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
|
|---|---|---|---|---|---|---|
Q9FHZ1
|
SCL23_ARATH
|
GRAS family protein 28
|
Arabidopsis
|
MTTKRIDRDLPSSDDPSSAKRRIEFPEETLENDGAAAIKLLSLLLQCAEYVATDHLREASTLLSEISEICSPFGSSPERVVAYFAQALQTRVISSYLSGACSPLSEKPLTVVQSQKIFSALQTYNSVSPLIKFSHFTANQAIFQALDGEDSVHIIDLDVMQGLQWPALFHILASRPRKLRSIRITGFGSSSDLLASTGRRLADFASSLNLPFEFHPIEGIIGNLIDPSQLATRQGEAVVVHWMQHRLYDVTGNNLETLEILRRLKPNLITVVEQELSYDDGGSFLGRFVEALHYYSALFDALGDGLGEESGERFTVEQIVLGTEIRNIVAHGGGRRKRMKWKEELSRVGFRPVSLRGNPATQAGLLLGMLPWNGYTLVEENGTLRLGWKDLSLLTASAWKSQPFD
|
Probable transcription factor involved in plant development.
|
Q9FHZ1
|
A8F8L8
|
DAPH_PSELT
|
Tetrahydrodipicolinate N-acetyltransferase
|
Pseudothermotoga
|
MNNDLTADSIIEMISSSKKKTPVIAYVKGHLSDIDMSGVQFFGTDNFGIIFADYEDLRQFLEKNGNKIHDVHIEAKARNSALPMADITKFNARVEPGAVIRDLVKIGDGAVIMMGAIINVGAVIGEKTMIDMNAVIGGRAIIGRNCHIGAGAVIAGVIEPPSATPVVIEDNVMVGANAVVLEGVKVGKGSVVAAGAVVVSDVDPYTVVAGIPAKFIKKVDEKTIEKTKIIEILRQRDH
|
Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate.
|
A8F8L8
|
Q9L4U5
|
AKNT_STRGJ
|
Protein AknT
|
Streptomyces
|
MQTQNAPETAENQQTDSELGRHLLTARGFHWIYGTSGDPYALTLRAESDDPALLTRRIREAGTPLWQSTTGAWVTGRHGVAAEALADPRLALRHADLPGPQRHVFSDAWSNPQLCHIIPLDRAFLHASDADHTRWARSASAVLGSAGGAPAEGVREHAGRVHREAADRTGDSFDLMADYSRPVATEAAAELLGVPAAQRERFAATCLALGVALDAALCPQPLAVTRRLTEAVEDVRALVGDLVEARRTQPGDDLLSAVLHAGSSAASAGQDALAVGVLTAVVGVEVTAGLINNTLESLLTRPVQWARLGENPELAAGAVEEALRFAPPVRLESRIAAEDLTLGGQDLPAGAQVVVHVGAANRDPEAFLAPDHFDLDRPAGQGQLSLSGPHTALFGAFARLQAETAVRTLRERRPVLAPAGAVLRRMRSPVLGAVLRFPLTTSA
|
Involved in the biosynthesis of the anthracycline antitumor agent aclacinomycin A. AknT is required for the glycosylation of aklavinone aglycone by AknS to yield aclacinomycin T (rhodosaminyl-aklavinone).
|
Q9L4U5
|
B8CX03
|
MTAD_HALOH
|
5-methylthioadenosine/S-adenosylhomocysteine deaminase
|
Halothermothrix
|
MKILIKNVDVIYTADSNRSIIKNGYIIIQDNKIKEINDMDNLVYQSNDFDDVISGKGKMALPGLVNAHTHSAMTLLRGFADDMPLHKWLQEKIWPFEKTLIPEDIYWGAKLAILEMIKTGTTTFADMYFEMGQVAKVVEEGGLRAVLSQGLIEANDGEEGLNRALKFCLEWNNRADGRILTMLAPHAPYTCSPDFFRRVVDLSQEYNLGIHTHIAETKEEFQQIREKYDCTPLQYLEKTGALKRPVLAAHCIYITEEDMDLMAQKPIGVAYNPQSNMKLGSGIAPVTRMLSKGIKVGIGTDGTSSNNNLDLIEEARSGSFLQKVNDLDSTALPVDTVLKMLTVNGAKILGFDKLGVLKEGYLADIILIGLNESTFYYPHYNNLSNLFYAGSGNDVTTVIVNGRVIMKDREVLTINEEEVYYKIEEIARRKL
|
Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
|
B8CX03
|
B5XRA3
|
MDCG_KLEP3
|
Malonate decarboxylase holo-[acyl-carrier-protein] synthase
|
Klebsiella
|
MSSTPRPHDLVWLNHASALEAIAEPWVAQQWRAALPVVVRRDVDDQARIPVGVRGMKREQRAAGWVQAHNIVRCVTPEMLVERERLLGSPFVSQPPVQAAIALTLHPWSWRWGVTGSTGYALATEIPVLHAASDLDLLIRAPQPLDREALREWLARVAQLPCRADTQVETPYGAFALNEWLRDGRALLKTSHGARLTATPWHREE
|
Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield holo-[acyl-carrier-protein].
|
B5XRA3
|
Q02K17
|
RECR_PSEAB
|
Recombination protein RecR
|
Pseudomonas
|
MSFSPLIRQLIESLRILPGVGQKSAQRMALMLLERDRSGGLKLAQALTAAMEGVGHCRRCRTLSEEELCPQCADPRRDDSLLCVVEGPLDVFAVEQTGYRGRYFVLKGHLSPLDGLGPEAIGIPELEARIRDGAFSEVILATNPTVEGEATAHYIAQLLAGRGLTLSRIAHGVPLGGELELVDGGTLAHALAGRRPIS
|
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.
|
Q02K17
|
Q7U317
|
CH60_HELHP
|
Chaperonin-60
|
Helicobacter
|
MASKEINFSDSARNKLYEGIKQLSDAVKVTMGPKGRNVLIQKSYGAPTITKDGVSVAKEIELADPIANMGAQLVKEVASKTADAAGDGTTTATVLAYSIYKEGLRNITAGANPIEVKRGMDKASAAIIEELKKSSKKIGGKSDIAQVATISANSDENIGALIAEAMEKVGKDGVITVEEAKGINDELSVVEGMQFDRGYLSAYFVTNTDKMTAQLENAYVLLTDKKISNMKEILPLLEATMQSGKPLLIIAEDIEGEALTTLVVNKLRGVLNVSAVKAPGFGDRRKAMLQDIAILTGGQVISEELGKTLEAATLADLGSAARIVIDKDNTTIVDGKGKTKDVKDRIAQIKTEIENTTSDYDREKLQERLAKLSGGVAVIKVGAASEVEMKEKKDRVDDALSATKAAVDEGIVIGGGSALIRASQKVKLKLEGDEAIGYDIIKRAIKAPLAQIATNAGYDAGVVVNEVEKNSKDGFGFNATTGEYVDMFKEGIIDPLKVTRVALQNAVSVSSLLLTTEATINEIKEDKPAPAMPDMGGMGGMGGMM
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
Q7U317
|
A5IEA1
|
AROC_LEGPC
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Legionella
|
MSGNTFGALFTVTTFGESHGPAIGCVVDGCPPGMSLTEADIQPFLDKRKPGQSKYTTQRREEDKVQILSGVFDGKTTGAPIALLIQNTDQRSRDYEDIKNLFRPGHADFTYHYKYGHRDYRGGGRSSARETAARVAAGAIARLYLKRYLNLDIIGYLQQMGDLKLQFENENEINKNPFFCPNNKQIQELADYVDRLRRQGDSVGARVKILARGVPTGLGDPVFDKLDATLAYAMMSINAVKGVEIGAGFNAVEQLGSHHRDQMTAKGFLSNHAGGILGGIATGQPIEVSIALKPTSSITTPGQTINTEGEEVTVVTKGRHDPCVGIRAVPIAEAMMALVLMDHYLRHKAQCK
|
Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
|
A5IEA1
|
Q01882
|
RAG2_ORYSJ
|
Seed allergenic protein RA14
|
Oryza sativa
|
MASNKVVFSALLLIIVSVLAATATMADHHKDQVVYSLGERCQPGMGYPMYSLPRCRAVVKRQCVGHGAPGGAVDEQLRQDCCRQLAAVDDSWCRCSALNHMVGGIYRELGATDVGHPMAEVFPGCRRGDLERAAASLPAFCNVDIPNGTGGVCYWLGYPRTPRTGH
|
Seed storage protein.
|
Q01882
|
Q9SCX9
|
GPDA1_ARATH
|
Glycerol-3-phosphate dehydrogenase [NAD(+)] 1, chloroplastic
|
Arabidopsis
|
MRFRSFFFSSSIFSLSHSRSPSLSSSRFSSLSAAMSPALEKSRQGNGGCNDDSKSKVTVVGSGNWGSVAAKLIASNALKLPSFHDEVRMWVFEEVLPNGEKLNDVINKTNENVKYLPGIKLGRNVVADPDLENAVKDANMLVFVTPHQFMDGICKKLDGKITGDVEAISLVKGMEVKKEGPCMISSLISKQLGINCCVLMGANIANEIAVEKFSEATVGYRGSREIADTWVQLFSTPYFMVTPVHDVEGVELCGTLKNVVAIAAGFVDGLEMGNNTKAAIMRIGLREMKALSKLLFPSVKDSTFFESCGVADVITTCLGGRNRRVAEAFAKSRGKRSFDELEAEMLQGQKLQGVSTAREVYEVLKHCGWLEMFPLFSTVHQICTGRLQPEAIVQYRENKL
|
Involved in glycerolipid metabolism.
|
Q9SCX9
|
B0KA56
|
YBEY_THEP3
|
Endoribonuclease YbeY
|
Thermoanaerobacter
|
MNILIDNRQDKVDAINLEELVEKVIKTVLEVEEVIDNVEVSVSFVDNEEIRKLNKYYRGIDKPTDVLSFPLAEFEDTYGEVEEIEEDSEEVQPIGDIVISLEKALEQSMEYGHSFEREVAYLTAHSMLHLLGYDHETEEERKIMREKEEEVMARLNIGR
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
B0KA56
|
B0K682
|
HPRK_THEPX
|
HPr(Ser) kinase/phosphorylase
|
unclassified Thermoanaerobacter
|
MDKIPVETLIKDLNLEVIVEAKNNKIDITTSDVNRPGLQFSGFYEHFAYERVQIIGKVETTFIEQLPDDVLAERADRFFNYPIPCLIVTRDLNIRQEIIDAAQKHDRYLLRTKEASTKFINRLINYLDEKLAPQITIHGDLVDVYGIGVLLLGESGIGKSETALELIKRGHRLVADDAVEISKISEDKLQGSSPEIIRHFIEIRGIGILDIKTLYGVGSVRNSMNIDLVIQLEEWDEDKYYDRLGLEDDYIKFLDVKVPKLTIPVRPGRNLAIIVEVAAMNHRQKQMGYNAAHELNKKLLKQIGN
|
Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of a specific serine residue in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Therefore, by controlling the phosphorylation state of HPr, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
|
B0K682
|
Q254T8
|
GUAA_CHLFF
|
Glutamine amidotransferase
|
Chlamydia
|
MSKILILDFGSQYTNVLAKKIRLLSVFCEVLPWNTPLEDILQESPSGLIFSGGPHSVYQENSPKVDREIYNANIPILGVCYGMQLIARDFGSEVRGGENEFGYTPIVFYPGKLFQGLVDKDAFHTEIRMSHCDSVTVPPKDFFITASSQHCPVAAIEYPEKKLFGLQFHPEVSDSQGIGDTILSNFVKHICRASETWKIETIEKQLIQRIKEQVGEKERVLLGLSGGVDSSVLAVLLHNALGDRLSCVFVDTGLLRKNEVEEVKQQFLSLGLEIIVEDASETFFYELSGIQDPEQKRKIIGSTFIEVFDKVSKNLEVQWLAQGTIYSDVIESAKSCDATQVIKSHHNVGGLPEKLNLKLLEPLRFLFKDEVRALGKVLGLPEVFISRHPFPGPGLGVRVLGEIRKEYVEIVKHADSIFIEELKKANLYDKVSQAFAVFLPVKSVAVKGDCRHYGYTIALRAVESSDFMTACWSPLSREFLNRCSSRIINEIPEVSRVVYDISDKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
Q254T8
|
P0C1B1
|
CBK1_EMENI
|
Serine/threonine-protein kinase cbk1
|
Aspergillus subgen. Nidulantes
|
MSEDQGQQGQRLSTARGSTCLKQTMTEPALSAGLGTDGPVGAAKDNIRVRIQSRRRSRLLSRLGRKIPTQGRFTVGWYFWFLLIYTSLAVEPVKSHETHSHSSDAEGTSHQDVSDRRNHPCHTPRPSSHSQADSFESVARGQQKEQSRTMREDAVSPVLLDVKRSQSTPVELAKLVSLKLSTSFGSRTVIRRSQPGVRQSVRAAQLQRMMLDRGNPKRERSSGSSTPSSKSSPVDSVSTAPTSVSPGSLAPSGSTNNDPASGFKHIDSQADLPERPLSPVRESPMVSPTIQTTEATAIVKVFLETHFHTLLSGLDARTQRRLELDQYIETFPLSPEEVVRVRKHWVTQERDYLRQYRVLKSRPQDKTSRAGTASLAGFEPLKILGRGSFGVVRLVREKRTDEQTQSGRVPLAPKTNHRQAMTGVKKDVFAMKVIRKSVMIRNCQEAHLRAERDFLVASAKSRWVVPLIASFQDQKHLYLVMDYMVGGDFLGLLIRHNILRESIARWYVAEMILCIEEAHRLRCIHRDVKPDNFLISESGHLKISDFGLAFDGHWAHDQWYFTYQRHSLLKRLGIQIDGDAEDQKLSHDANIQSLGTTREDGSMEDDWIHPPTNGLLHWRDKNQTRTMARSVVGTSQYMAPEVIRGHPYDGRCDWWSLGVILYECLYGFTPFASEDRHQTKLKIHRHLQTLYFPVHRPTDKLVSADAIDVINSLLQEKEFRLSSPKYKQNDAISSKPAKCSFYKPDSSNPSYQGHYVYPDDATDIKSHRFFRGINWEQIHRTSPPFIPMVRGWEDTRYFDDGEHPSDREDDSSDSELDGVQDKWHPLGGKGGLHKPDKPLKADVKPSSYPKGNDGAKDTAIASLKHKKRLKEAKRARDKILRDKRLRRTVLEMLRCLVVVAAT
|
Protein kinase that seems to play a role in the regulation of cell morphogenesis and proliferation.
|
P0C1B1
|
Q6ME71
|
FMT_PARUW
|
Methionyl-tRNA formyltransferase
|
Candidatus Protochlamydia
|
MRNRKMKVIFFGTPLFAAQVLEFLLQNQVEVVAVISKPDRPKGRSSIPVPTPVKLIAQSYHLPLYQPEVVSSLDFAPVLKNYEADLFVVVAYGEIIKQHLLDMPKRACINLHASLLPKYRGAAPIQRSIIEGEKETGVTIMHMVKKMDAGDMIKKVSVQITSEMTYGELEQALCQIGKHALLEVIKQFDRGEPSRQIQDSHLATFAPKIELEDCELDWNQSAQHLHDLVRGVNPYPGAWCYVKVNGEQKRLKISRTRVIPYPSNCPGTILDSSKGNLKILTGDQALELVEVQLEGKKTMTSEQWIRGMSKNQLKFLVN
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
Q6ME71
|
Q6EVZ5
|
NU1C_NYMAL
|
NADH-plastoquinone oxidoreductase subunit 1
|
Nymphaea
|
MIIEEAQAINSFFRSESSKEVYGLIWLLVPILTLVLGITIGVLVIVWLERKISAGIQRRIGPEYAGPLGILQALADGVKLLFKEDLLPSRGDIRLFSVGPSVAVVSILLSYSVIPFGYHLVLTDLSIGVFLWIAISSIAPIGLLMSGYGSNNKYSFSGGLRAAAQSISYEIPLTPCVLSISLLSNSSSTVDIVEAQSKYGFWGWNLWRQPIGFLVFIISSLAECERLPFDLPEAEEELVAGYQTEYSGIKFGLFYVASYLNLLVSSLFVTVLYLGGWNLPIPYIPITELFEINKTSEVFGTTISLLITLAKAYLFLFIPISTRWTLPRLRMDQLLNLGWKSLLPIALGNLLLTTSSQLVSL
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q6EVZ5
|
Q8MTX2
|
NDB42_OPIMA
|
Cytotoxic linear peptide IsCT2f
|
Opisthacanthus
|
MKTQFAILLVALVLFQMFAQSEAIFGAIWNGIKSLFGRRALNNDLDLDGLDELFDGEISQADVDFLKELMR
|
IsCT2f shows neither hemolytic, nor antibacterial activities, surely due to the fact that it cannot apply amphipathic alpha-helical structure.
|
Q8MTX2
|
Q08H50
|
NU4LM_PHOFA
|
NADH dehydrogenase subunit 4L
|
Phoca
|
MSMVYANIFLAFIMSLMGLLMYRSHLMSSLLCLEGMMLSLFVMMTVTILNNHFTLANMAPIILLVFAACEAALGLSLLVMVSNTYGTDYVQNLNLLQC
|
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.
|
Q08H50
|
P60973
|
LGT_RHOPA
|
Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
|
Rhodopseudomonas
|
MPFFAVAFPVFDPVAVAIGPFAIRWYALAYIAGIVIGWLYARMLLQRQRLWGGPSPISLEAFDDFILWVTIGIILGGRTGYVLFYNLDFFIRHPAEIFELWKGGMSFHGGFMGCVAAVVLFGWKRKVPILSLGDITCAVGPIGLFLGRIANFINGELWGRPADASVPWAMVFPNAGPLPRHPSQLYEAGLEGIGLFVILALMIRAGALKRPGLIIGAFLTFYGLARITGEFFREPDPQLGFLWGDMTMGMLLSIPMVIVGILVMITTWRRGRGAPAAATPSSEAAS
|
Catalyzes the transfer of the diacylglyceryl group from phosphatidylglycerol to the sulfhydryl group of the N-terminal cysteine of a prolipoprotein, the first step in the formation of mature lipoproteins.
|
P60973
|
Q2NAK3
|
RSMI_ERYLH
|
rRNA (cytidine-2'-O-)-methyltransferase RsmI
|
Erythrobacter
|
MQHDHSAEPLSPGLYIVATPIGNLGDITLRAIETLRRCDAVACEDTRMTGKLLKHLGISKSLWRYDDHSDAKAREKIVAAISEKAVALVSDAGTPLISDPGYRLVRDARDASLPVTTIPGACAAIAGLTLSGLPSDRFLFAGFLPVKDKARREMLEKLAPVDASLIFYETGPRLLKSLAAIDEMLPNREISVARELTKLHEECRRGMGAGLMAHYQANPPKGEIVLMVGPPPEAAPDDTDAELMLREALETMKPSQAAGHVAKATGLDRKDLYSRALELKT
|
Catalyzes the 2'-O-methylation of the ribose of cytidine 1402 (C1402) in 16S rRNA.
|
Q2NAK3
|
Q9D291
|
DESI2_MOUSE
|
Protein FAM152A
|
Mus
|
MGANQLVVLNVYDMYWMNEYTSSIGIGVFHSGIEVYGREFAYGGHPYPFSGIFEISPGNASELGETFKFKEAVVLGSTDFLEDDIEKIVEELGKEYKGNAYHLMHKNCNHFSSALSEILCGKEIPRWINRLAYFSSCIPFLQSCLPKEWLTPAALQSSVSQELQDELEEAEDAAASSAMASAAAGARTGRHTKL
|
Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked polyubiquitination of RPS7 leading to its stabilization.
|
Q9D291
|
Q2QQ99
|
SP1L3_ORYSJ
|
Protein SPIRAL1-like 3
|
Oryza sativa
|
MGRGVSSGGGQSSLGYLFGGGEAPKSAEKPAPVQKPAPSSSAEKLKEIPAGIQSSKANNYMRAEGQNCGNFLTDRPSTKVQAAPGGGSSLDYLFSGNKDGK
|
Acts in maintaining the cortical microtubules organization essential for anisotropic cell growth.
|
Q2QQ99
|
Q493C8
|
DXR_BLOPB
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Candidatus Blochmannia
|
MQSLTILGSTGSIGKATLSVIQQHTDKFFVHALVAKNNVAIMTEQCIAMSPKYACMISEDAARILKKNLITAGKYDIEVLSGVMHACELASTNDVDMVMSAIVGIAGLKPTFSALRAGKKILLANKETLVTGGKLFMKEANRYRACILPIDSEHNAIFQNLPEICQKSLGNTSLSECGISRIVLTASGGIFFKTPQKQLTKITPEQACVHPNWSMGRKISVDSATMMNKGLEYIEARHLFNAKPSEIEILLHPQSIVHAMVYYSDGNVLAHLAPPDMRIPIAYAMAYPKRIGLKISSNIDIYYLNKLHFDQLDNCSYPCFQLAIDADNCSQSATIILNAANEIAVEAFLRKMISFTDIPDVIRRVLDAINLNDPNDIEDILYIDQKAREKAISICVI
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q493C8
|
Q2IWG4
|
TATB_RHOP2
|
Sec-independent protein translocase protein TatB
|
Rhodopseudomonas
|
MFDIGWSELVVIGVVALVAIGPKELPGVLRMVGQWMGKARKLASEFQGQFQEAMREAEMADLKKSFDEVKEATAGLSTNNMLTKLGSELSEAAAIDKSALDSPPVEPTTPAPPTPETFIEATTHQAVTGEPLAIVSEAQAAGAHTTLPVPAETHALATTDLAPPDLAHPAPAHPEPTNSEPAKDAKAS
|
Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation.
|
Q2IWG4
|
B2WMJ3
|
MKAR_PYRTR
|
Microsomal beta-keto-reductase
|
Pyrenophora
|
MANILEPFGIRIDADNSFVQAAVTGFLLVGIASFAAPLISTIRVLLSLFVLPGKSLTTFGPRGTWALITGASDGIGKEFALSLAAKGYNLILVSRTQSKLDSLSADITSKYGPKIAVKTLAMDFALNKDADYNNMKKLIEGLDVSILINNVGLSHSIPVPFTETPKQEMTDIIMINCMATLRVTQLVTPGMVSRKRGLVLTMASFGGFFPTPLLATYSGSKAFLQQWSTALASELEPHGVYVQCVQSHLVTTAMSKIRKTSALVPNPKQFVDATLSKIGRSGGAQGVAFTSTPYWSHGLMHWFLSRFLGERSETVVKVNRGMHENIRRRALRKAERDAKKQ
|
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
|
B2WMJ3
|
P0DPT4
|
KAX47_TITST
|
T.sigmurus alpha-KTx
|
Tityus
|
MKAFYGILIIFILISMLDLSQQVFINAKCRGSPECLPKCKEAIGKAAGKCMNGKCKCYP
|
Potently blocks Kv1.1/KCNA1 (85%), Kv1.2/KCNA2 (91%), Kv1.3/KCNA3 (89%), Kv1.6/KCNA6 (94%), and Shaker (97%).
|
P0DPT4
|
B9WEC5
|
RSSA_CANDC
|
40S ribosomal protein S0
|
Candida
|
MSLPASFDLTPEDAKLLLAANVHLGAKNVQVHNKPYVYKTRPDGMNIINIGKTWEKIVLAARIIAAVPNASDVAVCSSRTFGQRAVLKFAAHTGATAIAGRFTPGNFTNYITRSFKEPRLVIVTDPRTDAQAIKESSYVNIPVIALTDMDSPSEYVDVAIPCNNKGKHSIGLIWWLIAREVLRLRGIIPDRTTEWSVMPDLYFYRDPEEVEQNAAEEAKTEEVEEAPVAEAETEWTGETEDVDWADSGATPAAEDAAASNW
|
Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
|
B9WEC5
|
Q9EP95
|
RETNA_MOUSE
|
RELMalpha
|
Mus
|
MKTTTCSLLICISLLQLMVPVNTDETIEIIVENKVKELLANPANYPSTVTKTLSCTSVKTMNRWASCPAGMTATGCACGFACGSWEIQSGDTCNCLCLLVDWTTARCCQLS
|
Probable hormone. Plays a role in pulmonary vascular remodeling.
|
Q9EP95
|
C3P3V9
|
SELO_BACAA
|
Protein adenylyltransferase SelO
|
Bacillus cereus group
|
MTKNNEAGWNLDHSYTTLPQSFYTEIPPTPVSSPELVKLNHSLAISLGFNPEELKKEAEIAIFAGNALPEGAHPLAQAYAGHQFGHFNMLGDGRALLIGEQMTPSGKRFDIQLKGSGPTPYSRRGDGRAALGPMLREYIISEAMYALDIPTTRSLAVVTTGEPTYRETKLPGAILTRVASSHIRVGTFQYAAARGSIEDLQSLADYTIKRHYPEIEAHENRYTALLQEVIKKQASLIAKWQLVGFIHGVMNTDNITISGETIDYGPCAFMDNYDQGTVFSSIDTQGRYAYGNQPYMAAWDLARLAESLIPILHEDEEEVLKIAQDEISKFSVQYEKQWFLGMKKKLGLFSNEEQDQSLIEQLLKMMEKFKADYTNTFRSLTLNTIENTALFESPEFKEWYKLWQSRLERQEESKENAYEMMKNNNPSIIPRNHRVEEALEAAVTNGDYSVMEKLLEALSNPYAYATEQEEYCVPPVPTNRPYRTFCGT
|
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
|
C3P3V9
|
Q4UUM0
|
DER_XANC8
|
GTP-binding protein EngA
|
Xanthomonas
|
MLPLVALVGRPNVGKSTIFNALTRTRDALVHDQPGVTRDRNYGVCRLDEQQPFIVVDTGGIAGDEEGLAGATARQARAAAGEADLVLFVVDGREGASSLDDEILAWLRKLARPTVLVINKIDGTDEESVRSEFSRYGFSDVVALSAAHRQGIDDLLEEVGARLPEEGAGELLDNDPARVRIAFVGRPNVGKSTLVNRLLGEERMIASEVPGTTRDSIAVDLERDGRQYRLIDTAGLRRRGKVEEAVEKFSAFKTLQAIEQCQVAVLMLDATEGVTDQDATILGAILDAGRALVVAINKWDGQSDYQRAQAEDLLSRKLGFVNWAEAVRISALHGSGMRELFQAIHRAHASATHEFSTSEVNQALEIAYETNPPPSIRGHVSKLRYVHPGGANPPTFIVHGTRLKVLPESYKRYLENFFRKRFKLVGTPVRFIFREGANPYEGKKNPLSDRQIARKRRLMRHVKGK
|
GTPase that plays an essential role in the late steps of ribosome biogenesis.
|
Q4UUM0
|
B2HDI5
|
ENO_MYCMM
|
2-phosphoglycerate dehydratase
|
Mycobacterium
|
MPIIEQVGAREILDSRGNPTVEVEVALIDGTFARAAVPSGASTGEHEAVELRDGGDRYGGKGVKKAVEAVLDEIGPAVIGLNADDQRLVDQALVDLDGTPDKSRLGGNSILGVSLAVAKAASESAELPLFRYIGGPNAHILPVPMMNILNGGAHADTGVDIQEFMVAPIGAPSFSEALRWGAEVYHALKAVLKKAGLSTGLGDEGGFAPDVASTTAALDLISQAIEAAGFKPGVDVALALDAAANEFHADGSYTFEGTPRTAAQMTEFYAGLLGSYPLVSIEDPLYENDWDGWAALTAEIGDRVQIVGDDVFVTNPERLEEGIDRGVANALLVKVNQIGTLTETLDAVALAHHSGYRTMISHRSGETEDTIIADLAVAVGSGQIKTGAPARSERVAKYNQLLRIEEALGDAARYAGDLAFPRFVADPK
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
B2HDI5
|
Q7NQF9
|
RL16_CHRVO
|
50S ribosomal protein L16
|
Chromobacterium
|
MLQPTRLKYRKQHKGRNTGIATRGNKVSFGDFGLKAIGRGRLTARQIEAARRAMTRHIKRGGRIWIRIFPDKPITSKPAEVRMGGGKGSPEYYVAEIQPGKMLYEMDGVSEELAREAFRLAAAKLPIATVFVTKQVGQ
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q7NQF9
|
P59463
|
CYAY_BUCBP
|
Iron-sulfur cluster assembly protein CyaY
|
Buchnera
|
MKKNNSNPLKINEYHTLVNKLFLLIEENIDKNQEKCDIDCELHHNMLIINLNNTNQVIINKQESLKQIWLATKKNGYHFEYINKQWICNRTKKDFWNVLQESCVYQTNKCIQFLKNIY
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
P59463
|
Q5HKB0
|
COPB_STAEQ
|
Probable copper-transporting P-type ATPase B
|
Staphylococcus
|
MNHSNQMHHDNHESHNHHSGHAHHHGNFKVKFFVSLIFAIPIILLSPLMGVNLPFQFTFPGSEWVVLILSTILFFYGGKPFLSGGKDEIATKKPGMMTLVALGISVAYIYSLYAFYMNNFSSATGHTMDFFWELATLILIMLLGHWIEMNAVGNAGDALKKMAELLPNSAIKVMDNGQREEVKISDIMTDDIVEVKAGESIPTDGIIVQGQTSIDESLVTGESKKVQKNQNDNVIGGSINGSGTIQVKVTAVGEDGYLSQVMGLVNQAQNDKSSAELLSDKVAGYLFYFAVSVGVISFIVWMLIQNDVDFALERLVTVLVIACPHALGLAIPLVTARSTSIGAHNGLIIKNRESVEIAQHIDYVMMDKTGTLTEGNFSVNHYESFKNDLSNDTILSLFASLESQSNHPLAISIVDFAKSKNVSFTNPQDVNNIPGVGLEGLIHNKTYKITNVSYLDQHGFEYDNDLFIKLAQQGNSISYLIEDQQVIGMIAQGDQIKESSKQMVADLLSRNITPVMLTGDNNEVAHAVAKELGISDVHAQLMPEDKESIIKDYQSNGNKVMMVGDGINDAPSLIRADIGIAIGAGTDVAVDSGDIILVKSNPSDIIHFLTLSNNTMRKMVQNLWWGAGYNIVAVPLAAGILAFIGLILSPAIGAILMSLSTVIVAINAFTLKLK
|
Involved in copper transport.
|
Q5HKB0
|
Q0ID14
|
RS17_SYNS3
|
30S ribosomal protein S17
|
unclassified Synechococcus
|
MALKERVGTVVSDKMDKTVVVAVENRFPHPIYQKTVSRTTRYKAHDEDNACRVGDRVRITETRPLSRHKRWAIAEVLSQSPKAEEVTK
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
Q0ID14
|
B0F2B4
|
NLGN4_MOUSE
|
Neuroligin-4
|
Mus
|
MPAPVPALLCLALALASAQPSPPPPPPFPVVATNYGKLRGVRAALPGDVLGPVTQFLGVPYAAPPTGERRFQPPEPPSSWAGVRDATRFAPVCPQHLDERALLRDCLPAWFAANLDAIAAYVQDQSEDCLYLNLYVPGGANGKKMADDVTGNDHGDDQDSRDPGVGGAAAAAARKPVMVYIHGGSYMEGTANIVDGSVLASYGDVIVVTVNYRLGVLGFLSTGDQAAKGNYGLLDQIQALRWVEENAGAFGGDPDRVTVFGSGAGASCVSLLTLSHYSEGLFQKAIIQSGTALSSWAVNYQPARYARALGERVGCATPDPGSPPGSPPGWDSASLVSCLRGKAAGELARARVTPATYHVAFGPTVDGDVIPDDPQILMEQGEFLNYDIMLGVNQGEGARFVDGLGGGHDGGYGGYGGGYGGGVEDDEVQDGGPDGAAGGVSAGEFDLAVSGFINDLYGRPEGRGDALRETVKFMYTDWADRDSPEARRKTLVALFTDHQWVAPAVATADLHARYGSPTYFYAFYHRCHGGGGGGGGVDGVAGGVAGGVGGEEARPAWADAAHGDEVPYVFGVHMAGPGDVFGCNFSRNDVMLSAVVMTYWTNFAKTGDPNQPVAQDTRFVHTRPNRFEEVAWAKYDPRGQLYLHIGLRPRVRDHYRAAKVAFWLELVPHLHGLAADPGAYLSAAATRAAPSGDPDRDPGGGGGGRRRPRPATRRPAVMTSSSMASGSGMTSSSGSGMTSSSGSSASAVLIETRRDYSTELSVTIAVGASLLFLNVLAFAALYYKKDKRRHETHRRPPPPRPPQAPPSAAAADRNPRPDPGPAGRRGGECGAVVTAMAAEASAGGLGHDGVGGVGVGGVIGGVAGLRLACPPDYALTLRRSPDDVPRAGAGPGTMTLIPGALGGGGGGAVHGFNTFGSGVGVAGVAGVATSQAGPGLPHGHSTTRV
|
Cell surface protein involved in cell-cell-interactions. Plays a role in the formation or maintenance of synaptic junctions via its interactions (via the extracellular domains) with neurexin family members. Plays a role in synaptic signal transmission.
|
B0F2B4
|
Q5YQ76
|
GLYA_NOCFA
|
Serine hydroxymethyltransferase
|
Nocardia
|
MTQTTASVNTQSLGELDPELAAAMAGELARERDTLEMIASENFVPRAVLQAQGSVLTNKYAEGYPGRRYYGGCENVDVVENLARERAKELFGAEFANVQPHSGAQANAAVLMSLMDPGDRLLGLDLAHGGHLTHGMRLNFSGKLYEVHSYGVSKEDHRVDMDEVRTIALGAKPKVIVAGWSAYPRHQDFAAFRAIADEVGAYLWVDMAHFAGLVAAGLHPSPVPYADVVSSTVHKTLGGPRSGLILAKQEFAKKINSAVFPGQQGGPLMHAIAAKAVAFKIAGTEEFRDRQQRTLSGAKILAERLTGADVADKGISVLTGGTDVHLVLVDLRNSQLDGQQGEDLLHEIGITVNRNAVPFDPRPPMVTSGLRIGTAALATRGFGDAEFTEVADIIATALAGGSDAETLRGRVRALAQRVPLYQGLEDWHLLG
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
Q5YQ76
|
Q9ZMA9
|
ILVC_HELPJ
|
Ketol-acid reductoisomerase type I
|
Helicobacter
|
MALPVYYDKDIDLGVIQSLQVGIIGYGVQGEAQALNLRDSKVKVRIGLYQGSLSVSKAKKEGFEVLGVKELVQQSDVIMALLPDELHKEVLEKEVIPFLKEGQIIGFAHGFSVHFNQVVLPKGVGAILVAPKGPGSALREEYLKNRGLYHLIAIEQESSIHNAKAVALSYAKAMGGGRMGVLETSFKEECESDLFGEQAVLCGGLEAIVRMGFETLIKAGYPEELAYFECVHEVKLVADLLHYKGVEGLRKHISNTAEFGAIKAREPMGNLLEKRMQKILKKIQNGAFAKDFLLEKSLNYPRLNTERKALKETKIEQIGEILRAPFNHKK
|
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.
|
Q9ZMA9
|
P46914
|
COTS_BACSU
|
Coat protein 40 kDa component 2
|
Bacillus
|
MYQKEHEEQIVSEILSYYPFHIDHVALKSNKSGRKIWEVETDHGPKLLKEAQMKPERMLFITQAHAHLQEKGLPIAPIHQTKNGGSCLGTDQVSYSLYDKVTGKEMIYYDAEQMKKVMSFAGHFHHASKGYVCTDESKKRSRLGKWHKLYRWKLQELEGNMQIAASYPDDVFSQTFLKHADKMLARGKEALRALDDSEYETWTKETLEHGGFCFQDFTLARLTEIEGEPFLKELHSITYDLPSRDLRILLNKVMVKLSVWDTDFMVALLAAYDAVYPLTEKQYEVLWIDLAFPHLFCAIGHKYYLKQKKTWSDEKYNWALQNMISVEESKDSFLDKLPELYKKIKAYREAN
|
Seems to be required for the assembly of the CotSA protein in spores.
|
P46914
|
B0U7Z5
|
TRPD_METS4
|
Anthranilate phosphoribosyltransferase
|
Methylobacterium
|
MDSFKPYLAKVATGAALTREEARTAFDHLLSGEVTHAQAGAFLMALRVRGEAQDEIVGAAGALRERMVRVVAPAGAIDIVGTGGDHSGSYNVSTLASILTAACGVPVAKHGNRAASSRSGAADVLAALGVRLGLDPEGLARCLEEAGLCFMFAQAHHASMRHVAPVRVELGTRTLFNLLGPLCNPAGVAGQLLGVYAGSLAEPLTRVLADLGSRRVWTVHGSDGLDEITTTGPTAVVALEDGAIRHFTIDPREVGLALASPEDLRGADPEHNAAALRAVLDGARTPYRDIAVLNAGAALVVAGACAGLGEGVARAAQAIETGAARAVLARLVAVSNA
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
B0U7Z5
|
C0HLV9
|
MP31_MOUSE
|
Micropeptide 31
|
Mus
|
MWRDSLCTAAGYALGRRDAAALSSLLSEAAAMMEV
|
Inhibits lactate dehydrogenase (LDH)-mediated conversion of lactate to pyruvate in mitochondria by competing with mitochondrial LDH for binding to NAD(+). Also inhibits cellular lactate utilization.
|
C0HLV9
|
A4TE84
|
RNH2_MYCGI
|
Ribonuclease HII
|
Mycolicibacterium
|
MPAVWPPRTVIRKSSGLRTLESALYRAGLGPVAGVDEVGRGACAGPLVVAACILGPNRLESLSALDDSKKLNESERERLFPLIRRYAVAFHVVFIPSVEVDRRGVHVANIEGMRRAVAGLAVRPGYVLSDGFRVPGLPMPSLPVVGGDAAAACIAAASVLAKVSRDRLMVAMDQEHPGYGFADHKGYSTRAHSAALNDLGPSTQHRFSFINVRRLVVDGEPGQGGELECGKLAVDVPVDMPVDRVLREGQLSR
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
A4TE84
|
A9KQ75
|
GAHP1_LACP7
|
D-galactosyl-1,4-L-rhamnose phosphorylase
|
Lachnospiraceae
|
MSEKLTGRVTVPTDVDMIQETKEIAERWGADALRDCDGTDMPDELKKMPAKIYSTYYTTRKDNAWANANPDEVQQVYLMTEFYTAMSQGELRIPLMKHLYKDQLKPNTIHDIKRWWEVVDRTTGEPLVLDAWEYDENNQEVIILNPDHFHDYTVSFLAFIIWDPVHMYNFITNDWQDVEHQITYDVRQPKTQKYVIEKLKRWMKENPDSDVVRFTTFFHQFTLVFNEFAKEKFVDWFGYSASVSPYILEQFEKEVGYKFRPEYIIDQGYHNNTNRVPSKEFRDFQEFQQREVAKLMKVLVDICHDNDKEAMMFLGDHWIGTEPFGEYFKHVGLDAVVGSVGNGTTLRLISDIPGVKYTEGRFLPYFFPDVFHEGGDPIKEAKVNWVTARRAILRKPVDRIGYGGYLKLALDFPEFIQYIEEVCDEFRLLYDNMGGQSPYSHFKVGVLNSWGKIRSWGTHMVAHAIDYKQTYSYAGVLEALSGMPFDVEFISFEDVIKNPVILNECGVVINVGDAYTGPSGGAYWTNEKVSSAVKAFVAQGGGFIGVGEPSACEHQGRYFTLANVLGVNKEIGFSMSTDKYNWDEHSHFITEDSNESINFGEGMKNIYALDGAQILRKDGQDVQMAVNQFGDGRSVYISGIPYSFENSRMLYRAIFWAAGMEQEMKKWYSSNYNVEVNYYPATKKYCIVNNTYEPQETMIYDGLGREYSMKLKANDILWFTFLED
|
Reversibly phosphorolyzes beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine to form alpha-D-galactopyranose 1-phosphate and acetyl-D-glucosamine. Active towards galacto-N-biose and lacto-N-biose. Does not phosphorolyze galacto-N-tetraose or lacto-N-tetraose. In the reverse reaction has activity toward N-acetyl-D-glucosamine and N-acetyl-D-galactosamine, but not L-rhamnose, D-glucose or D-galactose.
|
A9KQ75
|
A9KU74
|
RECF_SHEB9
|
DNA replication and repair protein RecF
|
Shewanella
|
MSLTRLNIEAFRNIQSAQLIPAPGINLIYGQNGSGKTSILEAIYFLGMGRSFRSHLSQRVINNDDDKLTLFATLNLARGDSKIGLRRFRSGETEVRIDGEKVKRLSTLAETLPIQVITPESFSLLFEGPKSRRQFIDWGAFHADPQFYGAWTNVRRVLKQRNQLLRNGSAYSNIQFWDQEFVRYAEQVTEIRNHYVDSLNELLKGIIGEFLPSVDVKVSFTRGWDSKTDFAELLENQYSRDLATGHTVSGPHKADLRLRVGTLPAQDALSRGQLKLLVCALRIAQGKLLKQQIDKHSIYLVDDLPSELDAQHRQLLLKQLTDTGAQVFVTAIDPAAIVDSLHTPPSRMFHVEQGRVTVIE
|
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.
|
A9KU74
|
P00847
|
ATP6_BOVIN
|
F-ATPase protein 6
|
Bos
|
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSIHNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT
|
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.
|
P00847
|
P83658
|
DIDS_ECHCA
|
Disintegrin schistatin
|
Echis
|
NSVHPCCDPVICEPREGEHCISGPCCENCYFLNSGTICKRARGDGNQDYCTGITPDCPRNRYNV
|
May bind to both alpha-IIb/beta-3 (ITGA2B/ITGB3) and alpha-V/beta-3 (ITGAV/ITGB3) integrins, and may inhibit platelet aggregation.
|
P83658
|
B1P1G1
|
JZ38D_CHIGU
|
Peptide F4-25.19
|
Chilobrachys
|
MKVSVLITLAVLGVMFLLTSAEERGSDQMDSPAWLKSMEIIFQSEERECRWLFGGCEKDSDCCEHLGCRRAKPSWCGWDFTVGKWEMLINMNIFRIVFSYSMCTV
|
Probable ion channel inhibitor.
|
B1P1G1
|
Q8DI68
|
ACSF2_THEVB
|
Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2
|
Thermosynechococcus
|
MVAIAPNPHSGQSVKTIRENLLTPRFYTTDFEQAAKLDLSRQQEQLEAMLAEMRADYNRHHFVRDDSFKGTWDLLDAQTRKAFIDYLERSCVSEFSGFLLFKELSRKLKDRNPLLAEIFHLMARDEARHAGFLNKAMMDFGHAMDLGYLSKTRTYTFFPLPWVLYTVYLSEKIGYWRYIIIYRHLEKHPEHSFYPLFNYFERWCQDENRHGDIFKALIHSQPQLIQGWGAKLWMRFFLLTVFATHTLTVHERAKFYEALGLDATAFDREVIAKTNETAARTFSVVLNVDHPEFYSRLQRCVEISNKLQAIEATHQPKWLKALRKLPHQLAIAGHLLRIYLLPPVNAQQEWGTVH
|
Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME).
|
Q8DI68
|
E7CLN1
|
SCX4_RHOJU
|
Putative beta-neurotoxin RjAa4
|
Rhopalurus
|
KEGYPMGRDGCKISCVINNNFCKVECQAKWRQSDGYCYFWGLSCYCTNLPDDAQVWDSSTNKCGG
|
Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
|
E7CLN1
|
Q6G3K0
|
YIDD_BARHE
|
Putative membrane protein insertion efficiency factor
|
Bartonella
|
MFNPYPQKKKRQTRNYTGPWRKTPGRLLGLLLIRFYQITLSGFIGNQCRHLPTCSEYTYEAIARHGLWAGAWMGFFRIIRCGPFGTHGFEPVPTSLGNSYCFYKPWCYWKISTKHNK
|
Could be involved in insertion of integral membrane proteins into the membrane.
|
Q6G3K0
|
Q6MS94
|
ATPB_MYCMS
|
F-ATPase subunit beta
|
Mycoplasma
|
MVSKNTTDKKKNQSIGKVIQVLGSVVDVKFSENSIPKIYDALIVDNNGKKLVLEVEQNIGDEIVRTIAMGPTEGLKRGLDVINTNSPITAPTGMEVLGRMFNVLGDPIDEKPDLDVKREPIHKDAPKYEELVTTTEILETGIKVIDLMIPFTKGGKVGLFGGAGVGKTILIQELINNIAKAHNGVSVFAGVGERTREGNDLYHEFIEAGVLNKTCLVFGQMNEPPGARMRVALTGLTIAEYFRDQKNMDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKNGSITSVQAVYVPADDLTDPAPATTFTHLDARIVLDRSIASLGIYPAVDPLASSSRVLDPEIVGQEHYDIALRVQIALQKYQDLQSIIAILGMDELSEEDKLIVQRARKIRNFLSQSFFVGEKFTGRPGVFVKVNDTVRSFKSILDGEVDYIPETYFLYSSIIDDVIEKYNKDKDK
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q6MS94
|
A5D178
|
LSPA_PELTS
|
Signal peptidase II
|
Pelotomaculum
|
MFLFIIIAVVLLVDQATKAAVQMLMCQGESIPVVPPAFYLTYIMNPGAAFGLLPHKKMLFVTVTVIIIAGVLVGYFKIRPRKPVLDYGLGLVAGGALGNLADRLRYGLVVDFLDFRIWPVFNLADTAIVTGAFLLAWALLNDSDKSSKKERK
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
A5D178
|
Q8K9C4
|
DCDA_BUCAP
|
Diaminopimelate decarboxylase
|
Buchnera
|
MPELLNKTKTNLNFENIKILIKKFQSPFWVYDSNIIHKKINLLKEFDIVRFAQKACSNIHILRLMKQKNIKVDAVSLGEIERALVAGFKPNSNEIIFTADLFDEETLSKVIDFKIPVNAGSIDMLEQLGKLSPGHHVWLRINPGFGHGHSKKTNTGGENSKHGIWNPRLAIPIIKKYKLKLIGLHMHIGSGVNYKHLKKVGQAMIEKAMEINEKILFISAGGGLPIPYTFNEKPIDTKKYFIIWDEARKKISRFLNTPIQLEIEPGRFLVAESGILISQVRAIKKMGDKNFVLIDAGFNDLMRPTMYGSYHHVSVVTKDDRNIHETETIDTIIGGPLCESGDIFTQKEGGNITTRKLPILKIGDYLIFHDVGAYGASMSSNYNTRPLIQEILLENNTFRTIRRRQKINELLNLEK
|
Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
|
Q8K9C4
|
A6SM77
|
EIF3E_BOTFB
|
Eukaryotic translation initiation factor 3 subunit E
|
Botrytis
|
MADNTPTTANDLLNDATQAAAKSPEEIAKENDLLPKLITHLDRHLIFPLLQFVGDQDDEPSPEITKAKFELLKKTNMTDYVASLHCEIEGVDEAPKEYANKRQEILQRLEIFGQESEKITDLLGREDVVTGLRSDKVANLEFLKKEHDVTIEMVNVLYDFGNFQYSCGNYGAAAELLYQFRVLSTDDDKVTAATWGKLACEILTGNWESAMEEVQKVKESIETKLFNKPLAQLHHRTWLIHWALFPFFNHEPARDVICDLFFSPAFINTIQTACPWILRYLTAAVITNRNRTRNTGQYQKQLKDIIRIVKQENYEYSDPVTDFIKALYLDFDFEEAQKKLSEAEEVLRSDFFLVAASENFVEAARHLISESYCKIHQRIDIKDLSARLGLNQDDGEKWIVNLIRDTRVDAKIDYKEGTVVMNHPPSSVYQQVIERTKGGFFRTQVLSAAVAK
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
A6SM77
|
Q9LE38
|
NLP4_ARATH
|
Nodule inception protein-like protein 4
|
Arabidopsis
|
MEDSFLQSENVVMDADFMDGLLLDGCWLETTDGSEFLNIAPSTSSVSPFDPTSFMWSPTQDTSALCTSGVVSQMYGQDCVERSSLDEFQWNKRWWIGPGGGGSSVTERLVQAVEHIKDYTTARGSLIQLWVPVNRGGKRVLTTKEQPFSHDPLCQRLANYREISVNYHFSAEQDDSKALAGLPGRVFLGKLPEWTPDVRFFKSEEYPRVHHAQDCDVRGTLAIPVFEQGSKICLGVIEVVMTTEMVKLRPELESICRALQAVDLRSTELPIPPSLKGCDLSYKAALPEIRNLLRCACETHKLPLAQTWVSCQQQNKSGCRHNDENYIHCVSTIDDACYVGDPTVREFHEACSEHHLLKGQGVAGQAFLTNGPCFSSDVSNYKKSEYPLSHHANMYGLHGAVAIRLRCIHTGSADFVLEFFLPKDCDDLEEQRKMLNALSTIMAHVPRSLRTVTDKELEEESEVIEREEIVTPKIENASELHGNSPWNASLEEIQRSNNTSNPQNLGLVFDGGDKPNDGFGLKRGFDYTMDSNVNESSTFSSGGFSMMAEKKRTKADKTITLDVLRQYFAGSLKDAAKNIGVCPTTLKRICRQHGIQRWPSRKIKKVGHSLQKIQRVIDSVQGVSGPLPIGSFYANFPNLVSQSQEPSQQAKTTPPPPPPVQLAKSPVSSYSHSSNSSQCCSSETQLNSGATTDPPSTDVGGALKKTSSEIELQSSSLDETILTLSSLENIPQGTNLLSSQDDDFLRIKVSYGEEKIRLRMRNSRRLRDLLWEIGKRFSIEDMSRYDLKYLDEDNEWVLLTCDEDVEECVDVCRTTPSHTIKLLLQASSHHFPERSSATEYSLWH
|
Probable transcription factor.
|
Q9LE38
|
Q1H004
|
NRDR_METFK
|
Transcriptional repressor NrdR
|
Methylobacillus
|
MKCPFCGADDTQVIDSRVNEEGDSIRRRRRCNACDKRFTTYETAELHLPQVVKQNGKREEFNRDKLRLSFTRPLHKRPVPTEYVDRALEHIVQKILAKGEREIMARDLGEIVMQELKAIDKVAYIRFASVYRSFQDVDDFNDVIRDLD
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
Q1H004
|
P76393
|
YEGI_ECOLI
|
Protein kinase YegI
|
Escherichia
|
MKTNIKVFTSTGELTTLGRELGKGGEGAVYDIEEFVDSVAKIYHTPPPALKQDKLAFMAATADAQLLNYVAWPQATLHGGRGGKVIGFMMPKVSGKEPIHMIYSPAHRRQSYPHCAWDFLLYVARNIASSFATVHEHGHVVGDVNQNSFMVGRDSKVVLIDSDSFQINANGTLHLCEVGVSHFTPPELQTLPSFVGFERTENHDNFGLALLIFHVLFGGRHPYSGVPLISDAGNALETDITHFRYAYASDNQRRGLKPPPRSIPLSMLPSDVEAMFQQAFTESGVATGRPTAKAWVAALDSLRQQLKKCIVSAMHVYPAHLTDCPWCALDNQGVIYFIDLGEEVITTGGNFVLAKVWAMVMASVAPPALQLPLPDHFQPTGRPLPLGLLRREYIILLEIALSALSLLLCGLQAEPRYIILVPVLAAIWIIGSLTSKAYKAEVQQRREAFNRAKMDYDHLVRQIQQVGGLEGFIAKRTMLEKMKDEILGLPEEEKRALAALHDTARERQKQKFLEGFFIDVASIPGVGPARKAALRSFGIETAADVTRRGVKQVKGFGDHLTQAVIDWKASCERRFVFRPNEAITPADRQAVMAKMTAKRHRLESALTVGATELQRFRLHAPARTMPLMEPLRQAAEKLAQAQADLSRC
|
Probable serine/threonine kinase.
|
P76393
|
P02257
|
H1_ECHCR
|
Histone H1, gonadal
|
Echinolampas
|
AASPQKRAASPRKSPKKSPRKSPKKKSPRKRKARSAAHPPVIDMITAAIAAQKERRGSSVAKIQSYIAAKYRCDINALNPHIRRALKNQVKSGALKQVSGVGATGRFRVGAVKRSAASANKLKATREKARARAKAKKAKAAARRKAAAAKRKAAAAKRRAAKKARKAKAKP
|
Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
|
P02257
|
P32014
|
CTRB_NEIMB
|
Capsule polysaccharide export inner-membrane protein CtrB
|
Neisseria
|
MSEQLPVAVATETKAERKKPKKKSWIKKLSPLFWVTVIIPTVISLVYFGFFASDRFTSQSSFVVRSPKSQSSLNGLGAILQGTGFARAQDDIYTVGEYMRSRSSLDELRKILPVREFYETKGDAFSRFNGFGFRGEEEAFYQYYKNQVMINFDTVSGISTLNVTSFDALESKKINEALLKQGEALINQLNDRARADTVRYAEEVVKTAAERVKEASQNLTDYRIANGVFDLKAQSEVQMGLVSKLQDELIVIQTQLDQVKAVTPENPQIPGLQAREQSLRKEIDQQLRAISGGGHSSLSNQAAEYQRVYLENQLAEQQLAAAMTSLESAKVEADRQQLYLEVISQPSLPDLAHEPKRLYNIVATLIIGLMVYGILSLLTASIREHKN
|
May form an ATP-driven capsule polysaccharide export apparatus, in association with the CtrC and CtrD proteins.
|
P32014
|
P69755
|
O16C_CONMA
|
Delta-conotoxin-like MVIC
|
Pionoconus
|
MKLTCVMIVAVLFLTTWTFVTADDSRYGLKNLFPKARHEMKNPEASKLNKRDECYPPGTFCGIKPGLCCSAICLSFVCISFDF
|
Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process.
|
P69755
|
Q9YI19
|
VM2MC_GLOBR
|
Disintegrin
|
Gloydius
|
MIQVLLVIICLADFPYQGTSIILESGNVNDYEVVYPRKVTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSKGYSETHYSPDGRKITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFKHQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQTNWKSDEPIKASQQQRFPQRYIELVVVADHGMFTKYDSNLDTIRTWVHELVNSINEFYRSLNIDVSLTELEIWSNQDLINVQSAAGDTLEAFGDWRETDLLNRISHDNAQLLTATELDGNTIGLAHVASMCDPKRSTGVVQDHSAINLLVAVTMAHETGHNLGMNHDGNQCHCGANSCVMGDVLSEGVSYEFSDCSENEYQTYLTDRNPQCILNEPLRTDTVSTPVSGNELLEAGKECDCGAPANPCCDAETCKLRPGQQCAEGLCCDQCRFMKEGTICQEAKGDWNDDTCNGISAGCPRNGFYG
|
Inhibits ADP-induced platelet aggregation.
|
Q9YI19
|
A7MIG6
|
LPLA_CROS8
|
Lipoate--protein ligase
|
Cronobacter
|
MSSLRLLISDSYDPWFNLAVEECIFRQMPATQRVLFLWRNADTVVIGRAQNPWKECNTRRMEEDNVRLARRSSGGGAVFHDLGNTCFTFMAGKPEYDKSVSTAIVINALAQLGIPASASGRNDLVVETAEGPRKISGSAYRETMDRGFHHGTLLLNADLSRLSNYLNPDKKKLQAKGITSVRGRVANIHDLKPGVTHAQICEAVTEAFFAYYGERVAAEVISPDAFPDLPGFAETFARQSSWEWNFGQAPAFTHQLDERFVWGGVELHFDVEKGHITRTQLFTDSLNPAPLEALASRLQGCVYQASALQGVCEALVSEFPAQAAELREVGAWMAQAVR
|
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
|
A7MIG6
|
Q21Y67
|
CLPP_ALBFT
|
Endopeptidase Clp
|
Rhodoferax
|
MGAMQTQALGMVPMVIEQSGRGERSYDIYSRLLKERVIFLVGPVNDYVANLVVAQLLFLESDNPDKDISFYINSPGGSVSAGMAIFDTMNFVKPDVSTLCTGMAASMGAFLLAAGAKGKRFSLPNSKVMIHQPSGGSQGQATEIEIQAREILKTREQLNKILAERTGQPLARIERDTERDYYMSADECKEYGLIDQVISKRA
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q21Y67
|
P44620
|
LEP4_HAEIN
|
N-methyltransferase
|
Haemophilus
|
MIYFTMFLLGGILGIALWFYLSGFITRLQQNIYAIYVELFPQNRSPFQPHFASIQQKKCGHILRYFFSIGVGFIFLQIAFKDSIFTVWIGLTLIILWTISYLDWHYQLISTTPCLWLLTLGLFGADNNFSLLTLSESIKSAASFFIVFYVIYWLAKFYYGKEAFGRGDYWLAMALGSFIHLETLPHFLLLASVLGICFSLIHRKKKEFLPFAPFMNLSAVIIYFVKYYGY
|
Plays a role in type II pseudopili formation by proteolytically removing the leader sequence from substrate proteins and subsequently monomethylating the alpha-amino group of the newly exposed N-terminal phenylalanine. Substrates include proteins required for biogenesis of the type II general secretory apparatus.
|
P44620
|
Q9HYL1
|
NOSD_PSEAE
|
Probable ABC transporter binding protein NosD
|
Pseudomonas
|
MIHAARSLAGSRAGPLLALLLLGLATARAEPVDGLPLRADGDGRWSLAAGRYAGNFVIDRPLHLRCEAGAELDGGGHGSLLTLTSPGITVEGCRLRNWGRNLTELDAAIFVGKAASGAVIRGNDLRGAGFGVWLDATVGAQVLDNRIEGDESVRSQDRGNGIHLYAVKDALVRGNRVSHTRDGVYIDTSNDSSIEANRFEELRYGVHYMFTHNSRVTDNLTRRTRTGYALMQSRKLTVTGNRSIDDENYGILMNYITYSTLAGNRVEGVRSGSTGDAMISGAEGKALFIYNSLFNRIEGNSFADSALGIHLTAGSEDNRIAGNAFIGNRQQVKYVASREQEWSADGRGNYWSDYLGWDRDDDGLGDVAYEPNDNVDRLIWLYPQVRLLLNSPSIELLRWVQRAFPVVRSPGVRDSHPLMRMPAAEPRP
|
Required for the assembly of the copper chromophores of nitrous oxide reductase. Could be part of the ABC transporter complex NosDFY.
|
Q9HYL1
|
A8FK14
|
ARGC_CAMJ8
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
Campylobacter
|
MKIKVGILGASGYAGNELVRILLNHPKVEISYLGSSSSVGQNYQDLYPNTPLNLCFENKNLDELELDLLFLATPHEFSAKLLNENLLKKMKIIDLSADFRLKNPKDYELWYKFTHPNQELLQNAVYGLCELYKEEIKKASLVANPGCYTTCSILSLYPLFKEKIIDFNSVIIDAKSGVSGAGRSAKVENLFCEVNENIKAYGLASHRHTPEIEEHLSYAAKEKITLQFTPHLVPMQRGILISAYANLKEDLQEQDIRDIYTKYYQNNKFIRLLPPQSLPQTRWVKSSNFADINFSVDQRTKRVIVLGAIDNLIKGAAGQAVQNMNLMFDFDEDEGLKFFANL
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
A8FK14
|
C0HLR8
|
TX1_OCUSU
|
Kappa-lycotoxin-Os1a
|
Oculicosa
|
RLALPPGAVCNGHKSDCQCFGAKYKCSCPFFWRFRKSAECHCKKGWAWTAIKKRSCHNRYQWSD
|
Insecticidal to house crickets . It induces an excitatory slow-onset impact that leads to irreversible spastic paralysis . It also modifies human voltage-gated potassium channel Kv1.5/KCNA5 . Most likely, it binds to the voltage-sensing domain of the channel, suggesting it does not block the pore but prevents its opening at physiological membrane potentials . The recombinant peptide binds to the channel in an irreversible manner and slows down the hKv1.5 current activation kinetics . It is not toxic to mice, when intracranially injected (at 0.5 ug/g mouse) .
|
C0HLR8
|
Q53WI0
|
HOA_THET8
|
4-hydroxy-2-oxopentanoate aldolase
|
Thermus
|
MSWDLSTAKPPVVVDTTLRDGSHAHRHQYTVEEARAIAQALDEAGVYAIEVSHGDGLGGSSLQYGFSRTDEMELIRAVRETVRRAKVAALLLPGIGTRKELKEAVEAGIQMVRIATQCTEADISEQHFGMAKEMGLEAVGFLMMSHMRPPEFLAEQARLMEGYGADVVYIVDSAGAMLPEDAYARVKALKEALSRAKVGFHAHNNLGLAIGNTLAALAAGADWVDATLRGYGAGAGNAPLEVLAAVLDKAGLNPGLDVFKLLDAAEYVMGPILHFQPYPDRDSVAIGYAGVYSTFLLHAKRIGKELGVDPLAILLELGRRQAVAGQEDWILRVALELKEKEAGALAD
|
Catalyzes the retro-aldol cleavage of both 4-hydroxy-2-oxopentanoate (HOPA) and 4-hydroxy-2-oxohexanoate (HOHA) to pyruvate and acetaldehyde or propanaldehyde, respectively. The aldehydes produced by this reaction are directly channeled to the dehydrogenase TTHB247, ensuring that these toxic aldehydes are sequestered from cellular components. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds. Appears to be stereospecific since it can cleave (4S)-4-hydroxy-2-oxopentanoate but not the (4R) isomer. Is not able to catalyze the aldol addition of 2-oxobutyrate with acetaldehyde; this indicates that the enzyme is specific for pyruvate as the carbonyl donor.
|
Q53WI0
|
Q65RT1
|
HSCB_MANSM
|
Co-chaperone protein HscB homolog
|
Basfia
|
MNNPFALFDLPIEFQLDQNRLSERYLALQKALHPDNFANSSAQEQRLAMQKSAEVNDALQILKDPILRADCIIALNTGEQQNTEEKSTQDMAFLMQQMQWREQLEEIENTQDIDGLMTFSAEIEQSNKEKISEISTALSMKDWQQAKLINDRLRFIKKLMTEIERIEDKLADF
|
Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA.
|
Q65RT1
|
B6EJ04
|
KTHY_ALISL
|
dTMP kinase
|
Aliivibrio
|
MSKFIVIEGLEGAGKSTAIKNVLATLAKHGITAPVTTREPGGTPLAEKMRELVKQGHPDEPLTDMAELLLLYAARAQLVGNVIKPALAAGNWVVGDRHDLSSQAYQGGGRGFDRELMATMKRTVLGDFTPDLTIYMDIDPKLGLQRASARGELDRIEQMKLDFFERSRERYLEFANNDESIITIDAGQDLDTVTASIIAALEIWLATNGN
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
B6EJ04
|
O16259
|
STIP1_CAEEL
|
Hsc70/Hsp90-organizing protein
|
Caenorhabditis
|
MTDAAIAEKDLGNAAYKQKDFEKAHVHYDKAIELDPSNITFYNNKAAVYFEEKKFAECVQFCEKAVEVGRETRADYKLIAKAMSRAGNAFQKQNDLSLAVQWFHRSLSEFRDPELVKKVKELEKQLKAAERLAYINPELAQEEKNKGNEYFKKGDYPTAMRHYNEAVKRDPENAILYSNRAACLTKLMEFQRALDDCDTCIRLDSKFIKGYIRKAACLVAMREWSKAQRAYEDALQVDPSNEEAREGVRNCLRSNDEDPEKAKERSLADPEVQEILRDPGMRMILEQMSNDPGAVREHLKNPEIFQKLMKLRDAGVIQMR
|
Plays a role in gonad development. Up-regulates longevity and thermotolerance. Binds daf-21/hsp90 and inhibits its ATPase activity.
|
O16259
|
Q1CSC6
|
FMT_HELPH
|
Methionyl-tRNA formyltransferase
|
Helicobacter
|
MRIVFMGTPGFAEVILRALVENKNNHIEVVGLFTQMDKPFGRKKELKAPETKTYILENHLNIPIFQPQSLKEPEVQILKDLKPDFIVVVAYGKILPKEVLTIAPCINAHASLLPKYRGASPIHEMILNDDRIYGISTMLMDLELDSGDILESASFLREDYLDLDALSLKLAHMGADLLFSTLKNFSSITRKPQDHMQATFCKKITKADGLVGFKDAKSLFLKSLAFKSWPEIFLENSLKLLEVGLVENEKSHKEGEILEIDEKGVLVGCLKGSVRVAWLQAVGKKPLKAKDYLNGRRLKIGGILA
|
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
|
Q1CSC6
|
A9H3S4
|
RL7_GLUDA
|
50S ribosomal protein L7/L12
|
Gluconacetobacter
|
MADLTKLVDELSALTVLEAAELSKLLEEKWGVSAAAPVAVAAAPAAGAAAAPAEEQTEFTVVLAKAGDKKINVIKEIRGITGLGLKEAKDLVEGAPKTVKEGVNKDEAEKIKKLLEDNGASVEVK
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
|
A9H3S4
|
B5F6A8
|
MUG_SALA4
|
Mismatch-specific uracil DNA-glycosylase
|
Salmonella
|
MVKDILAPGLRVVFCGINPGLSSANTGFPFAHPANRFWKVIHLAGFTDRQLKPEEAEKLLDFRCGVTKLVDRPTVQATEVKLHELRSGGRNLIEKIEDYQPAALAVLGKQAFEQGFSQRGIAWGKQKIAIGATMVWVLPNPSGLNRIKTEKLVEAYRELDQALIMRGL
|
Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.
|
B5F6A8
|
Q9TLY2
|
CFXQ1_CYACA
|
Protein CfxQ homolog
|
Cyanidium
|
MGITPTALEKTDKHTLVNLQEEFNKTKIQEVLDDLNQELIGLKPVKNRIREIAALLLVDRLRQKVGLSSSNPGLHMSFTGPPGTGKTTVATKMADILYKLNYIKKGHLVTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLYKPDNERDYGSEAIEILLQVMENQREDLVIIFAGYKEKMDKFYASNPGLASRVANHVDFPEYRPEELLKIAEMMLQEQQYQLTKEAELVFLDYIKKRMLQPHFANARSVRNAIDRARMRHANRIFNLSSKIVTKSNLTTIQAEDILKSRLFNT
|
Necessary for the expression of RuBisCO.
|
Q9TLY2
|
Q9M2R1
|
GIG1_ARATH
|
Protein UV-B-INSENSITIVE 4-like
|
Arabidopsis
|
MPEARDRTERPVDYSTIFANRRRHGILLDEPDSRLSLIESPVNPDIGSIGGTGGLVRGNFTTWRPGNGRGGHTPFRLPQGRENMPIVTARRGRGGGLLPSWYPRTPLRDITHIVRAIERRRGAGTGGDDGRVIEIPTHRQVGVLESPVPLSGEHKCSMVTPGPSVGFKRSCPPSTAKVQKMLLDITKEIAEEEAGFITPEKKLLNSIDKVEKIVMAEIQKLKSTPQAKREEREKRVRTLMTMR
|
Negative regulator of the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase required for proper mitotic and meiotic progression and cell fate determination. Involved in entry into both meiosis I and meiosis II. Prevents endomitosis by preferentially inhibiting APC/C(CDC20). Required for megagametophyte and endosperm development. Triggers mitotic cyclins (e.g. CYCB1-1 and CYCB1-2) accumulation. Confers immunity to bacterial pathogens (e.g. Pseudomonas syringae pv. tomato DC3000), which is associated with increased expression of disease resistance (R) genes. GIG1 and PANS1 are part of a network linking centromere cohesion and cell cycle progression through control of APC/C activity.
|
Q9M2R1
|
Q22835
|
ZIP10_CAEEL
|
Transcription factor zip-10
|
Caenorhabditis
|
MTTMTNSLISNSVSSVPESLFSSASIHRPVAINPAMLAQFSINLPVLPFESSASLGTSTTSSSRCSSTESSAAPGKIRRGRPQQEIADGQDAHSQKKRHRRLYARQYRAQMRQKVENVKSLHDEKEQLELEVKALRQAVSGLQQENAQKDFLISILQLNNQINHS
|
Transcription factor that regulates the expression of genes in response to changes in temperature. In particular, binds to the promoter region of genes such as asp-17 in response to severe cold to warm temperature transitions to promote gene expression. Promotes stress-induced death, particularly in older animals, following cold shock followed by warming and this may have evolved as a form of kin survival under thermal stress conditions, favoring the survival of younger animals.
|
Q22835
|
P83186
|
BRA_BASAL
|
Alpha-basrubrin
|
Basella
|
GADFQECMKEHSQKQHQHQG
|
Possesses antifungal activity against B.cinerea, M.arachidicola and F.oxysporum but not C.comatus and R.solani. Inhibits HIV-1 reverse transcriptase and cell-free translation.
|
P83186
|
Q3YJT4
|
PT1K2_SOLTU
|
Patatin-1-Kuras 2
|
Solanum
|
MILATTSSTFASLEEMVTVLSIDGGGIKGIIPGTILEFLEGQLQKMDNNADARLADYFDVIGGTSTGGLLTAMITTPNENNRPFAAANEIVPFYFEHGPHIFNSSTGQFFGPKYDGKYLMQVLQEKLGETRVHQALTEVAISSFDIKTNKPVIFTKSNLAKSPELDAKMYDICYSTAAAPTYFPPHYFATNTINGDKYKFNLVDGAVATVADPALLSVSVATRRAQEDPAFASIRSLNYKKMLLLSLGTGTTSEFDKTHTAEETAKWGALQWMLVIQQMTEAASSYMTDYYLSTVFQDLHSQNNYLRVQENALTGTTTKADDASEANMELLAQVGENLLKKPVSKDNPETYEEALKRFAKLLSDRKKLRANKASY
|
Probable lipolytic acyl hydrolase (LAH), an activity which is thought to be involved in the response of tubers to pathogens.
|
Q3YJT4
|
A5VRI0
|
MRAY_BRUO2
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Brucella
|
MLMFLTHFAEHVTPFNVFRYITFRTGGAMITSALIVFLFGPTIINSLRVRQGKGQPIRADGPQTHFKKAGTPTMGGLMIMTGILASCLLWANLASVYVWVVLMVSVGFGAIGFYDDYLKVTKQSDKGFSGKARLGIEFLIAAIAAFTIMRAGQEPFSSSLTFPFVKQLVINLSWFFILFAAFVMVGAGNAVNLTDGLDGLAIVPVMVAAASFGFIAYLSGNAIFADYLQIHFVPGTGELAVVLGAVIGAGLGFLWFNAPPAAIFMGDTGSLALGGMLGTVAVATKHEIVLAIIGGLFVMEALSVIIQVGFFKMTGRRVFLMAPIHHHFEKKGWTESQVVIRFWIVAIILAMIGLSTLKLR
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
A5VRI0
|
A8WMY4
|
NRA1_CAEBR
|
Nicotinic receptor-associated protein 1
|
Caenorhabditis
|
MNQPIAAIGISDSTRPKTNVRLTISAEHLMDTDVFSKSDPICLVYEKTSGKKATTTEPVQVPTWQDSQWTERGRTEVVMNNLNPQFTKTFLLPYFFEETQLLRFEIYDADSPNVGQDLSPHDFLGRFECVLAQIVSYSTLKAHLGKAEGIGAQWRNKDKNTRTGSITIRAEEDEKCEKIQFDVCGEGLDKKDFFGKSDPYLNFKRKFDDGSAHLVHRTEVKQKTLDPRWATVQINTQTLCGKDGERPIIIECYDHDKWKKGEEPRGEAKFSRDDHIGTAHTTLNELLRGGAGDPVELLLTNEKKKAKKGDKYKCSGTLKIWNSKIIVEPTFLDFISGGTQLEFAVAVDFTASNGAPKNSSSLHYMSADRPNQYELALRSVLSICQHYNSSKTFEAFGFGAKLPNSVSVSAIFSLDLLRGTPEVVGISGVMSAYRHALQNVQLYGPTNFAPIIDTVAQKAQNMIHDSARYQILLIITDGIISDMHATIRSIINASGLPLSIIIIGVGNEDFEKMHELDSDDSLLQQDSRIAQRDIVQFVTIREFLNNGRGVYLDPDVVQENLAREVLFEVPGQLTGYMKQRGFQPRPVENPWTRNSPPPDYDPVLDGIGRRAQAPSPGFQMPVASAPPMY
|
Exhibits calcium-dependent phospholipid binding properties. May function in membrane trafficking. Regulates synaptic levels of nicotinic acetylcholine receptor subunit lev-1 and unc-38 in the nerve cord. Involved in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine and levamisole. Affects directional sperm motility.
|
A8WMY4
|
C3MZI0
|
PSB2_SULIA
|
Proteasome core protein PsmB 2
|
Sulfolobus
|
MEELPATAIGLKVNDGIVLASERRLSYGGYVLSKQAKKVHKIGKFLMAGAGIYGDLQTLTRIMNVEIKYYEISTGKPISVHAAAKLLSVILYQYKVMPFISEILFGGVDEKGPQLYVLDPIGSLIEDNYAAVGSGARIAIGVLESEYDPNMNLDIAAQLITKAIKASIERDITSGDGIDLAIMDKKGNYENKFIPY
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
C3MZI0
|
A5UDB0
|
RLMC_HAEIE
|
23S rRNA(m5U747)-methyltransferase
|
Haemophilus
|
MIDCQYYQQNECRSCQWLEIPYDQQIAEKQHHLKQQLISLDCSDVHWLAPFKSNEQGFRNKAKMLVSGSVERPILGILKNPNDPQSAIDLCDCPLYPAHFSIIFSILKDFIGRAGLVPYNIAKQKGELKYILLTESIATGKLMLRFVLRTENKLPLIRRELPKLLEKLPHLEVISINLQPQHAAILEGEQEIFLTEQQFLPENFNGIPLFIRPQGFFQTNPKVAAGLYATAQQWVAEFPIYNLWDLFCGVGGFGLHCAKALQEKWGKPIKLTGIEISSSAILAASHSAKILGLEHVNFQSLNAASVMENKNENKPDLVIVNPPRRGIGKQLSEFLNQIQPHFILYSSCNAMTMGKDLQHLTCYKPLKIQLFDMFPQTSHYEVLVLLERKKIN
|
Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA.
|
A5UDB0
|
A7ZCN3
|
RL11_CAMC1
|
50S ribosomal protein L11
|
Campylobacter
|
MAKKVIGEIKLQIAATKANPSPPVGPALGQKGVNIMEFCKAFNEKTKDMVGFNIPVVITVYADKSFTFITKQPPATDLIKKAAGITKGTDNPLKNKVGKLTKAQVLEIVEKKLVDLNTNDKEQAAKIIAGSARSMGVEVVD
|
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
|
A7ZCN3
|
Q2JDQ7
|
CLPX_FRACC
|
ATP-dependent Clp protease ATP-binding subunit ClpX
|
Frankia
|
MARIGDGGDLLKCSFCGKSQKQVKKLIAGPGVYICDECIDLCNEIIEEELSESSELKWDELPKPREIYEFLDSYVVGQETAKKTLSVAVYNHYKRVQAGGSSGDGSKGEVELAKSNILLLGPTGCGKTLLAQTLARMLNVPFAIADATALTEAGYVGEDVENILLKLIQAADYDVKKAETGIIYIDEVDKIARKSENPSITRDVSGEGVQQALLKILEGTTASVPPQGGRKHPHQEFIQIDTTNVLFIVGGAFAGLDRIIESRIGKKSLGFRAVLHGKDDPDGSDVFGDIMPEDLLKYGMIPEFIGRLPVITSVSNLDREALIRILTEPKNALVRQYKRLFELDSVDLDFTSDALEAIADQAILRGTGARGLRAIMEEVLLSVMYDIPSRKDVARVVVTREVVLEHVNPTLVPRDVVSKRAPRQEKSA
|
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
|
Q2JDQ7
|
B5EBU6
|
TRPD_CITBB
|
Anthranilate phosphoribosyltransferase
|
Citrifermentans
|
MIRKAIARVVERQDLSEAEMIEVMDQVMSGGATPAQIASFITALRMKGETVDEITGAARVMRDRALPIRVGKSVLGIDRDDINLDRETILDTCGTGGSGTNSFNISTTVAFIVSACGVKVAKHGNRAVSSSCGSADVLEALGVNLDVTPDVVERSIAQIGIGFLFAPALHGAMKHAIGPRREIGIRTIFNILGPLTNPAGADCQVLGVYREDLVEKLAQVLKKLGCRSGFVVHGCDGMDEITLTGESTVAEITADGVKLYKVTPEQFGLERAPLAELHGGDALGNAVIVRDILSGKDGAKRRIVLLNAGYALVATGKAKDVAEGIRLAAETIDSGAAMKQLERLVALTNEAE
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
B5EBU6
|
A0A1S4AX27
|
SCI1A_TOBAC
|
Style cell-cycle inhibitor 1-A
|
Nicotiana
|
MGSDKKTPEEKRKHKRSSPSSPLDEVKSKRQNIKGDEERRKEKKDKSKKEKHKSHSSEEKKSGEKHKTKSHKHKDKSKNKFEELSKDDYFSKNNEFATWLKDKKNLFFSDLSSETARDLFSDFVIQWNKGKLDSQYYEGIATGPRSSHAWNIKK
|
Component of the auxin signaling transduction pathway that regulates cell proliferation and differentiation during flowers stigmas and styles development . Involved in the regulation of auxin-related genes .
|
A0A1S4AX27
|
B1XAJ3
|
METE_ECODH
|
Methionine synthase, vitamin-B12 independent isozyme
|
Escherichia
|
MTILNHTLGFPRVGLRRELKKAQESYWAGNSTREELLAVGRELRARHWDQQKQAGIDLLPVGDFAWYDHVLTTSLLLGNVPARHQNKDGSVDIDTLFRIGRGRAPTGEPAAAAEMTKWFNTNYHYMVPEFVKGQQFKLTWTQLLDEVDEALALGHKVKPVLLGPVTWLWLGKVKGEQFDRLSLLNDILPVYQQVLAELAKRGIEWVQIDEPALVLELPQAWLDAYKPAYDALQGQVKLLLTTYFEGVTPNLDTITALPVQGLHVDLVHGKDDVAELHKRLPSDWLLSAGLINGRNVWRADLTEKYAQIKDIVGKRDLWVASSCSLLHSPIDLSVETRLDAEVKSWFAFALQKCHELALLRDALNSGDTAALAEWSAPIQARRHSTRVHNPAVEKRLAAITAQDSQRANVYEVRAEAQRARFKLPAWPTTTIGSFPQTTEIRTLRLDFKKGNLDANNYRTGIAEHIKQAIVEQERLGLDVLVHGEAERNDMVEYFGEHLDGFVFTQNGWVQSYGSRCVKPPIVIGDISRPAPITVEWAKYAQSLTDKPVKGMLTGPVTILCWSFPREDVSRETIAKQIALALRDEVADLEAAGIGIIQIDEPALREGLPLRRSDWDAYLQWGVEAFRINAAVAKDDTQIHTHMCYCEFNDIMDSIAALDADVITIETSRSDMELLESFEEFDYPNEIGPGVYDIHSPNVPSVEWIEALLKKAAKRIPAERLWVNPDCGLKTRGWPETRAALANMVQAAQNLRRG
|
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
|
B1XAJ3
|
O08556
|
CCR5_RAT
|
MIP-1 alpha receptor
|
Rattus
|
MDFQGSIPTYIYDIDYSMSAPCQKVNVKQIAAQLLPPLYSLVFIFGFVGNMMVFLILISCKKLKSMTDIYLFNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKLFTGIYHIGYFGGIFFIILLTIDRYLAIVHAVFAIKARTVNFGVITSVVTWVVAVFVSLPEIIFMRSQKEGSHYTCSPHFLHIQYRFWKHFQTLKMVILSLILPLLVMVICYSGILNTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLLLTTFQEYFGLNNCSSSNRLDQAMQVTETLGMTHCCLNPVIYAFVGEKFRNYLSVFFRKHIVKRFCKHCSIFQQVNPDRVSSVYTRSTGEQEVSTGL
|
Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor.
|
O08556
|
B9DMC0
|
LUXS_STACT
|
Autoinducer-2 production protein LuxS
|
Staphylococcus
|
MPKMNVESFNLDHTKVVAPFVRLAGTVEGANGDVIKKYDIRFKQPNKEHMKMPGLHSLEHLMAENIRNHTDKVVDLSPMGCQTGFYVSLINHDDYEDVLNIIEATLKDVLAADEVPACNEVQCGWAASHSLEGAKEIAQDFLDKRDQWDKIFSE
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
B9DMC0
|
Q566I1
|
IN80D_XENLA
|
INO80 complex subunit D
|
Xenopus
|
MYEGKHIHFSEVDNKPLCSYSPKLCKQRRLNGYAFCIRHVLEDKTAPFKQCEYVAKYNSQRCTNPIPKSEDRRYCNSHLQVLGFIPKKERKKKNDALEDVKTKHQMETMAFSLTVPPLALKMPNGHDGLNLSPPGARLPIHYLETDLEDPFSFEEEEEELKKGTSVKKKLQSKLAQNWQRLRETEIVNVHQEHFSPHPAHSPLQSPSLQEQHTLVQPISTLPKPTGLPQNLVCKSPQPSNISQPVQGASPVTHTVAQTRHQSSKRPFPVLPPVTELPRNDRIQLAATALPAYSSYVSRLQRLVKLCTRKQQLDTDLFPHFGLDWSEDSGEEQEDSDQSSPYRTAWSFRESFRYDCKKLDIEEAHSRSSRIAQLCTYFQQKYKHLCRLERAESCQKKYRHTFRRALQQAAHRESETTGQLLQELRTTTCIRTRPIQPELRGTEVTLCSATISNGACRNRALPYTRNCFQHILSNSSQQLFSSCTAKFADGQQCSVPVFDITHQTPLCEEHAKKMDNFLRGDNSRKVQHHQQRKPRKKTKPPALTKKTKKKRRRGPRRPQKPIPPAVPQGNLCMPSSLSLPVEVSSIRSPSTPNLSTEELPDDITSEITDIPHDLELNQEDFSDVLPRLPDDLQDFDFFEGKNGDLLPTTEEAEELERALQAVTSLECLSSIAVLTQADNATGQDLSDRGISAFSTGSGGSVIQSLSREDHPDLGDLLNGHIGHNFASLELDENLLGSTTLSNPSATLSGHIQGQFSSPANVGLSSATLISRSGERLGREVMSHHVDAAAPILDKQRVSGALYSGMVKHSAEWV
|
Putative regulatory component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
|
Q566I1
|
Q9UTR7
|
MCP3_SCHPO
|
Meiotically up-regulated gene 7 protein
| null |
MTKETHENHLRTHNGIFPVSLLSTQARQLLNFKLKSPSYYLLNSFKLLVKSEGNNQSTTADVTLTKSPNAYHASSAREEKDLQVSRRDTCFYCSRKIIKCICNEEHVGIESVQLKLILLLCQNLPNVTTNAKKYFSSLADGHNFTLTLYKFSLDNQTFSQLLSRFKSFATLTELLQVHNVMLQVNFSFQARQLNTEIQLRRCHSLEKTWKFLFGDYELPDVLKDMESSNSDWSDTSLKRIAYLCSLVEELKLHSSIMNDKYVCLVSKHNNALEDKFNSEAARQLLQKSLSIVASNLKQAENKTISYEEKLSIAQNSINEIQTQNRDLKLETEKLQDQIKALLERNQSLQEALETVKNDEKNLREMNANYETEMKEARQKLNNKEALISHYDDDFRAKELKISRLSESLREKAGLLEFQSSVSEQRDLLYQEQIQSSIKDMENVFRKNEYLMEELNELKNNLEVESSKVLRLDEEMKCLKDEQLSQFDTVFSLTDERDGLQKDLKNTKGNLDDEIGRSAFLKSQIRDQELTIEKLHDSLETLSQTNNSLQCEISEKNAELNSVNSKLSEGRAHLETANKENEILKQQLELSESKLASLLNSYQSFINKKEHLYSFLQLVEPSFAKSDSSNATESQISESVRKGISIFNLLFIVYKNVCSQAGINPSTKLEDLDEHTLSDELTYITKKFVQKDQEYQTKEIELRNYKITLQSLLEDKLIGVNTDCRSPSCSDFEQLGQESENNTSISGRVSKLVKSFNDSSSISNNTKISITKSPSGEKVSVFKEMSDIALRDMDKNRKLLGENVDVRNIVVQKDESLNIDLQNNAVVPELHFKEGMVYDSLENAYTYLAESKRMLANELQMKQEDLEKVILELEAYKEIFLEEKQIPCEEFMPGKNAKSEKSLRSVFQEQLMRETKRVRKLEKVNSELKLHCFELSERLREREHTLQQTFGDK
|
Has a role in meiosis.
|
Q9UTR7
|
C7MWV7
|
PSB_SACVD
|
Proteasome core protein PrcB
|
Saccharomonospora
|
MEHTPRNAGFALPAAYMSTMTSSFIDFLKAEAPDLLPRARVENMPAVPGGGSAFEPPHGTTIVASTFNGGVLIAGDRRATTGNTIASRDLEKVYVTDAYSAVGIAGTAGIALELVRLYTVELAHYEKIEGVSLSLDGKANKLANMVKGNLDGALAGLAVLPLFVGYDIDADDPKRAGRIVSFDVTGGRYEENAGYHAIGSGAVYAKSSLKKLYDPEADADTAVRTAIEALYDAADDDTATGGPDLVRRIYPTVVTITAEHGAVMLPQEETASIAESVVRERSERPGQLG
|
Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
|
C7MWV7
|
Q8K2B0
|
SC65_MOUSE
|
Synaptonemal complex protein SC65
|
Mus
|
MARGAWGLLWLLLGSAGAQYEKYSFRGFPPEDLMPLATAYGHALEQYEGESWRESARYLEAALRLHRLLRDSEAFCHANCSGPATSQPRPASGPDGDHDGDGEDWARELRLFGHVLERAACLRRCKKTLPAFQVPYPPRQLLRDFQSRLPYQYLHYAHFKANRLEKAVAAAYTFLQRNPKHELTAKYLNYYRGMLDIGDESLTDLEAQPYEAVFLRAVKLYNSGDFRSSTEDMERALAEYMTVFARCLAGCEGAHEQVDFKDFYPAIADLFAESLQCKVDCETNLTPNVGGFFVDKFVATMYHYLQFAYYKLNDVRQAARSAASYMLFDPKDSVMQQNLVYYRFHRARWGLEDEDFQPREEAMLYHNQTSELRELLDFTHMYLQSDDEMELEETESLPEPEEPLSDAEFEGEGDYEEGLYADWWQEPEAKGDEAEAEPEPELT
|
Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils . Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly .
|
Q8K2B0
|
C4ZUV5
|
ALLA_ECOBW
|
Ureidoglycolatase
|
Escherichia
|
MKLQVLPLSQEAFSAYGDVIETQQRDFFHINNGLVERYHDLALVEILEQDCTLISINRAQPANLPLTIHELERHPLGTQAFIPMKGEVFVVVVALGDDKPDLSTLRAFITNGEQGVNYHRNVWHHPLFAWQRVTDFLTIDRGGSDNCDVESIPEQELCFA
|
Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate.
|
C4ZUV5
|
Q9U539
|
OCT1_CAEEL
|
CeOCT1
|
Caenorhabditis
|
MSFQAMETFAEISQEILMSATKPPDFDFVLEQVGNYGTYQIVFFFIICLPTSLPSAFSAFNIPFVVGNPPHTCHIPEGKEYLRPLTNDTQILSCKQYNETQINVFRAFTSAPVDTYSDRISLVPCQNGWDYDNSTYLDSLVTEFNLVCDQQAWIEISTTSFYVGSFIGNCLFGYVADKFGRRRSFFVILTVLIVCGTASSFAKDIESFIILRFFTGLAFPALFQIPFIICMEFMGNSGRIFSGLMTSLFFGAAMALLGVVAMFIRRWRQLTFFCNAPFAFYIIYYFFLPESPRWSVSVGKWADAKKQLKKIAKMNGKSNVDVDELVDSMKNHQNAAEEKETKRSHNVTDLFKTPNLRRKTLIVTYIWVMNAIIYNGLTLNVSNLPVDDYWSFIINGAVELPGYFVVWPLLQCAGRRWTLAATMIVCGIGCVSAMFMPDGYPWLVASASFIGKFGVGSGFAVIYIFAGELYPTVVRAIGMGMSSMVAGSGLLLAPHIVNLGKIVKILPLLIMGLMALSAGILTFFLPETLGAPLPMTIEDAENFGKKPEPDSGMFTQAAKKRESQPLLEPHTPMDRRRRSSRLMNI
|
Transports organic cations such as tetraethylammonium (TEA). Displays a broad substrate specificity.
|
Q9U539
|
O05337
|
PDRP_STAAU
|
Putative pyruvate, phosphate dikinase regulatory protein
|
Staphylococcus
|
MEKIKIIVASDSIGETAELVARAGISQFNPKQCKNELLRYPYIESFEDVDEVIQVAKDTNAIIVYTLIKPEMKQYMSEKVAEFQLKSVDIMGPLMDLLSASVEEKPYNEPGIVHRLDDAYFKKIDAIEFAVKYDDGKDPKGLPKADIVLLGISRTSKTPLSQYLAHKSYKVMNVPIVPEVTPPDGLYDIDPKKCIALKISEEKLNRIRKERLKQLGLGDTARYATDQEELNYFEEIVSEIGCPVIDVSQKAIEETANDIIHYIEQNKSK
|
Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
|
O05337
|
P25966
|
ATPL_ALKAL
|
Lipid-binding protein
|
Alkalihalobacillus
|
MGLLGAAIVAGLAAVGGAIAVAIIVKSTIEGVTRQPELKGTLQTLMFIGVPLAEAVPIIAIVMGFLIMGNA
|
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.
|
P25966
|
Q89ZR7
|
PAND_BACTN
|
Aspartate 1-decarboxylase alpha chain
|
Bacteroides
|
MMIEVLKSKIHCARVTEANLNYMGSITIDEDLLDAANMIPGEKVYIADNNNGERFETYIIKGERGSGKICLNGAAARKVQPDDIVIIMSYALMDFEEAKSFKPTVIFPDPATNSVVK
|
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
|
Q89ZR7
|
B3EWH2
|
AON_AZEFE
|
Azemiopsin
|
Azemiops
|
DNWWPKPPHQGPRPPRPRPKP
|
In vitro, reversibly blocks human muscle-type nicotinic acetylcholine receptors (nAChR) alpha-1-beta-1-epsilon-delta/CHRNA1-CHRNB1-CHRNE-CHRND (EC(50)=0.44 uM) and alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND (EC(50)=1.56 uM). Binds to nAChR from T.californica (IC(50)=0.03-0.18 uM), human neuronal nAChR alpha-7/CHRNA7 (IC(50)=22 uM) and acetylcholine-binding proteins (AChBP) from L.stagnalis (IC(50)=63 uM) and A.californica (IC(50)=230 uM).
|
B3EWH2
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.