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
|
|---|---|---|---|---|---|---|
Q94C57
|
U73B2_ARATH
|
UDP glucose:flavonoid 7-O-glucosyltransferase
|
Arabidopsis
|
MGSDHHHRKLHVMFFPFMAYGHMIPTLDMAKLFSSRGAKSTILTTSLNSKILQKPIDTFKNLNPGLEIDIQIFNFPCVELGLPEGCENVDFFTSNNNDDKNEMIVKFFFSTRFFKDQLEKLLGTTRPDCLIADMFFPWATEAAGKFNVPRLVFHGTGYFSLCAGYCIGVHKPQKRVASSSEPFVIPELPGNIVITEEQIIDGDGESDMGKFMTEVRESEVKSSGVVLNSFYELEHDYADFYKSCVQKRAWHIGPLSVYNRGFEEKAERGKKANIDEAECLKWLDSKKPNSVIYVSFGSVAFFKNEQLFEIAAGLEASGTSFIWVVRKTKDDREEWLPEGFEERVKGKGMIIRGWAPQVLILDHQATGGFVTHCGWNSLLEGVAAGLPMVTWPVGAEQFYNEKLVTQVLRTGVSVGASKHMKVMMGDFISREKVDKAVREVLAGEAAEERRRRAKKLAAMAKAAVEEGGSSFNDLNSFMEEFSS
|
Catalyzes the glycosylation of flavonoids from UDP-glucose. Uses a wide range of flavonoid substrates including flavonols (quercetin, kaempferol, isorhamnetin, 3-OH 7,2',4'-MeO-flavone), flavones (luteolin, apigenin), flavanones (naringenin, hesperetin), flavanonols (taxifolin), isoflavones (genistein, daidzein), flavonol glycosides (quercitrin, isoquercitrin, rutin), and chalcones (isoliquiritigenin). Specific for the C-7 position, with a 20-fold lower activity for the C-3 position.
|
Q94C57
|
Q5L0N2
|
HSLV_GEOKA
|
ATP-dependent protease subunit HslV
|
Geobacillus thermoleovorans group
|
MGAFHATTIFAIRHNGASAMAGDGQVTFGNAVVMKHTAKKVRRLFQGNVLAGFAGSVADAFTLFEMFEGKLEQWNGNLPRAAVELAKEWRSDKVLRRLEAMLIVMDKQHLLLVSGTGEVIEPDDGMLAIGSGGQYALAAGRALKKYAGGSMTAKEIAKAALEIAADICVYTNGHIIVEEL
|
Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
|
Q5L0N2
|
B6I424
|
GLNE_ECOSE
|
Adenylyl transferase
|
Escherichia
|
MKPLSSPLQQYWQTVVERLPEPLAEKSLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQSPQADEWQHYAAWLQEALSNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSHLAETLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSEGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSVIAALHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPSDELNRARLAWAMDFADWPQLTGALTAHMTNVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLTLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTTYLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNDREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRDRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVPEDCFTAERELVRASWQKWLVEE
|
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
|
B6I424
|
Q0A738
|
HTPG_ALKEH
|
High temperature protein G
|
Alkalilimnicola
|
MATDAHKETLEFQAEVQQLLHLMIHSLYSNKDIFLRELISNASDAIDKLRFQSLQDESLLEGEGDLRIRVSVDKDARTITVADNGIGMTRDEVAENLGTIARSGTKAFLDQLTGDQQKDAKLIGQFGVGFYSAFVVAEHVTVHTRKAGLGAEHGVRWSSDGKGAYTLENEEVAERGTRVVLTLPESQSEYLDDWRLKGIIRRYSDHIDVPIQMPAQAEDKDEPEDEAEKAEAAETWETVNNTNALWMRPKSEISDDDYKAFYKHVAHDFDDPMVWLHNHVEGRQSYTSLLYIPKNPPFDLYEREPAHGIKLYVRRVFIMEDTEKLMPRYLRFVRGLVDSDDLPLNVSRELLQHNPLLDKIRSASVKRILDRLEKMAKNEPEQYAEFYGNFGKVLKEGVAEDFANRERIAKLLRFSTTQDENETPDVSLDDYIARMKEGQEAIYYVTAESFNAARNSPHLEVFRKKGVEVLLLPDPVDEWVITHLNEYDGKPLKSVAKGGLDLGELEDQAEKKAAEEATESHKDLLEKLKGALEDKVSEVRVSTRLTDSPACLVVGEYDFGMGMQRLLKAAGHAMPQGKPALEINIDHPIVQRMDTGLDDARFSDWAAVLYDQALLTEGGQLEDPAAFVKRVNALLTEQARAGEAKSNAARGD
|
Molecular chaperone. Has ATPase activity.
|
Q0A738
|
Q06438
|
PEX2_CRIGR
|
Peroxisome assembly factor 1
|
Cricetulus
|
MAGREKTKSANRVLRISQLDALELNKALEQLVWSQFTQCFHGFKPGLLARFEPEVKACLWLFLWRFTIYSKNATVGQSVLNIQYKNDFSSNSRYQPPSKNQKLWYAVCTIGGRWLEERCYDLFRNRHLASFGKVKQCMNVMVGLLKLGELINFLIFLQKGKFATLTERLLGIHSVFCKPQNIREVGFDYMNRELLWHGFAEFLIFLLPLINIQKFKAKLSSWCIPLTGAASSDSALASSGKECALCGEWPTMPHTIGCEHVFCYYCVKSSFLFDMYFTCPKCGIEVHSVQPLKSGIEMSEVNAL
|
Somewhat implicated in the biogenesis of peroxisomes.
|
Q06438
|
Q15147
|
PLCB4_HUMAN
|
Phospholipase C-beta-4
|
Homo
|
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVLECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPEVTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEKVIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVDQLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDENAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELDCWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKMSKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSMMEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLVTVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVGLGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQLNQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGTYVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNKLIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKKFLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAALASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQVDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQHTKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQAKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQLEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
|
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction.
|
Q15147
|
Q5LDB2
|
HCP_BACFN
|
Prismane protein
|
Bacteroides
|
MSMFCFQCQETAKGTGCILSGVCGKTPEVANMQDLLLFVVRGIAVYNQALRKDGRSSARADKFIFDALFTTITNANFDKHAIIKKIKKGLELKKDLSNQVTIEHAPDECTWYGDETEFEEKAQTVGVLRTSDEDIRSLKELVHYGIKGMAAYVEHAYNLGYENPEIFAFMQYALAELTREDITVDELITLTLATGNHGVQAMAQLDTANTSHYGNPEISEVNIGVRNNPGILVSGHDLKDIEELLQQTEGTGIDIYTHSEMLPAHYYPQLKKYKHLVGNYGNAWWKQKEEFESFNGPILFTTNCIVPPRPNATYKDRIYTTGATGLEGATYIPERKDGKQKDFSVIIEHARRCQPPVAIESGKIVGGFAHAQVIALADKVVEAVKSGAIRKFFVMAGCDGRMKSRSYYTEFAEKLPADTVILTAGCAKYRYNKLPLGDINGIPRVLDAGQCNDSYSLAIIAMKLQEVFGLKDINDLPIVYNIAWYEQKAVIVLLALLALGVKKIHLGPTLPAFLSPNVKQVLIDNFGIGGISTADEDIAKFLA
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
Q5LDB2
|
A5WHC9
|
PANC_PSYWF
|
Pantoate-activating enzyme
|
Psychrobacter
|
MTITFNAIQDLQQALHPLRTDKKIALVPTMGNLHDGHISLVKLAQEHADVVVVSIFVNPTQFGVGEDLDSYPRTLEADTQKLTEAGVDYIFAPSVEEMYPVMPPPTQVLAGAISQYLCGKSRPTHFDGVGIVVTKLFNIVQPNVAVFGKKDYQQLAIIKQLVRDLSYNIEIIGAPLVRAVDGLALSSRNQYLTETERQIAPMLNQHLSKLAQKLKNTPIANNQQLQALIEDTIAQINNAGFRVDYLEVSNQDLSKITDFYGQKQWVIAVAAWLGKARLLDNQEVNG
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
A5WHC9
|
Q9XAB7
|
6PGL_STRCO
|
6-phosphogluconolactonase
|
Streptomyces albidoflavus group
|
MSDTPQLVVHRDKELMAEAAAARLITKIVDAQASRGSASVVLTGGRNGNGLLAALAGSPARDAIDWSRLDLWWGDERFLPEGDPERNVTQAQQALLDSVPLDPKRVHAMAASDGPYGSDVEAAAAAYAQELATASVPENHAAVPSFDVLLLGVGPDTHVASLFPEHPGVRETERTVIGVHGSPKPPPIRISLTLPAIRAAREVWLLAAGEDKANAVAMALSGAGEIQAPAAGARGRARTLWLLDSAAASQLPRSLYPPASA
|
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
|
Q9XAB7
|
Q87MI6
|
DAPE_VIBPA
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Vibrio
|
MTDSPVLALAKDLISRQSVTPEDAGCQDLMIERLKALGFEIEVMVFEDTTNFWARRGNEAPLFAFAGHTDVVPAGKLEQWDTPPFEPTIIDGYLHGRGAADMKGSLAAMVVAVERFIAEHPDHKGSIGFLITSDEEGPFINGTVRVVEALMERGENIDMCIVGEPSSTEIVGDVVKNGRRGSITGDLTVKGTQGHVAYPHLANNPVHASLLAIHELATTEWDKGNDYFPPTSFQIPNVSAGTGASNVIPGEFNVQFNLRFSTELNNDTIVQRVTETLDKHDLNYDLHWTFNGDPFLTDTGALLDAVVAAVAEVNNTKPALLTTGGTSDGRFIARMGGQVVELGPVNATIHKVNECVKVDDLEKLTDMYENTLKHLLAK
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
Q87MI6
|
A2SFM8
|
NUOC_METPP
|
NDH-1 subunit C
|
Methylibium
|
MDHKIDLLQPALEAALAGKIQALVRDRGELTLTVTAADYLAVCTTLRDHAELKLEQLIDLCGLDYSSYKDGAGSPYTEGPRYCVVLHLLSVSKNWRLRLKVFCADDGLPVVPSVNEIWAAANWFEREAFDLYGIVFEGHADLRRILTDYGFIGHPFRKDFPTTGHVEMRYDAEQRRVIYQPVTIEPREITPRIIREDNYGGLH
|
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.
|
A2SFM8
|
O52334
|
RL23_MYCGA
|
50S ribosomal protein L23
|
Mycoplasma
|
MQITDVLIKPILTEKTYGIMMSEPRKYTFLVNAKANKNYIKQAFKAIYGVTPIAVNTKIKKPARVRTGTQNPGYSRLEKIAIITVPFGVEVAITGEKPEPKEESSSKK
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
O52334
|
P97355
|
SPSY_MOUSE
|
Spermidine aminopropyltransferase
|
Mus
|
MAAARHSTLDFKLGAKADGEAILKGLQSIFQEQGMTESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDSDVQGKQETDSLLNKIEEKMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRRTCGDVLDNLRGDCYQVLIEDCIPVLKMYAKEGREFDYVINDLTAVPISTSPEEDSTWDFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP
|
Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) . Required for normal viability, growth and fertility .
|
P97355
|
Q0V9S0
|
SYTC2_XENTR
|
Threonyl-tRNA synthetase protein 3
|
Silurana
|
MAAHIAQRLTVQEQEIRRLNEEIGRLLELGLQGSVEHSPNPVLEQLRAENEKLKYRISHLQRSLREEQERARPGQYGEPGLKDAAPVEEPKQQNNKAKEKGQATKGENSVGGKPSACEGNKKNEKKAGKEVDGHKQEGPCAPGFIKDRLALYETLKNEHDALLAARAAHQSKPIKITLADGKQVDGESWKTTPYQVAIGISKGLADNVVIAKVNNELWDLDRPLEQDSNVELLKFDSEEAQAVYWHSSAHILGETMENFYGGCLCYGPPIENGFYYDMYLDGRGVSSNEFPSLENMCKAIIKEKQPFERLEVSKDLLLEMFKYNKFKCRILNEKVDTPTTTVYRCGPLIDLCRGPHVRHTGKIKTLKIYKNSSTYWEGRADMETLQRIYGISFPDSKLMKEWEQFQEEAKNRDHRKIGRDQELFFFHDLSPGSCFFLPRGAHIYNTLTDFIKGEYQIRNFTEVASPNIYNSKLWEMSGHWQHYSENMFSFEVEKETFALKPMNCPGHCLMFGHRPRSWRELPLRFADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTMDQIQEEMNGCLQFLQSVYKVFGFTFQLHLSTRPENYLGEIEIWNEAEKQLESSLNQFGEPWKLNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGDDKKRPVIIHRAILGSVERMIAILCENYGGKWPFWLSPRQVMVIPVGPSCDEYAQQVCKDVFEAGFMAEVDLDHSCTLNKKIRNAQLAQCNFILVVGEKEKTDSAVNVRTRDNKVHGEILLTSAIEKLKTLKKLRSKNAEEEF
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage.
|
Q0V9S0
|
Q3AZZ7
|
UPPP_SYNS9
|
Undecaprenyl pyrophosphate phosphatase
|
unclassified Synechococcus
|
MIDTTAPLSLLEALVLGIVQGLTEFLPISSTAHLRVVPALLGWDDPGVSVTAAIQLGSVAAVIAYFRRDLTQVLTGISRAVRHGQWRDPDARLGVAMVIGTLPILVLGLGIKFFWHAGYASSPLRSVPSIAIVSIVMALFLAMAECMGPRLKQLGGVTGRDGFVVGLAQALAVIPGVSRSGSTLTASLFDGWNRADAARFSFLLGIPAISIAGLVELKSALSTSAGAGPLPLLVGIFSAAVVSWLAIDWLLRFLQRNSTWIFVGYRLVFGAGLLVWWAFKSAN
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
Q3AZZ7
|
Q11V49
|
SYA_CYTH3
|
Alanyl-tRNA synthetase
|
Cytophaga
|
MTSAEIRQQFLDFFASKGHQIVPSAPIVNKNDPTLMFTNAGMNQFKDYFLGNETPKYRRIADTQKCLRVSGKHNDLEEVGIDTYHHTMFEMLGNWSFGDYFKEEAIAWSWELLTSVYKLPKDRLYVTIFEGDDKEKLARDTEAYNFWKKWIAEDRILLGNKKDNFWEMGEQGPCGPCSEIHVDLRTDEEVKAVDGKTLVNNDHPQVVEIWNNVFIQFNRKADGSLEELPDKHVDTGMGFERLCMAIQKKKSNYDTDVFTPMIDFVAKAAGIKYGADEKTDIAMRVMADHIRAISFVIADGQLPSNNKAGYVIRRILRRAVRYAYTFLNLKEPFLYKLVAVLADQLAHVFPELKSQQDFVAKVVQEEEISFLRTLDIGLSKLEQIREELKAKKATTIDGKTAFELYDTFGFPLDLIQLIARENGLTVDEAGFDTEMAAQKQRSKKAASVETSDWTIVTEDDEVEFVGYDHLISTSRIIKYRQVKTKGKDQYQLVLDTTPFYAESGGQAGDTGTLVQGDKKIKVLNTVKENNLIIHITEQLPADLKAPVDCKVNVLQRSLTENNHSATHLLHAALKQVLGSHVNQKGSLVNESVLRFDFSHFSKVTEEELKKVELIVNEKIRENISLNERRNVPIEEAKKLGAMALFGEKYGEYVRMITFDDSFSRELCGGTHVSSTGKIGFFKITSESSVAAGVRRIEALTATAAEVFVDEQQTTLAKITELMKNPKDLVKSLEDLLEERIVLQKQLDEYQAEKSKAIAKSLKDTVEKVGDINVIRAKLVLPSVDAMRQVAYDLKQTVDNLLLVLAVNVDGKPNIAVMISDNLVADKGLNASQMIRELSKEIQGGGGGQPFYATAGGKELNGLDKVIAKSKDLIQVHA
|
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.
|
Q11V49
|
Q9BSJ6
|
PIMRE_HUMAN
|
Regulator of chromosome segregation protein 1
|
Homo
|
MASRWQNMGTSVRRRSLQHQEQLEDSKELQPVVSHQETSVGALGSLCRQFQRRLPLRAVNLNLRAGPSWKRLETPEPGQQGLQAAARSAKSALGAVSQRIQESCQSGTKWLVETQVKARRRKRGAQKGSGSPTHSLSQKSTRLSGAAPAHSAADPWEKEHHRLSVRMGSHAHPLRRSRREAAFRSPYSSTEPLCSPSESDSDLEPVGAGIQHLQKLSQELDEAIMAEERKQALSDRQGFILKDVYASP
|
During mitosis, may play a role in the control of metaphase-to-anaphase transition.
|
Q9BSJ6
|
A7Z4M3
|
TRMD_BACVZ
|
tRNA [GM37] methyltransferase
|
Bacillus amyloliquefaciens group
|
MKIDFLTLFPEMFQGVLGSSILQKAQEKEAVRFDVINFRAFSDNKHQTVDDYPYGGGAGMVLKPQPVFDAVEKLTAGTDAKPRIILVCPQGERYTQKKAEELAQEEHLMFICGHYEGYDERIREHLVTDEISIGDFVLTGGELPAMMIADSVVRLLPGVLGKEASHVEDSFSTGLLEHPHYTRPADYRGLKVPETLLSGNHAKIQKWRNKESIRRTFLRRPDLLKNYPLTDEQRKWISEWENE
|
Specifically methylates guanosine-37 in various tRNAs.
|
A7Z4M3
|
Q2W4A0
|
SYS_MAGSA
|
Seryl-tRNA(Ser/Sec) synthetase
|
Magnetospirillum
|
MHDLKSIRDNPDGFDAGLKRRGLEPKAAAILDLDTRRRAAQTAFQEMQARRNDASKQIGALKKSGGDASALMDEVASLKERMPAAEEEDKALGAEIESILASIPNLPASDVPDGPDEDHNVELRKWGTPKSFAFTALDHDAIGAKLGLMDFDGAAKLSGARFVVLKGQLARLQRAIGQFMLDLQTVEHGYTEMDPPLMVKDGAAFGTGQLPKFGEDLFKTNTGHWLIPTAEVPLTNLVSDEILDEKALPLRMTALTPCFRSEAGAAGKDTRGMIRQHQFHKVEMVSIAHPDASGAEHERMTQCAETVLQRLGLAYRVIVLCTGDMGFSAQKTYDIEVWLPGQQRYREISSCSNCGDFQARRMKARFRPEGEKGTRFVHTLNGSGLAVGRTLIAVMENYQREDGTIEVPEALRPYMGGLEVIG
|
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).
|
Q2W4A0
|
Q9VZD2
|
BN3D3_DROME
|
Probable RNA methyltransferase CG11342
|
Sophophora
|
MDIRNNDPGAVQYGNFFNYYQFSSAAERVKLLPDADIWLPALEDGETQKDKPYFILDVGCNCGVLTQLMHKYLEERLHRSVKVLGVDIDPRLIQRASEENESPKDVSYACVDVLDDEAFESVKTYMEVNNLEKFDAICCYSITMWIHLNHHDQGLRFFLQKLSNLAELLVVEPQPWKCYQKAERRLKKAGEIFPLFLELKWRSDVDLQIQKYLEESLDRRKIFKSAPTKWQRKICFYR
|
Probable RNA methyltransferase.
|
Q9VZD2
|
A9GCQ1
|
RSMG_SORC5
|
16S rRNA 7-methylguanosine methyltransferase
|
Sorangium
|
MPPDERAPLPLPAPAPLTPPEGFAERLAAIGVTLDAAVIAKLGDYLARLLAMNELMNLTSITDPVEVWEKHVLDSLTLLPLLEELSAGARLADIGSGGGLPGLPLAIARPDLKVTLVEATQKKASFLVAVAAGLGLTNVSVRAERAEQLGKGDLCGAFDAVTARAVGRLVMLIPLTVPFVRPSGLVLLVKGQRAEEELAEASWVLGRQRAAFVKTVATPTGKIVMLRKSGEEPKRHPGR
|
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
|
A9GCQ1
|
Q73K21
|
RNH_TREDE
|
Ribonuclease H
|
Treponema
|
MNIEIYTDGACSKNPGPGGWAYIMVNKDSKEEICRENGGEKSTTNNRMELMAVIRALKKIKEGAASLADKSGKALDYKSISVHTDSQYVQQGISSWIFNWKKNNWKTASKQPVKNQDLWQELDSLSASIKPEWIWVKGHAGNPLNEACDRLAVEACQKMM
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q73K21
|
P21693
|
DBPA_ECOLI
|
ATP-dependent RNA helicase DbpA
|
Escherichia
|
MTAFSTLNVLPPAQLTNLNELGYLTMTPVQAAALPAILAGKDVRVQAKTGSGKTAAFGLGLLQQIDASLFQTQALVLCPTRELADQVAGELRRLARFLPNTKILTLCGGQPFGMQRDSLQHAPHIIVATPGRLLDHLQKGTVSLDALNTLVMDEADRMLDMGFSDAIDDVIRFAPASRQTLLFSATWPEAIAAISGRVQRDPLAIEIDSTDALPPIEQQFYETSSKGKIPLLQRLLSLHQPSSCVVFCNTKKDCQAVCDALNEVGQSALSLHGDLEQRDRDQTLVRFANGSARVLVATDVAARGLDIKSLELVVNFELAWDPEVHVHRIGRTARAGNSGLAISFCAPEEAQRANIISDMLQIKLNWQTPPANSSIATLEAEMATLCIDGGKKAKMRPGDVLGALTGDIGLDGADIGKIAVHPAHVYVAVRQAVAHKAWKQLQGGKIKGKTCRVRLLK
|
DEAD-box RNA helicase involved in the assembly of the 50S ribosomal subunit. Has an RNA-dependent ATPase activity, which is specific for 23S rRNA, and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short rRNA duplexes. Requires a single-stranded RNA loading site on the 3' side of the substrate helix.
|
P21693
|
A7ND52
|
RECF_FRATF
|
DNA replication and repair protein RecF
|
Francisella
|
MYISNLRLQNFRNIPAKSFDFKNSINFIVGKNGSGKTSILESIYFLSHSRSFRSSQLNRIINHNADEFIIYTKAYNPDEITISLSRKKNSNNISKLNLEIQKNHTEITRNLPIQLINPESFNIINSGAQQRCKVIDWGAFYLDKTFLKIWQQTKFLVKQRNSALKQNYPYSYILSIDKKLCEFAEILDYKRQAYFTKLKPKIYEILSHFNPNLQLDIDYFRGWNLHKSLAQVLEESFNYDNKYKVTNHGPHKADIVLSVSHKPIQDIFSRGQQKLLICALKLAQGEIHNSENDNKCIYLIDDITSELDSIHTLTLFNYLKQLKSQVFITTTEKNKINEFIDTNSYILEI
|
The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP.
|
A7ND52
|
Q72JC0
|
PILA4_THET2
|
Type IV major pilin PilA4
|
Thermus
|
MRNAKGFTLIELLIVIAIIAILAAVLIPNLLAARKRANDTVVTAYLNDAVKFQEMYQIDNNSYTSNQAALISLGLKSTPANVTFSIVSASANSYCMIAGHSGGTVWFAATPDKGVYKTNTAVTSSQPESCP
|
Plays an essential role in the assembly of two types of T4P pili: a wide and a narrow that participate in natural transformation and twitching motility . Major component of the wide pilus that is essential for natural transformation working as a DNA translocator structure that spans the inner and outer membranes . In addition, participates in the assembly of the narrow pilus composed of the PilA5 subunit that is required for twitching motility .
|
Q72JC0
|
B5F7G2
|
SYT_SALA4
|
Threonyl-tRNA synthetase
|
Salmonella
|
MPVITLPDGSQRHYDHPVSPMDVALDIGPGLAKATIAGRVNGELVDASDLIENDATLSIITAKDEEGLEIIRHSCAHLLGHAIKQLWPHTKMAIGPVVDNGFYYDVDLDRTLTQEDVEALEKRMHELAEKNYDVIKKKVSWHEARETFVKRGESYKVSILDENIAHDDKPGLYHHEEYVDMCRGPHVPNMRFCHHFKLMKTAGAYWRGDSNNKMLQRIYGTAWADKKALNAYLQRLEEAAKRDHRKIGKQLDLYHMQEEAPGMVFWHNDGWTIFRELEVFVRSKLKEYQYQEVKGPFMMDRVLWEKTGHWDNYKDAMFTTSSENREYCIKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGSCHRNEPSGALHGLMRVRGFTQDDAHIFCTEEQIRDEVNACIRMVYDMYSTFGFEKIVVKLSTRPDKRIGSDEMWDRAEADLAVALEENNIPFEYQLGEGAFYGPKIEFTLYDCLDRAWQCGTVQLDFSLPSRLSASYVGEDNERKVPVMIHRAILGSMERFIGILTEEFAGFFPTWLAPVQVVVMNITDSQSEYVNELTQKLQNAGIRVKADLRNEKIGFKIREHTLRRVPYMLVCGDKEVEAGKVAVRTRRGKDLGSLDVNDVIEKLQQEIRSRSLQQLEE
|
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).
|
B5F7G2
|
Q7UPM4
|
KPRS_RHOBA
|
Phosphoribosyl pyrophosphate synthase
|
Rhodopirellula
|
MRELKIFSGRANHDLAEKLCRHLHLKPARITLGQFPDGENYCKLDEDVRGRDVFLVQPTCPPVNDNLIELLTMIDCCKRASAERITAVIPYFGYARQDRKDEGRVPITAKLVANLITRAGADRVLTMDLHAAQIQGFFDVPVDHLYAAPVINDHFVSRRFAGDEVVVVSPDEGSIKRALGHTKRLGGNLAIVDKRRTNALEVRQNTIIGGPVEGKVALMFDDMISTAGSICGAARLVHEAGAKEIHIACTHGVLCGPAIERLREAPIDSITVTDTIPVTGEKLLPNLVQLSVAPLLAEAIKRIHHDQSISELFRER
|
Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P).
|
Q7UPM4
|
B8F769
|
ATPL_GLAP5
|
Lipid-binding protein
|
Glaesserella
|
METVITATIIGASILLAFAALGTAIGFAILGGKFLESSARQPELASSLQTKMFIVAGLLDAIAMIAVGISLLFIFANPFIDLLK
|
Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
|
B8F769
|
P45835
|
RHO_MYCLE
|
ATP-dependent helicase Rho
|
Mycobacterium
|
MTETDLITVGENTDDTELTNAVTTDTPDVKATAATVSLGSLSTMVLPELRALANQAGVKGTSGMRKSELIAAIEECRGQANGTSVNDGPSRDHGGSATAISTEALAAQEEQNYAIVEVSRRERRGASREADVTAGTSTAEATESDCQGTADDDTRTLQGGQSDTKTEERGPDVGNDQGVEQQSSSLQPRGDDDGEGRQGRRGRRFRDRDRRRRGERSGDGAEAELRQDDVVQPVAGILDVLDNYAFVRTSGYLAGPHDVYVSMSMVRKNGLRRGDAVTGAVRVPREGEQGHQRQKFNPLVRLDSINGGSVEDAKKRPEFGKLTPLYPNQRLRLETTPDRLTTRVIDLIMPIGKGQRALIVSPPKAGKTTILQDIANAITRNNLECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDRPPSDHTSVAELAIERAKRLVEQGKDVVVLLDSITRLGRAYNNASPASGRILSGGVDSTALYPPKRFLGAARNIEEGGSLTIIATAMVETGSTGDMVIFEEFKGTGNAELKLDRKIAERRVFPAVDVNPSGTRKDELLLSPDEFGIVHKLRRVLSGLDSHQAIDLLMSQLRKTKTNYEFLVQVSKTTPGSMDDD
|
Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.
|
P45835
|
P0DMY9
|
GIG4_ANEVI
|
Gigantoxin-4
|
Anemonia
|
MALFRMLFLCAVLVLLTSKEGMSYEEPENDEGVACTGQYAESFCLNGGTCRYIQSIGEYYCICNGDYTGHRCEKKQV
|
Has both toxic and EGF activity. Its EGF activity consists of rounding cells (morphological change) and inducing tyrosine phosphorylation of the EGFR in A431 cells, but with a lower potency that human EGF.
|
P0DMY9
|
A8FSV7
|
CSRA_SHESH
|
Carbon storage regulator
|
Shewanella
|
MLILTRRVGETLMIGDEVTVTVLGVKGNQVRIGVNAPKEVSVHREEIYQRIQSEKAGNPSEGGNF
|
A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
|
A8FSV7
|
A9R154
|
RAPA_YERPG
|
ATP-dependent helicase HepA
|
Yersinia
|
MPFTLGQRWISDTESELGLGTVVAIDVRMITLLFPATGENRLYARNDSPITRVMFNPSDTITHHEGWQLKVEEVTQENGLITYIGTRLDTEETGVAMREVLLDSKLTFSKPQDRLFAGQIDRMDRFALRFRARKYQSEQFRLPWSGLRGIRASLIPHQLHIAYEVGQRHAPRVLLADEVGLGKTIEAGMIIHQQLLAGRAERVLIVVPESLQHQWLVEMLRRFNLRFSLFDDSRYSEALLDSSNPFDTEQMVICSLDFVRRNKQRLEQLADASWDLLVVDEAHHMAWSEEAPSREYQVIEQLAEHIPGVLLLTATPEQLGQQSHFARLRLLDPDRFHDYEEFVNEQQKYRPIADAVTLLLGGERLTDDKLNLLGELIDEQDIEPLLKAANSQSEDSEAARQELVTMLMDRHGTSRVLFRNTRNGVKGFPHRVLHQIKLPLPTQYQTAIKVSGIMGAKKTLDARAKDMLYPEQIYQEFEGENATWWNFDPRVEWLLNYLVANRGEKVLVICAQAATALQLEQVLREREAIRAAVFHEGLSLIERDRAAAYFASEEDGAQVLLCSEIGSEGRNFQFACQLVMFDLPFNPDLLEQRIGRLDRIGQNREIQIMVPYLEDTAQAILVRWYHEGLDAFEHTCPTGRTIYDSSYQELISYLATPSEQEGLDEFIHTCRQQHEGLKLQLEQGRDRLLEMHSNGGEHGQELAQSIAEQDNDINLVSFALNLFDIVGINQEDRSDNLIVLTPSDHMLVPDFPGLPPDGCTVTFDREQALSREDAQFVSWEHPIIRNGLDLILSGDTGSCAVSLLKNKALPVGTLLAELVYVVEAQAPKHLQLTRFLPPTPVRMLMDRNGTNLAAQVEFESFNRQLNAVNRHTSSKLVNAVQQEVHTMLQQAEALVEAQAQALIETAKREADDKLSTELARLEALKAVNPNIRDDEIEALEHNRKMVLENLNQAGWRLDAIRLVVVTHQ
|
Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair.
|
A9R154
|
P14233
|
TGA1B_TOBAC
|
HSBF
|
Nicotiana
|
EFCDFSGNQAAGGVMVMDTSSPELRQSSSGSDVLNATSSTSSHQVSGDVAGYLNVPSPESNGSNHEGSRESANDNKGLGDARVLNCHSPESQGSGNYGSNVSEGLNYPSDSNKSVHSSPNFENNSIKNGAVEEKIKLEGVNANISKCSSLLKRKKSSEDSNNINIHQKLTNVALSDNVNNDEDEKKRARLVRNRESAQLSRQRKKHYVEELEDKVRIMHSTIQDLNAKVAYIIAENATLKTQ
|
Binds specifically to the DNA sequence 5'-TGACG-3'.
|
P14233
|
Q24SU9
|
DEOC_DESHY
|
Phosphodeoxyriboaldolase
|
Desulfitobacterium
|
MRTMNLAGMIDHTFLKPEATEKDIVNLCHEAKQHKFATVCINPAYICTAAKLLHGSGVGVATVIGFPLGATMTEIKVQEIFAAKAHGAREVDIVINIGWAKSGNWEAVAKDITRAVEAAHCCGVTIKVIIETSLLTEEEKQKAAEIVKASGADYIKTSTGFAGGGATVEDVRNLKAWVGQSVKVKASGGIRSRETALQMVEAGADRLGTSSGVQIITV
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
Q24SU9
|
Q5MFV6
|
PME37_ARATH
|
Pectin methylesterase VGDH2
|
Arabidopsis
|
MAVGKVVVSVASLLLVVGVAIGVITFVNKGGGANGDSNGPINSHQKAVQTICQSTTDQGSCAKTLDPVKSDDPSKLVKAFLMATKDAITKSSNFTASTEGGMGTNMNATSKAVLDYCKRVLMYALEDLETIVEEMGEDLQQSGTKLDQLKQWLTGVFNYQTDCLDDIEEVELKKIMGEGISNSKVLTSNAIDIFHSVVTAMAQMGVKVDDMKNITMGAGAGGAARRLLEDNDSKGLPKWFSGKDRKLMAKAGRGAPAGGDDGIGEGGGGGGKIKATHVVAKDGSGQFKTISEAVMACPDKNPGRCIIHIKAGIYNEQVRIPKKKNNIFMFGDGATQTIITFDRSVKLSPGTTTSLSGTVQVESEGFMAKWIGFKNTAGPLGHQAVALRVNGDRAVIFNCRFDGYQDTLYVNNGRQFYRNIVVSGTVDFIFGKSATVIQNSLILVRKGSPGQSNYVTADGNEKGAAMKIGIVLHNCRIIPDKELEADKLTIKSYLGRPWKKFATTVIIGTEIGDLIKPEGWTEWQGEQNHKTAKYIEFNNRGPGAATTQRPPWVKVAKSAAEVETYTVANWVGPANWIQEANVPVQLGL
|
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
|
Q5MFV6
|
Q9LV63
|
Y5851_ARATH
|
BTB/POZ domain-containing protein At5g48510
|
Arabidopsis
|
MATPTNKEHFSGGLAKVLAEKWQVDVMLKAKNSDEGSAISAHKLILASRSEVFKNMFELDEFKTSTKHVETITLSEMKHEELEAFVEFICSDGSMLSANVKQHARSLYLAADKYEILHLRDLCRTELISSLSLLNSLDLLVLAQIPFDKVLNDESFSYIKNNISTIASSDEFKLFVAGNPNLAVEIMKVSLITLTLRCSSCGSNHSLQGMYCCNCCRYGTLRLI
|
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
|
Q9LV63
|
A6SXP9
|
FABH_JANMA
|
3-oxoacyl-[acyl-carrier-protein] synthase III
|
Janthinobacterium
|
MTIYSKIIGTGSYLPPNRVTNQELTAQLASNGIETSDEWIVSRSGISARHYADAGVQSSDLAVEAAKRALEMAKLGVDDVDLIILATSTPDFFGGFPSTACVVQRKLGITNDCAAVDVQAVCSGFVYAVSIADNFIKAGTHKNVLVIGAEVFSRIIDFEDRTTCVLFGDGAGAVLMTASQEPGVLATKLHANGNYGDILCLPGKVSKGVVEGSAFLYMDGPAVFKLAVSVLDKVAHEALEIAGMQSSEVDWIIPHQANIRIMQSTAKKLGLGMDKMIVTVDQHGNTSAASIPMALDVGVRDGRIKPGQNVMMEGVGGGFTWGAVLARM
|
Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
|
A6SXP9
|
Q2J164
|
ISPE_RHOP2
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Rhodopseudomonas
|
MPTTALSDQARAKVNLTLRVVGRRVDGYHDLESVVAFADCADRLTLHPGAELSLVTSGPGAQDCGDTADNLVLKATRLLAERVPKLRSGAFVLDKHLPVAAGIGGGSADAAAALRLLARANDLAADDPRVVEAARLTGADVPVCLPSRPCVMTGVGDTLTPLPLPRLPAVMVNPRVPVATKDVFKALGLRAGQLNVGIVDVLKSKGWPAVDASVADWIVAVRRGTNDLEAPALKVEPIVGDVLRALAALPGVRMSRMSGSGATCFALFASDEDTKAGAEVLRAAHPGWWIHAGSLS
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
Q2J164
|
P65319
|
LPRI_MYCBO
|
Lysozyme inhibitor LprI
|
Mycobacterium tuberculosis complex
|
MRWIGVLVTALVLSACAANPPANTTSPTAGQSLDCTKPATIVQQLVCHDRQLTSLDHRLSTAYQQALAHRRSAALEAAQSSWTMLRDACAQDTDPRTCVQEAYQTRLVQLAIADPATATPPVLTYRCPTQDGPLTAQFYNQFDPKTAVLNWKGDQVIVFVELSGSGARYGRQGIEYWEHQGEVRLDFHGATFVCRTS
|
Strongly binds and inhibits lysozyme, may help bacteria survive in lysozyme-producing host cells such as monocyte-derived macrophages.
|
P65319
|
O49073
|
SODC_PAUKA
|
Superoxide dismutase [Cu-Zn]
|
Paulownia
|
MVKGVAVLSSSEGVSGTIYFTQEGDGPTTVTGNVSGLKPGPHGFHVHALGDTTNGCLSTGPHFNPAGKEHGAPDDEVRHAGDLGNVTVGEDGTAAFTIVDKQIPLTGPHSIIGRAVVVHADPDDLGKGGHELSKTTGNTGGRVACGINGLQG
|
Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
O49073
|
Q110Q9
|
MNMG_TRIEI
|
Glucose-inhibited division protein A
|
Trichodesmium
|
MNQTFDFQDEYDIIVVGAGHSGCEAALATARLGCHTLLLTLNLDKIAWQPCNPAVGGPAKSQLTHEVDALGGEIGKMADRTYLQKRILNSSRGPAVWALRAQTDKREYATIMRNIVENQENLRVRESMVTDLVLGDNEEIIGVETYFGVAFKCKAVILTTGTFLGGVIWVGNKSMPAGRAGEFSAIGLSETLNKLGFETGRLKTGTPARVDKRSVDYTDLEAQPGDEKVRWFTFDPEVWVEREQMCCYLTRTTPETHKLIRDNLHLSPVYGGWVDAKGPRYCPSIEDKIVRFADKHSHQIFIEPEGRDIPELYIQGFSTGLPEKLQLQMLQSLPGLENCLMLRPAYAVEYDYLPATQCYPTLMTKKIEGLFCAGQINGTTGYEEAAAQGLVAGINAVKFVKNEEMIIFPREQSYIGTLIDDLCTKDLREPYRMLTSRSEYRLILRSDNADQRLTPLGREIGLIDDRRWELFESKQANINSEKSRLNSTRIKELDEVAINIVADTHTKIKGSITLADLLRRPGFHYVDLEKYNLGNLDLKLVEKEGAEIDIKYSGYLQRQQNQIDQISRQKNRRLPTNLDYLSISTLSLEAREKLSKVQPLTIGQASRIGGVNPADINALLVYLEVQYRQFQLTSANV
|
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.
|
Q110Q9
|
P55163
|
GEX3_CAEEL
|
Gut on exterior protein 3
|
Caenorhabditis
|
MAYKDARQVKIAEKLVILNDRAAGMMTRIYNIKKSSGDSKVKPQFLSDKKMEGAIKHIVRKFPVVDCRSNSSTFEYVQEKSTEITKSLSLYYYTFADILDLKDHIMQVLTTMESCQCQLDVTLNYDLTTSYLNLVVHLVTMMILLSRIEDRKAVLGLFNAAYDLQHGQSEASFPRLGQMILDYENPLKKLHEDLGPLNRLIYSALSSVTHTYQRRNKTADSWRTSNVFSLTAAPAQILYAAQTETIACEYLSLDVIDRWIVFCGTVCHSTLLNDDNIRHMWQLALQMNLCLRVFRDETFIVHQEIQAFLESSKEKSKRLQDVKDAFNHASVTAVAVHADRRRFLRSSLRELSLLLRDQPGLLGPKILYVWMALGAGRDEVIWLLRHQVEVPAISKKGSRMVEELVDRQLPELLFYMLELRDLVTKYYAVIQRYYLQYVSSYDSIVVSEEINQANGLTQEEAVLLTDFANEIGNINSDTDLRALRLDWFRFQAWTSAARSHFQLSRHKKLAIYMNTSVFHLKMIDLQDEMLRETSDLSLYCFYPKLAEKHWLNCLQLPAQARYVLSFARLAAHFTSALHDMCPEEKAFITEKALAQCNSVIEETCKQLSYILEKVAEHEFGLAYQMTPSAVAVRVVAQVVQQKGSGKAAAAAAAAARDYFIAGEESYRVDRQALTMPDKLQTTLLEISAALGAHRQIYVADHTFAPRTYLAQSLETKFVELLHGMFWEGQPHASNPKRPSEMLLALQAYMTVLQNLDTAISVDISNTMQTTLLQQTQLVDSKNKDTIAALYTKWYLEVLLRRASSGHMVWSEHLRTMLSSGQEQLSFMPDHYSDPQELRALVQIIGPYGVKLMTERLIWHVASQIMEMSKIVATYKDALQIARSNFDNAEKMKDVLNLLSVEPKDKKTPNATCAADAILQRTIIIGQICLFRDALHDALRHIVESKLPFLQASFDMLYHNLDDVDKVKIGEMSAAMGVTGPVDMSLVNAVRAQNPNIHPQEHYVNSCLLMVAVAICIPRIGMSDLSSYKPSIQASLNNSHCVPMAINTIGSALFHLHEQNDIQSRMKEFLALASSGILRTIHERDNSRQISDDVLRSHTTLYIILEQMVRKNRWLSMDVLETCFPYNLVRTAYQQCYEADAQ
|
Rac effector required for tissue morphogenesis, cell migrations and egg laying . May play a role in egg laying and in yolk protein clatherin-mediated endocytosis by oocytes during oogenesis . Plays a role in the formation of gap junctions between EA and EP endodermal precursor cells in embryos .
|
P55163
|
A4J9S6
|
DNAA_BURVG
|
Chromosomal replication initiator protein DnaA
|
Burkholderia cepacia complex
|
MNDFWQHCSALLERELTPQQYVTWIKPLAPVAFDASANTLSIAAPNRFKLDWVKSQFSGRIADLAREFWNTPIEVQFVLDPKAGMRGAPAGVAPAAPRMPLTPNGPAAAVAAIAANLTAHASAAPSAPADVPLTPSAAAAHHLHGDDADIDLPSLPAHEAAAGRRTWRPGPGAAPANGAEADSMYERSKLNPVLTFDNFVTGKANQLARAAAIQVAHNPGISYNPLFLYGGVGLGKTHLIHAIGNQLLLDKAGARIRYIHAEQYVSDVVKAYQRKAFDDFKRYYHSLDLLLIDDIQFFSGKSRTQEEFFYAFEALVANKAQVIITSDTYPKEISGIDDRLISRFDSGLTVAIEPPELEMRVAILMRKAQSEGVNLSEDVAFFVAKHLRSNVRELEGALRKILAYSKFHGREISIELTKEALKDLLTVQNRQISVENIQKTVADFYNIKVADMYSKKRPANIARPRQIAMYLAKELTQKSLPEIGELFGGRDHTTVLHAVRKIADERGKDAQLNHELHVLEQTLKG
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
A4J9S6
|
A0L4Y8
|
TRMD_MAGMM
|
tRNA [GM37] methyltransferase
|
Magnetococcus
|
MRFSILTLFPEMFAPLQASILGRGQKSGRLDLNLVQIRDFATDRHQNVDDTPFGGGPGMVLKPDILSHALRATLQGETAHVVYMSPQGSRFDQATAQRLAGYGHVVLLCGRYEGVDERFIDAHVDEELSVGDFVLTGGELPAMMVVDAVSRMVPGVLGDLESAQADSFQTGLLDHPHYTRPAHWVVDGDHYGAPEVLLSGNHGAIAEWRRRQALLRTLIRRPDLLGKAPLSRVEKRLIEALAVDLDALENKH
|
Specifically methylates guanosine-37 in various tRNAs.
|
A0L4Y8
|
A3P5E2
|
THIM_BURP0
|
4-methyl-5-beta-hydroxyethylthiazole kinase
|
pseudomallei group
|
MESISWNTPSVRDALAAVKRDAPFVYGLTNYVAANLSANVLLAVGAAPAIGAAADWPARFGAGANALWINTAALMSSGADTLLTAARAASKAGTRWVLDPVALGAGAPEYDAIVRDLLALRPTVIRGNASELIALAGGTAAGKGVDTTASPESALAFIGDLARRSGAVVAVSGPTDYVTDGVATLAVAGGDARLTRVTGAGCALGALIAALLAQRGAALAAASAAHAIYATAAERAADARGTASFAVRFVDELSLLDPAESSRDRSAGQIGAKRRE
|
Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
|
A3P5E2
|
Q5QD14
|
TAAR5_MOUSE
|
Trimethylamine receptor
|
Mus
|
MRAVLLPGSGEQPTAFCYQVNGSCPRTVHPLAIQVVIYLACAVGVLITVLGNLFVVFAVSYFKVLHTPTNFLLLSLALADMLLGLLVLPLSTVRSVESCWFFGDFLCRLHTYLDTLFCLTSIFHLCFISIDRHCAICDPLLYPSKFTVRTALRYIVAGWGIPAAYTAFFLYTDVVERALSQWLEEMPCVGSCQLLFNKFWGWLNFPAFFVPCLIMISLYLKIFVVATRQAQQIRTLSQSLAGAVKRERKAAKTLGIAVGIYLVCWLPFTVDTLVDSLLNFITPPLVFDIFIWFAYFNSACNPIIYVFSYRWFRKALKLLLSREIFSPRTPTVDLYHD
|
Olfactory receptor specific for trimethylamine, a trace amine enriched in the urine of male mice, playing a role in social behavior. Trimethylamine is present at high concentration in the urine of male mice after puberty and acts as an attractant. This receptor is probably mediated by the G(s)-class of G-proteins which activate adenylate cyclase.
|
Q5QD14
|
A6SZR5
|
DAPE_JANMA
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Janthinobacterium
|
MSKTLALTEELIALSSVTPEDKGCQSRLIELLEPLGFVCETIESDGVTNLWARKGTTQPLLVFAGHTDVVPTGPLEQWTSPPFVPTQREGKLYGRGAADMKTSIAAMVVAAEEFVQAHPAHKGSIGFLITSDEEGPATDGTVIVCNALKARGEQLDYCVVGEPTSSDVLGDTIKNGRRGSMSGKLTVKGIQGHIAYPQLARNPIHQCAPALAELVAEKWDDGNEYYLPTSWQVSNIHGGAGASNVIPGNVVIDFNFRFCTASTVDGLQKRVHAILDKHGLEYDLKWSISGHPFLTPKGTLSDAMSDAIKSETGVTTELSTTGGTSDGRFIAQICPQVVEFGPPNGSIHKIDEHIEVRFIDPLKNIYRRTMENLLL
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
A6SZR5
|
Q3M929
|
DER_TRIV2
|
GTP-binding protein EngA
|
Trichormus
|
MGLPIVAIIGRPNVGKSTLVNRLAGEQTAIVHDEPGVTRDRTYLPAYWSDREFQVVDTGGLVFNDDTEFLPLIRQQALAALHEASAAIFVVNGQTGPNSADEEIAEWLRQQPVPVFLAVNKCESPDQGSIQASEFWELGLGEPYPISAIHGNGTGELLDELIKHLPPTTELEENNEIKIAIIGRPNVGKSSLLNAFAGEERVIVSPISGTTRDAIDTFIERNGQNYRLIDTAGIRKKKSIDYGTEFFSINRAFKAIRRADVVLLVIDALDGVTEQDQKLAGRILDEGKACVVVVNKWDAVEKDSYTIYDYEKNLEARLHFTEWADTIYVSAVTGQRVEKILELVTKANEEHKRRVSTSVINEVLEDAVSWHSPPTSRGGRQGRIYYGTQVSTQPPTIALFVNEAKRFNDNYRRYIERQFRQQLGFKGTPIRLLWRSKKVRDVESGSANRATRV
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q3M929
|
Q4J8L7
|
VATD_SULAC
|
V-ATPase subunit D
|
Sulfolobus
|
MSSRKVLPTKINLINLRRQIRLIRTIKRLLENKREVLLLYLRQYADEYEKVYNEVSKVLSDVYSTYLQGVASEGLSTIQTYADSIPSSLNVNTSIKVLFGVKIPVVDLDESTIQQQPFGNLEISPYILKSREQMSYAFKKILTLIEIESSIRALSGELRKTQRLINAIDTSILPFYQSSSKYIKSVLDDRTREEFTRLKMVRKLLQRRR
|
Produces ATP from ADP in the presence of a proton gradient across the membrane.
|
Q4J8L7
|
Q96283
|
RAA2C_ARATH
|
Ras-related protein Rab11A
|
Arabidopsis
|
MTHRVDQEYDYLFKIVLIGDSGVGKSNILSRFTRNEFCLESKSTIGVEFATRTTQVEGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDITKRQTFDNVLRWLRELRDHADSNIVIMMAGNKSDLNHLRSVAEEDGQSLAEKEGLSFLETSALEATNVEKAFQTILGEIYHIISKKALAAQEAAAANSAIPGQGTTINVDDTSGGAKRACCSS
|
Intracellular vesicle trafficking and protein transport.
|
Q96283
|
B0UCF0
|
MDH_METS4
|
Malate dehydrogenase
|
Methylobacterium
|
MARKKIALIGAGQIGGTLAHLAGLKELGDVVLFDIADGVPQGKGLDIAESAPVDGFDAKYAGASDYAAIAGADVVIVTAGVPRKPGMSRDDLIGINLQVMEKVGAGIRTHAPNAFVICITNPLDAMVWALQKFSGLAPNKIVGMAGVLDSARFRHFLAEEFQVSVEDVTAFVLGGHGDDMVPLVRYSTVAGVPLPDLVKMGWTTQEKLDAMVERTRKGGGEIVNLLKTGSAFYAPAASAIAMAESYLKDKRRVLPCAAYLTGQYGIDGLFIGVPIVIGENGVERVVEVEFSAEEKAMFDKSVASVKGLVEACKGINAALA
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
B0UCF0
|
B5R2Y9
|
MENH_SALEP
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
|
Salmonella
|
MMLHAQHMPGQPGAPSLVFLHGFSGDCREWQPVGEQFHGCSRLYIDLPGHGGSAAIPVGGFADVIRLLRATLISYNILKFWLVGYSLGGRVAMMAACQGIPGLCGLVVEGGHPGLQNEQARAERRLSDGRWAERFRHEPLTEVFHDWYQQPVFASLTAQQRQALTALRSQNNGETLAAMLEATSLAVQPDLREALNALAFPFYYLCGERDSKFRALAQEVAATCHVIRNAGHNAHRENPAGVVDSLAQILRL
|
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
|
B5R2Y9
|
B7HDW5
|
RIMM_BACC4
|
Ribosome maturation factor RimM
|
Bacillus cereus group
|
MTKWFNVGKIVNTHGVRGEIRVISRTDFPEERYKVGNTLYISNEKGTDYLPVKVTSHRQHKTFDLLTFEGYNNVDEVEKFKGSLIKVPEEQLGELAEGEYYYHEIIGCSVVTEEGEALGTIKEILSPGANDVWVIKRPKGQDLLIPYIDDVVLQVNIENKLVTIHVMEGLL
|
An accessory protein needed during the final step in the assembly of 30S ribosomal subunit, possibly for assembly of the head region. Probably interacts with S19. Essential for efficient processing of 16S rRNA. May be needed both before and after RbfA during the maturation of 16S rRNA. It has affinity for free ribosomal 30S subunits but not for 70S ribosomes.
|
B7HDW5
|
P50069
|
RNPA_BORBU
|
Protein C5
|
Borreliella
|
MRKRNISLKSKIEIQKIFKEGKLIRFSNLNLKMFYKSNHLVYSRILVTFSKGFRGSVKRNRIRRLFKEAFRKRLELLEGIALDIIFVVSYGKLTLTYFSIESLMKGLVLRCERGIGESK
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
P50069
|
P0CV21
|
RLR70_PLAVT
|
Secreted RxLR effector protein 70
|
Plasmopara
|
MRGAYYIITALLVVASSQELRGSGHQLQIYDHDVVKAVKAVMKTLPNRFLRESRDVHDDLANEERSFYSILADIINKGMDTMPRAAEGVELMPNAAEGVEKMPRAAEGVETIPHAAEGVENMPHVPDEGLSKALTGAKTALNKLWGPFSATTPIGDASHDVSSREQIDFEIGSWSIDLRGFKPIAVHDQHKDMIQRVYTKFGQLCGNNLNPTAEETSLIWTMFDSRIVPSSSKDDRLKLIWQARQNVRSDMRSISSSKKWRYRWQGSPDSLTLDVLNSLLNMHYQRWVRMYDIFKQERPDLIDAPSNSKHTLGGNKDSSSATTLHKHSKGLSSRPFEPLNAVMMSHGDRFVSTQRSKRTFGSNADTVSLPLKQPKMRSSKALMPLSATLGDYSVPPLKSRLNFGGASSAFVPYTHPKAHTSKSLAPASTTLTLKDSELELSLGGIYDKNTG
|
Secreted effector that completely suppresses the host cell death induced by cell death-inducing proteins.
|
P0CV21
|
Q3KRC5
|
DUS3L_RAT
|
tRNA-dihydrouridine synthase 3-like
|
Rattus
|
MAEVAEVAAESGGGGDSGVGACERGVAPIKAQYRTTKERFHEYLDADKQEGACQETPTEGPAEPEAKRIRLEDGQENGKTEVAVESHERQVPKRARGQNKSRPHMKPAHYDKERLCPSLLQESATPCAFGDRCRFLHDVGRYLETKPADLGPHCVLFNTFGRCPYSMTCRFAGAHLGPEGQNLVQEEVVARCAQLPSVRNGLDRALQQQLRKRQVCFERAEQALSHLTQGPMPTIAPESTVATLTPKHSSCHVQLDNVGGDGARQGSPVPTCGPLTDEDVVRLRPCEKKRLDISGKLYLAPLTTCGNLPFRRICKRFGADVTCGEMAMCTNLLQGQMSEWALLKRHPCEDIFGVQLEGAFPDTMTKCAELLNRTIDVDFVDINVGCPIDLVYKKGGGCALMNRSAKFQQIVRGMNEVLDVPLTVKMRTGVQERVSLAHRLLPELRNWGVALVTLHGRSREQRYTRLADWPYIEQCAKVASPMPLFGNGDILSFEDANCAMQTGVAGIMVARGALLKPWLFTEIKEQRHWDISSSERLDILRDFTHYGLEHWGSDTQGVERTRRFLLEWLSFLCRYVPVGLLERLPQRINERPPYYLGRDYLETLMASQQAADWIRISEMLLGPVPPGFVFLPKHKANAYK
|
Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs. Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regulating their translation.
|
Q3KRC5
|
B6J5E3
|
RL24_COXB1
|
50S ribosomal protein L24
|
Coxiella
|
MAIKKIKKDDTVIVITGRDKGRQGKVLKVLPNSRLLVEGINLVKKHVKPNPNKNEQGGILERELSIHVSNVAIYNPAAKKADRVGIKTLEDGSKVRIFKSNGEVIDV
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
B6J5E3
|
B3PMA2
|
TRMD_META1
|
tRNA [GM37] methyltransferase
|
Metamycoplasma
|
MKINILSLFPEYFKAFQENSMIAKAIKLGHLEINVINFRDFSKEKHQKVDDTVYGGGDGMLLQVEPIDLALESVPNSYKILLSPQGQVFNQTKAHELAKHQEITLVCGHYEGFDERVLEFVDEELSVGDFILTGGEIPAMLITEAVARLVPGVLKKGSHENESFEGDGLLDYPQYTKPAIYKGLKVPEVLLSGNHALIDRWRKEASYSKTLKNRKDILAKRKEKPHEN
|
Specifically methylates guanosine-37 in various tRNAs.
|
B3PMA2
|
A7ZS62
|
RS15_ECO24
|
30S ribosomal protein S15
|
Escherichia
|
MSLSTEATAKIVSEFGRDANDTGSTEVQVALLTAQINHLQGHFAEHKKDHHSRRGLLRMVSQRRKLLDYLKRKDVARYTQLIERLGLRR
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
A7ZS62
|
P49770
|
EI2BB_HUMAN
|
eIF-2B GDP-GTP exchange factor subunit beta
|
Homo
|
MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL
|
Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.
|
P49770
|
A6T4R5
|
SPED_KLEP7
|
S-adenosylmethionine decarboxylase alpha chain
|
Klebsiella
|
MKKLKLHGFNNLTKSLSFCIYDICYAKTAEERDGYIAYIDELYNANRLTEILTETCSIIGANILNIARQDYEPQGASVTILVSEEPVDPKLIDQTEHPGPLPETVVAHLDKSHICVHTYPESHPEGGLCTFRADIEVSTCGVISPLKALNYLIHQLESDIVTIDYRVRGFTRDINGMKHFIDHEINSIQNFMSDDMKSLYDMVDVNVYQENIFHTKMLLKEFDLKHYMFHTRPEELTAEERKVITDLLWKEMREIYYGRNIPAV
|
Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
|
A6T4R5
|
B1W3Z0
|
RS5_STRGG
|
30S ribosomal protein S5
|
Streptomyces
|
MAGPQRRGSGAGGGERRDRKGRDGGASAAEKTAYVERVVAINRVAKVVKGGRRFSFTALVVVGDGDGTVGVGYGKAKEVPAAIAKGVEEAKKNFFKVPRIQGTIPHPITGEKAAGVVLLKPASPGTGVIAGGPVRAVLECAGVHDILSKSLGSSNAINIVHATVAALQGLQRPEEIAARRGLPLEDVAPAALLRARAGAGA
|
Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body.
|
B1W3Z0
|
Q7VNI7
|
MUTH_HAEDU
|
Methyl-directed mismatch repair protein
|
Haemophilus
|
MQLSIQPQSEAELLAKANWLAGFTLGELAQQLNTVVPPDLTRDKGWVGQIIERALGATAGSKPEQDFAHLGIELKTIPINNHGLPLETTFICLAPLIHNQGITWQTSHVKYKLQRVLWIPIQAERSIPIKDRYIGRAILWSPSYQQEQQLRNDWEELMEYIVLGRLDQINGHLGEVMQLRPKGRNRLSITQSIDQHGEQIQSLPLAFYLRKPFTAAILQNFLQQSD
|
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
|
Q7VNI7
|
A0KF24
|
RL2_AERHH
|
50S ribosomal protein L2
|
Aeromonas
|
MAIVKCKPTSPGRRHVVKIVNQDLYKGKPFAALLDKKDKSGGRNNNGRITTRHIGGGHKQHYRIVDFKRDKDGIPAKVERLEYDPNRTANIALVLYADGERRYILAPKGLKAGDAIASGADAAIKVGNTLPMRNIPVGSTVHAVEMKPGKGAQLARSAGTFIQILAREGNYVTLRLRSGEVRKVLAECRATIGEVGNSEHMLRQLGKAGANRWRGIRPTVRGMAMNPVDHPHGGGEGRNKGMQPVSPWGQKAKGFKTRKNKRTDKYIVRRRNK
|
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.
|
A0KF24
|
Q39JC5
|
PANB2_BURL3
|
Ketopantoate hydroxymethyltransferase 2
|
Burkholderia cepacia complex
|
MTYLQESSRPAVTVPKLQAMRDAGEKIAMLTCYDASFSALLDRSGVDVLLIGDSLGNVLQGHTTTLPVSLDDIAYHTACVARAQPRALIMADLPFGTYGTPAEAFASSVKLMRAGAQMVKLEGGEWLAETIRFLVERAVPVCAHVGLTPQSVHAFGGFKVQGKTEAGAAQLLRDARAVEAAGAQVVLLEAVPTLIGSEVTHMLRVPTIGIGAGADCSGQVLVLHDMLGVFPGKRPRFVKDFMQGEPNIQAAVEAYVRAVKDGSFPGPEHSF
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
Q39JC5
|
Q3ZC10
|
SMD1_BOVIN
|
snRNP core protein D1
|
Bos
|
MKLVRFLMKLSHETVTIELKNGTQVHGTITGVDVSMNTHLKAVKMTLKNREPVQLETLSIRGNNIRYFILPDSLPLDTLLVDVEPKVKSKKREAVAGRGRGRGRGRGRGRGRGRGGPRR
|
Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes. Is also a component of the minor U12 spliceosome. May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through non-specific electrostatic contacts with RNA.
|
Q3ZC10
|
C1DNF9
|
RNPA_AZOVD
|
Protein C5
|
Azotobacter
|
MVSRDFGREKRLLIPRQFKAVFDSPTAKVPGKHVLLLARPNALDHPRLGLVIGKKSVKLSVGRNRLKRLIRESFRLNQDSLAGWDIVVVARKGLGELENTEVTQQFGKLWKRLARSRPQTAVEAAGSSHA
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
C1DNF9
|
Q9C6L5
|
KCS5_ARATH
|
Very long-chain fatty acid condensing enzyme 5
|
Arabidopsis
|
MSDFSSSVKLKYVKLGYQYLINNFLTLLLIPVIATVAIELLRMGPEEILSVLNSLHFELLHILCSSFLIIFVSTVYFMSKPRTVYLVDYSCYKPPVTCRVPFSSFMEHSRLILKDNPKSVEFQMRILERSGLGEETCLPPAIHYIPPTPTMESARNEAQMVIFTAMEDLFKNTGLKPKDIDILIVNCSLFSPTPSLSAMIINKYKLRSNIKSYNLSGMGCSASLISVDVARDLLQVHPNSNAIIISTEIITPNYYKGNERAMLLPNCLFRMGGAAILLSNRRSDRWRAKYKLCHLVRTHRGADDKSYNCVMEQEDKNGNVGINLSKDLMTIAGEALKANITTIGPLVLPASEQLLFLSSLIGRKIFNPKWKPYIPDFKQAFEHFCIHAGGRAVIDELQKNLQLSGEHVEASRMTLHRFGNTSSSSLWYELSYIEAQGRMKRNDRVWQIAFGSGFKCNSAVWKCNRTIKTPTDGAWSDCIERYPVFIPEVVKL
|
Mediates mostly the synthesis of VLCFAs from 26 to 30 carbons in length (e.g. C20:1, C26, C28, C30).
|
Q9C6L5
|
A3PNF6
|
TRUB_CERS1
|
tRNA-uridine isomerase
|
Cereibacter
|
MGRTRKGRAISGWLVVDKPAGMTSTAVVNKVRWALEAQKAGHAGTLDPDATGVLAVALGEATKTVPYITDALKCYRFMVRLGLSTRTDDASGEVIATSEARPTDAEIAAALAAFRGEIQQVPPQFSAVKVEGERAYDLARDGERLDLAARPLWVESLEILSRPDADHVELEMVCGKGGYVRSIARDLGEALGCYGHVAWLRRTWSGPFEAEDGISVATIDELARSEALLSLVLPLAKGLADLPELPATPEGAARLRCGNPGMVIASDVEFGEEAWASYQGQPVAVGIYKSGELHPSRVFNL
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
A3PNF6
|
Q4QLH8
|
DEOC_HAEI8
|
Phosphodeoxyriboaldolase
|
Haemophilus
|
MTSNQLAQYIDHTALTAEKNEQDISTLCNEAIEHGFYSVCINSGYIPLAKEKLAGSNVKICTVVGFPLGANLTSVKAFETQEAIKAGANEIDMVINVGWIKSQKWDAVKQDIQAVFNACNGTPLKVILETCLLTKDEIVKACEICKEIGVAFVKTSTGFNKGGATVEDVALMKQTVGNIGVKASGGVRDTETALAMIKAGATRIGASAGIAIISGTQDTQSTY
|
Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate.
|
Q4QLH8
|
A9IJ97
|
MNME_BORPD
|
tRNA modification GTPase MnmE
|
Bordetella
|
MASSTHVPIAAIATAPGRGGIGVVRISGPDLSALARRLFGRELTPRHAHYLPFTAETGEHLDEGIALYFRAPQSYTGEDVLELQGHGGPAVLRRILERCLQAGADLGVRLAEPGEFTRRAFLNDRMDLAQAEAVADLIDASSVAAARGAMASLSGEFSARVNALSDRIVHLRMLVEATLDFPEEEIDFLEKYQARPTLQALAADLATLIAQARQGVILREGLHVVLAGKPNVGKSSLLNALAGDDIAIVTPIAGTTRDKVVQEIHIDGVPLHIVDTAGLRDTDDTVESIGIARTWKEIERADVILHLQDATQPADELDAQIVARLPARTPLLTVFNKVDLLDQPFQAQAGQLGISAREGAGLDELRARLLALAGWNPGAESPWLARERHVHALQRAAEHLEAATEHAAQDDRVLDLFAEELRLAHDSLSSITGKFTSDDLLGEIFSSFCIGK
|
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
A9IJ97
|
Q8Z9J5
|
RLUA_SALTI
|
tRNA pseudouridine(32) synthase
|
Salmonella
|
MGMENYNPPQEPWLVILYQDEHIMVVNKPSGLLSVPGRLEAHKDSIMTRIQRDYPQAESVHRLDMATSGVIVVALTKAAERELKRQFREREPKKQYVARVWGHPSPAEGLVDLPLICDWPNRPKQKVCYETGKPAQTEYNVVEFAADNTARVVLKPITGRSHQLRVHMLALGHPILGDQFYASPEALSLAPRLQLHAEMLTITHPAYGNSMTFKVPADF
|
Dual specificity enzyme that catalyzes the synthesis of pseudouridine from uracil-746 in 23S ribosomal RNA and from uracil-32 in the anticodon stem and loop of transfer RNAs.
|
Q8Z9J5
|
Q1MPK3
|
FABZ_LAWIP
|
Beta-hydroxyacyl-ACP dehydratase
|
Lawsonia
|
MSHPLPPNIQEILQLLPHRYPFLLVDRVIEFNAGKYIKAYKNVSINEPFFQGHFPGFPVMPGVLILEAMAQSGGITVLQSFPINELQGKVFLFAGIENVKFRQQVIPGDQLILECEIIRHKLQLWKMSCQAFVNNKLVAEAILTAAMTNKENF
|
Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.
|
Q1MPK3
|
Q8EGH4
|
EFTS_SHEON
|
Elongation factor Ts
|
Shewanella
|
MAISAAQVKELRERTGAGMMDCKKALEETNGDMELAIDNMRKSGAAKAAKKAGNIAADGTILIKNGEGFAVLLEVNCQTDFVAKDANFLGFANAVLDVAAASKVTLEDLKAQFEEARVALVAKIGENINVRRVEYIDGAKLASYRHGERIGVVVTGDADEETLKHLAMHVAASKPEYVNPEDVPADVVAREQALQIEISMNEGKPADIAEKMVVGRMKKFTGEISLTGQAYIMEPKKTVGEFLKEKGAKVTNFIRLEVGEGIEKKEEDFAAEVAAQIAASKKA
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
Q8EGH4
|
Q9AMJ9
|
CH10_ANASL
|
Chaperonin-10
|
unclassified Anabaena
|
MAAVSLSVSTVKPLGDRVFVKVSASEKRPRRLYFPDTAKEKPQVGEVVALGAGKRNDDGSRQELEVKVGDLLLYSKYAGTDVKLGTEEYVLLSEKDILAMVG
|
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.
|
Q9AMJ9
|
P17245
|
EFTU_CYAPA
|
Elongation factor Tu, cyanelle
|
Cyanophora
|
MARQKFDGNKPHVNIGTIGHVDHGKTTLTAAITTALASQGKGKARKYDEIDAAPEEKARGITINTAHVEYETEKRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLAKQVGVPNMVVFLNKEDQIDDADLLELVELEVRELLSKYDFPGDQIPFVSGSALLALESLSSNPKLMRGEDKWVDKILALMDAVDEYIPTPERPIDKSFLMAIEDVFSITGRGTVATGRIERGAIKVGETVELVGLKDTKSTTVTGLEMFQKTLEEGMAGDNIGILLRGVQKTDIERGMVLAKPGSITPHTQFESEVYVLTKDEGGRHTPFFSGYRPQFYVRTTDVTGSIDAFTADDGSNAEMVMPGDRIKMTVSLVHPIAIEQGMRFAIREGGRTIGAGVVSKILK
|
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
|
P17245
|
Q94A73
|
Y5656_ARATH
|
BTB/POZ domain-containing protein At5g66560
|
Arabidopsis
|
MASEKSTSKGQAWFCTTGLPSDIEIEVDDMTFHLHKFPLMSKSRKLHRLITEQETRSSSSMALITVIDPKVEETDKKGKGHEIEDDKEEEEVEEQEIEENGYPHIKLEDFPGSSESFEMVAKFCYGVKMDLSASTVVPLRCAAEHLEMTEEYSPDNLISKTERFLSHSVYKSLRESIKALKACESVSPLAGSLGITEQCIDSIVSRASSADPSLFGWPVNDGGGRGNISATDLQLIPGGAAKSRKKPSRDSNMELWFEDLTQLSLPIFKTVILSMRSGDLSSDIIESCLICYAKKHIPGILRSNRKPPSSSSTAVSENEQRELLETITSNLPLDKSSISSTTRFLFGLLRTAIILNAAEICRDLLERKIGSQLERATLDDLLVPSYSYLNETLYDVDLVERILGHFLDTLEQSNTAIVEVDGKSPSLMLVGKLIDGFLAEIASDANLKSDKFYNLAISLPDQARLYDDGLYRAVDVYLKAHPWVSEAEREKICGVMDCQKLTLEACTHAAQNERLPLRAVVQVLFFEQLQLRHAIAGTLLAAQSPSTSQSTEPRPSAAIRNLTITEEDGDEAEGERQVDAGKWKKTVRENQVLRLDMDTMRTRVHRLERECSNMKKVIAKIDKEGSSPATTTDRPRSWSITKKFGCKFKTQVCDSHEATMVDHRSRRS
|
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
|
Q94A73
|
P45268
|
Y1604_HAEIN
|
Putative phosphate permease HI_1604
|
Haemophilus
|
MEIISQYGSWLVWITAVFGFFMAFGIGANDVSNSMGTSVGSGTITAKQAIIIALIFESAGAYLAGGEVTQTIKSGVIEPIQFVDTPDILALGMLSTLFASGAWLFIATKMGWPVSGTHTIIGAIIGFACITIGPSSVDWSKIGSIVGSWFVTPVIAGILAYAIFASTQKLIFDTEQPLKNAQKYGPYYMGITVFVLCIVTMKKGLKHVGLNLSNSETLIISLAISLIGMFFFHFYFKSKIFTQSANKGTFGAVEKVFSILMLLTACAMAFAHGSNDVANAIGPLSAVVSIVNEGGKIVSGGALTWWILPLGALGIAVGLITMGQKVMATVGSGITDLTPSRGFAAQFATAMTVVVASGTGLPISTTQTLVGAILGIGFARGIAALNLTVIRNIISSWIVTLPAGAFFAIIIFYVLRTIFN
|
Potential transporter for phosphate.
|
P45268
|
Q9LCJ2
|
NQRF_COLPS
|
NQR-1 subunit F
|
Colwellia
|
GGSCGQCRVEVHSGGGDILPTEEGHINKREAKSGCRLACQVAVKQDMEIEVEDEIFGVQQWECEVISNDNQATFIKELKLQIPNGESVPFKAGGYIQIEAPAHHVKYKDFDIDEQYKGDWNHFGFFDVESKVDEPTLRAYSMANYPEEEGIIMLNVRIATPPPGRLHLPAGKMSSFIFSLKEGDKVTISGPFGEFFAKETDNEMVFIGGGAGMAPMRSHIFDQLKRLQSKRKMSFWYGARSKREMFYEDDYNGLAADNDNFQWHVALSDPQPEDNWEGMTGFIHNVLFEEYLKDHEAPEDCEY
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
|
Q9LCJ2
|
Q6AQ16
|
SYA_DESPS
|
Alanyl-tRNA synthetase
|
Desulfotalea
|
MKGNEIRSRFLEYFKGNGHTVAESSSLVPKDDPTLLFTNAGMVQFKRVFMGDDKRGYVRAVTSQKCVRAGGKHNDLENVGYTARHHTFFEMLGNFSFGDYFKEEAIRLAWNFLTVELGLPAEKMWVSVFEDDDEAFALWEKVEDLPKGRIVRLGEKDNFWAMGDTGPCGPCSEIHIDQGVGSSPCDNPNCAVGCDCDRFLELWNLVFMQFNRAEDGSLTALPRPSIDTGMGLERVAAVLQGKFNNYDSDLFAPIIAVLEDISGVKYGAAADTDTAIRVIADHARATSFLVADGVLPSNEGRGYVLRRIMRRAVRYGKKLGLEKPFMDRVTKAVCAEMQNAYPQLVATAALLEKVVNNEEERFRETLEHGLVQLDEKISQLLTSGGDAVIDGPFIFKLYDTFGFPFDIVRDIALERGVGFDEAGFATAMAEQRAKSRASRKGEGVKLHDEGVKALADAGKKAEFLGYEGLEADSVVEGLLSEQGSGVEKLVAGEKGRVFVAATPFYAEAGGQMGDRGSVRWQGGQASVYATQAEGTGLILHDLLVEEGELSLGLEVTLQVDDEERKATASNHSATHLLQAALISVLGDHVKQSGSLVGPERLRFDFTNFSQLTAAEIAQVETLVNEQIRNNAVIATDVLSKQEAIAGGATALFGEKYDDDVRVVSMGDYSRELCGGTHVGATGEIGLFVILSESGIAAGVRRIEALTGRAALAYVQGRLSTGNELADLLSCKSGDLVPKVESLLTAVKEGEKRVAQLAGQLASSGLDDLLNNALTVAGIKVVVAEVPLENAKALRELGDKVRDNLESGIAVIGGAVGGKVALLAIVTKDLVDRIQAGRIVSEVSGIVGGKGGGRPDMAQAGGTMPDKLSEAIASVPAIIEAML
|
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.
|
Q6AQ16
|
A1UUD5
|
IF3_BARBK
|
Translation initiation factor IF-3
|
Bartonella
|
MTPNQKDGPRSNQEIRVPCIQLINDEGQNQGIVSTQEALAMAANIGLDLVEIVPNAEPPVCKIVDLGKLKYQNQKKAAETRKKQKIIEIKEIKLRPNVDVHDYGVKLKAIHRFIEHGNKVKITLRFRGREMAHQDLGVKLLERMKEDVSEIAKIESEPKLENRQMMMVIAPKS
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
A1UUD5
|
C5C0R4
|
NUON_BEUC1
|
NDH-1 subunit N
|
Beutenbergia
|
MNFVQPVIQWASLAPILIVLGAAVLGVLIEAFAPRRVRRPVQVTLALLAAAGAFGAIAWRWAEVIGGGGGAPSTVVVGQLVEDGPALAAQGIIAILAFVGILVIAERGRRGAPGSEDAFAPQGASVPGSDYEDRARRAGLVQTEVYPLVLFSVGGMLVFPAAGDLLTLFIALEVLSLPLYLLSGLARRRRLLSQEASMKYFLLGAFSSALLLFGIALLYGYSGSVAIGEIHAATQATTGMDGLLVVGLVLLISGLLFKVGAVPFHAWTPDVYQGAPTPITGFMAACTKVAAFGALLRVVYVVAPAMTWDIQPFLWVVAVLTMVVGTVLAIVQTDMKRTLAYSSVAHAGFLLVGVVAMSPEGISSVFFYLLAYGLATIGAFALVALVRERDAEGNVTAEASHLAQWAGLGRRSPVVATVFALYLLSFAGIPLTSGFVGKFVAFAAAIDGGAWPLVVVGVLASAAAAFFYVRIIVLMFFTSPAEEAGAPSTTVVRSQGFTAVAVALTAAATLVLGVWPTPVLDLLAQATKFVV
|
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.
|
C5C0R4
|
Q475M4
|
RECA_CUPPJ
|
Recombinase A
|
Cupriavidus
|
MDDKKAGAGLSAEKQKALAAALSQIEKQFGKGSIMRMGDGEVEKDIQVVSTGSLGLDIALGVGGLPRGRVVEIYGPESSGKTTLTLQVVAEMQKLGGTCAFIDAEHALDVNYASKLGVDVGELLISQPDTGEQALEITDALVRSGSIDLIVIDSVAALVPKAEIEGEMGDSLPGLQARLMSQALRKLTGTIKRTNCLVIFINQIRMKIGVMFGSPETTTGGNALKFYASVRLDIRRIGSIKKGDDVIGNETKVKVVKNKVSPPFREAFFDILYGQGISRQGEIIDLGVDAKIVEKSGAWYSYNGDKIGQGKDNAREYLRENPDIAQEIENKVRAALGVAPMNSVPAAEVVTED
|
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.
|
Q475M4
|
P53254
|
UTP22_YEAST
|
U three protein 22
|
Saccharomyces
|
MATSVKRKASETSDQNIVKVQKKHSTQDSTTDNGSKENDHSSQAINERTVPEQENDESDTSPESNEVATNTAATRHNGKVTATESYDIHIARETAELFKSNIFKLQIDELLEQVKLKQKHVLKVEKFLHKLYDILQEIPDWEEKSLAEVDSFFKNKIVSVPFVDPKPIPQNTNYKFNYKKPDISLIGSFALKAGIYQPNGSSIDTLLTMPKELFEKKDFLNFRCLHKRSVYLAYLTHHLLILLKKDKLDSFLQLEYSYFDNDPLLPILRISCSKPTGDSLSDYNFYKTRFSINLLIGFPYKVFEPKKLLPNRNCIRIAQESKEQSLPATPLYNFSVLSSSTHENYLKYLYKTKKQTESFVEATVLGRLWLQQRGFSSNMSHSGSLGGFGTFEFTILMAALLNGGGINSNKILLHGFSSYQLFKGVIKYLATMDLCHDGHLQFHSNPENSSSSPASKYIDEGFQTPTLFDKSTKVNILTKMTVSSYQILKEYAGETLRMLNNVVQDQFSNIFLTNISRFDNLKYDLCYDVQLPLGKYNNLETSLAATFGSMERVKFITLENFLAHKITNVARYALGDRIKYIQIEMVGQKSDFPITKRKVYSNTGGNHFNFDFVRVKLIVNPSECDKLVTKGPAHSETMSTEAAVFKNFWGIKSSLRRFKDGSITHCCVWSTSSSEPIISSIVNFALQKHVSKKAQISNETIKKFHNFLPLPNLPSSAKTSVLNLSSFFNLKKSFDDLYKIIFQMKLPLSVKSILPVGSAFRYTSLCQPVPFAYSDPDFFQDVILEFETSPKWPDEITSLEKAKTAFLLKIQEELSANSSTYRSFFSRDESIPYNLEIVTLNILTPEGYGFKFRVLTERDEILYLRAIANARNELKPELEATFLKFTAKYLASVRHTRTLENISHSYQFYSPVVRLFKRWLDTHLLLGHITDELAELIAIKPFVDPAPYFIPGSLENGFLKVLKFISQWNWKDDPLILDLVKPEDDIRDTFETSIGAGSELDSKTMKKLSERLTLAQYKGIQMNFTNLRNSDPNGTHLQFFVASKNDPSGILYSSGIPLPIATRLTALAKVAVNLLQTHGLNQQTINLLFTPGLKDYDFVVDLRTPIGLKSSCGILSATEFKNITNDQAPSNFPENLNDLSEKMDPTYQLVKYLNLKYKNSLILSSRKYIGVNGGEKGDKNVITGLIKPLFKGAHKFRVNLDCNVKPVDDENVILNKEAIFHEIAAFGNDMVINFETD
|
Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
|
P53254
|
B4RSL8
|
SYT_ALTMD
|
Threonyl-tRNA synthetase
|
Alteromonas
|
MPVITLPDGSQRAFDNPVSVLDVANDIGPGLAKATIAGKVNGELVDAVDMIDADAQLQIITAKDEEGLEILRHSCAHLLGHAIKQLWPNTKMAIGPVIDNGFYYDVDMEESLTQEDLAKLEKRMLELAKTNYNVVKNKVSWQEARDAFEARGESYKMEILDENISKDDRPALYQHEEYTDMCRGPHVPNMKFCHHFKLMKVAGAYWRGDSDNKMLQRIYGTAWADKKQLKSYLQRLEEAEKRDHRKIGKALNLFHWQEEAPGMVFWHNDGWSIYTELESFVRKKLREYGYDEVKGPLMMDRSLWEKSGHWDKYAENMFTTESEKREYAVKPMNCPGHVQIFNQGLKSYRDLPLRMAEFGCCHRNEPSGALHGLMRVRGFTQDDAHIFCTEEQILEEVSGCIKMVYETYAAFGFENIKVKLSTRPEKRVGADEIWDKSEAALAEALKANDIEFDYQPGEGAFYGPKIEFTLHDCLDRAWQCGTVQLDFSMPGRLGSTYVAEDGERKVPVMIHRAILGSLERFIGILTEEFAGFFPLWLAPQQVVVMNITDKQADYASDCVKKLQDLGFRAKSDLRNEKIGFKIREHTLKRIPYMLVVGDKEMEAGEVAVRSRRGDDLGKMGLEDFIAMAQQEVVEKTIK
|
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).
|
B4RSL8
|
Q698K8
|
VM2L4_GLOBR
|
Disintegrin halystatin
|
Gloydius
|
EDEAPKMCGVTQNWESYEPIKKASQSNLTPAHQRYIELVIVADHGMFTKYNGDSDKIREWVRQMVNTVDEIYSYMYIDVALAGLEIWSNEDLINVQPAAPHTLDSFGKWRERDLLHRIHHDNAMLLTAIDFDGPTIGLAYVGTMCKPKGSTGVVQDHSTINLRVAVTMAHEIGHNLGIHHDTGSCSCGGYSCIMSPVISHEPSKYFSDCSYTQCWDFIMNQKPQCILNKPLRTDTVSTPVSGNELLEAGEECDCGSPGNPCCDAATCKLRQGAQCAEGLCCDQCRFMKKGTVCRIARGDDMDDYCNGISAGCPRNPFHA
|
Inhibits platelet aggregation induced by ADP (IC(50) is 100 nM), collagen (IC(50) is 500 nM), thrombin and epinephrin (IC(50) is 300 nM). Does not inhibit aggregation induced by ristocetin. Significantly inhibits angiogenesis both in vivo and in vitro.
|
Q698K8
|
P32826
|
SCP49_ARATH
|
Serine carboxypeptidase-like 49
|
Arabidopsis
|
MEKLTFLSLLLHFVVFIASTIPSSSFLLNDRTFERSNLPSTRAEKLIRELNLFPQQDLNVIDVADLPLTAAEGPGIVERKFVFPNILADGGPTVDDLGHHAGYYKLPKSRGASMFYFFFESRNKKDAPVVIWLTGGPGCSSELAVFYENGPFKITSNMSLAWNEYGWDQVSNLLYVDQPVGTGFSYTTDKSDIRHDETGVSNDLYDFLQAFFAEHPKLAKNDFYITGESYAGHYIPAFASRVHKGNKANEGVHINLKGFAIGNGLTDPALQYPAYPDYALEMGLITQKEHDRLEKIVPLCELSIKLCGTDGTTSCLASYLVCNSLFSGVMSHAGGVNYYDIRKKCVGSLCYDFSNMEKFLNLQSVRKSLGVGDIDFVSCSTSVYQAMLVDWMRNLEVGIPTLLEDGISLLVYAGEYDLICNWLGNSRWVNAMEWSGKTNFGAAKEVPFIVDGKEAGLLKTYEQLSFLKVRDAGHMVPMDQPKAALKMLKRWMENSLIEDATVTVAAQGGEELVAQM
|
Probable carboxypeptidase.
|
P32826
|
Q07981
|
FAR1_CORAP
|
NDPYLRF-amide
|
Cornu
|
MTSLCLTIAPAVLSLICLSSYGWAEGDTTDNEYLRFGRENNNGYIRFGRNDPFLRFGKKSDPFLRFGKQDPFLRIGRQDPFLRFGKQDPFLRFGKQDPFLRIGKQDPFLRFGRSEPYLRFGRNDPYLRFGRNDPYLRFGRNDPYLRFGRNDPYLRFGKNDPFLRFGKSVDGEIEAGVDAVTLSREHEFAHENAASDRQKRSAYTDAIDKDNSLTSLVREAREASDSNGQINDGKVVEVPVFRDTRNGHYMRFGKKNEVDVTDGDTYDRDYSDSDVSNLLRYYGNTVPLPAYDKRSEHKQEYMRFG
|
Can function as both cardioregulatory hormones and transmitters and may regulate cardiovascular function.
|
Q07981
|
C1D5E0
|
RECR_LARHH
|
Recombination protein RecR
|
Laribacter
|
MKTPASLESLITALRVLPGVGPKTAQRMAYHLMQRDPGGADRLARAIDHARSHLKHCARCNTFSETELCVLCADDQRRQDVLCVVEMPADALMIEQTHSYDGLYFVLMGKVSPLDGLTARDIPLEQLARRALDGTVNEVILATNFTAEGEATAHVLATLFKDRGLSVSRIARGLPVGGELEHVDAGTLAQALYERRRLSTGDA
|
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.
|
C1D5E0
|
B0S230
|
PFKA_FINM2
|
Phosphohexokinase
|
Finegoldia
|
MKTIAILTSGGDAPGMNACIRSIARTCIYNGIRVMGIRSGYDGLMNGNIYEMNVSSVADIIHRGGTILGSARCPEFKTEEGQKKGAQILKDFGIDGLVVLGGDGSFKGASALSKIGISTIGIPCTIDNDMGYTDYTIGFFTAVETVSDAISKLRDTSSSHGRANIIEVMGRNCGDIALYSGVASGAESILVPEVELNIDEVTEKIERGRKRGKLHHLIMLAEGVGGAYDIKNMIEEKTGVETKVTILGHVQRGGTPCTFDRLMATQMGNLAVKLIMEEKTDLAIAMKDNKIITVPIDEAVTTKRKFRDDLYEISKEISI
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
B0S230
|
P16497
|
KINA_BACSU
|
Stage II sporulation protein J
|
Bacillus
|
MEQDTQHVKPLQTKTDIHAVLASNGRIIYISANSKLHLGYLQGEMIGSFLKTFLHEEDQFLVESYFYNEHHLMPCTFRFIKKDHTIVWVEAAVEIVTTRAERTEREIILKMKVLEEETGHQSLNCEKHEIEPASPESTTYITDDYERLVENLPSPLCISVKGKIVYVNSAMLSMLGAKSKDAIIGKSSYEFIEEEYHDIVKNRIIRMQKGMEVGMIEQTWKRLDGTPVHLEVKASPTVYKNQQAELLLLIDISSRKKFQTILQKSRERYQLLIQNSIDTIAVIHNGKWVFMNESGISLFEAATYEDLIGKNIYDQLHPCDHEDVKERIQNIAEQKTESEIVKQSWFTFQNRVIYTEMVCIPTTFFGEAAVQVILRDISERKQTEELMLKSEKLSIAGQLAAGIAHEIRNPLTAIKGFLQLMKPTMEGNEHYFDIVFSELSRIELILSELLMLAKPQQNAVKEYLNLKKLIGEVSALLETQANLNGIFIRTSYEKDSIYINGDQNQLKQVFINLIKNAVESMPDGGTVDIIITEDEHSVHVTVKDEGEGIPEKVLNRIGEPFLTTKEKGTGLGLMVTFNIIENHQGVIHVDSHPEKGTAFKISFPKK
|
Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. It also autophosphorylates in the presence of ATP.
|
P16497
|
P58393
|
GLGA1_RHIME
|
Starch [bacterial glycogen] synthase 1
|
Sinorhizobium
|
MNILSVASEVYPLVKTGGLADVVGALPSALLPHGVRTRTLVPGYPSVLKKLKKKKPVGRFDNLFGHPATVLAAEVNGVDLLVLDQPALYARDGGPYLDSTGRDYPDNFRRFAALSLAAAEIAGNGIIPNWKPDIVHVHDWQTALTPVYMRFGPAPDLPTVMTIHNIAFQGQFGASVFPELALPPDAFSTQFVEYYGDVGFLKGGLQTASAITTVSPSYAQEILTPEFGMGLDGLLSSRVADLTGIVNGIDGETWDPQTDPHIPAHYGPGTLKRRAGNRKALEERFGLEKGPGPIFCVISRLTWQKGMDLVAEAADDIVALGGKLVVLGSGDPALESALMAAASRNRGHIGMVTGYDEPLSHLMQAGADAILIPSRFEPCGLTQLYGLRYGCVPVVARTGGLTDTIIDANEAALSAKCATGFHFLPVTTDGLRLAIRRVLRAYNEPKLWARLQYQGMKSDVSWAKSAERYVSLYSALLAKG
|
Synthesizes alpha-1,4-glucan chains using ADP-glucose.
|
P58393
|
Q9H3J6
|
MTRFR_HUMAN
|
Mitochondrial translation release factor in rescue
|
Homo
|
MSTVGLFHFPTPLTRICPAPWGLRLWEKLTLLSPGIAVTPVQMAGKKDYPALLSLDENELEEQFVKGHGPGGQATNKTSNCVVLKHIPSGIVVKCHQTRSVDQNRKLARKILQEKVDVFYNGENSPVHKEKREAAKKKQERKKRAKETLEKKKLLKELWESSKKVH
|
Part of a mitoribosome-associated quality control pathway that prevents aberrant translation by responding to interruptions during elongation . As heterodimer with MTRES1, ejects the unfinished nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for MTRES1 and MTRF during mitoribosome rescue .
|
Q9H3J6
|
P40649
|
SOX13_XENLA
|
Transcription factor Sox-12
|
Xenopus
|
MDTIQGELVYCPANEQECRISAKIPISPSEDTGGPCLKVEEDYEEVSLQTGIVPVFIKQDYESSSQDANDLCKPQGDAPASDRKEENLKLSKTVSDAMPALEKFLSNDWKEILLGNSTVGSKDFKGTKESLAEKELQLLLMIHQLTGLRDQLLSAHSEHRNLAAMLFEKQQQQMDLARQQQEQIAKQQQQLIQQQHKINMLQQQIQQVNMPYVMIPAFPSAQTVSAEPQMSLPIQPIPCKPVEYPMPLLHNSHAGRGSASAKHQETSQPLNLTAKPKCPDQFPNSSSSPEFRMSPVGSQCGGTMDSASSSQKANLPLGFLGEGDAITKAIQEACQLLHGQNTSPEHCQQNYRKELLDTLPEKNIQDVTSLHHTEASLLRCSMDIDGSRGNHIKRPMNAFMVWAKDERRKILQAFPDMHNSSISKILGSRWKSMSNGEKQPYYEEQARLSRQHLERYPDYKYKPRPKRTCIVEGKRLRVGEYKALMKNRRQDTRSLGSLQCPPSPSGFSSQSLLGNLSQSPQECNIQVVTSQCLMSHELHGAIHMAKDICSDSEDSVKSDGELVVITD
|
Transcription factor that binds to DNA at the consensus sequence 5'-AACAAT-3'.
|
P40649
|
A6VGV3
|
RS12_METM7
|
30S ribosomal protein S12
|
Methanococcus
|
MAGSKSPKGEFAGRKLLLKRRASRWHHYKYVNKALSLKLKADPLEGAPMGRGIVVEKVGLEAKQPNSAIRKCVRVQLIKNGRQVTAFAPGNHAINFIDEHDEVVIEGIGGPSGQAKGDIPGVRYKVVMVGKNSIRELVRGRQEKVKR
|
With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits.
|
A6VGV3
|
P03919
|
NU5M_HYLLA
|
NADH dehydrogenase subunit 5
|
Hylobates
|
MAMYTTMAILTLTSLIPPITATLINPNKKNLYPHYVKMTIASTFMISLFPTMMFMCTDQETIISNWHWTATQTLELSLSFKLDYFSMMFIPIALFVTWSIMEFSLWYMHSDPNINQFFKYLLIFLTTMLILVTANNLFQLFIGWEGVGIMSFLLIGWWHAREEANTAAIQAILYNRIGDIGFILALAWFLLHTNSWEPQQMILLNSNPNFLPLAGLLLAARGKSAQLGLHPWLPSAMEGPTPVSALLHSSTMVVAGVFLLIRFHPLTENNQLIQTLTLCLGAITTLFTAICALTQNDIKKIVAFSTSSQLGLMVVTIGINQPYLAFLHICTHAFFKAMLFMCSGSIIHNLNNEQDIRKMGGLFKTLPLTSTSLTIGSLALTGMPFLTGFYSKDLIIETANMSYTNAWALSTTLIATSLTSAYSTRMILLTLTNRPRFPTLTNINENNPTLLNPIKRLTIGSLLAGFLIINSIPPTSPSQTTIPLYLKLTALSITLLGFLTAFDLHLLTNKLKMKNPSHTFHFSNMLGFYPNTIHRTIPYASLTMSQNLASLLLDLAWLEKLMPKTISHHQISASVTISSQKGMIKLYSLSLLIPLSLTLLLIM
|
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.
|
P03919
|
Q57HL7
|
SRKA_SALCH
|
Serine/threonine-protein kinase SrkA
|
Salmonella
|
MNDNAFTFQTLHPETIMDALFEQGIRVDSGLTPLNSYENRVYQFQDEDRRRFVVKFYRPERWSVDQIREEHQFALELVKDEVPVAAPLAFNGQTLLAHQGYHYAIFPSVGGRQFEADNIDQMEAVGRYLGRLHQTGRKRPFTFRPDIGLAEYLFEPRQVFEDAALIPSGQKAAFLKATDTLLSAVTECWRTDFATLRLHGDCHAGNILWRDGPLFVDLDDARNGPAIQDLWMLLNGDKAEQRMQLETIIEAYEEISEFDTAEIGLIEPLRAMRLVYYLAWLIRRWGDPAFPKNFPWLTGEDYWQRQTTTFIEQTKILHEPPLQLTPMY
|
A protein kinase that phosphorylates Ser and Thr residues. Probably acts to suppress the effects of stress linked to accumulation of reactive oxygen species. Probably involved in the extracytoplasmic stress response.
|
Q57HL7
|
P54799
|
NIFH1_METBA
|
Nitrogenase reductase
|
Methanosarcina
|
MTRKIAFYGKGGIGKSTTQQNTAAAMAYYHGKKIFIHGCDPKADCTRLVLGGVAQTTIMDTLRELGEDAVTAENVINTGFDGIKCVESGGPEPGVGCAGRGVITAINLMEEMGAYSEDLDFIHFDVLGDVVCGGFAMPIREGKAQEVYIVASGEMMATYAANNICKGLLKYAEQSGVRLGGIICNSRRVDNELEMMEEFASALGTQLLYFVPRDNIVQKAEFNKKTVVEYDPTCNQALEYKELAKKILENDMFVIPKPLSMDQLEKMVERYGLMD
|
The key enzymatic reactions in nitrogen fixation are catalyzed by the nitrogenase complex, which has 2 components: the iron protein and the molybdenum-iron protein.
|
P54799
|
B0B9Q4
|
DNLJ_CHLT2
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Chlamydia
|
MGAVSRDDYIALCTELVEHDRRYYALNQPTISDYSYDMKMRELQEIEVQHPEWKVSWSPTMYLGDRPSGQFPVVPHSSPMLSIANVYSLQELEEFFSRTEKLLGYSPGYSLELKIDGIAVAIRYEKRLFAQALSRGNGVKGEDITANVSTIRSLPMRLPQEAPEDLEVRGEVFLSYEAFEELNACQREQGKLEFANPRNAAGGTLKLLSSKEAAKRKLDLSVYGLITDQKKRSHFENLQLCSQWGFFVAGMPKQCRSRQEVVERIREIEEMRAALPMAIDGVVIKVDNIAHQDRLGLTSKHYRWAIAYKYAPERAETILEDIVVQVGKTGILTPVAELAPVFLSGSRVSRASLYNQDEIEKKDIRIGDSVYVEKGGEVIPKIVGINLAKRSLESEPWKMPSLCPVCHEPVVKEKVSVRCINPLCSGGMLEKICFFASKSALNIDHLGEKVVTKLFEVGLISSCSDIFALTEEDLKQVPGFKDRSIQNLLASIAGAKKVALDRLLTALSIPFVGSSGAIALADHFGTLDKVIEASLDELMSIEGIGPKVAASIVAFFSKHENREEIRRMQELGVQVLSKQSDKEAPLQGKVFVLTGTLQQMTRTQAEERIRSLGGKVSSSVSKSTYAVIAGSEAGGKLKKAQDLGLSIWNESKLSRILDAKSVS
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
B0B9Q4
|
A0A455LLW0
|
ATNJ_ARTSZ
|
Arthripenoid biosynthesis cluster protein J
|
unclassified Arthrinium
|
MSTTKPICLVPLHVVIVGAGIGGLSAAVALANRGHSVLILESTSELSHVGAGVALPPTTRKWYESEGVLQVDDTACVPLEGIEITKWDTGELVTRTAANPAGKQTAIHHGDMQLALLARARELTNVEIRLGARVVDVDLEATVALLADGQRVAGDLIIAADGVKSTLKAKVCPPEAVVPLPTGEAAYRFTLPRELLESDAELRELVQRPWGVRWDGPSCHVVAYPLRNHRLLNVVLIHPDNGDAKESWTSVTDKQNVLADYQGWNPTLLKLIALAPPEVPNFRMFLYSPAPVWVKGSTILLGDSCHAMLPYLGQGVAQAVEDATAIATVLSLIETRKQLPLALRAYESSRKERVDQIQAATYRAREQLHLRDGDAQAARDSQRKATSGTGQNSDVVKMQQSYWTWDAAGVAEKTLAALIIA
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FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the meroterpenoids arthripenoids . The pathway begins with the HR-PKS atnH that catalyzes two chain-extension steps to form a reduced triketide, which then primes the SAT domain in the NR-PKS atnG to initiate three more cycles of extension to give a linear hexaketide corresponding to the polyketide part of arthripenoids . The FAD-dependent monooxygenase atnJ then performs an oxidative decarboxylation at C11 of the atnH/atnG product, via an electrophilic aromatic hydroxylation with concomitant ipso-decarboxylation . The membrane-bound polyprenyl transferase atnF then introduces a farnesyl group before the FAD-dependent monooxygenase atnK functions as the first epoxidase on terminal C12'-C13' olefin, followed by a second epoxidation on C7'-C8' catalyzed by atnA . The terpene cyclase/mutase atnI then initiates the sequential tricyclic ring formation through protonation of the terminal epoxide and catalyzes the regioselective and stereoselective 6/6/6-tricyclic ring formation . The cytochrome P450 monooxygenase atnM is responsible for hydroxylating both C1' and C10' (Probable). The next steps may involve ketoreduction and acetyl transfer by the ketoreductase atnB and the acetyltransferase atnC, and lead to the production of arthripenoid B, the final biosynthetic product of the atn cluster . The hydroquinone moiety in arthripenoid B is prone to undergo spontaneous oxidation to afford a benzoquinone compound, a key intermediate for generating structure diversity (Probable). For instance, addition of a cysteine followed by ring contraction gives arthripenoid A, tautomerization gives the main product arthripenoid C, addition of a molecular of water or amine affords arthripenoid D or E, respectively, and loss of one water forms arthripenoid F (Probable).
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A0A455LLW0
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