVGLVFLFLQHRLRGKLRAEVENLHRTFDPHFLRVPCWKITLFVIVPVLGPLVALIICYNWLHRRLAGQFLEELRNPF
|
Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. Mediates homophilic cell-cell adhesion.
|
Q61885
|
A1WXL3
|
RLMM_HALHL
|
23S rRNA 2'-O-ribose methyltransferase RlmM
|
Halorhodospira
|
MELQGWILHCRAGYEQTLASEATMAAHERDVHGYCRARAQSAYVVFHAPAGDAPLPPQLVFARAGAGLIGELQGLPEGGRAEAIAAALPPAVGSATPWVEHPDSDAGRPLARFCRRFTGPLRHALTQTGVTSGDPQRRLRLLFPDSRHCFAGIGPREGWPSGIPRLRMPRNAPSRSVLKLEEALHRLVPENERPYPGEHAVDLGAAPGGWTWLLRERGLTVTAIDNGPLAPALADDPGVEHQRTDAFRFRPRTEVDWLVCDVVDRPQGIARLMTQWLREEWARAAIFNLKLPMRRPLETVRQALDAVRTTGARAHAAQLYHDREEITVYARRMASRNRP
|
Catalyzes the 2'-O-methylation at nucleotide C2498 in 23S rRNA.
|
A1WXL3
|
P64706
|
Y495_MYCBO
|
Transcriptional regulator Mb0495
|
Mycobacterium tuberculosis complex
|
MYSTNRTSQSLSRKPGRKHQLRSHRYVMPPSLHLSDSAAASVFRAVRLRGPVGRDVIAGSTSLSIATVNRQVIALLEAGLLRERADLAVSGAIGRPRVPVEVNHEPFVTLGIHIGARTTSIVATDLFGRTLDTVETPTPRNAAGAALTSLADSADRYLQRWRRRRALWVGVTLGGAVDSATGHVDHPRLGWRQAPVGPVLADALGLPVSVASHVDAMAGAELMLGMRRFAPSSSTSLYVYARETVGYALMIGGRVHCPASGPGTIAPLPVHSEMLGGTGQLESTVSDEAVLAAARRLRIIPGIASRTRTGGSATAITDLLRVARAGNQQAKELLAERARVLGGAVALLRDLLNPDEVVVGGQAFTEYPEAMEQVEAAFTAGSVLAPRDIRVTVFGNRVQEAGAGIVSLSGLYADPLGALRRSGALDARLQDTAPEALA
|
Positively regulates the expression of PE13 and PPE18.
|
P64706
|
A7N1G7
|
YBEY_VIBC1
|
Endoribonuclease YbeY
|
Vibrio
|
MAIELDLQLAVENEEGLPSEQDFQLWLDKTIPLFQPQAELTIRIVDEQESHELNHEYRGKDKPTNVLSFPFEVPPGMEMDLLGDLIICRQVVEKEAVEQNKPLLAHWAHMVVHGSLHLLGYDHIEDDEAEEMESLETEIMQGMGYEDPYIAEKE
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
A7N1G7
|
A3MUI7
|
CREN7_PYRCJ
|
Chromatin protein Cren7
|
Pyrobaculum
|
MDQDVAEEILNKEYEVVYEGKRFLLKPAKAWVLQPPGKPGVIVALFKLPNGKTVRKVIARLPP
|
A probable chromatin protein, binds double-strand DNA without sequence specificity. Constrains negative DNA supercoils.
|
A3MUI7
|
Q5LCA5
|
THIC_BACFN
|
Thiamine biosynthesis protein ThiC
|
Bacteroides
|
MEQRIKFPRSEKVYLSGKLFPEIRVGMRKVEQVPSTTFEGEKKVITPNPHVYIYDTSGPFSDPDIEIDLKKGLPRLREEWILNRGDVEQLPEISSEYGRMRRDDGSLDHLRFEHIALPYRAKAGRHITQMAYAKQGIVTPEMEYVAIRENMNCEELGIETHITPEFVRQEIAEGRAVLPANINHPEAEPMIIGRNFLVKINTNIGNSATTSSIDEEVEKAMWSCKWGGDTLMDLSTGENIHETREWIIRNCPVPVGTVPIYQALEKVNGKVEDLTWELYRDTLIEQCEQGVDYFTIHAGIRRHNVHLAEKRLCGIVSRGGSIMSKWCLVHDRESFLYEHFDDICDILAQYDVAVSLGDGLRPGSTHDANDEAQFAELDTMGELVVRAWEKNVQAFIEGPGHVPMHKIRENMERQIEKCHNAPFYTLGPLVTDIAPGYDHITSAIGAAQIGWLGTAMLCYVTPKEHLALPDKEDVRVGVITYKIAAHAADLAKGHPGAQVRDNALSKARYEFRWKDQFDLSLDPERAFSYFHAGRHTDGEYCTMCGPNFCAMRLSRDLKKTQKQK
|
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
|
Q5LCA5
|
Q4VZJ4
|
RK20_CUCSA
|
50S ribosomal protein L20, chloroplastic
|
Cucumis
|
MTRIKRGYIARRRRTKIRLFASSFRGAHSRLTRTITQQKIRALASAYRDRGRQKRNFRQLWIARINAVIRSNNVDYSYSRFIHNLYKRQLLLNRKILAQIAILNRNCLYMISNEIIK
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
Q4VZJ4
|
B2ITM5
|
RF1_NOSP7
|
Peptide chain release factor 1
|
Nostoc
|
MAESYLLDKLKSVEQTFNELTRRLGDPDTASNPDEYQEIAKSRSSLEEVVNTYEIWKTAQEDLIGAREVYKESASDPELQEMASLEVKELEEKIEHLESRLKVLLLPRDPNDEKNIMLEIRAGTGGDEASIWAGDLMQMYTRYAQTQGWKVSLVSESRGEMGGWKEVILEIKGNDVYSQLKFEAGVHRVQRVPATESGGRVHTSTATVAIMPEVDDVEIHIDPKDIEMTTARSGGAGGQNVNKVETAVDLMHKPTGIRIFCTEERSQLQNKERAMQILRAKLYDIKLGEQQAAVTSMRRSQVGTGSRSEKIRTYNYKDNRATDHRLGQNYSLTPVLDGDLETLIQSCISLDQQERLAELATSAAN
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
B2ITM5
|
B8NM75
|
USTT_ASPFN
|
Ustiloxin B biosynthesis protein T
|
Aspergillus subgen. Circumdati
|
MSGTSPPTPKDHITMVDHDYSDCSEDVSLIGADREHRRSSTPDGLYQHKINRHYNPLYIAVVASLTFLITDIAGQIIVAPRLAIFEHIICKAYYTQVSGAAGTGMGDCKVEPVQSELALINGWREMFDNIPGTSYTLDRFGRKKVLLIAMVGCLLSDIWVGVVTWFPDTFPLRAVWFSGIWQLIGGGGASISSMAFAMIADSCPADLRTTAFSQVHAAVLVAELVSVPAGAALANFNPWIPVFGAAIFMVLGILFAYVVVPDVRPAGSKREGGSDGDFLSSAQESHPTWLMSIHHRWRKIVDEFRKDSSWIRDVNVLLIMASFFVCQLGRMISGITLQYAAAKFHWKFDKASLLVSLRAGVNLFVLAAIIPALSYILVKRFKLNDVVKDKRITQINGVCLIIGSFVMFLAASPGTLVFGQTVFALGFAFSVTARSFLTGMVDPMHIGTVFTGVTTMLYGGLVIGSPMLAKTLQWGLQLGGIWVGLPFLLAAVLFTLALGAISAARSY
|
Efflux pump; part of the gene cluster that mediates the biosynthesis of the secondary metabolite ustiloxin B, an antimitotic tetrapeptide . Probably involved in self-resistance through the export of ustiloxin B .
|
B8NM75
|
A5GAG2
|
KDPA_GEOUR
|
Potassium-translocating ATPase A chain
|
Geotalea
|
MNPYEWLETILFFVVLLALIKPFGTYMAKVFQGERTLLSPVFVPCENLLYRICGVDKDDEMGWKRYACAMLLFNLVFAVSLFAMLLLQGILPLNPQKLPAFSWPLALNTAISFTTNTNWQNYGGEAAASYFTQMFGFAVHNFTSAATGIVIAIAAIRGLVRRKSSALGNFWVDTTRCTLYILLPLSLIAAIFLVSQGVIQNFSPYKTVPLVQATSFEKPRLDAKGTPIKDAKGNPVTESVTVKEVTIPMGPVASQEAIKELGTNGGGFFNANSAHPFENPTPLSNIFEVFLILLISGGLTYTFGRMAGNTRQGWALLAVMLAILILAIGVFYRAESSGNPLVAKLGVHGINMEGKETRFGLAGSALFATATTGTSCGAVNTMHDSLTPIGGMVPLSLILLSEVIFGGVGTGLYTMLAFVVIAVFVAGLMIGRTPEYLGKKIEVREMWMSITTVLASGILVLIFSGIAMILPAGVSSMNNSGAHGLSEVLYAFASMSNNNGSAFAGLNGNTLFYNLTGAVAMLLGRFVPAVAVLAMAGGLAEKKYVPPSLGTLPTDQAPFALWLTLVILIVGALTFFPALAMGPIAEQLIMMR
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the periplasmic potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
|
A5GAG2
|
Q53B46
|
3SDC5_OPHHA
|
OH-84
|
Ophiophagus
|
MKTLLLTLVVVTIVCLDLGYTRKCLNTPLPLIYKTCPIGQDKCIKMTIKKLPSKYDVIRGCIDICPKSSADVEVLCCDTNKCNK
|
Acts as a beta-blocker by binding to beta-1 and beta-2 adrenergic receptors (ADRB1 and ADRB2). It dose-dependently decreases the heart rate (bradycardia), whereas conventional cardiotoxins increases it. At 100 mg/kg, intraperitoneal injection into mice provokes labored breathing, impaired locomotion, lack of response to external stimuli, and death (after 30 min).
|
Q53B46
|
B6I6Q5
|
FADI_ECOSE
|
Fatty acid oxidation complex subunit beta
|
Escherichia
|
MGQVLPLVTRQGDRIAIVSGLRTPFARQATAFHGIPAVDLGKMVVGELLARSEIPAEVIEQLVFGQVVQMPEAPNIAREIVLGTGMNVHTDAYSVSRACATSFQAVANVAESLMAGTIRAGIAGGADSSSVLPIGVSKKLARVLVDVNKARTMSQRLKLFSRLRLRDLMPVPPAVAEYSTGLRMGDTAEQMAKTYGITREQQDALAHRSHQRAAQAWSDGKLKEEVMTAFIPPYKQPLVEDNNIRGNSSLADYAKLRPAFDRKHGTVTAANSTPLTDGAAAVILMTESRAKELGLVPLGYLRSYAFTAIDVWQDMLLGPAWSTPLALERAGLTMSDLTLIDMHEAFAAQTLANIQLLGSERFAREVLGRAHATGEVDDSKFNVLGGSIAYGHPFAATGARMITQTLHELRRRGGGFGLVTACAAGGLGAAMVLEAE
|
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.
|
B6I6Q5
|
A8FYR5
|
PNP_SHESH
|
Polynucleotide phosphorylase
|
Shewanella
|
MVHVNPIVKSFEYGQHTVTLETGVIARQADAAVLASMGDTTVLVTVVGKKFEEPGRDFFPLTVNYQEKTYAAGKIPGGFFKREGRPSESETLIARLIDRPIRPLFPNGFKNEVQVIITVVSVDPEINPDVISMIGTSAALAISGLPFNGPLGVARVGYTDGEYVLNPNVSQLVDSDLDLIVAGTQGAVLMVESEAAALPEEVMLGGVVYGHDQQQVVISAINELKAEASKPAWDWTAPVQDADLVAKIKDLAEAEMAAAYQIEVKQDRYTQVGVVKSAAKEALLAENPEADLREIDGLLGSLEKQVVRSRIIAGNPRIDGREPDMVRGLNVMAGVLPRTHGSALFTRGETQALVTCTLGTERDAQKVDSIMGEYTNRFMLHYNFPPYSVGETGFVGSPKRREIGHGKLAWRGINAVMPSAEEFPYSVRVVSEITESNGSSSMASVCGTSLALMDAGVPIKTSVAGIAMGLVKEGDDFVVLSDILGDEDHLGDMDFKVAGTRDGITALQMDIKIEGINKEIMQIALQQAYGARVHILNVMDQAIGEHRDDISDHAPRITTLKINPEKIRDVIGKGGATIRALTEETGTTIELEDDGTVKIASANGDATKEAIRRIEEITAEVEVGTIYNGKVVRIVDFGAFVTILPGKDGLVHISQIAEERVANVSDYLQVGQEVKVKVMEVDRQGRVRLSMKEAAPKAEAAPAE
|
Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.
|
A8FYR5
|
Q57HR5
|
CYAY_SALCH
|
Iron-sulfur cluster assembly protein CyaY
|
Salmonella
|
MNDSEFHRLADTLWLAIEERLDSWDGDSDIDCEINGGVLTLSFENGSKIIINRQEPLHQVWLATKQGGYHFDLKDDEWVCDRSGETFWDLLEQAATQQAGEKVSFR
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
Q57HR5
|
O22914
|
CP121_ARATH
|
Chloroplast protein 12-1
|
Arabidopsis
|
MTTIAAAGLNVATPRVVVRPVARVLGPVRLNYPWKFGSMKRMVVVKATSEGEISEKVEKSIQEAKETCADDPVSGECVAAWDEVEELSAAASHARDKKKAGGSDPLEEYCNDNPETDECRTYDN
|
Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.
|
O22914
|
C3PN29
|
HSLV_RICAE
|
ATP-dependent protease subunit HslV
|
spotted fever group
|
MSDNLSLHGTTILCLKKNEEIIIAADGQVSHGNTVLKSTARKLRTIANNKIIAGFAGSTADGLALFEKLAVKIEQHKHNLLRSAVELAKDWRSDKYLRRLEAMMIVADRSHILILTGNGDVVEPENNVAAIGSGGLFALSAARALMSYENNLTAEEIALKSMNIAADLCVFSNHNIIMEKVV
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
C3PN29
|
Q04599
|
RM01_YEAST
|
Mitochondrial large ribosomal subunit protein uL1m
|
Saccharomyces
|
MLSVVAIPKICVTGPARRCFFHTAKKLYADDYKPAAMSSNAPSLTKDQAKKRELKRLVQRKAEAKRPATASPLYMPVTKALRYLRAAEVGRPQSQQTINLTTLVVGERGTAPLSGSVTFPKPLRYIKIAAFTNDESKLEELREKYPNHLIGGADLVAKIKSGEISVDFDKAFATPDIVPALQSQVARILGPRGVLPSVKKGTVSDDISSLLQESLGSMPFRQRGNSISIGVGKCYFTDREILQNIISARAAFKTAVDNQKSKKPNILSKTTLSSTHGPGIVIDFA
|
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
|
Q04599
|
C0HKR2
|
ALLA_AGRIP
|
Allatostatin-A-9
|
Agrotis
|
MLSTSLPVCFLVIGAALCAPERMQNDPDPHDSTAQGSDNHSDHIAPLAKRSPHYDFGLGKRAYSYVSEYKRLPVYNFGLGKRSRPYSFGLGKRSVDEDQTNDDQQQIMNNDLDQAALAEFFDQYDDAGYEKRARPYSFGLGKRFADDDTSEEKRARAYDFGLGKRLPLYNFGLGKRARSYNFGLGKRLASKFNFGLGKRERDMHRFSFGLGKRSADDASTEDSDNYFDV
|
Neuropeptide inhibitors of juvenile hormone synthesis and gut muscle contraction.
|
C0HKR2
|
Q5X7G8
|
YQGF_LEGPA
|
Putative pre-16S rRNA nuclease
|
Legionella
|
MPRGVYLGFDFGYKRIGVAVGQRLTCSASPLSTIEAKAGIPDWNTIQKVITQWNPQALIVGLPTCIDDRELYTTSAARHFAKQLHKRFSLPVHLVDERLSTVEARGYLFEQGGYRQIKKAEVDSIAACVILEQWLQQSE
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q5X7G8
|
O02721
|
LSHR_CALJA
|
Luteinizing hormone receptor
|
Callithrix
|
MKQPLLALQLLKLLLLLLLPLPPLPRALREARCCPEPCNCTPDGALRCPGPGAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQSDSLERIEANAFDNLLNLSEILIQNTKNLIHIEPGAFTNLPRLKYLSICNTGIRKFPDVTKIFSSETNFILEICDNLHITTIPGNAFQGMNNESITLKLYGNGFEEVQSHAFNGTTVISLVLKENVHLERIHNGAFRGATGPSILDISSTKLQALPSHGLESIQTLIATSSYSLKKLPSREKFANLLDATLTYPSHCCAFRNVPTKDYPAIFAESGQSGWDYDYGFHLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCNTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQIYILTILILNVVAFIIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKMPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFRRDFFLLLGKFGCCKHRAELYRRKDFSAYTSNYKNGFTGSSKPSQSTLKLPALHCQGTALLDKTCYKEY
|
Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
|
O02721
|
A1UKW4
|
RIR2H_MYCSK
|
Ribonucleotide reductase small subunit homolog
|
unclassified Mycobacterium
|
MTRTRSDSLAAGGLNWNSMPLKLFAGGNAKFWDPADIDFSRDRADWESLSNLERDWATRLCAQFIAGEEAVTQDIQPFMAAMRAEGRLGDEMYLTQFAFEEAKHTQVFRMWLDAVGMTDDLQCYLDDLPSYRQMFYEELPASLEALATDPSPAAQVRASATYNHVIEGMMALTGYYAWHRICVDRKVLPGMQELVRRIGDDERRHMAWGTFTCRRHVAADDANWEVFENRMNELIPLALSNTDDSFALYDEIPFGFAKEEFQQYAADKGMRRFGTISSARGRALAEIDVDYSPLQLEDTFAAEDSRVLATSA
|
Probable oxidase that might be involved in lipid metabolism.
|
A1UKW4
|
Q9SDK9
|
RFA3_ORYSJ
|
Replication protein A 3
|
Oryza sativa
|
MDTSGPAAFVNGEILKMFVGRRVRTVVQAQREEGGLLIGQSTDGHQLTIKGASGAPMSHYVEIIGIAEPNQAIRAEVCTDFGENFDPAPFNGLCKLANGQMKDLFL
|
As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
|
Q9SDK9
|
B8EDS6
|
TDH_SHEB2
|
L-threonine 3-dehydrogenase
|
Shewanella
|
MKALSKLKAEKGIWLVDAPKPVMGHNDLLIKIKKTAICGTDMHIYNWDEWSQKTIPVPMVVGHEYVGEVVDIGQEVRGFKIGDRVSGEGHITCGHCRNCRAGRTHLCRNTSGVGVNREGSFAEYLVIPAFNAFKIPDDISDDLASIFDPFGNAVHTALSFDLVGEDVLITGAGPIGIMAAAVCRHVGARHVVITDVNEYRLELARKMGATRAVNVSKESLKDVMKELGMTEGFDVGLEMSGVPSAFHAMLDTMNHGGKVAMLGIPGGEMAIDWSKVIFKGLVIKGIYGREMFETWYKMASLIQSGLDISPIITHHFKIDDFQQGFDAMGSGQSGKVILSWD
|
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate.
|
B8EDS6
|
B5ZAR3
|
RECA_UREU1
|
Recombinase A
|
Ureaplasma
|
MKENDKLEKLDPIATLEAKFAKSTYFIADEIKNEKVSAISTGSIHIDQITGINGIPVGKITEIYGNESSGKTTIALQTIAECQKKGGTAVLLDLEGSFDLNYAKSLKVDLTKLIITQPQTGEQAFDMIETLIKTNSIDLIVVDSVAAMIPESEYQANMSEALMGAHARLMSKGLRKIQPLMNKSQTAIIFINQLREKINTFFGNPEMTTGGKALKFYASLRIETRKADLIKEGINKIGIKTKVTTVKNKLAPPLQTCFIDVFFGHGFDYDNEIIDFAIQYGILKKNGSWFYFDDNKIGQGREQLKNTLLKNNELFTQVSEKTLAFVNNEKINQ
|
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.
|
B5ZAR3
|
P01036
|
CYTS_HUMAN
|
Salivary acidic protein 1
|
Homo
|
MARPLCTLLLLMATLAGALASSSKEENRIIPGGIYDADLNDEWVQRALHFAISEYNKATEDEYYRRPLQVLRAREQTFGGVNYFFDVEVGRTICTKSQPNLDTCAFHEQPELQKKQLCSFEIYEVPWEDRMSLVNSRCQEA
|
This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively.
|
P01036
|
Q9KUR9
|
LPTD_VIBCH
|
LPS-assembly protein LptD
|
Vibrio
|
MSCFSRTFLAASISAALFAPQIQAEASVDDNRAQLPNGEQCLVNQPEPTNPGQQPINVEADKLEAINGQKATYSGNVVVVQGKKRIAADNVTLHQQENVVVAEGNVQFSDGEIKTHSTKATNHLNTDEMTLENTRYQFLCEPGRGEAVYVSKTGKAVYEIEDGSITSCPDGDNAWRMRASSIDVDQNEEIATFYNPRLEVQNVPVFYLPYLTVPIGDTRKTGFLYPTASYGSRNGYSFEVPIYWNLAPQYDLETTFNYMQKRGTQLNSVFRYLTDFGAGQIKSEYLADDQLHTELGDRWAFQYEHNGIFQQAWKFEIDYSKVSDINYFSDLDSGVGNREDGQLIQEGRATYRSDNWDSALLVRDFQLLTKDTTSTNLPYRLMPQLSYNYYAPETMKYLDLDLVSHVSRFETDARGKPSATRVHIEPGLKIPFSNTWGNWTTEARVLGTYYQQDLDKTTDAKLEESVTRVIPEIRSVAGIVLERDTVLLDDYTQTLEPKIQYLYVPEKYQDNIGLYDSTLLQTDYYGLFRSRKYSGVDRIESANQVSYGASTRFFDSNYKERLNIAFGQIFYLDSKLNPSNKNPDSTSDKTSYSAWAVEMDFNFADYLFYHGGIQYDIDSQAVQLGNSTLEYRVASGYIQANYRYVAKDYIRNTVGDSITNIDDITRDGISQAGILAGYQLSRKWSASGQYYYDLTTDEALEWLANLTYTSDCWYVGFTYSNQLKSWNGNFVTDPYATPIYENNFSFNIGIIGFGTSIGAGSSMTGVDSAGNSLGYGRPFFLNN
|
Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane.
|
Q9KUR9
|
Q2SDF9
|
CH10_HAHCH
|
Chaperonin-10
|
Hahella
|
MKIRPLHERVVVRRKEEETKTAGGIVLPGNAAEKPSQGEVLAVGEGRILDNGDVRPLAVKVGDKVVFGQYAGSTVKIDGEELLIMSESDIFGVIEG
|
Together with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.
|
Q2SDF9
|
Q5ZXH8
|
NEUCH_LEGPH
|
UDP-N,N'-diacetylbacillosamine 2-epimerase (hydrolyzing)
|
Legionella
|
MIRKIIYVTGTRADYGLMREVLKRLHQSEDIDLSICVTGMHLDALYGNTVNEIKADQFSICGIIPVDLANAQHSSMAKAIGHELLGFTEVFESETPDVVLLLGDRGEMLAAAIAAIHLNIPVVHLHGGERSGTVDEMVRHAISKLSHYHFVATEASKQRLIRMGEKEETIFQVGAPGLDEIMQYKTSTRDVFNQRYGFDPDKKICLLIYHPVVQEVDSIKIQFQSVIQAALATNLQIICLEPNSDTGGHLIREVIQEYIDHPDVRIIKHLHRPEFIDCLANSDVMLGNSSSGIIEAASFNLNVVNVGSRQNLRERSDNVIDVDVTYDAILTGLREALNKPKIKYSNCYGDGKTSERCYQLLKTIPLHSQILNKCNAY
|
Involved in biosynthesis of legionaminic acid (5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic acid)(Leg), a sialic acid-like derivative that is incorporated into virulence-associated cell surface glycoconjugates such as lipopolysaccharide (LPS) which could be a key determinant in the ability of L.pneumophila to inhibit the fusion of phagosomes with lysosomes. LPS contains a majority alpha2,4-linked homomer of legionaminic acid. Catalyzes the conversion of UDP-N,N'-diacetylbacillosamine (Bac2Ac4Ac) into 2,4-diacetamido-2,4,6-trideoxymannose and UDP.
|
Q5ZXH8
|
A4J804
|
COBS_DESRM
|
Cobalamin-5'-phosphate synthase
|
Desulforamulus
|
MFSSLRLAISFLTIFPFYNKMADNKELAQSVSYYPLVGFLLGSIAAGVCYAMHSIGLNLAADVLGLVTIITLTGGLHQDGLMDTADGIFSGRELHRKLEIMKDSRVGAMGVIALATVLLLKIAFLFELDLAQKLTAFIMAPMAGRWAMVLAITRYPYARATGGLGACLKQAGKTQLALATLILVAGCLWLFGLPGLALLGIVFFITWLTVEFIVKRLGGMTGDTYGALGEMIETWVIFLILLGQQIRML
|
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
|
A4J804
|
B5FNU2
|
CYAY_SALDC
|
Iron-sulfur cluster assembly protein CyaY
|
Salmonella
|
MNDSEFHRLADALWLTIEERLDNWDGDSDIDCEINGGVLTLSFENGSKIIINRQEPLHQVWLATKQGGYHFDLKGDEWVCDRSGETFWDLLEQAATQQAGEKVSFR
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
B5FNU2
|
P59748
|
PQQE_KLUIN
|
Pyrroloquinoline quinone biosynthesis protein E
|
Kluyvera
|
MNPSKSVTPPLWLLAELTYRCPLQCPYCSNPLDFSQQKKELTTEQWIEVFRQARAMGSVQLGFSGGEPLTRKDLPELIRAARDLGFYTNLITSGIGLTAKKLDAFADAGLDHIQISFQASDETLNAALAGSKKAFQQKLEMAKAVKAHGYPMVLNFVLHRHNIDQIDKIIDLCIELDADDVELATCQFYGWAQLNREGLLPTREQIANAEAVVADYRQRMGASGNLTNPAVRDAGLLRRAAETLHGRMGIDLPQRHADCTALPCHSARQLPVAFPSVLERTLDDIWYNSFGFNRYRGFDWMPEPCRSCDEKAKDFGGCRCQAFMLTGDADNTDPVCSKSPHHGKILEARREANCSDIKIQQLQFRNRSNSELIF
|
Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
|
P59748
|
A3CXW9
|
RIBL_METMJ
|
Flavin adenine dinucleotide synthase
|
Methanoculleus
|
MIRVVATGTFDILHPGHLYYLEESRNLGDELSVIVARDANVKHKPRPFLPEDQRLRMIRALKPVDHALLGDLHDMFRPIAEIRPDIITLGFNQHFDEEHLRQKLRERGLDADVVRIPGYPGSLASSSKIIERILNTRGPPDPTGSHGEE
|
Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.
|
A3CXW9
|
A0PXT7
|
RL7_CLONN
|
50S ribosomal protein L7/L12
|
Clostridium
|
MTREEMIQAIKEMSVLELNELVKACEEEFGVSAAAPVAVAGVAGAVGAAEEKSEFDVVLANAGSQKIKVIKAVRELTGLGLKEAKEIVDGAPKTLKEGVAKEAAEEMKAKLEEVGATIELK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A0PXT7
|
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