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
|
|---|---|---|---|---|---|---|
Q8VFT4
|
OL734_MOUSE
|
Olfactory receptor 734
|
Mus
|
MEPANDTTVTEFILTGLSQTREVQLVLFVIFLSFYLFILPVNILIICTIRLDSHLSSPMYFLLANLAFLDIWYSSITAPKMLVDFFVERKIISFGGCIAQLFFLHFVGASEMFLLTVMAFDRYAAICRPLHYATIMNRRLCCILVALSWTGGFVHSIIQVALIVRLPFCGPNELDNYFCDITQVVRIACANTFLEEMVMIFSSGLISVVCFIALLMSYAFLLTMLKKHSSSGESTSRAISTCYSHITIVVLMFGPSIYIYARPFDSFSLDKVVSVFHTVIFPLLNPIIYTLRNKEVKAAMRKLVNRYIFCKEK
|
Olfactory receptor that acts as a receptor of Asprosin hormone at the surface of hepatocytes to promote hepatocyte glucose release . Also binds Asprosin in the arcuate nucleus of the hypothalamus, thereby stimulating appetite by promoting orexigenic AgRP neuronal activity . In testis, Asprosin-binding promotes sperm progressive motility and enhances male fertility . The activity of this receptor is mediated by G proteins which activate adenylyl cyclase, resulting in an elevation of intracellular cAMP .
|
Q8VFT4
|
Q038V7
|
ADDA_LACP3
|
ATP-dependent helicase/nuclease AddA
|
Lacticaseibacillus
|
MTQFTTSQQAAITHDGHDVLVSASAGSGKTTVLVERIIQKILKQHADITRMLIVTFTRAATAEMRTKIQTALKKALTERRHELSGEDRRHLANQIAMVNAAKISTLDAFSLQIVQTYYYVIDLDPGFRLLTDETERYMLQERVWDDLREQLYASDEAPAFEQLTANFSGDRDDSGLQDLMFELIRQAGATTDPKAYLEGLATPYAPEKWEATFSQQIWPRVKGQLLQIATSLTQASALANQLPNPIWYQQIQADLAPLQTLLETNAPTYDTVRSVLISHEFAAWSRISKGLDDADKDTKNAAKDLRDAAKKTWQNKLAPTFALAAEQIGDLLREAQPLVATLANVALKFEDALTAEKAARHVQDYSDIAHNALRILQQKDPQTGAPIADNYRASFDEVMVDEYQDISPLQEALLAAVSTTTPGDRFMVGDVKQSIYGFRLADPQLFIHKYQTFQDAPTDPAAPERIILAENFRSTKNVLAFTNLIFSQIMDPEVGDLSYDNAAALKYGALDYGDAHPAVKVLLYSKATSDEDSSDASELPGDADDNEPVDIATGQTQLVLAEIQRLINDPDAQLWDRQAQEYRRIHYRDITLLTRQTSQNSLIQTQFAAAGVPLFVADTKNFFKTTELMVMLALLKVIDNQKQDIPLVAVLRSPIVGLSADQLALIRLAAKQVPYYDAVTAFLQAEPKTPLAQRTHDMLTHFFNQLSHFRDLARENDLVTLLWAIYQDTGFLDYVGGTPGGSQRQANLQALIDRARTYEAGGFKGLFAFIHFITLMQKQDQDLAMPAQVDPDNDAVKLMTIHKSKGLEFPVVFLMQANKHFNMSDQTGTAILTKQGIGIKWLDPETRVEYELPQYQAAKAARQNQTLAEEMRLLYVALTRAQQRLYVVGATMSGNQLTSADKTVEKWAAAAEGEARVLAPQVRSGATSYLDWIGPALIRHPQARGLAETTIKPALVGDETEFTIEIDVNPQVTPTATPEKVSDDSGTMVDLSAWFKKAYPFQAATTTTGFQSVSEIKRAFDDPDTIDLVNADRFLGPKPPMRDLTAPAFLTETPSGISPAAIGTATHLLLQLVDLAKPITMASLRALRDQLTTTQVIAVDVAKHIDLTALIRFFETDLGRLLLAKPQQVHREVPFSMLLPADQVFEALADDPGEDVLIHGIIDGYVSDEQGVTLFDYKTDHNPNTAVLVDRYRGQLNLYAQALQDLQPKPVLHRYLVFLRTGTVVDLVASGAGK
|
The heterodimer acts as both an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the chi site generating a DNA molecule suitable for the initiation of homologous recombination. The AddA nuclease domain is required for chi fragment generation; this subunit has the helicase and 3' -> 5' nuclease activities.
|
Q038V7
|
Q0V7V2
|
P2C42_ARATH
|
Probable protein phosphatase 2C 42
|
Arabidopsis
|
MSGSLMNLFSLCFKPFGHVCDNSEAGSGGGGGVSGGTGGEGKDGLLWFRDLGKYCGGDFSMAVIQANQVLEDQSQVESGNFGTFVGVYDGHGGPEAARYVCDHLFNHFREISAETQGVVTRETIERAFHATEEGFASIVSELWQEIPNLATVGTCCLVGVIYQNTLFVASLGDSRVVLGKKGNCGGLSAIQLSTEHNANNEDIRWELKDLHPDDPQIVVFRHGVWRVKGIIQVSRSIGDMYMKRPEFNKEPISQKFRIAEPMKRPLMSATPTILSHPLHPNDSFLIFASDGLWEHLTNEKAVEIVHNHPRAGSAKRLIKAALHEAARKREMRYSDLRKIDKKVRRHFHDDITVIVVFLNHDLISRGHINSTQDTTVSIRSALEH
|
Dephosphorylates and represses plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness . Promotes the apical hook maintenance of etiolated seedlings .
|
Q0V7V2
|
P11081
|
TRPA_PSEPU
|
Tryptophan synthase alpha chain
|
Pseudomonas
|
MSRLEQRFAELKAEGRSALVTFVTAGDPGYDASLQILKGLPAAGADVIELGMPFTDPMADGVAIQLATLRALEAGQTLAKTLQMVREFRVDNHTTPIVLMGYYNPIHRFGVEKFVAEAKQAGVDGLIIVDLPPEHDAELATPAQAAGIDFIRLTTPTTDDARLPRVLERSSGFVYYVSVAGVTGAGSATTEHVTEAIARLRRHTDLPISVGFGIRTPEQAANIARLADGVVVGSALVDKIAQATSADQAVNDVLSLCSALAEGVRGARR
|
The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
|
P11081
|
Q9LFH3
|
LOG4_ARATH
|
Protein LONELY GUY 4
|
Arabidopsis
|
MEVNNETMQKSKFGRICVFCGSSQGKKSSYQDAAVDLGNELVLRNIDLVYGGGSIGLMGLVSQAVHDGGRHVIGVIPKTLMPRELTGETVGEVRAVADMHQRKAEMARHSDAFIALPGGYGTLEELLEVITWAQLGIHDKPVGLLNVDGYYNSLLSFIDKAVEEGFISTNARQIIISAPTAKELVKKLEEYSPCHESVATKLCWEIERIDYSSED
|
Cytokinin-activating enzyme working in the direct activation pathway. Phosphoribohydrolase that converts inactive cytokinin nucleotides to the biologically active free-base forms.
|
Q9LFH3
|
Q68XR7
|
RL9_RICTY
|
50S ribosomal protein L9
|
typhus group
|
MEIILIKPVRKLGKIGDILKVANGFGRNYLLPQKLAIRATKSNKELIVKQKHEFEAKDKQIRAEVEKINTLIKDQQLVFIRQTSDDCKLFGSVTNKDIADKLSKNISYNISHSNVILDKQIKSTGIYTVEIRLHAELTAIVTVIVARSDSEAQDYLREQKTENSADLAESE
|
Binds to the 23S rRNA.
|
Q68XR7
|
Q67YU0
|
CKX5_ARATH
|
Cytokinin oxidase 5
|
Arabidopsis
|
MNREMTSSFLLLTFAICKLIIAVGLNVGPSELLRIGAIDVDGHFTVHPSDLASVSSDFGMLKSPEEPLAVLHPSSAEDVARLVRTAYGSATAFPVSARGHGHSINGQAAAGRNGVVVEMNHGVTGTPKPLVRPDEMYVDVWGGELWVDVLKKTLEHGLAPKSWTDYLYLTVGGTLSNAGISGQAFHHGPQISNVLELDVVTGKGEVMRCSEEENTRLFHGVLGGLGQFGIITRARISLEPAPQRVRWIRVLYSSFKVFTEDQEYLISMHGQLKFDYVEGFVIVDEGLVNNWRSSFFSPRNPVKISSVSSNGSVLYCLEITKNYHDSDSEIVDQEVEILMKKLNFIPTSVFTTDLQYVDFLDRVHKAELKLRSKNLWEVPHPWLNLFVPKSRISDFDKGVFKGILGNKTSGPILIYPMNKDKWDERSSAVTPDEEVFYLVALLRSALTDGEETQKLEYLKDQNRRILEFCEQAKINVKQYLPHHATQEEWVAHFGDKWDRFRSLKAEFDPRHILATGQRIFQNPSLSLFPPSSSSSSAASW
|
Catalyzes the oxidation of cytokinins, a family of N(6)-substituted adenine derivatives that are plant hormones, where the substituent is an isopentenyl group.
|
Q67YU0
|
Q14JC3
|
RS7_FRAT1
|
30S ribosomal protein S7
|
Francisella
|
MSRRNRAPKRDILPDPKYKSQVVAKFVNHIMLSGKKSIAEKIVYGAFDKIKAKDASANEVEVFEKALESVSPMVEVKSRRVGGATYQVPVEVRPERRQTLGMRWIIDAARKRKENTMGDRVAAEILEAVEGRGAAVKKREDTHKMAEANKAFAHFRW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA.
|
Q14JC3
|
Q60879
|
OLF3_MOUSE
|
Olfactory receptor 136-14
|
Mus
|
MRLKNHSSVSEFLLLGFPIRPEQGGIFFSLFLAMYLITVLGNLLIILLIRLDSHLHTPMYFFLSHLAFTDISFSSVTVPKMLTKVQNQPIPITYEECVSQTYFFIFFADLDSFLITSMAYDRYMAICHPLHYITIMSQSRCAMLVAVSWVIASACALLHSLLLDQLSFCADHTVPHFFCDLGALLKLSCSDTSLNQLVIFTAGLAAIMLPFLCILISYGRIGFTILQVPTTKGICKALSTCGSHLSVVALYYGSIIGLYFLPPSNSKINNNIVASVMYTVVTPMLNPFIYSLRNKDMKGALKKLLSKKTEFSK
|
Odorant receptor.
|
Q60879
|
A5E625
|
YAE1_LODEL
|
Protein YAE1
|
Lodderomyces
|
MQPSYKDLHCACQSNSQTNQSSVYSMSDDIWEDDDEDEEQEEYDRGDNSNDYNKDGVGSRQQNKQTQSLAMNEIARRHRKQGYVDGLAKHQEENLQKGFDFAYSIGADLGIKVGRLLARACIADGANNDLKDKSGGSGNDLGSLKECMNALNISKVLDLKYFDDHLNLKDGKHGLIEEWQNKSN
|
The complex LTO1:YAE1 may function as a target specific adapter that probably recruits apo-RPLI1 to the cytosolic iron-sulfur protein assembly (CIA) complex machinery. May be required for biogenesis of the large ribosomal subunit and initiation of translation.
|
A5E625
|
Q3T905
|
CBPB_HELZE
|
Carboxypeptidase B
|
Helicoverpa
|
MKFLLVLALCAVVYAKHEAYIGWKSYYVGVATDAQAKALEPLIQKYELDFLSHPTKSREGVVLVKPQHQAGFVQDIEAGGITYRIHADDVKRQLEFDDQLIEMQRMSSFTRTAGRQLPYDNYQELEVIDEYLDYIGEKYPDVATVVNAAESFEGRPIKYIKISTTNFEDENKPVIFIDGGIHAREWISPPSVTWAIHKLVEDVTENDLLEKFDWILLPVVNPDGYKYTFTNERFWRKTRSTNNNPLSQICRGADGNRNFDFVWNSIGTSNSPCSDIYAGTSAFSEVETRVVRDILHEHLARMALYLTMHSFGSMILYPWGHDGSLSQNALGLHTVGVAMASVIQSNALPNFPPYTVGNSALVIGYYIAGSSEDYAHSIGVPLSYTYELPGLSSGWDGFHLPPQYIEQVCRETWEGIVVGARRAGDLFRK
|
Metalloprotease which cleaves a single amino acid from the C-terminal end of polypeptide chains. Shows a strong preference for peptides with a terminal lysine residue.
|
Q3T905
|
P48651
|
PTSS1_HUMAN
|
Serine-exchange enzyme I
|
Homo
|
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECEDGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
|
Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine . Catalyzes mainly the conversion of phosphatidylcholine . Also converts, in vitro and to a lesser extent, phosphatidylethanolamine .
|
P48651
|
A1DH62
|
NAGS_NEOFI
|
N-acetylglutamate synthase
|
Aspergillus subgen. Fumigati
|
MSPHTGWPRTVNSSLLKKHRSSLCTCQHTSSFLPRSFSTTADRHVQQSADFSSTSRSYDRLGRRAKEKLLDREFFLSLLSSASTKREAKSYLARLKAQYPKSPDENKPEPEKLATAPTLPSGVNLGSFYGASRSVYESPVFRQGPSPTAPPSLEPVERLHLALVRLSTPQSLDDNIIDGVAKTLSQLNRLGLTCCVVVDPGTEGVASTLRQVAIEQADRLAVAIQKQPDSKSLRLDSVFSIDASRPGLPQVSSRKALLNPLRHGHTVILTPIAYTEDVPRAIIVPANDAVLALTKELAGLASTPDPDEDPMVTAERIGRLQKEVSLDRVILLDSLGGIPAFNRRQTSHVFINMEQEYDDIENELLQAREMVPATETSLLKAGPSSIADNNPVSKFVNAEVVPVPSGPTQELKTAAPQRSAIEGHLENLRVAQKALTMLPAASSGIITSPFEVASSAQPSPTSEFSAVGTRRQRNPLIHNLLTDKPLLSSSLPMSRRGPTNNGQGTVYPVTSHTTFVKRGMPLTMLPNPWTEPWTPQSRPRLKLDDPSIDLPRLVHLIEDSFDRKLDVQDYLNRVNDRLAGLIIAGEYEGGAILTWELPPGVEDDGSEASNARMVPYLDKFAVLKRSQGAGGVADIVFNAMVRSCFPNGVCWRSRKNNPVNKWYFERSLGTWKLSDTNWTMFWTTPSLVEDSQKFRDYEAVCRSTQPSWADDTGVVD
|
N-acetylglutamate synthase involved in arginine biosynthesis.
|
A1DH62
|
A6GVQ2
|
SYM_FLAPJ
|
Methionyl-tRNA synthetase
|
Flavobacterium
|
MIQNPKRYTITAALPYTNGPIHIGHLAGVYMPSDIYSRYLRLQGKDVAFMCGSDEHGVAISMKAKKEGITPQEVIDKYDGIIRKSFVDFGISFDNYSRTSAKIHHDTASEFFKKLYDKGDFIEEVTEQLYDAKADQFLADRFVVGTCPKCGNEEAYGDQCEKCGSTLNATDLINPKSTITGETPIMKSTKHWFLPLDRYSDFLTKWILEGHKSDWKPNVYGQVKSWIDGGLEPRAVTRDLDWGIDVPVAGAEGKKLYVWFDAPIGYISATKEWAAREGKDWELYWKNEDTKLVHFIGKDNIVFHCIIFPAMLKAEGSYILPDNVPANEFLNLEGNKLSTSKNWAVWLHEYLEDFPNQQDVLRYALTANAPESKDNDFTWKDFQARNNNELAAIFGNFINRVVVLTNKYYEGVVPTPNKFSEVDEATLTELKAYPAVISSSIERYRFREALGELMNVARLGNKYLADEEPWKMVKTDPERVKTQMYVALQIATALRVLCEPFLPFTAEKLNKMLKIDAKLSWNDVTTNSDLILAGHKIGEGEILFAQIEDEQIQKQIDKLEATKTANIAENKKAEPQKELIQYDDFAKMDLRVGTIIEAEKMPKANKLLVLKVDTGIDVRTIVSGIAESFSPEEIIGKQVTVLVNLAPRALRGIESQGMILMTNLPDGKLAFVNPDVAGVGNGEGIN
|
Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
|
A6GVQ2
|
B7NL16
|
LPXH_ECO7I
|
UDP-2,3-diacylglucosamine diphosphatase
|
Escherichia
|
MATLFIADLHLCAEEPAITAGFLRFLAREARKADALYILGDLFEAWIGDDDPNPLHRQMAAAIKAVSDSGVPCYFIHGNRDFLLGKRFARESGMTLLPEEKVLELYGRRVLIMHGDTLCTDDIGYQAFRAKVHKPWLQTLFLALPLFVRKRIAARMRANSKEANSSKSLAIMDVNQNAVVSAMEKHQVQWLIHGHTHRPAVHELIANQQPAFRVVLGAWHTEGSMVKVTADDVELIHFPF
|
Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
B7NL16
|
P42890
|
COL_RABIT
|
Colipase
|
Oryctolagus
|
MEKVLVLLLVALSVAYAAPGPRGIVINLEEGELCLNSAQCKSGCCHHSSALSLARCAPKASENSECSPQTIYGVYYKCPCERGLTCEGDKSIVGSITNTNFGVCLDV
|
Enterostatin has a biological activity as a satiety signal.
|
P42890
|
Q97A63
|
CBID_THEVO
|
Cobalt-precorrin-6A synthase
|
Thermoplasma
|
MMYASDGSGVNPFQQYGITTGLTAAAAAKACTLTVLKGVQNRVVVPTPIGIRIEVKVVESVRIDESSGYASAEKFSGDNPDQLNGITIRCHCKVVKKQENGRSKITISGNAGIGVVEKDGLGIRPGEKAISQGARKMIEDAVREAAGGYDVELSISVPNGEEFAKLTMNEKVGVFGGISVLGTTGIEEPVSTEEYELHLKYIVAAGRCVSKIIVLCPGNTALKFAKKYFALPDKAFVLIGDKVGAAVSASIESAYDHVVIFGLPGKLVKIAAGIYNTHSKVADGRMETLAAVAAMYGISKGAVKRIMESSNTGEAISIIEQEGIVAEVLNTIASRISNRLKADFSRSVGFSVVIIDHDGKIIGSHLDGHIKEVLKYGK
|
Catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A.
|
Q97A63
|
C1F127
|
RSMA_ACIC5
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Acidobacterium
|
MRGGWGRFPPKSREVAAISGKHKPKLGQNFLVSEAACRSIVEALGNLGARTVVEIGPGKGAITELLANRAERLIAIELDRELAPRLRERFARRETVTVIEDDVLRVDLSALARPGEKLLVVGNLPYYMTSEILLHLIRHEAAIERAVVMVQREVADRVAAGPGSRDYGLLSVTAQLHARVEKLLTLPPGAFSPPPEVYSTVLRWTMHSRTDELGVDPTRFTGFLRSCFAQKRKTLGNNLRAAKYEPAAIAGAMQSAGVAAGVRAEELSLEALAALWRTLEDRS
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
C1F127
|
A1K1R8
|
ATPF_AZOSB
|
F-type ATPase subunit b
|
Azoarcus
|
MNLNATLIAQLVVFFILAWFTMKFVWPPIVKALDERAKKIADGLAAADKAKADLALAEKKVVEELRKARESAGDVRASAEKQASQLVDEARAEASRIIAQAREAAEAEAGAAAQRAKEALRDQVAHLAVAGAEKILRREINAQVHAELLANLKQELQ
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
A1K1R8
|
Q5F5T0
|
RL2_NEIG1
|
50S ribosomal protein L2
|
Neisseria
|
MAIVKMKPTSAGRRGMVRVVTEGLHKGAPYAPLLEKKNSTAGRNNNGHITTRHKGGGHKHHYRVVDFKRNKDGISAKVERIEYDPNRTAFIALLCYADGERRYIIAPRGIQAGVVLVSGAEAAIKVGNTLPIRNIPVGTTIHCIEMKPGKGAQIARSAGASAVLLAKEGAYAQVRLRSGEVRKINVDCRATIGEVGNEEQSLKKIGKAGANRWRGIRPTVRGVVMNPVDHPHGGGEGRTGEAREPVSPWGTPAKGYRTRNNKRTDNMIVRRRYSNKG
|
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.
|
Q5F5T0
|
Q6PR31
|
ECTC_VIRPA
|
N-acetyldiaminobutyrate dehydratase
|
Virgibacillus
|
MIVKSLDDIIGTDDETSSDNWTSRRFIMKKDNVGFSLNDTLIKAGTTNFFWYKNHIEAVYCIEGEGEIEKLETGEIYKLKAGTMYLLNEHDKHELRAKTQMRMVCVFNPPLVGTETHTEEGYYPLLTE
|
Catalyzes the circularization of gamma-N-acetyl-alpha,gamma-diaminobutyric acid (ADABA) to ectoine (1,4,5,6-tetrahydro-2-methyl-4-pyrimidine carboxylic acid), which is an excellent osmoprotectant.
|
Q6PR31
|
A6LLN8
|
RS13_THEM4
|
30S ribosomal protein S13
|
Thermosipho
|
MARIVGVEIPNDKKVEIALTYIYGIGKTRAKQICEATNIDPNKRVRELGDEEISKIATFIQQNYKVEGELRTEVMQNIKRLIDIGCYRGLRHKLGLPVRGQKTKSNARTRKGPRPSRIKKKK
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites.
|
A6LLN8
|
B4S5M3
|
RS19_PROA2
|
30S ribosomal protein S19
|
Prosthecochloris
|
MPRSLKKGPFIEGKLEKRILDMNSREEKKVVKTWARSSMISPDFVGHTVAVHNGKTHVPVYISENMVGHKLGEFAPTRTYRGHAGGKAEKGGSAPKRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
B4S5M3
|
C7GPS8
|
ASA1_YEAS2
|
ASTRA-associated protein 1
|
Saccharomyces
|
MRGFSNEIILKRTLTLSDFTLRYHKRGITALQVIKAPSVSNVPVLLSGDNYGYFVMWDLVTKRPITHMEIEGNSHIIAFWWVETTNVLYILSKDSMLRIFELDSSTQRSIDLVRKLSQANKTDHLQWTKIYEMPINTLNFANFIIEAEVKPTKDNKSYRLVCCHTDDSETIDIYQIIEDSTFKLKRPFNNINFPRFLKQQNFLGISKDSKFGIIMRFAKLNDVIFLGYENGFVVGFKITFDEGLQRDIAELVHVSNDHYPNPILDMCVSGDELYSCSTDDFITKYKIPVNLQLETKYLRDDALLIKCPSSLRVSEPSKVHLPLKNIGHIDKVKDDYLVVSSWSGMTIVYNMRTSEVEQTFVKSKNNLVVSDSSMGDLTNGSGSNTESSSKSHNYKVGAMTCLESFDVQSDGLRLGQLRRIKALAKCNWCLIGYEDGTIKLNKI
|
Component of the ASTRA complex involved in chromatin remodeling.
|
C7GPS8
|
Q4QJK4
|
RPOZ_HAEI8
|
Transcriptase subunit omega
|
Haemophilus
|
MARVTVQDAVEKIGNRFDLILTAARRARQLQLNQSAPLVPEDNDKPTVIALREIEKGLINQDIMDAQEFQKMAKVQETEEAAVALITE
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
Q4QJK4
|
A2C9T2
|
COAD_PROM3
|
Pantetheine-phosphate adenylyltransferase
|
Prochlorococcus
|
MRALYPGSFDPLTLGHLDLIERGCALFGEVVVAVLSNPAKTPAFTLQQRFNQIHVATAHCKGVSVISFDGLTVRCARHNQVDLILRGLRAMSDFEYELQIAHTNRSLAPDFETIFLATAAHHSFLSSSMVKEVARFGGNIDHMVPEVVAQDLHRLFN
|
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
|
A2C9T2
|
P24202
|
MRR_ECOLI
|
Mrr restriction system protein
|
Escherichia
|
MTVPTYDKFIEPVLRYLATKPEGAAARDVHEAAADALGLDDSQRAKVITSGQLVYKNRAGWAHDRLKRAGLSQSLSRGKWCLTPAGFDWVASHPQPMTEQETNHLAFAFVNVKLKSRPDAVDLDPKADSPDHEELAKSSPDDRLDQALKELRDAVADEVLENLLQVSPSRFEVIVLDVLHRLGYGGHRDDLQRVGGTGDGGIDGVISLDKLGLEKVYVQAKRWQNTVGRPELQAFYGALAGQKAKRGVFITTSGFTSQARDFAQSVEGMVLVDGERLVHLMIENEVGVSSRLLKVPKLDMDYFE
|
Involved in the acceptance of foreign DNA which is modified. Restricts both adenine- and cytosine-methylated DNA.
|
P24202
|
P39802
|
CHEW_BACSU
|
Coupling protein CheW
|
Bacillus
|
MTAEIKTGEKMIVFMVNGKEYAISVTQVKSIEKWQKPTRVPGVEPYICGVINLRGVVTPVIDLRKRLNLPEYEITDETRIIIIAYRDIEVGWIVDEANDVITVHESEIESAPEGVQKDTDVSIEQIVKQENRLLNIIDANAVLDKESSQSAVPDQA
|
Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two-component kinase CheA; they are both necessary for efficient chemotaxis.
|
P39802
|
Q6FRT5
|
FLR2_CANGA
|
Flucytosine exporter FLR2
|
Nakaseomyces/Candida clade
|
MYIGAFQDTLFVDMLEYFGWVTVGKEYLDIYRPNGVPVAPNAVAASISGKEEMKQDNQTSTDSMSTSTQQETDASNEDIERAMDTDNGLDKAMSGGQGVFGTEEDDSSTKDASKPEEADPFLVEFLGEDDPRKPWNWSFSKKTFVIVQLMVLTCINYMGSSIYTPGQEQIQHEFHVGHVVGTLNLSMYVLGYAIGPIIFSPLSEVSSIGRMPLYLWTFILFTILQVACALVRNIAGLVILRFITGILCSPVLATGGASVGDVCFPRYVPRFLGAWAVGAVAAPVMAPILGAAMVVAKDWRWIFWLMLFMCGATLLSIIFFFPETSHECILHRRAKRLRKLTGDDRYYTKKEKQEEALPVSVFIKNTLWRPIKMIALEPIILAFDVYIALCYGAFYLFFEAFPIVFAGIYHFTLVEVGLAFLGFCVGCVFAYTALIIFQEKVIRKKFLEGKFRPELFLILAMCLGWCLPFSLFFFGWTARIHWILPIIAELFFVLSVFNLFQATFSYLAVCYPEYVASVFAGNGLCRGAFAAAFPLFGKAMYDRLSTKKYPVAWGSTLIGFITVVLSLIPFVLYKYGPALRARSRFSPDS
|
Multidrug transporter that confers resistance to 5-flucytosine (5-FC) and clotrimazole . Further confers azole drug resistance . Plays direct roles in extrusion of 5-flucytosine and clotrimazole .
|
Q6FRT5
|
Q7V3V8
|
UREG_PROMM
|
Urease accessory protein UreG
|
Prochlorococcus
|
MSSKLRLGVAGPVGSGKTALVEAMCRRLRDQLQLAVVTNDIYTQEDAEFLTRVGALEPERIRGVETGGCPHTAIREDCSINRAAVEDLERNFPDLDVVLVESGGDNLAASFSPELVDLCIYVIDVAAGDKIPRKGGPGITRSDLLVINKIDLAVHVGADLEVMKRDTTRMRGERPWCFTNLRSGDGLESVLHFLLQQLPNRP
|
Facilitates the functional incorporation of the urease nickel metallocenter. This process requires GTP hydrolysis, probably effectuated by UreG.
|
Q7V3V8
|
O42945
|
DHX15_SCHPO
|
Probable pre-mRNA-splicing factor ATP-dependent RNA helicase prp43
|
Schizosaccharomyces
|
MEPAQKKLRQESKNPYLAHLNNGDDSEEVVSSKGLTRRATTVAQAAKAEEGPNNFFNDKPFSQNYFKILETRRELPVYQQREEFLKIYHENQIIVFVGETGSGKTTQIPQFVLYDELPHLTNTQIACTQPRRVAAMSVAKRVADEMDVDLGEEVGYNIRFEDCSGPNTLLKYMTDGMLLREAMTDHMLSRYSCIILDEAHERTLATDILMGLMKRLATRRPDLKIIVMSATLDAKKFQKYFFDAPLLAVPGRTYPVEIYYTQEPERDYLEAALRTVLQIHVEEGPGDILVFLTGEEEIEDACRKITLEADDLVREGAAGPLKVYPLYGSLPPNQQQRIFEPTPEDTKSGYGRKVVISTNIAETSLTIDGIVYVVDPGFSKQKIYNPRIRVESLLVSPISKASAQQRAGRAGRTRPGKCFRLYTEEAFRKELIEQTYPEILRSNLSSTVLELKKLGIDDLVHFDYMDPPAPETMMRALEELNYLNCLDDNGDLTPLGRKASEFPLDPNLAVMLIRSPEFYCSNEVLSLTALLSVPNVFVRPNSARKLADEMRQQFTHPDGDHLTLLNVYHAYKSGEGTADWCWNHFLSHRALISADNVRKQLRRTMERQEVELISTPFDDKNYYVNIRRALVSGFFMQVAKKSANGKNYVTMKDNQVVSLHPSCGLSVTPEWVVYNEFVLTTKSFIRNVTAIRPEWLIELAPNYYDLDDFDNNKEVKSALQKVYQMAARSKKNARR
|
Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA.
|
O42945
|
Q6YXM0
|
PETL_PHYPA
|
Cytochrome b6-f complex subunit VI
|
Physcomitrium
|
MLTIISYFGFLFGALTLALILFIGLNKIQLI
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions. PetL is important for photoautotrophic growth as well as for electron transfer efficiency and stability of the cytochrome b6-f complex.
|
Q6YXM0
|
Q97E91
|
SP5G_CLOAB
|
Putative septation protein SpoVG
|
Clostridium
|
MQITDVRIRKITSEGKMKAIVSVTFDNEFVVHDIKVIEGQNGLFIAMPSRKTPDGEFKDIAHPINTATREKIQSAILAEYEKVKNEEETKTETEE
|
Could be involved in septation.
|
Q97E91
|
Q8GQN9
|
BCLA_THAAR
|
Benzoyl-CoA synthetase
|
Thauera
|
MYTLSVADHSNTPPAIKIPERYNAADDLIGRNLLAGRGGKTVYIDDAGSYTYDELALRVNRCGSALRTTLGLQPKDRVLVCVLDGIDFPTTFLGAIKGGVVPIAINTLLTESDYEYMLTDSAARVAVVSQELLPLFAPMLGKVPTLEHLVVAGGAGEDSLAALLATGSEQFEAAPTRPDDHCFWLYSSGSTGAPKGTVHIHSDLIHTAELYARPILGIREGDVVFSAAKLFFAYGLGNGLIFPLAVGATAVLMAERPTPAAVFERLRRHQPDIFYGVPTLYASMLANPDCPKEGELRLRACTSAGEALPEDVGRRWQARFGVDILDGIGSTEMLHIFLSNRAGDVHYGTSGKPVPGYRLRLIDEDGAEITTAGVAGELQISGPSSAVMYWNNPEKTAATFMGEWTRSGDKYLVNDEGYYVYAGRSDDMLKVSGIYVSPIEVESALIAHEAVLEAAVVGWEDEDHLIKPKAFIVLKPGYGAGEALRTDLKAHVKNLLAPYKYPRWIEFVDDLPKTATGKIQRFKLRSA
|
Catalyzes the ligation of benzoate and CoA to form benzoyl-CoA at the expense of ATP. The enzyme also ligates 2-aminobenzoate and CoA. The enzyme shows activity toward a number of benzoate derivatives.
|
Q8GQN9
|
Q6N075
|
MFSD5_HUMAN
|
Molybdate transporter 2 homolog
|
Homo
|
MLVTAYLAFVGLLASCLGLELSRCRAKPPGRACSNPSFLRFQLDFYQVYFLALAADWLQAPYLYKLYQHYYFLEGQIAILYVCGLASTVLFGLVASSLVDWLGRKNSCVLFSLTYSLCCLTKLSQDYFVLLVGRALGGLSTALLFSAFEAWYIHEHVERHDFPAEWIPATFARAAFWNHVLAVVAGVAAEAVASWIGLGPVAPFVAAIPLLALAGALALRNWGENYDRQRAFSRTCAGGLRCLLSDRRVLLLGTIQALFESVIFIFVFLWTPVLDPHGAPLGIIFSSFMAASLLGSSLYRIATSKRYHLQPMHLLSLAVLIVVFSLFMLTFSTSPGQESPVESFIAFLLIELACGLYFPSMSFLRRKVIPETEQAGVLNWFRVPLHSLACLGLLVLHDSDRKTGTRNMFSICSAVMVMALLAVVGLFTVVRHDAELRVPSPTEEPYAPEL
|
Mediates high-affinity intracellular uptake of the rare oligo-element molybdenum.
|
Q6N075
|
Q8RU95
|
4CLL6_ORYSJ
|
4-coumarate--CoA ligase-like 6
|
Oryza sativa
|
MSKRSPPPQPAHIPMAEQRWRPPYPYASSAAGGGGVDRRSRSGFCAATRTFHSLRSVGPLPPEELPLTVAAYAFSLLSSAPPLVVAGRGPALVDAATGIAVSYPAFVARVRFLAGGLWCSLGLRPGDVALVVSPSCLDVAVLYFALMSIGVVVSPANPASTADEYAHQVRLSRPAIAFVAPEVAARLPRHVSRVVIGSEVFDRLASASAAGGWAAPPAVAMKQPSTAALLYSSGTTGRVKAVAITHRNLIAQISAYNAIRETVAREAATDAGKGKPPPPSPSPPAAVTLFPLPLFHVMGFGLLTRTISSGETAVVMRRFDLAAAARAVERYRVTKLSAAPPVVVALTKSDEARRRDLSSLVAIVVGGAPLGREVSQRFATVFPSVQIVQSYGLTESTGPVATMAGPEESAAYGSVGRLAPRVQAKIVDTATGEVLGPGRRGELWIRGPVVMKGYVGDPEATAATITPDGWLKTGDLCYFNEDGYLYVVDRLKELIKYKGYQVPPAELEHILQSRPEIADAAVVPYPDEEAGQLPMAFVVRQPGAYLTEQQVMNCVAKHVAPYKKVRRVAFVNAIPKSPAGKILRRELVLQAMASTSRL
|
Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
|
Q8RU95
|
A9M383
|
IHFA_NEIM0
|
Integration host factor subunit alpha
|
Neisseria
|
MTLTKAELADILVDKVSNVTKNDAKEIVELFFEEIRSTLASGEEIKISGFGNFQLRDKPQRPGRNPKTGEEVPITARRVVTFHASQKLKSMVEHYYDKQR
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
A9M383
|
Q8EFV9
|
FABA_SHEON
|
Trans-2-decenoyl-[acyl-carrier-protein] isomerase
|
Shewanella
|
MNKANSFNKEELIACGHGKLFGPNSPRLPVDNMLMIDRIITINDNGGEFGKGEIVAELDIKPELWFFDCHFITDPVMPGCLGLDAMWQLVGFYLGWEGAEGKGRALGVGEVKFTGQVLPGAKKVTYKLNIKRTIHRKLVMGIADAILEVDGRQIYSATDLKVGVFSDTSTF
|
Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length.
|
Q8EFV9
|
Q18JW6
|
G1PDH_HALWD
|
sn-glycerol-1-phosphate dehydrogenase
|
Haloquadratum
|
MLKKTTWIKLPRNVLVGHDVIGDLAAAIEELYLDGRPLIVTSPTPDQLIGNRVRSQFADPQTVSVDHASFDAVEAVIDTAKATDAGYLIGLGGGKPIDTAKMASDRLGCGFVSVPTAASHDGIVSGRSSIPEGDTRHSVAADPPLAVVADTAVLAEAPWELTTAGCADIISNYTAVKDWQLAHRLQDVEYSEYAGALSQMTAEMLVDNSDAIKQGFEESAWLVAKALVSSGVAMSIAGSSRPASGAEHLISHQLDRLVPDAALHGHQVGVASIVTAYLHTGENGEWEDIRAALADVGAPTTATELGIDEEIFIQAITSAHAIRDRHTILGNGVSEAAAREAAVFTDVC
|
Catalyzes the NAD(P)H-dependent reduction of dihydroxyacetonephosphate (DHAP or glycerone phosphate) to glycerol 1-phosphate (G1P). The G1P thus generated is used as the glycerophosphate backbone of phospholipids in the cellular membranes of Archaea.
|
Q18JW6
|
O66426
|
YZ38_AQUAE
|
Probable protein adenylyltransferase aq_aa38
|
Aquifex
|
MTYQNGVEVLLEEFLDYLTKEETICSLEIEKLKVSIDELEKETDEPRVLQGINYFRTAKEVYQLSRKAYETKEEVVSEALILWIYENLWKGFNVPKGYRKSDMVIFGAKFSPPPPYVVPNLIRTIVNWLRNEKTIDVVKKSIIFHTLFEVIHPFPDGNGRVGRILLNAILVENGLLNVAFRNREKYISALREAEEGAIVVVEKLSRGRKIDYSSITETVEYYGNLNVFDELIRTEMMHSLKVYSNIKQVFLTPEEAAKLLGLKNKDYVRVLIHRGKLKAVKEEGKWKIPLSEVVKNFEHKLKGEEFKLANNLFKGKLSPS
|
Probable adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.
|
O66426
|
Q8K0C4
|
CP51A_MOUSE
|
Sterol 14-alpha demethylase
|
Mus
|
MVLLGLLQSGGWVLGQAMEQVTGGNLLSTLLIACAFTLSLVYLFRLAVGHMVQLPAGAKSPPHIYSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNSKNEDLNAEEVYGRLTTPVFGKGVAYDVPNAIFLEQKKIIKSGLNIAHFKQYVPIIEKEAKEYFQSWGESGERNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFTHAAWLLPAWLPLPSFRRRDRAHREIKNIFYKAIQKRRLSKEPAEDILQTLLDSTYKDGRPLTDEEISGMLIGLLLAGQHTSSTTSAWMGFFLAKDKPLQEKCYLEQKAVCGEDLPPLTYDQLKDLNLLDRCIKETLRLRPPIMTMMRMAKTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWAERLDFNPDRYLQDNPASGEKFAYVPFGAGRHRCVGENFAYVQIKTIWSTMLRLYEFDLINGYFPTVNYTTMIHTPENPVIRYKRRSK
|
A cytochrome P450 monooxygenase involved in sterol biosynthesis. Catalyzes 14-alpha demethylation of lanosterol and 24,25-dihydrolanosterol likely through sequential oxidative conversion of 14-alpha methyl group to hydroxymethyl, then to carboxylaldehyde, followed by the formation of the delta 14,15 double bond in the sterol core and concomitant release of formic acid. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
|
Q8K0C4
|
Q2K9C7
|
AZOR1_RHIEC
|
FMN-dependent NADH-azoreductase 1
|
Rhizobium
|
MSSILLLTSSPRAESLSTPIAADLAEKLKNQKPGSVVVRRDLAATPLPHIDDLFTGAIRKPAEARTAEEIAAVKTSDELVAELFAADTIVISTGLINFNIYSSLKTWIDNVARAGVTFKYTESGPVGLVTGKKVYVVLASGGVYSQGPAAPLNHAVPYLKSVLGFLGITDIETIYVEGLAFGPEAAEKAIGAAKSRVEEIALAA
|
Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines.
|
Q2K9C7
|
Q75WV3
|
TPP1_ORYSJ
|
Trehalose 6-phosphate phosphatase
|
Oryza sativa
|
MDLSNSSPVITDPVAISQQLLGGLPSNLMQFSVMPGGYSSSGMNVGVSRLKIEEVLVNGLLDAMKSSSPRRRLNVAFGEDNSSEEEDPAYSAWMAKCPSALASFKQIVASAQGKKIAVFLDYDGTLSPIVDDPDKAVMSPVMRAAVRNVAKYFPTAIVSGRSRNKVFEFVKLKELYYAGSHGMDIMAPSANHEHSAEKSKQANLFQPAHDFLPMIDEVTKSLLQVVSGIEGATVENNKFCVSVHYRNVAEKDWKLVARLVNEVLEAFPRLKVTNGRMVLEVRPVIDWDKGKAVEFLLQSLGLNDSENVIPIYIGDDRTDEDAFKVLRQRNCGYGILVSQVPKETEAFYSLRDPSEVMEFLNFLVRWKKHSV
|
Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant improves abiotic stress tolerance.
|
Q75WV3
|
Q5F5X9
|
RNH2_NEIG1
|
Ribonuclease HII
|
Neisseria
|
MHILTAGVDEAGRGPLVGSVFAAAVILPETFDLPGLTDSKKLSEKKRDALAEMIKEQAVAWHVAASTPEEIASLNILHATMLAMKRAVYGLAARPEKIFIDGNRIPEHLGIPAEAVVKGDSKIIEISAASVLAKTARDAEMYALAQRRPQYGFDKHKGYGTKQHLEALKQYGVLPEHRRDFAPVRNLLAQQALF
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q5F5X9
|
Q7FZF1
|
CNBL5_ARATH
|
SOS3-like calcium-binding protein 4
|
Arabidopsis
|
MGCVCSKQLEGRRQEDISLLASQTFFSEAEVEVLHGLFIKLTSCLSNDNLLTKEKFQFILIKNTKKRSLSAERIFGLFDMRNDGAIDFGEFVHTLNIFHPNSSPRDKAIFAFRLYDTRETGFIEPEEVKEMIIDVLEESELMLSESIIDSIVSKTFEEADWKKDGIIDLEEWENFVATYPLTLKNMTIPFLKDIPRIFPTFLR
|
Acts as a calcium sensor. CBL proteins interact with CIPK serine-threonine protein kinases. Binding of a CBL protein to the regulatory NAF domain of a CIPK protein lead to the activation of the kinase in a calcium-dependent manner. May function as a positive regulator of salt or drought responses.
|
Q7FZF1
|
O87877
|
BCRD_THAAR
|
3-hydroxybenzoyl-CoA reductase subunit delta
|
Thauera
|
MTITAGIDIGTGAVKTVLFRVEGDKTEWLAKRNDRIRQRDPFKLAEEAYNGLLEEAGLKASDVDYVATTGEGESLAFHTGHFYSMTTHARGAVYLNPEARAVLDIGALHGRAIRNDERGKVETYKMTSQCASGSGQFLENIARYLGIAQDEIGSLSTQADNPEVVSSICAVLAETDVINMVSRGISAPNILKGIHISMAGRLAKLLKSVGARDGVVLCTGGLALDEGLLKTLNESIQEQKMAVVAYNHPDSPYAGAIGAALWGAFRHEKLARLGQQQVAEAA
|
Catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring.
|
O87877
|
A1B028
|
RL4_PARDP
|
50S ribosomal protein L4
|
Paracoccus
|
MKLDVITLDAGKAGDIDLSDDIFGLEPRADLLHRVVRWQRAKAQAGTHSVLGKSDVSYSTKKIYRQKGTGGARHGSRKAPIFRHGGVYKGPTPRSHAFDLPKKVRALGLKHALSAKAAAGELVVVDSLNIAEAKTAAVAKAVKENGWKRVLVIDGAEVNENFARAARNLEGVDVLPSMGANVYDILRRDTLVLTRAGVEALEARLK
|
Forms part of the polypeptide exit tunnel.
|
A1B028
|
B1G889
|
OIAK_PARG4
|
3-oxo-isoapionate kinase
|
Paraburkholderia
|
MNGTEPAEPTNGTNATAWPAGLLLAYYGDDFTGSTDAMEAMQAAGVPTVLCLQKPTPELLARFPEVRCVGMAGSSRGRSSAWMDDELPDVLASLAALGAPILQYKVCSTFDSSPEVGSIGRAIDIGVRHMPGNWSPMVIGAPRLKRYQMFGNLFAAVDGVGYRLDRHPTMSRHPVTPMNEADLRLHLARQTARRIELIDMLELRGADVATRVRALCAPDMPVVLIDVLDEETLAEAGRLVWEQRGEGIFTASSSGLQYALAAHWRARGLLPPTPSLPAADPVQAIAAVSGSCSPVTAAQIGWARAHGFHTERLDLPRALDSRDGAAEIERVVTAATQALTRGISVIVHSAEGPDDPAVTGFDAIASAAGFARHDAARKVGRALAEVMRRLLDSVELTRVVVAGGDSSGEVASVLGIDALSVMAGLVPGAPLCRAWSAEPRRDGLQIVLKGGQIGDATFFGMVREGRLAGA
|
Involved in catabolism of D-apiose. Catalyzes the phosphorylation of 3-oxo-isoapionate to 3-oxo-isoapionate 4-phosphate.
|
B1G889
|
Q3HVN1
|
AGUB_SOLTU
|
N-carbamoylputrescine amidase
|
Solanum
|
MAEKNRLVTVAALQFACTDDVSTNVATAERLVRAAHQKGANIILIQELFEGYYFCQAQKEEFFHRAKPYLGHPTIVRMQNLAKELGVVIPVSFFEEANNAHYNSVAIIDADGTDLGLYRKSHIPDGPGYQEKFYFNPGDTGFKVFQTKYAKIGVAICWDQWFPEAARAMALQGAEVLFYPTAIGSEPQDDGLDSRDHWRRVMQGHAGANVVPLVASNRIGKEIIETEHGNSEITFYGYSFIAGPTGELVAAAGDKEEAVLVAQFDLDKIKSKRHGWGVYRDRRPDLYKVLLTLDGSNPVK
|
Involved in polyamine biosynthesis.
|
Q3HVN1
|
B7HII4
|
PDXT_BACC4
|
Pyridoxal 5'-phosphate synthase glutaminase subunit
|
Bacillus cereus group
|
MVKIGVLGLQGAVREHVKSVEASGAEAVVVKRIEQLEEIDGLILPGGESTTMRRLIDKYAFMEPLRTFAKSGKPMFGTCAGMILLAKTLIGYEEAHIGAMDITVERNAFGRQKDSFEAALSIEGVGEDFVGVFIRAPYVVEVADNVEVLSKHGNRMVAVRQDQFLAASFHPELTDDHRVTAYFVEMVKEAKMKKVV
|
Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS.
|
B7HII4
|
Q5E9Q4
|
NECP2_BOVIN
|
NECAP endocytosis-associated protein 2
|
Bos
|
MEEAEYESVLCVKPDVHVYRIPPRATNRGYRAAEWQLDQPSWSGRLRITAKGQVAYIKLEDRTSGELFAQAPVDQFPGTAVESVTDSSRYFVIRIEDGNGRRAFIGIGFGDRGDAFDFNVALQDHFKWVKQQCEFAKQAQNPDQGPKLDLSFKEGQTIKLNIASMKKKDGAAGTPRARPTSTGGLSLLPPPPGAKTAALAPLSGEHLSVGGSVVQPAVSPSSGGATVSWPQPKPATTATADIWGDFTKSTGSTSSQTQPGAGWVQF
|
Involved in endocytosis.
|
Q5E9Q4
|
Q6DGV1
|
CELF4_DANRE
|
RNA-binding protein BRUNOL-4
|
Danio
|
MATLTNGQVDAAVHGGAASTNGLVNGISHTHSPASCATIPMKDHDAIKLFIGQIPRNLDEKDLRPLFEEFGKIYELTVLKDRFTGMHKGCAFLTYCARESALKAQTALHEQKTLPGMNRPIQVKPADSESRGEDRKLFVGMLNKQQCEDDVRRLFESFGSIEECTILRGPDGNSKGCAFVKYSTHAEAQAAISALHGSQTMPGASSSLVVKFADTDKERTIRRMQQMAGQMGIFNPMALQFGAYGAYAQVQQQAALMASVGQGGYLSPMAAFAAAQMQHMATINGLPGAPMTPTSGGSTPPGITAPTVTSIPSPISVNGFTGLPPPQANGQAPAEAMFTNGIHPYPVLQEVVFREDSEKGGLGVAQRSCFGVQGSCFLSSLSEAQSPTAADPLQQAYAGVQQYAAFPAAYGQISQAFPQPPPIIPQQQREGPEGCNLFIYHLPQEFGDGELMQMFLPFGNVISSKVFVDRATNQSKCFGFVSFDNPGSAQAAIQSMNGFQIGMKRLKVQLKRPKDANRPY
|
RNA-binding protein that may be implicated in the regulation of pre-mRNA alternative splicing.
|
Q6DGV1
|
A0A1D8PQG0
|
NAG3_CANAL
|
Transmembrane protein 1
|
Candida
|
MSDNTTLDNISVNSEKVVDYTIHHDDRKELERLVSHNKGVEKIVSELAEGAGQLGPLEQPYDIHKVETHPDPHTDYNDADPWKYPIDKETKLRLVDWTEGDKHNPKNFGKGFKWLCTVLLGMICFVVALGSAIVTGDLERPAADFGVSEEVIILASVTMFVIGFGVGPLVFAPMSEEVGRKPIYVVTLFVAVVFIVPCGAAQNIATLLICRLIDGTAFSAPMTLIGGSLADIWEGPERGTAMAVFSAAPFLGPVCGPIFGGLLCDYAPTWRWVYWTFLIVAGFFYVVFIVVVPETHHGILLKKRAKKLRKDTGDSRYRSFNELQIRTFAQVAKTSLLRPFVLLSELIVFLVTMYMSVLYGLLYMFFFAYPIVYQEGKGWSASKTGVMFIPIGVGVIASSLAAPFFNKDYNRRAQEYRDRGELPPAELRLIPMMIGCWFVPAGLFAFAWSSYQRLSWAGPCFSGFAVGFGFLLLYNPANNYIVDSYQHYAASALAAKTFVRSIWGACVPLFTIQMYHRLGDEWATSLMAFISLACCAIPYLFYIFGARIRTFSKYAYAPNMD
|
MFS transporter involved in N-acetylglucosamine (GlcNAc) uptake . Confers resistance to cycloheximide, 4-nitroquinoline-N-oxide, and 1,10-phenanthroline, and contributes to virulence .
|
A0A1D8PQG0
|
O14981
|
BTAF1_HUMAN
|
TBP-associated factor 172
|
Homo
|
MAVSRLDRLFILLDTGTTPVTRKAAAQQLGEVVKLHPHELNNLLSKVLIYLRSANWDTRIAAGQAVEAIVKNVPEWNPVPRTRQEPTSESSMEDSPTTERLNFDRFDICRLLQHGASLLGSAGAEFEVQDEKSGEVDPKERIARQRKLLQKKLGLNMGEAIGMSTEELFNDEDLDYTPTSASFVNKQPTLQAAELIDSEFRAGMSNRQKNKAKRMAKLFAKQRSRDAVETNEKSNDSTDGEPEEKRRKIANVVINQSANDSKVLIDNIPDSSSLIEETNEWPLESFCEELCNDLFNPSWEVRHGAGTGLREILKAHGKSGGKMGDSTLEEMIQQHQEWLEDLVIRLLCVFALDRFGDFVSDEVVAPVRETCAQTLGVVLKHMNETGVHKTVDVLLKLLTQEQWEVRHGGLLGIKYALAVRQDVINTLLPKVLTRIIEGLQDLDDDVRAVAAASLVPVVESLVYLQTQKVPFIINTLWDALLELDDLTASTNSIMTLLSSLLTYPQVQQCSIQQSLTVLVPRVWPFLHHTISSVRRAALETLFTLLSTQDQNSSSWLIPILPDMLRHIFQFCVLESSQEILDLIHKVWMELLSKASVQYVVAAACPWMGAWLCLMMQPSHLPIDLNMLLEVKARAKEKTGGKVRQGQSQNKEVLQEYIAGADTIMEDPATRDFVVMRARMMAAKLLGALCCCICDPGVNVVTQEIKPAESLGQLLLFHLNSKSALQRISVALVICEWAALQKECKAVTLAVQPRLLDILSEHLYYDEIAVPFTRMQNECKQLISSLADVHIEVGNRVNNNVLTIDQASDLVTTVFNEATSSFDLNPQVLQQLDSKRQQVQMTVTETNQEWQVLQLRVHTFAACAVVSLQQLPEKLNPIIKPLMETIKKEENTLVQNYAAQCIAKLLQQCTTRTPCPNSKIIKNLCSSLCVDPYLTPCVTCPVPTQSGQENSKGSTSEKDGMHHTVTKHRGIITLYRHQKAAFAITSRRGPTPKAVKAQIADLPAGSSGNILVELDEAQKPYLVQRRGAEFALTTIVKHFGGEMAVKLPHLWDAMVGPLRNTIDINNFDGKSLLDKGDSPAQELVNSLQVFETAAASMDSELHPLLVQHLPHLYMCLQYPSTAVRHMAARCVGVMSKIATMETMNIFLEKVLPWLGAIDDSVKQEGAIEALACVMEQLDVGIVPYIVLLVVPVLGRMSDQTDSVRFMATQCFATLIRLMPLEAGIPDPPNMSAELIQLKAKERHFLEQLLDGKKLENYKIPVPINAELRKYQQDGVNWLAFLNKYKLHGILCDDMGLGKTLQSICILAGDHCHRAQEYARSKLAECMPLPSLVVCPPTLTGHWVDEVGKFCSREYLNPLHYTGPPTERIRLQHQVKRHNLIVASYDVVRNDIDFFRNIKFNYCILDEGHVIKNGKTKLSKAVKQLTANYRIILSGTPIQNNVLELWSLFDFLMPGFLGTERQFAARYGKPILASRDARSSSREQEAGVLAMDALHRQVLPFLLRRMKEDVLQDLPPKIIQDYYCTLSPLQVQLYEDFAKSRAKCDVDETVSSATLSEETEKPKLKATGHVFQALQYLRKLCNHPALVLTPQHPEFKTTAEKLAVQNSSLHDIQHAPKLSALKQLLLDCGLGNGSTSESGTESVVAQHRILIFCQLKSMLDIVEHDLLKPHLPSVTYLRLDGSIPPGQRHSIVSRFNNDPSIDVLLLTTHVGGLGLNLTGADTVVFVEHDWNPMRDLQAMDRAHRIGQKRVVNVYRLITRGTLEEKIMGLQKFKMNIANTVISQENSSLQSMGTDQLLDLFTLDKDGKAEKADTSTSGKASMKSILENLSDLWDQEQYDSEYSLENFMHSLK
|
Regulates transcription in association with TATA binding protein (TBP). Removes TBP from the TATA box in an ATP-dependent manner.
|
O14981
|
Q03W30
|
RSMH_LEUMM
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Leuconostoc
|
MPFEHVTVLLHEAIALLDIKPEGTYVDATLGGGGHTGEILKQLTTGTLYSFDQDDTAIQYNAEQYADEIAAGKLVIIHKNFRTLTSALADYGVTAVDGIVYDLGVSSVQFDDGQRGFSYKYDAELDMRMDQRQALTAKTIVNEWPFNELMRVLSRYGEDRFPKQIARKIEQHRENAPINTTFELVDIIKEAIPAPARRKGGHPAKRSFQAFRIAVNDELGALEDSLTQALELLATDGKISVITFQSLEDRLVKQMFREKSSAPELPAGLPVLPGQFEADYELLTRKPISPSTEEMAINHRAESAKLRGIRRK
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
Q03W30
|
A1E9Z6
|
PSBM_AGRST
|
Photosystem II reaction center protein M
|
Agrostis
|
MEVNILAFIATALFILIPTAFLLIIYVKTASQND
|
One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface.
|
A1E9Z6
|
Q2JCG8
|
TAL_FRACC
|
Transaldolase
|
Frankia
|
MSNPLSELSAAGVAVWLDDISRDRLRTGNLAHLVENRGVVGVTSNPTIFQKAISSSDLYDEQLHDLAIRGVDVGEAVRAITAADVRDACDVLRGVYDASGGVDGRVSLEVDPRLAHEAERTLAEARALWWLVDRPNLFIKIPATRAGLSAITETLAQGISVNVTLIFGLDRYDAVIDAFMTGLEKALAAGRDITDLASVASFFVSRVDTEVDQRLEKIGTSEAKALRGRAAVANARLAFERYEKAFATPRWAALAAAGAKPQRPLWASTSTKDPSLPDTIYVTELIAPGTVNTMPEATLEAFADHGSVTGETIRPRYEEAHEVFAQLTAVGIDLDDVIETLESQGVQKFEDSWTQLLDTIAAHLGSAGSSA
|
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
|
Q2JCG8
|
A1WU59
|
IHFA_HALHL
|
Integration host factor subunit alpha
|
Halorhodospira
|
MSLTKADMAERLFEEVGLNKREAKELVELFFEEIRTALENGEPVKLSSFGNFELRDKNERPGRNPKTGEEIPISARRVVTFRPGQKLKSRVESYAGTREEQ
|
This protein is one of the two subunits of integration host factor, a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control.
|
A1WU59
|
B4S4T8
|
PAND_PROA2
|
Aspartate 1-decarboxylase alpha chain
|
Prosthecochloris
|
MRLHLLKSKIHNAIVTSGDLEYEGSITIDSQLLELADMLPNEKVLCVNNNNGERFETYIIKGKAGSREIQLNGAAARCALPGDEIIIMTFAEIEAEKAKDFKPMILIVDHQNNPKRRHLVGEEDTPLPH
|
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
|
B4S4T8
|
P74180
|
FTSW_SYNY3
|
Peptidoglycan polymerase
|
unclassified Synechocystis
|
MITAANLLRIIFPFYDPEVLRWSGEARLMRTLFFAWMAMGVVVLFSASYAESLDTSGTGLSIILKQIAYLWLGLNIFNFLVRLPLQVCLKLVPWFLIVVLLLIFLTKSGLGVEVNGARRWISLGPILIQPSEFMKPCLVLQAANLFGNWHRFPWRSRLIWLGIFALTLGSILLQPNLSTTALCGMGLWLIALASGLPWIYLISTALLGITTAVTSISIRDYQRARVTSFLDPFADPRGDGYQLVQSLYAIASGGVLGRGFGMSQQKLFYLPIQTTDFIFAVFAEEFGLVGCITFLAFLGLFTTMGLRVAMRCRHRVKRLIGLGVVIFLVGQSLLNIGVASGALPTTGLPLPFFSYGGSSCLSSLVLAGLLVRVARESNEAEVIPLGTKTAPAV
|
Peptidoglycan polymerase that is essential for cell division.
|
P74180
|
A4QL18
|
PSAB_DRANE
|
PsaB
|
Draba
|
MALRFPRFSQGLAQDPTTRRIWFGIATAHDFESHDDITEERLYQNIFASHFGQLAIIFLWTSGNLFHVAWQGNFETWIQDPLHVRPIAHAIWDPHFGQPAVEAFTRGGALGPVNIAYSGVYQWWYTIGLRTNEDLYTGALFLLFLSALSLIGGWLHLQPKWKPRVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGEYVRWNNFLNVLPHPQGLGPLFTGQWNLYAQNPDSSSHLFGTSQGSGTAILTLLGGFHPQTQSLWLTDMAHHHLAIAILFLIAGHMYRTNFGIGHSIKDLLEAHIPPGGRLGRGHKGLYDTINNSIHFQLGLALASLGVITSLVAQHMYSLPAYAFIAQDFTTQAALYTHHQYIAGFIMTGAFAHGAIFFIRDYNPEQNEDNVLARMLDHKEAIISQLSWASLFLGFHTLGLYVHNDVMLAFGTSEKQILIEPIFAQWIQSAHGKTSYGFDVLLSSTNGPAFNAGRSIWLPGWLNAINENSNSLFLTIGPGDFLVHHAIALGLHTTTLILVKGALDARGSKLMPDKKDFGYSFPCDGPGRGGTCDISAWDAFYLAVFWMLNTIGWVTFYWHWKHITLWQGNVSQFNESSTYLMGWLRDYLWLNSSQLINGYNPFGMNSLSVWAWMFLFGHLVWATGFMFLISWRGYWQELIETLAWAHERTPLANLIRWKDKPVALSIVQARLVGLAHFSVGYIFTYAAFLIASTSGKFG
|
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
|
A4QL18
|
Q4KGL6
|
CYNS_PSEF5
|
Cyanate lyase
|
Pseudomonas
|
MLQSQFAQAPRLALADTIIDAKARKNLSWQDLTDGTGLSLAFVTAALLGQHALPATAADLVCDKLGLDQDASRLLQSIPLRGSIAGGIPTDPTVYRFYEMLQVYGSTLKALVHEQFGDGIISAINFKLDIKKVEDPEGGSRAVITLDGKYLPTKPF
|
Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
|
Q4KGL6
|
Q8CG19
|
LTBP1_MOUSE
|
Transforming growth factor beta-1-binding protein 1
|
Mus
|
MAGAWLRWGLLLWAGLLAWSAHGRVRRITYVVRPGPGLPAGALPLAGPPRTFNVALDARYSRSSTAASSRALAGPPAERTRRTSQPGGAALPGLRSPLPPEPARPGGPSRQLHSKAGAQTAVTRFAKHGRQVVRSQVQQDAQSAGGSRLQVQQKQQLQGINVCGGQCCHGWSKPPGSQRCTKPSCVPPCQNGGMCLRPQLCVCKPGSKGKACEITAAQDTMPPAFGGQNPGSSWAPLEQAAKHTSTKKADTLPRVSPVAQMTLTLKPKPSMGLSQQIHPQVAPLSSQNVMIRHGQTQEYLLKPKYFPAPKVVSAEQSTEGSFSLRYGQEQGTAPFQVSNHTGRIKVVFTPSICKVTCTKGNCQNSCQKGNTTTLISENGHAADTLTATNFRVVICHLPCMNGGQCSSRDKCQCPPNFTGKLCQIPVLGASMPKLYQHAQQQGKALGSHVIHSTHTLPLTMTSQQGVKVKFPPNIVNIHVKHPPEASVQIHQVSRIDSPGGQKVKEAQPGQSQVSYQGLPVQKTQTVHSTYSHQQLIPHVYPVAAKTQLGRCFQETIGSQCGKALPGLSKQEDCCGTVGTSWGFNKCQKCPKKQSYHGYTQMMECLQGYKRVNNTFCQDINECQLQGVCPNGECLNTMGSYRCSCKMGFGPDPTFSSCVPDPPVISEEKGPCYRLVSPGRHCMHPLSVHLTKQICCCSVGKAWGPHCEKCPLPGTAAFKEICPGGMGYTVSGVHRRRPIHQHIGKEAVYVKPKNTQPVAKSTHPPPLPAKEEPVEALTSSWEHGPRGAEPEVVTAPPEKEIPSLDQEKTRLEPGQPQLSPGVSTIHLHPQFPVVVEKTSPPVPVEVAPEASTSSASQVIAPTQVTEINECTVNPDICGAGHCINLPVRYTCICYEGYKFSEQLRKCVDIDECAQVRHLCSQGRCENTEGSFLCVCPAGFMASEEGTNCIDVDECLRPDMCRDGRCINTAGAFRCEYCDSGYRMSRRGYCEDIDECLKPSTCPEEQCVNTPGSYQCVPCTEGFRGWNGQCLDVDECLQPKVCTNGSCTNLEGSYMCSCHRGYSPTPDHRHCQDIDECQQGNLCMNGQCRNTDGSFRCTCGQGYQLSAAKDQCEDIDECEHHHLCSHGQCRNTEGSFQCVCNQGYRASVLGDHCEDINECLEDSSVCQGGDCINTAGSYDCTCPDGFQLNDNKGCQDINECAQPGLCGSHGECLNTQGSFHCVCEQGFSISADGRTCEDIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQAPQDGQGCVDVNECELLSGVCGEAFCENVEGSFLCVCADENQEYSPMTGQCRSRVTEDSGVDRQPREEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGAGWGDNCEIFPCPVQGTAEFTEMCPRGKGLVPAGESSYDTGGENYKDADECLLFGEEICKNGYCLNTQPGYECYCKQGTYYDPVKLQCFDMDECQDPNSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCVQPTESNEQIEETDVYQDLCWEHLSEEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPMKDSDDYAQLCNIPVTGRRRPYGRDALVDFSEQYGPETDPYFIQDRFLNSFEELQAEECGILNGCENGRCVRVQEGYTCDCFDGYHLDMAKMTCVDVNECSELNNRMSLCKNAKCINTEGSYKCLCLPGYIPSDKPNYCTPLNSALNLDKESDLE
|
Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space. Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta. Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta.
|
Q8CG19
|
A7FVZ3
|
IF2_CLOB1
|
Translation initiation factor IF-2
|
Clostridium
|
MAKIRVYELAKELNISSKELITLLEEEFSVEVKNHMSAIEDEDANLIKELLSGKEKSEKTKEEDDEIETTAKNPIKESMNNKKSNKRDDKNEKVNTENAEDMGIITMTSDTITVKEISDKLEKSYAEVIKELMLMGVMASVNQEINFEMAEKLAAKFDMEILKEDEDEKEDLEDILKDNEEEEYLQKRSPIITVMGHVDHGKTSLLDAIRKSKVTSTEAGGITQHIGAYTVELNGEAITFLDTPGHAAFTAMRARGAQVTDIVILVVAADDGIMPQTQEAISHCKAANVPLIVAINKIDRPGANIDKVKQELTEYGLVAEDWGGDTICVPVSAHTKEGIDDLLEMILLSSEILELKANPNRKAKGTVVEAKLDKGRGPVATLLIQNGTLRVGDSIVVGSTYGRIRAMFNDKGRNIESAGPSTPVEILGLSEVPEAGDKFYQVKEEKTARGIADKRKEKIRDEYLQSTHKVSLEDLYNQIQEGTVKELGLIVKADVQGSVEALKQSLEKLSTEEVKVRVIHGGVGAINETDVTLATASNGIILGFNVRPDNNAIIASERDGVDIKTYRVIYDAIEDIKSAMLGMLEPEFKEVVIGTAEVRQVYKISSVGTIAGAYIQTGKLARNAGARVIRDGIVIFESELASLKRFKDDAKEVAQGYECGLSIEKFNDIKEGDIIECFIMEEIKKKTL
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A7FVZ3
|
P83220
|
MIH_JASLA
|
Probable molt-inhibiting hormone
|
Jasus
|
RFTFDCPGMMGQRYLYEQVEQVCDDCYNLYREEKIAVNCRENCFLNSWFTVCLQATMREHETPRFDIWRSILKA
|
Inhibits Y-organs where molting hormone (ecdysteroid) is secreted. A molting cycle is initiated when MIH secretion diminishes or stops. Has little or no hyperglycemic activity.
|
P83220
|
A6LCQ4
|
HCP_PARD8
|
Prismane protein
|
Parabacteroides
|
MFCYQCQETAQGKGCTLKGVCGKTAEVAGLQDLLMYLMKGISKLTTTLRKQGVESSTANKFIVDGLFMTITNANFDSSRFVSKIKEAYQLRENLLNELHRLGIHLSLTCDCLTWKSDKVEEMEVKAKEVGILATENEDIRSLCELLTYGVKGMAAYVEHAYNLGFEDTSLYAFMQDALVATTRSDLTVADLTQWVLTCGEYGVKAMALLDKANTSTYGNPEITKVNIGVGKNPGILISGHDLRDIQDLLEQTEGTGIDVYTHGEMLPAHYYPAFKKYKHFVGNYGSAWWKQTSDFETFNGVILFTTNCLVPPRSSATYADRVYTTGSTGFEGFPHIADRKPGGSKDFSALIEHAKKCAPPTEIEHGEIIGGFAHEQVFQLADKVIDAVKSGAIRKFFVMAGCDGRMKSRSYYTEFAEKLPKDTVILTAGCAKYRYNKLPLGEIRGIPRVLDAGQCNDSYSLVMIALKLKEIFGLDDVNELPIAYNIAWYEQKAVIVLLALLYLGVKNIHLGPTLPAFLSPNVAKVLVDNFGIAGIGSVDEDMELFLGK
|
Catalyzes the reduction of hydroxylamine to form NH(3) and H(2)O.
|
A6LCQ4
|
Q11HP9
|
EFG_CHESB
|
Elongation factor G
|
unclassified Chelativorans
|
MAREFKIEDYRNFGIMAHIDAGKTTTTERILYYTGKSHKIGEVHDGAATMDWMEQEQERGITITSAATTTFWKGRDEKLRRFNIIDTPGHVDFTIEVERSLRVLDGAIALLDANAGVEPQTETVWRQADKYHVPRMIFCNKMDKIGADFYRSVEMVKSRLGATAVVMQLPIGAESDFKGVIDLVEMKALIWRDETLGAAWDVVEIPAEFKEKAEEYREKLIEAAVEMDEGAMERYLEGEMPSIEEIRALVRKGTIEVKFFPMFCGSAFKNKGVQPLLDAVVDFLPSPIDIPAIKGVDAKTEEPIERHAEDSEPLSMLAFKIMNDPFVGSLTFCRIYSGVLKKGVSLENTVKGKRERIGRMLQMHANSREDIEEAYAGDIVALAGLKETTTGDTLCDPLKPVILERMEFPEPVIQIAIEPKTKGDQEKMGLALNRLAAEDPSFRVKTDEESGQTIIAGMGELHLDIIVDRMKREFKVEANIGAPQVAYRETITKTAEIDYTHKKQTGGSGQFARVKIVFEPNPDGEDFLFESKIVGGSVPKEYVPGVQKGIESVLSSGPIAGFPMLGVKATLVDGAYHDVDSSVLAFEIAARAAFREGAQKAGAQLLEPIMKVEVVTPEEYVGSVIGDLNSRRGQIQGQEARGVAVVVNAMVPLANMFKYVDNLRSMSQGRAQYTMQFDHYEPVPSAVAQEIQKKFA
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
|
Q11HP9
|
Q5R6J1
|
S6A19_PONAB
|
System B(0) neutral amino acid transporter AT1
|
Pongo
|
MVRLVLPNPGLDTRILSLAELETIEQEEASSRPKWDNKAQYLLTCVGFCVGLGNVWRFPYLCQSHGGGAFMIPFLILLVLEGIPLLHLEFAIGQRLRRGSLGVWSSIHPALKGVGLTSMLVSFVVGLYYNTIISWIMWYLFNSFQEPLPWSECPLNENQTGYVDECARSSPVDYFWYRETLNISTSISDSGSIQWRMLLCLACAWSVLYMCTIRGIETTGKVVYITSTLPYVVLTIFLIRGLTLKGATKGIIYLFTPNVTELANPVTWLDAGAQVFFSFSLAFGGLISFSSYNSVHNNCERDSVIVSIINGFTSVYVAIVIYSIIGFRATQRYDDCFSTNILTLINGFDLPEGNVTQENFVEMQRQCNASNPAAYAQLVFQTCDINSFLSEGVEGTGLAFIVFTEAITKMPVSPLWSVLFFIMLFCLGLSSMFGNMEGVVVPLQDLKVIPPKWPKELLTGLICLGTFLIGFIFTLNSGQYWLSLLDSYAVSIPLLIIAFCEMFSVVYVYGVDRFNKDIEFMIGHKPNIFWQVTWRVVSPLLMLIILVFFFVVQVSQELTYSIWNPGYEEFPKSQKISHPNWVYAVVVIVAGVPSLTIPSYAIYKLIRNCCQKPGDRQGLVSTLSTASMNGDLKY
|
Transporter that mediates resorption of neutral amino acids across the apical membrane of renal and intestinal epithelial cells. This uptake is sodium-dependent and chloride-independent. Requires CLTRN in kidney or ACE2 in intestine for cell surface expression and amino acid transporter activity.
|
Q5R6J1
|
A8F2V3
|
IF1_RICM5
|
Translation initiation factor IF-1
|
spotted fever group
|
MIMSKDDLIQFTGTVLELLPNATFRVKLENDHVIIAHTAGRMRKNRIRILLGDKVMVEMTPYDLTKGRVIHRH
|
One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
|
A8F2V3
|
Q96375
|
ABA2_CAPAN
|
Xanthophyll epoxidase
|
Capsicum
|
MYASSARDGIPGKWCNARRKQLPLLISKDFPAELYHSLPCKSLENGHIKKVKGVKATLAEAPATPTEKSNSEVPQKKLKVLVAGGGIGGLVFALAGKKRGFDVLVFERDISAIRGEGQYRGPIQIQSNALAALEAIDMDVAEEIMNAGCITGQRINGLVDGISGNWYCKFDTFTPAVERGLPVTRVISRMTLQQILARLQGEDVIMNESHVVNFADDGETVTVNPELCQQYTGDLLVGADGIRSKVRTNLFGPSELTYSGYTCYTGIADFVPADIDTAGYRVFLGHKQYFVSSDVGGGKMQWYAFHNEPAGGVDAPNGKKERLLKIFGGWCDNVIDLSVATDEDAILRRDIYDRPPTFSWGKGRVTLLGDSVHAMQPNLGQGGCMAIEDSYQLALELEKAWSRSAESGSPMDVISSLRSYESARKLRVGVIHGLARMAAIMASAYKAYLGVGLGPLSFITKFRIPHPGRVGGRFFIDLGMPLMLSWVLGGNGEKLEGRIQHCRLSEKANDQLRNWFEDDDALERATDAEWLLLPAGNSNAALETLVLSRDENMPCTIGSVSHANIPGKSVVIPLSQVSDMHARISYNGGAFLGTAFRSDHGTWFIDNEGRRYRVSPNFPMRFHSSDVIVFGSDKAAFRIKAMKFAPKTAAKEDRQAVGAA
|
Converts zeaxanthin into antheraxanthin and subsequently violaxanthin. Acts also on beta-cryptoxanthin. Involved in the epoxidation of zeaxanthin.
|
Q96375
|
P24754
|
OMPA_ATLHE
|
Outer membrane protein 3A
|
Atlantibacter
|
LTAKLGYPITDELDIYTRLGGMVWRADSKYNIPGGASFKDHDTGVSPVFAGGLEWAVTRDIATRLEYQWTNNIGDANTVGTRPDNGLLSVGVSYRFGQQEAAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQQALDQMYTQLSNLDPKDGSVVVLGFTDRIGSDAYNQGLSEKRAQSVVDYLISKGIPSDKISARGMGESNPVTGNTCDNVKPRAALIDCLAPDRRVEIEVKGI
|
With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm. Acts as a porin with low permeability that allows slow penetration of small solutes; an internal gate slows down solute passage.
|
P24754
|
Q3YRU2
|
DUT_EHRCJ
|
dUTP pyrophosphatase
|
Ehrlichia
|
MKNNTDILIKVIKLNSNNLPLPSYSTENSSGMDLYSAMTQDVILAPGCRACINTGIAISVPNGYEAQVRPRSGLALKFGITVLNTPGTIDADYRGEIKVILINLGHETYTIKYGDRIAQMVIAPVIHASWNLVKDLDDDTTKRGDQGFGSTGI
|
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
|
Q3YRU2
|
D4D675
|
MCPAL_TRIVH
|
Metallocarboxypeptidase A-like protein TRV_02598
|
Trichophyton
|
MQSLLLLATLLGSALGGAIPSQSANYNGYKVMRVSGDDTSKISHIVSKLGLETWKFPKAANANVDIVVPPKKVAEFEKMSHAAGLKKQVMHENLGDSIKSEMSFRPYSCELLTLDGGANDTWFQSYHKYEDHLKFMQDFQSAHSQNSEIVTSGKSHEGRDITGVHVWGSGEKGSKPAVVFHGTVHAREWITTMTVEYILAQLFDDKEAGAALLEKFDFYIFPIANPDGFVFTTESDRMWRKNREQNEGGCYGTDLNRNWPYKWEGDGSTTDPCSETYRGPSPGFAPETKASTSFIKGLADGAGVKMFVDWHSYSQLFMTPYGYSCSARAPNDDVLQEMASSFADAVKAVHGTSFTTGPICNTIYQANGNSVDWIVDEIKGETAFAAELRDTGMYGFVLPPEQIIPSGEETWAGVKAMFSKLK
|
Extracellular metalloprotease that contributes to pathogenicity.
|
D4D675
|
Q39DH2
|
PDXH_BURL3
|
Pyridoxal 5'-phosphate synthase
|
Burkholderia cepacia complex
|
MTTLADLRINYSRASLDEADVAHDPFAQFDRWFKEALAAKLPEPNTMTLATVGDDGRPSARIVLIKGVDERGFVFFTNYESRKGRDLAAHPQAALLFYWIELERQVRIEGRIEKTSAEESDRYFASRPLGSRIGAWASEQSAVIDSRATLEAQEQAVSERYGDNPPRPPHWGGYRLVPDSIEFWQGRPSRLHDRLLYTRDADTSPSWSISRLSP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
Q39DH2
|
B9HBA8
|
ACCC1_POPTR
|
Acetyl-coenzyme A carboxylase biotin carboxylase subunit A 1
|
Populus
|
MEATLPVCKSVTSTPGLFMGKTSGIRSSQCSFMMGNKVNFPRQRAQTAHVHCAKNGGALGVTCRAEKILVANRGEIAVRVIRTAHEMGIPCVAVYSTIDKDALHVKLADESVCIGEAPSSQSYLVIPNVLSAAISRRCTMLHPGYGFLAENAVFVEMCREHGINFIGPNPDSIRVMGDKSTARETMKKAGVPTVPGSDGLLQSTEEGVRLANEIGYPVMIKATAGGGGRGMRLAKEPDEFVKLLQQAKSEAAAAFGNDGVYLEKYVQNPRHIEFQVLADKFGNVVHFGERDCSIQRRNQKLLEEAPSPALTPELRKAMGDAAVSAAASIGYIGVGTVEFLLDERGSFYFMEMNTRIQVEHPVTEMISSVDLIEEQIRVAMGEKLRYKQEDIVLRGHSIECRINAEDAFKGFRPGPGRITAYLPSGGPFVRMDSHVYPDYVVPPSYDSLLGKLIVWAPTREKAIERMKRALDDTIITGVPTTIDYHKLILEIEDFKNGNVDTAFIPKHEKELAAPQQIIPAKQLTNSAA
|
This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA.
|
B9HBA8
|
Q1QQS4
|
ATPD_NITHX
|
F-type ATPase subunit delta
|
Nitrobacter
|
MAAVDSSVSGVSGRYATALFELAREDKSIDAVKADLDRFDAMLADSPELARLVRSPVFSADTQAKALAAVLDKAGFGGTTAKFLKVLTANRRLFAVTEVIRAFRALVARFKGEVTAEVTVAETLNKKNLDALTTALKSVTGKDITLNVKVDPSIIGGLVVKLGSRMVDSSLRTKLNSIKHAMKEAG
|
This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.
|
Q1QQS4
|
C1FTF1
|
GLYA_CLOBJ
|
Serine hydroxymethyltransferase
|
Clostridium
|
MDFTNLKNTDPELLDMIKKEEERQEYNIELIASENFTSLSVMEAMGSLLTNKYAEGYPHKRYYGGCEFVDEVEDLARERLKKLFAAEHANVQPHSGSQANMAVYMSVLQTGDTILGMDLSHGGHLTHGSPVNFSGKLYNFISYGVDKETETIDYEKLKKIALENRPKMIVSGASAYPRIIDFQKIREICDEIDAYMMVDMAHIAGLVATGLHPSPVPYADFVTTTTHKTLRGPRGGAILCKEKYAKAVDKAIFPGIQGGPLMHTIAAKAVCFGEALREDYKEYMQQVVKNTKVLGEELKNYGFRLISGGTDNHLLLIDLTNKNITGKDAEKLLDSVGITVNKNTIPFETLSPFITSGIRIGTPAVTTRGFKEEEMKKIAYFMNYSIEHREENLSQIKEQIKEICKKYPLYQNA
|
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.
|
C1FTF1
|
Q8DDK6
|
FADB_VIBVU
|
3-hydroxyacyl-CoA dehydrogenase
|
Vibrio
|
MIYQAETLQVKEVQDGVAEILFCAPNSVNKLDLATLASLDKALDALTAHSGLKGVMLTSDKEAFIVGADITEFLGLFAKPEEELDQWLQFANSIFNKLEDLPVPTVAVVKGHTLGGGCECVLATDLRIGDKTTSIGLPETKLGIMPGFGGCVRLPRVIGADSAMEIITQGKACRAEEALKIGLLDAVVDSDRLYASALQTLTDAINEKIDWKARRQQKTSALTLSKLEAMMSFTMAKGLVAQVAGPHYPAPMTAVVTIEEGARFARNQALDIERKHFVKLAKSEEAKALVGLFLNDQYIKGIAKKAAKSANKETQRAAVLGAGIMGGGIAYQSALKGVPVIMKDIAQASLDLGMTEASKLLNKQLERGKIDGFKMAGILASITPSLHYAGIDNADIIVEAVVENPKVKAAVLSEVEEQVSEETVLTSNTSTIPINLLAKSLKRPENFCGMHFFNPVHRMPLVEIIRGEHTSDETINRVVAYAAKMGKSPIVVNDCPGFFVNRVLFPYFGGFSMLLRDGADFTQIDKVMERKFGWPMGPAYLLDVVGIDTAHHAQAVMAQGFPERMGKQGRDAIDALFEANKYGQKNGSGFYTYTMDKKGKPKKAFSDEIVPILAPVCAAQQAFDDQTIIQRMMIPMINEVVLCLQEGIIASAQEADMALVYGLGFPPFRGGVFRYLDSVGIANFVAMAQQHVELGAMYQVPQMLIDMAEKGQTFYGAQQQGSI
|
Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
|
Q8DDK6
|
Q8FSF7
|
HEM3_COREF
|
Pre-uroporphyrinogen synthase
|
Corynebacterium
|
MTLRIGTRGSKLATTQAGHMRDRLKHFGRDAELTIVTTPGDVNMSPVERIGVGVFTQALRDALVADEIDVAVHSFKDLPTAPDPRFHLVVPTRADARDALIARDGLTLEELPEGAKVGTSAPRRISQLKALRPDLEILPLRGNIDTRMGKVTSGELDAVVLAFAGLSRVGMQDRATQVFDPDMLMPAPAQGALAIECRVEDEDIITGLNMLMHADTYVTAVAERTVLNRLEAGCTAPVAAHATLDGYAGDTMTLTAGVFALDGSEQLVFSAQGAGERPEELAEQVAAQLIEQGAATLLG
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q8FSF7
|
Q0V6M5
|
LCPS_PHANO
|
Phytoene synthase
|
Parastagonospora
|
MGFDYAIVHVKYTIPPAVLLTLLYRPLFTKLDAFKVLFLVTVAVTATIPWDSYLIRTNIWSYPDHVVIGPTLLDIPLEEVFFFFIQTYNTTLLYLILSKPTFQPAYLRAGRPTASSPWKYQKLAGQLFLVGATVWAGLRVHENAKGTYTGLIVVWAAPIILLQWTLAYQFILGLPWTNTVLPIAIPTLYLWLVDTLALRRGTWVISPGTKYGVHLWDGLEIEEALFFFVTNTLIVFGQLAFDNALAVLYTFPALFPKPPSMPTPLDLINALWVSPYKYDRARLAGLQDAVLRLKRKSRSFYLASATFPGPLRSDLLLLYSFCRVADDLVDNAATAEEAKEWISKLHQYLDLVYSDAKSSTVSEDFVQAHFPSDARSALLQLPAHKLPRQPLQDLLHGFEMDLAFNTSSPIKTETDLRLYSERVAGTVAQMCIELIFRLYPSNMTSGEERKVVDAGNQMGMALQYVNIARDISVDAHIGRVYLPLDWLQESGLTYDEVLISPEGARMESLRMRLLEKAFSIYDGARGAIETLPVEARGPIRVAVESYMEIGRTLRQKGYTVRAGRATVSKWRRVIVAWRTLNKSIA
|
Bifunctional enzyme that catalyzes the reactions from geranylgeranyl diphosphate to phytoene (phytoene synthase) and lycopene to beta-carotene via the intermediate gamma-carotene (lycopene cyclase).
|
Q0V6M5
|
Q889Y0
|
RL10_PSESM
|
50S ribosomal protein L10
|
Pseudomonas
|
MAIKLEDKKAIVAEVNEAAKAGLSAVVADARGVTVGAMTGLRKEAREAGVYVRVVRNTLLKRAVADTEFSVLNDVFTGPTLIAFSNEHPGAAARLFKEFAKGQDKFEIKAAAFEGKFLAANQIDVLATLPTRNEAISQLMSVIQGATSKLARTLAAVRDQKEAAAA
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q889Y0
|
Q9HAV4
|
XPO5_HUMAN
|
Ran-binding protein 21
|
Homo
|
MAMDQVNALCEQLVKAVTVMMDPNSTQRYRLEALKFCEEFKEKCPICVPCGLRLAEKTQVAIVRHFGLQILEHVVKFRWNGMSRLEKVYLKNSVMELIANGTLNILEEENHIKDALSRIVVEMIKREWPQHWPDMLIELDTLSKQGETQTELVMFILLRLAEDVVTFQTLPPQRRRDIQQTLTQNMERIFSFLLNTLQENVNKYQQVKTDTSQESKAQANCRVGVAALNTLAGYIDWVSMSHITAENCKLLEILCLLLNEQELQLGAAECLLIAVSRKGKLEDRKPLMVLFGDVAMHYILSAAQTADGGGLVEKHYVFLKRLCQVLCALGNQLCALLGADSDVETPSNFGKYLESFLAFTTHPSQFLRSSTQMTWGALFRHEILSRDPLLLAIIPKYLRASMTNLVKMGFPSKTDSPSCEYSRFDFDSDEDFNAFFNSSRAQQGEVMRLACRLDPKTSFQMAGEWLKYQLSTFLDAGSVNSCSAVGTGEGSLCSVFSPSFVQWEAMTLFLESVITQMFRTLNREEIPVNDGIELLQMVLNFDTKDPLILSCVLTNVSALFPFVTYRPEFLPQVFSKLFSSVTFETVEESKAPRTRAVRNVRRHACSSIIKMCRDYPQLVLPNFDMLYNHVKQLLSNELLLTQMEKCALMEALVLISNQFKNYERQKVFLEELMAPVASIWLSQDMHRVLSDVDAFIAYVGTDQKSCDPGLEDPCGLNRARMSFCVYSILGVVKRTCWPTDLEEAKAGGFVVGYTSSGNPIFRNPCTEQILKLLDNLLALIRTHNTLYAPEMLAKMAEPFTKALDMLDAEKSAILGLPQPLLELNDSPVFKTVLERMQRFFSTLYENCFHILGKAGPSMQQDFYTVEDLATQLLSSAFVNLNNIPDYRLRPMLRVFVKPLVLFCPPEHYEALVSPILGPLFTYLHMRLSQKWQVINQRSLLCGEDEAADENPESQEMLEEQLVRMLTREVMDLITVCCVSKKGADHSSAPPADGDDEEMMATEVTPSAMAELTDLGKCLMKHEDVCTALLITAFNSLAWKDTLSCQRTTSQLCWPLLKQVLSGTLLADAVTWLFTSVLKGLQMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEIQKDSLDQFDCKLLNPSLQKVADKRRKDQFKRLIAGCIGKPLGEQFRKEVHIKNLPSLFKKTKPMLETEVLDNDGGGLATIFEP
|
(Microbial infection) Mediates the nuclear export of adenovirus VA1 dsRNA.
|
Q9HAV4
|
Q39XZ9
|
RL16_GEOMG
|
50S ribosomal protein L16
|
Geobacter
|
MLMPKRVKYRKQMKGRMTGAAMRGATLSYGDFGLQATECGWVDSRQIEAARIAMTRYIKRGGKIWIRMFPDKPLTSKPAETRMGKGKGSPDSWVCVVKPGKVLYEMEGVSEEIAREAFRLAANKLPVGTKFISRKEGYES
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q39XZ9
|
O13682
|
SWR1_SCHPO
|
Helicase swr1
|
Schizosaccharomyces
|
MTYEESEKNKNGLSSYIKKEGSSDLKVRVRFREPKLLVTHSGHITEQPKYEHLEQYLDSYVSLEDGDHDPKEAKELVFREVQLRHRINEFRKKGYFTAEAPVELKKAPSSNNIPISYRDNLLSHVNGYARSMHNDRKVRASRSRRISGMILAHFKRLSGADEKKAKEEDKRIRLLAKRTAWEIRKKWKVIEREVRRRRAERAAEAQRVAGKEQLANILKHSTDLLEARIERANINISAQTSESAVDWNYLLKTSDDLLSVDELKLKYSNPDLIKNIEREEEAEETSDDEPLSSEDEENEDEDITEESNLRKRKVSDKTRVVNKHPPSLRRSRRFFAKKSYNHVSDLDGEVIVMKKEDITDGVSTKKDLNDGDQNEVPLHDTGSSSSLSLLYNEDVASKKKRRVNDDGLARKKSIAGISEQRKFDEPNGSPVLHANKIQVPFLFRGTLREYQQYGLEWLTALHDSNTNGILADEMGLGKTIQTIALLAHLACEKENWGPHLIIVPTSVMLNWEMEFKKFLPGFKILTYYGNPQERKEKRSGWYKPDTWHVCITSYQLVLQDHQPFRRKKWQYMILDEAHNIKNFRSQRWQSLLNFNAEHRLLLTGTPLQNNLVELWSLLYFLMPAGVTQNNSAFANLKDFQDWFSKPMDRLIEEGQDMNPEAMNTVAKLHRVLRPYLLRRLKTEVEKQMPAKYEHVVYCQLSKRQRFLYDDFINRARTREILASGNFMSIINCLMQLRKVCNHPNLHEERPIVTSFALRRSAIADLEIKDLLVRKRLLHEEPMTKLDLSTLRLIRTDSEAFDTFVSDELNSLCATNAYNRISTFLRMQIDEECKPCQFKKSNFKEHFQNKIYQEQLDKLNFQKYLNESKCSHSPIYGSNLIRLAEKLPKHSTSIDYTLYAKDDPLYLLNTTKALRSCILSTEERASNMKEIIQRFACITPKAVVVDLPELFCKTIPRDLLYEVSRKINPLHQASTRLAIAFPDKRLLQYDCGKLQVLDRLLKDLVSNGHRVLIFTQMTKVLDILEQFLNIHGHRYLRLDGATKIEQRQILTERFNNDDKIPVFILSTRSGGLGINLTGADTVIFYDSDWNPQLDAQAQDRSHRIGQTRDVHIYRLISEYTVESNMLRRANQKRMLDKIVIQGGEFTTEWFRKADVLDLFDLDDESLKKVKADSDSGSTKNEENWEVALAAAEDEEDVQAAQVARKESALEQTEFSETSTPQAMLTKDSTPLSSDSATPGFERDSTEEQSNTNDMDEDRSELEEDLDETVGHIDEYMISFLEQEGTSDEW
|
Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
|
O13682
|
P37885
|
SOMA_VICPA
|
Growth hormone
|
Vicugna
|
FPAMPLSSLFANAVLRAQHLHQLAADTYKEFERTYIPEGQRYSIQNAQAAFCFSETIPAPTGKDEAQQRSDVELLRFSLLLIQSWLGPVQFLSRVFTNSLVFGTSDRVYEKLKDLEEGIQALMRELEDGSPRAGQILRQTYDKFDTNLRSDDALLKNYGLLSCFKKDLHKAETYLRVMKCRRFVESSCAF
|
Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
|
P37885
|
O45657
|
PLX2_CAEEL
|
Plexin-2
|
Caenorhabditis
|
MLPESVFLLLISHFLRAVTQPPFETEGVKQKLFHFSGHIDDFIVSRDQQTIYVASLNRLTSLSISNFSIQHEVSLGPVQDSPWCSADGKSCLKDNRPFPTDVRTKILQILPTNQILQCGSVKLGSCSTFNSKLSLITESTIAVAANSPDASTVSKIIDNRLIVAASATKESPYRDPFPAVAIRNLPGLNVENAGDLEGEAAVFLRAAYKNAFKFLYTFTHQHFVFVVAMVTPRESRLPMTTRLIRFCRNDTKFESYSEIELQCRGEDNTNYPFLNAIIQSYDKLIASFSTSSTSPKSSICVFSMQKVKLTFWYNVDRCRSGTDSIRLPHIGRDTKCVNKAHIPLDEDSCELGVGGSIELVEMSTKDIMGKVTSLMAVDQKAIFAGTTTSQIVMFKWDEHHSNQLEEYGRKEVGDGRTGSEVSKMVKFGDFVIVQMPYGIILEELSTCSHHSSCTECLVSVDPLCQWCHPTQSCTTSARCTSPVTSQCPIVDGDPIPSIVSVNSSTPISFNIHHLPPPVGFTYRCQFGTSTSSIKANWTTTGVSCPSEIFTSPNTFEILLLTSISNNPISRHNFTVYDCSGYGTCSSCMSSEYNCAWCSGLHKCSNSCGALEKSKACVKIQPMRLPIAIGSQQEIVLEASNLDTLDRRHEHFCKVNEQVSLAKIASDSIRCGKIQLTLSNTTSANMVVPLSLITRDSVIDIANVSLYSCTNLASDCSSCLALSPSLSCGWCNRQCSHECHESKATAVCDPPRIDKFEPTSGPIEGGTIIKIYGNDLGMSVEDVRGKIYVAGSRCNIVEYHVSNMIACQVDKGVSSGPIRISVGRATVAVAESSELYSFVRTSIFSAYPLYGPISGGTRITLYGQNLSSGSQTSVTVGGMPCPIERVNSSTVLTCLTPSGTRIGKSARVVVHVDHSQTQLDQPFEYRSDPSISSIFPMTSFKAGGRIVYVQGNSLNTVQTAKLFLISSPTPPFYIISDLAPCHIINSTLMTCMTPKILETITRRVEYTRQPMGIYPNPTLSPFKGVRYHQGEQSLILEGHNLNLAAEPNDFKIFIGNERCYVTLVDVRQLVCSGPVRQPKATDERGIPINGDNPLVTVIVGSLRMELGLIEYSDHALPSRLSLLILGLLLFIVVTLTVMCLVFKRRRQEREKEYRKIQLQMENLENNVRKECKQAFAELQTNLVLSPKSANSVNLGPELINFPHFVENLLWSDNNLTSAPSLARTLPVTLAQFHALLSFKGFIFTIVEAAESDVSISTSEKSMLASLLISVLLRNFSYCTEVVVDLLRAHIARSVQNKRAELLFRNSDSVVEKMFSKWMSICLYSHLTPQMNSYFYLYKALQYQTDKGPVDAVTGDARYTINEAKLLRESVDTKTLKIRVIPFEKCDESIDLEVHACDAICQVKQKVASAVYRETPYSQRPRITQFELKYKCPKRGDVKLTDVLPIETLSQKKLPVKLFTLADYGISDGCTLEMSPAVYTAESYRNSLADSGQSSWSSLDRCSPIYSSSKYYHLTNPSSGTMTFKKKSSNDSNLLPKSIPEVYLTRLLTSKGTVETYVEDFLESVLYMHDSSYPPILKFFFDILDREASVNGVSENICQQWKANGYVLRVWANFVRNPQLVFDVPHSISMDANLSTVAQTMMDCFSFSEPVLGAHSPSSRLLFAKDVARLRPLSVDLFKRVKNSPPLGMDELRTELVNMANDVSTCKGSSLALSELLSWVRGNGIRISQLLSSNEQFSQQRLPQKLSQVLHVCLETDNHIYSTISDYE
|
Involved as a receptor for mab-20/sema-2a in the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis . In early embryonic development, required for proper ventral closure of the epidermis . During male tail morphogenesis, involved in precursor cell sorting and in the formation of distinct sensory rays . Involved in axon guidance of SDQL neurons during neurogenesis . Probably in response to stimulation by mab-20, regulates fln-1-mediated remodeling of the actin cytoskeleton and thus axon guidance and/or fasciculation of DD/VD neurons .
|
O45657
|
Q6AZW1
|
KISHB_DANRE
|
Transmembrane protein 167B
|
Danio
|
MTNVYSFDGILVFGLLFICTCAYLKKVPRLNSWLLSEKKGVWGVFYKAAVIGTRLHVVVAASCLCMAFYLIFLK
|
Involved in the early part of the secretory pathway.
|
Q6AZW1
|
B7H3S1
|
RUVC_ACIB3
|
Holliday junction resolvase RuvC
|
Acinetobacter calcoaceticus/baumannii complex
|
MPLIIGIDPGSRLTGYGIIEKDGSKLRFVDAGTIRTETQEMPERLKRIFAGVERIVKFHGPTEAAVEQVFMAQNPDSALKLGQARGAAIAALVNLDLQVAEYTARQIKQSVVGYGAADKEQVQMMVMRLLNLTIKPQADAADALAAAICHAHASGSMSKLTVLNALGGMARGRSRSSSRRR
|
Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group.
|
B7H3S1
|
Q8VL14
|
KAIB_RIPO1
|
Circadian clock protein KaiB
|
Rippkaea orientalis
|
MVNFKKTYVLKLYVAGNTPNSVRALKTLKNILEDEFKGVYALKVIDVLKNPQLAEEDKILATPTLSKILPPPVRKIIGDLSDREKVLIGLDLLYEEIRERESEL
|
Component of the KaiABC clock protein complex, which constitutes the main circadian regulator in cyanobacteria. The KaiABC complex may act as a promoter-non-specific transcription regulator that represses transcription, possibly by acting on the state of chromosome compaction. In the complex, it decreases the phosphorylation status of KaiC. It has no effect on KaiC by itself, but instead needs the presence of both KaiA and KaiC, suggesting that it acts by antagonizing the interaction between KaiA and KaiC.
|
Q8VL14
|
P46205
|
CCMO_SYNE7
|
ORF II
|
Synechococcus
|
MSASLPAYSQPRNAGALGVICTRSFPAVVGTADMMLKSADVTLIGYEKTGSGFCTAIIRGGYADIKLALEAGVATARQFEQYVSSTILPRPQGNLEAVLPISRRLSQEAMATRSHQNVGAIGLIETNGFPALVGAADAMLKSANVKLICYEKTGSGLCTAIVQGTVSNVTVAVEAGMYAAERIGQLNAIMVIPRPLDDLMDSLPEPQSDSEAAQPLQLPLRVREKQPLLELPELERQPIAIEAPRLLAEERQSALELAQETPLAEPLELPNPRDDQ
|
Beta-carboxysome assembly initiates when soluble RuBisCO is condensed into a liquid matrix in a pre-carboxysome by the RbcS-like domains of probably both CcmM58 and CcmM35. CcmN interacts with the N-terminus of CcmM58, and then recruits the CcmK2 major shell protein via CcmN's encapsulation peptide. Shell formation requires CcmK proteins and CcmO. CcmL caps the otherwise elongated carboxysome. Once fully encapsulated carboxysomes are formed, they migrate within the cell probably via interactions with the cytoskeleton.
|
P46205
|
Q2JHK3
|
NU1C_SYNJB
|
NDH-A
|
unclassified Synechococcus
|
MTNAGIDLQLGFETALQNLGLGAGAAHALWMPLPMLLLIIAATLGVMVMTWLERKISAAAQQRIGPNMAGPQGVLIPIADGIKLLTKEDVLPILADPVLFTLGPILVFLPVFLCYLVVPFGQNLLISNIAIGVFFLIAISSVQPIGLLMSGYGSNNKYSLLGGLRAAAQSISYELPLALSVLAVVLMSNGLDTVGIVEQQSGLGILSWNVWRQPIGFVIFLISALAETERIPFDLPEAEEELVAGYQTEYSGMKFALFYLGSYANLLLASLIAAVLYLGGWSFVVPVETIAALAGIPLDNPFLQIGAAALGIVMTMVKAFIFIFLAILLRWTLPRVRIDQLLDLGWKFLLPVSFVNLLLTAALKLAFPTFFGG
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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.
|
Q2JHK3
|
Q087L5
|
LIPA_SHEFN
|
Sulfur insertion protein LipA
|
Shewanella
|
MNRPERLQPGVKLRDADKVARIPVKVVPSERETMLRKPDWLRVKLPSSNQRILEIKAALRKNGLHSVCEEASCPNLAECFNHGTATFMILGAICTRRCPFCDVAHGRPLKADADEPKKLAQTIKDMKLKYVVITSVDRDDLRDGGAQHFADCIREIRLLNPEIKIETLVPDFRGRIDAALDILATEPPDVFNHNLETAPAHYRKARPGANYQWSLDLLKRFKERHPTIPTKSGLMMGLGETNEEIAEVLRDLRAHNVEMLTLGQYLQPSKFHLPVERYVPPAEFDELKALADELGFTHAACGPLVRSSYHADLQAQGKEVK
|
Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
|
Q087L5
|
Q9UUG9
|
TSC2_SCHPO
|
Tuberous sclerosis 2 protein homolog
|
Schizosaccharomyces
|
MNNKSLLDLSSEPAIKDTDILSYFDANLPFKKRHQIVRSIYHGLKYYIYSSTSIIQVWQNIQDFISTKNDNAAFRELVYNLMMRYVSTQKHLSIIERHTFFQTIEKDPFQDIAELQLRLKSLSVLTDEGHKISGIENRVGPLLSAWFNQYLQWQSQATELQGKDADSKLVHLLFFKSLFKFSTNLVKFQWFLVPEPQMLQLVNSVVQICNHARLEDVVTEVLMFFDSMIRYSVIPKASLYDTVLILCSTYISTYSYSKLAQSVIFNLISSPVSNLAFENVFNILQYNRSNVNAVRGAVRLMRFLMLQEVKNDAIASITLSSSIEFTEFPLGFNENVDFEILGTVYLFLRTPSILNRLNFLDWHRILNILMYCSQYLPLKASTSKEAFSKTAAFANIYDRVLDFLDFEALIPLLQQFQVKLVFFLKDVLPVLKPKIRKKLLRLFETYNLIFPCNQYWVFNLEFLLGIYQCKTFDLEDRALLFKLVEDACSVADENSAPILCSKFLFPVIESFSKESDDCVVSPVYNMLFFLSVNFQNPGLKDCIDHIFQQLISDTSSVTVRRLATSTLIRLFYYYYDLRDAVPIQETLAKMLEILETPSFPFVSRMLCLQFFLRFRANGTSIYICENIDLNEPFKVLNVDSELIPAVYPISDSFVNSATVEKHIWERKENDLIKISNHSTEYGKDFVTFPTSSLLRFYRKSMATESNWTILMFMITHLADQISNRSMFIGALEEIYNLLDFMCDIVFERVSISAEIPSNIRKANIMIPILQNVQMLFVYHDQFSRAQEDELVSVFFAGLQKWNEACHVSIHSLMLCCYELPVSIRKQLPAILVTLSRLITKPDLSVHILEFLCSLARLPDLIANFTDADYRQIFAIALKYIQHRDFTKESKDSNDTESILKNSYSSYVLALAYSVLQIWFLSLRLTERKKFVPWILRGLKLASEGKPLEDLCLVQYDMMQQFCYSNSDINNQTSTFVDSDVESETWIRGNSLFTINVSVNSGFLEAVIRRPTGTTQYTFRNEASLQKFLWEENLTSSKALTRGLLCTPSSFVSHFLDPHGISLYNQPLLLPSNDDSVRRAISVFDRIPVIESLKAGLVYVGYQQRREADILANTNPSEDFLTFLNGLGTLFELKTDQKVFAGGLDRENDIDGAFAYCWKDKVTQMVFHCTTMMPTNIEHDPGCTLKKRHIGNDFVTIIFNESGLEYDFDTIPSQFNFVNIVITPESESIRRTGRQIKFYKVKALTKYDIDFSLFRRYKIVSSDALPAIVRDVTLNAAVFSHIYHRSAGDYVHIWAERLRQLKRLREKFQASVLPEDYNLDEQTKTKLQNGTNFSDFTSYL
|
Together with tsc1, required for uptake of various amino acids from the environment and for proper conjugation. Involved in induction of gene expression of permeases and genes required for meiosis upon nitrogen starvation. May act as a GTPase-activating protein (GAP) for the small GTPase rhb1.
|
Q9UUG9
|
Q969S2
|
NEIL2_HUMAN
|
Nei-like protein 2
|
Homo
|
MPEGPLVRKFHHLVSPFVGQQVVKTGGSSKKLQPASLQSLWLQDTQVHGKKLFLRFDLDEEMGPPGSSPTPEPPQKEVQKEGAADPKQVGEPSGQKTLDGSSRSAELVPQGEDDSEYLERDAPAGDAGRWLRVSFGLFGSVWVNDFSRAKKANKRGDWRDPSPRLVLHFGGGGFLAFYNCQLSWSSSPVVTPTCDILSEKFHRGQALEALGQAQPVCYTLLDQRYFSGLGNIIKNEALYRAGIHPLSLGSVLSASRREVLVDHVVEFSTAWLQGKFQGRPQHTQVYQKEQCPAGHQVMKEAFGPEDGLQRLTWWCPQCQPQLSEEPEQCQFS
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Has DNA glycosylase activity towards 5-hydroxyuracil and other oxidized derivatives of cytosine with a preference for mismatched double-stranded DNA (DNA bubbles). Has low or no DNA glycosylase activity towards thymine glycol, 2-hydroxyadenine, hypoxanthine and 8-oxoguanine. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates.
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Q969S2
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O13849
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CBPY_SCHPO
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Carboxypeptidase Y
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Schizosaccharomyces
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MLMKQTFLYFLLTCVVSAQFNGYVPPEQNGGDIVVPKDFYEKFGEDFIREQEESSAPLMNPVPERDEAEAPHHPKGHHEFNDDFEDDTALEHPGFKDKLDSFLQPARDFLHTVSDRLDNIFDDDEDEHVREKRPHDSADEDAPRRKHGKCKGKGKHHKGKHAKGKGKKSHPKPEDDSVFFDDERPKHHEFDDEDREFPAHHEPGEHMPPPPMHHKPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPMHHEPGEHMPPPPFKHHELEEHEGPEHHRGPEDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHKGPKDKEHHQGPKEKHNERPEQNMQSSHELLVIEAFADLINSVPVEEIAEEFSRFLDTLGIEYYGNIPVHIQENAPKDSSIPPLFEFDDDLELSDLTPEQFAYLEMLKAEGIDPMTAFRDQSHPAKPSNAQPADSSRPYAVFSQEENGEHVNLKAFPDHTLRVKDSKPESLGIDTVKQYTGYLDVEDDRHLFFWFFESRNDPENDPVVLWLNGGPGCSSLTGLFMELGPSSINIETLKPEYNPHSWNSNASVIFLDQPINTGFSNGDDSVLDTVTAGKDVYAFLNLFFAKFPQYAHLDFHIAGESYAGHYIPQFAKEIMEHNQGANFFVASGYEMEKQYINLKSVLIGNGLTDPLVQYYFYGKMACESPYGPIMSQEECDRITGAYDTCAKLITGCYQTGFTPVCIGASLYCNNAMIGPFTKTGLNIYDIREECRDQEHLCYPETGAIESYLNQEFVQEALGVEYDYKGCNTEVNIGFLFKGDWMRKTFRDDVTAILEAGLPVLIYAGDADYICNYMGNEAWTDALEWAGQREFYEAELKPWSPNGKEAGRGKSFKNFGYLRLYEAGHMVPFNQPEASLEMLNSWIDGSLFA
|
Involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate.
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O13849
|
Q6JDS8
|
CYB_NEOJL
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Blanfordimys
|
MTNIRKKHPLIKIINHSFIDLPAPSNISSWWNFGSLLGLCLIIQILTGLFLAMHYTSDTATAFSSVAHICRDVNYGWLIRYMHANGASMFFICLFLHVGRGVYYGSYNMIETWNMGIILLFAVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVLVHLLFLHETGSNNPTGLNSDADKIPFHPYYTIKDFLGVLILLMVSMILTLFFPDVLGDPDNYTPANPLNTPPHIKPEWYFLFAYAILRSIPNKLGGVLALILSILILALMPLLHTSKQRALTFRPITQTMYWILVADLFILTWIGGQPVEYPFIIIGQAASIAYFTIIVILMPIAGMIENNIMDLD
|
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
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Q6JDS8
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Q4ZVC2
|
AROC_PSEU2
|
5-enolpyruvylshikimate-3-phosphate phospholyase
|
Pseudomonas syringae
|
MSGNTFGKLFTVTTAGESHGPALVAIVDGCPPGLELDLQDLQRDLDRRKPGTSRHTTQRQEADEVEILSGVFEGKTTGASIGLLIRNTDQKSKDYSAIKDLFRPAHADYTYHHKYGIRDYRGGGRSSARETAMRVAAGAIAKKYLASQGIVIRGYMSQLGPIQIPFKTWDSVEDNAFFCPDPDKVPELEAYMDQLRRDQDSVGAKITVVADGVMPGLGEPIFDRLDAELAHALMSINAVKGVEIGAGFDCVAQRGTEHRDEMTPQGFLSNHAGGILGGISSGQPIIAHLALKPTSSITTPGRSIDVDGNAADVITKGRHDPCVGIRATPIAEAMMAIVLLDHLLRHRGQNADVSVNTPVLGQV
|
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.
|
Q4ZVC2
|
Q45715
|
CR1KA_BACTM
|
Insecticidal delta-endotoxin CryIK(a)
|
Bacillus cereus group
|
MNSNRKNENEIINALSIPAVSNHSAQMDLSPDARIEDSLCVAEGNNIDPFVSASTVQTGISIAGRILGVLGVPFAGQLASFYSFLVGELWPSGRDPWEIFMEHVEQIVRQQQITDSVRDTAIARLEGLGRGYRSYQQALETWLDNRNDARSRSIIRERYIALELDITTAIPLFSIRNEEVPLLMVYAQAANLHLLLLRDASLFGSEWGMSSADVNQYYQEQIRYTEEYSNHCVQWYNTGLNRLRGTTAETWVRYNQFRRDLTLGVLDLVALFPSYDTRTYPIPTTAQLTREVYTDPNGVVAGPNNSWFRNGASFSAIENAIIRQPHLYDFLTNLTIYTRRSQVGTTIMNLWAGHRITFNRIQGGSTSEMVYGAITNPVSVSDIPFVNRDVYRTVSLAGGLGSLSGIRYGLTRVDFDMIFRNHPDIVTGLFYHPGHAGIATQVKDSDTELPPETTEQPNYRAFSHLLSHISMGPTTQDVPPVYSWTHQSADRTNTINSDRITQIPLVKAHTLQSGTTVVKGPGFTGGDILRRTSGGPFAFSNVNLDFNLSQRYRARIRYASTTNLRIYVTVAGERIFAGQFDKTMDAGAPLTFQSFSYATINTAFTFPERSSSLTIGADTFSSGNEVYVDRFELIQVTATFEAESDLERARKAVNALFTSTNPRGLKTDVTDYHIDQVSNLVECLSDEFCLDKKRELLEEVKYAKRLSDERNLLQDPTFTSISGQTDRGWIGSTGISIQGGDDIFKENYVRLPGTVDECYPTYLYQKIDESQLKSYTRYQLRGYIEDSQDLEIYLIRYNAKHETLSVPGTESPWPSSGVYPSGRCGEPNRCAPRIEWNPDLDCSCRYGEKCVHHSHHFSLDIDVGCTDLNEDLGVWVIFKIKTQDGHAKLGNLEFIEEKPLLGKALSRVKRAEKKWRDKYEKLQLETKRVYTEAKESVDALFVDSQYDKLQANTNIGIIHGADKQVHRIREPYLSELPVIPSINAAIFEELEGHIFKAYSLYDARNVIKNGDFNNGLSCWNVKGHVDVQQNHHRSVLVLSEWEAEVSQKVRVCPDRGYILRVTAYKEGYGEGCVTIHEFEDNTDVLKFRNFVEEEVYPNNTVTCNDYTTNQSAEGSTDACNSYNRGYEDGYENRYEPNPSAPVNYTPTYEEGMYTDTQGYNHCVSDRGYRNHTPLPAGYVTLELEYFPETEQVWIEIGETEGTFIVGSVELLLMEE
|
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of insects. Selectively toxic to Artogeia rapae but not active on Plutella xylostella.
|
Q45715
|
Q5HZ38
|
GRIK2_ARATH
|
SnRK1-activating protein kinase 1
|
Arabidopsis
|
MFRDSFLFARTIGCFGCFGSSGSRNQQSPKPYDDDTHSCDSDVTSTARGEEEEDEEEVEQKSRSKRSEEILKYRLDNGLICRHIPVRETNELIRGEDENGDKTINEYVRVCKIGSGSYGKVVLYRSTLDGQYYAIKAFHKSHLLRLRVAPSETAMSDVLREVMIMKILEHPNIVNLIEVIDDPETDHFYMVLEYVDGKWVYDGSGPPGALGEKTARKYLRDIVTGLMYLHAHDVIHGDIKPDNLLVTSSGTVKIGDFSVSQVFKDDDDQLRRSPGTPVFTAPECCLVSGITYSGRAADTWAVGVTLYCMILGQYPFLADTLQDTYDKIVNNPLIIPDGLNPLLRDLIEGLLCKDPSQRMTLKNVSEHPWVIGEDGHVPEYFCWCKRNAASKIEEGEANGISETSDPN
|
Activates SnRK1.1/KIN10 and SnRK1.2/KIN11 by phosphorylation of their activation-loop 'Thr-198' and 'Thr-176', respectively. Required for the regulation by SnRK1 kinases of the transcription of a large set of genes, the modification the activity of metabolic enzymes, and the control of various nutrient-responsive cellular developmental processes.
|
Q5HZ38
|
Q1Q893
|
ATP6_PSYCK
|
F-ATPase subunit 6
|
Psychrobacter
|
MAGEQTTTEYISHHLTNWTYGYLPGEGWKVAYNAEEASAMGFKAIHLDSMLWSIGLGIVFCAIFWMVARKVTSGVPGKTQAAVEMIVEFVDNNVRDSYSGTSKLIAPLALTIFVWIFLMNLMDLLPVDFIPMIAGQIGALMGHDPHHVYFKIVPTTDPNITLGMSFSVFILILFYSIKEKGLGGFVGELTLHPFSAKNPIVQIILIPINFILEFVTLIAKPISLGLRLFGNMYAGELIFILIALMPFWIQWALSVPWAIFHILIITLQAFVFMMLTIVYMSLASSTEH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
Q1Q893
|
Subsets and Splits
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