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
|
---|---|---|---|---|---|---|
A6MMP3
|
RR8_DIOEL
|
30S ribosomal protein S8, chloroplastic
|
Dioscorea
|
MGRDTIANIITSIRNADMDKKGTVRIASTNITENIVKILLREGFIENVRKHQENQRFFLVSTLRHRRTSKGVYRTILKRISRPGLRIYSNYQRIPKILGGIGIVILSTSQGIMTDREARLKKIGGEILCYIW
|
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
|
A6MMP3
|
B9KAT4
|
TIG_THENN
|
PPIase
|
Thermotoga
|
MEVKELERDKNRVVLEYVFNREEVLEAEDKAARYLNQRVEIPGFRKGRVPKNILKMRLGEDFQEYTLDFLMDLIPDTLKDRNLIMSPVVTEREIKEDTARFVVEVHEEPEVKIGDVSKIEVEKVDEEKVLEKYVERRLEDLREKHALLEPKEGPAEVGDLVRISMEVYNEEGKNLTTREYEYVIKEGEDRPFVKDLIGKKKDDVVEIEREYEGKKYTYRLKVQEVYRRTLPEIGDELARTVNNEFETLEQLKEELKKEGKDIYDVEMKESMREQLLEKLPEVVEIEISERTLDLLVQETINRLKREGRYDQIVSSYESEEKLKEELKKRILDDIKRDRAIEVIAKERNVDVSDEELEKEAEELAPFWGISPERAKSLVKSRRDLREDLRWAILKRKVLDLLLEEVTVKVVEPRGEGDGDERKGDN
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
B9KAT4
|
Q0T203
|
RODZ_SHIF8
|
Cytoskeleton protein RodZ
|
Shigella
|
MNTEATHDQNEALTTGARLRNAREQLGLSQQAVAERLCLKVSTVRDIEEDKAPADLASTFLRGYIRSYARLVHIPEEELLPGLEKQAPLRAAKVAPMQSFSLGKRRKKRDGWLMTFTWLVLFVVIGLSGAWWWQDHKAQQEEITTMADQSSAELSSNSEQGQSVPLNTSTTTDPATTSTPPASVDTTATNTQTPAVTAPAPAVDPQQNAVVSPSQANVDTAATPVPTAATTPDGAAPLPTDQAGVTTPAADPNALVMNFTADCWLEVTDATGKKLFSGMQRKDGNLNLTGQAPYKLKIGAPAAVQIQYQGKPVDLSRFIRTNQVARLTLNAEQSPAQ
|
Cytoskeletal protein that is involved in cell-shape control through regulation of the length of the long axis.
|
Q0T203
|
Q98QU4
|
ATPG_MYCPU
|
F-ATPase gamma subunit
|
Mycoplasmopsis
|
MPSLQKTKNRIALIDNIKKITKAMELVATSKMKKTQKHFLEVNEFSQSVLDIFSKIVSQIDPQIKLYPDGQKNSTLYIVISSDIGLAGSYNSNIFKILNSNIKNEDKLILIGQKAINFFSNRQDQIIETFKALPDYVTYKIAKLISDSALNSFLNKDVNQIKVVYTKFINLINQQEKISTILPIKKNPMKSEIKENAILEFEPDVESVFHKAIPLYLASIIFGFLTESKVSELAARRTAMESASKNAIDLIGNLKIEYNQTRQAKITQEISEIVAGSVE
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
|
Q98QU4
|
Q46LV5
|
KHSE_PROMT
|
Homoserine kinase
|
Prochlorococcus
|
MGPPKIGQTVVVEVPSTTANIGPGFDCLGAALDLSNQFTIKRIEGNAERFELIMESTEGNHLRGGPENLFYRAAQRVWRTAGIEPVALEARVKLAVPPARGLGSSATAIVAGLVGANALAGYPLPKEKLLELAIDIEGHPDNVVPSLIGGLCVTAKTASDRWRVVRCDWDKSIKAVVAIPSIRLSTSEARRVMPENIPVNDAVINLGALTLLLQGLRTGNEDLITDGMHDKLHEPYRWGLIKGGLEVREAAKAAGALGCAISGAGPSILALCKATKGREVSVAMVKAWEAAGVASRAPLMSLQLTGSECISNTFG
|
Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate.
|
Q46LV5
|
Q5X0C7
|
RPIA_LEGPL
|
Phosphoriboisomerase A
|
Legionella
|
MSELKIKAAKAAIAYIEDDMVIGVGTGSTVNFFIKELAAIKHKIEACVASSKATEALLRAEGIPVIDLNSVQDLPIYVDGADEVNERGEMIKGGGGALTREKIVANVATQFICIVDESKVVKRLGEFPVAVEVIPMARSFVARQIVKLGGDPEYREGFITDNGNIILDVFNLNFSTPMALEDSLNVIPGVVENGVFAKRLADKVLVASASGVNNLK
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q5X0C7
|
Q8U089
|
TRPD_PYRFU
|
Anthranilate phosphoribosyltransferase
|
Pyrococcus
|
MLEKIVENRHLSFEEAYDLFNILKEESEVRIAAYLAALQTKGYTSEEIAGFAKAMRDNAIKLDLGEVLDTAGTGGDKSFTINVSTASALILSEYTKVAKHGNVSVTSRSGSANLLEALGINIKISPEKAKEMIEKVNFTFIFAPMYHPALKRIMPVRKELGIKTIFNILGPLANPANPAYQVVGVNSRDLVEKMARALNYLGVKRATVVHGSGLDEISPEKETIVAEVNRGDIDFYTVTPEDFGLARTKVIPCYSPEESAERIRAVLRGNGKNEDRNFVLINSAMALYTIGIASDLKEGVELAENVLGEKIIKKLEEIACLSKS
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
Q8U089
|
P96195
|
LEUC_AZOVI
|
Isopropylmalate isomerase
|
Azotobacter
|
MAGKTLYDKLWDMHEVKRRDDGSSLIYIDRQILHEVTSPQVRGAAPGRANVARGCQHRHPGPQRADHPGSPVGGRRHRRRNLAHPGADPGRELRRVRHRRVQDERPAPGHRPCGRPGAGRHLPGMTVVCGDSHTSTHWCGALAHGIGTSEVEHVLATQCLVAKKMKNMQVRVEGELPLGVSAKDIVLAVIGRIGTAGGTGHALEFAGSAIRGLSMEGRMTLCNMAIEAGARVGMVAVDEKTIDYVKGRPYAPQGADWDKAVAQWRELVSDADAGFDTVVELKAEEIRPQVTWGTSPEMVLPVDERVPDPASESDPVKRDSIVRALKYMGLAANQPIGEIKVDRVFIGSCTNSRIEDLRAAAEVAKGARSPRASSRRWWCRAPGWSRSRRRRRGWTGSSSRPVSSGATGCSMCLAMNPDRLESGEHCASTSNRNFEGRQGAGGRTHLVSPAMAAAAAVAGRFVDVRQLLQA
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
P96195
|
B1VEY1
|
RS4_CORU7
|
30S ribosomal protein S4
|
Corynebacterium
|
MARYTGPVTRKSRRLRVDLVGGDRSFERRPYPPGQAGRARIKESEYLIQLQEKQKARFTYGVMEKQFRRYYAEANAMPGKTGDNLVILLEARLDNVIYRAGLARTRRQARQLVSHGHFTVNGKKINVPSFRVSQYDIIDVRDRSRSMLWFDEAQDNLVDANVPAWLQVVPSTLRILVHQLPERAQIDIPLQEQLIVEYYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
B1VEY1
|
Q9VXA8
|
DXO_DROME
|
NAD-capped RNA hydrolase CG9125
|
Sophophora
|
MAENAGFISVPWGQHKLGAMYNTPFPSISRPKCIGVCSINASREFVDDASCASYLAGQPWPPLPFDLNGGIEDVIRKPVENGKRDLEIMLTYIKQHQKELLRQSSSDARNLRLDSDFVTLRGILRQIMCLQYDNRSFRVKATLLNGNVYMCKEETPEQQLENANMSRAQRVMCSWGFKFEQYLTSAQAQGKPVTNVPVNEAEEFMGVYRTNLAGILMLYGAELDCVDSKEPVDFKDCRVLDSLKFVELKTSVFNMNPHQIRTFKSFKSANWWSQSFLVGITTLYVGLRDTKGMLQRIDEIDVATLARNKPWSASAMAWYLEQFLRNLKKLLVNINDPFAVVQVTFLNKHASYEVLRGPEHQILPNWYRDLLKTRS
|
Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control.
|
Q9VXA8
|
Q9HAZ2
|
PRD16_HUMAN
|
Transcription factor MEL1
|
Homo
|
MRSKARARKLAKSDGDVVNNMYEPNRDLLASHSAEDEAEDSAMSPIPVGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPADFELRESSIPGAGLGVWAKRKMEAGERLGPCVVVPRAAAKETDFGWEQILTDVEVSPQEGCITKISEDLGSEKFCVDANQAGAGSWLKYIRVACSCDDQNLTMCQISEQIYYKVIKDIEPGEELLVHVKEGVYPLGTVPPGLDEEPTFRCDECDELFQSKLDLRRHKKYTCGSVGAALYEGLAEELKPEGLGGGSGQAHECKDCERMFPNKYSLEQHMVIHTEEREYKCDQCPKAFNWKSNLIRHQMSHDSGKRFECENCVKVFTDPSNLQRHIRSQHVGARAHACPDCGKTFATSSGLKQHKHIHSTVKPFICEVCHKSYTQFSNLCRHKRMHADCRTQIKCKDCGQMFSTTSSLNKHRRFCEGKNHYTPGGIFAPGLPLTPSPMMDKAKPSPSLNHASLGFNEYFPSRPHPGSLPFSTAPPTFPALTPGFPGIFPPSLYPRPPLLPPTSLLKSPLNHTQDAKLPSPLGNPALPLVSAVSNSSQGTTAAAGPEEKFESRLEDSCVEKLKTRSSDMSDGSDFEDVNTTTGTDLDTTTGTGSDLDSDVDSDPDKDKGKGKSAEGQPKFGGGLAPPGAPNSVAEVPVFYSQHSFFPPPDEQLLTATGAAGDSIKAIASIAEKYFGPGFMGMQEKKLGSLPYHSAFPFQFLPNFPHSLYPFTDRALAHNLLVKAEPKSPRDALKVGGPSAECPFDLTTKPKDVKPILPMPKGPSAPASGEEQPLDLSIGSRARASQNGGGREPRKNHVYGERKLGAGEGLPQVCPARMPQQPPLHYAKPSPFFMDPIYSRVEKRKVTDPVGALKEKYLRPSPLLFHPQMSAIETMTEKLESFAAMKADSGSSLQPLPHHPFNFRSPPPTLSDPILRKGKERYTCRYCGKIFPRSANLTRHLRTHTGEQPYRCKYCDRSFSISSNLQRHVRNIHNKEKPFKCHLCNRCFGQQTNLDRHLKKHEHENAPVSQHPGVLTNHLGTSASSPTSESDNHALLDEKEDSYFSEIRNFIANSEMNQASTRTEKRADMQIVDGSAQCPGLASEKQEDVEEEDDDDLEEDDEDSLAGKSQDDTVSPAPEPQAAYEDEEDEEPAASLAVGFDHTRRCAEDHEGGLLALEPMPTFGKGLDLRRAAEEAFEVKDVLNSTLDSEALKHTLCRQAKNQAYAMMLSLSEDTPLHTPSQGSLDAWLKVTGATSESGAFHPINHL
|
Binds DNA and functions as a transcriptional regulator . Functions as a repressor of TGF-beta signaling . May regulate granulocyte differentiation .
|
Q9HAZ2
|
A0A096P8D3
|
IDH_OSTTA
|
Isocitrate dehydrogenase (NAD(+)), mitochondrial
|
Ostreococcus
|
MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA
|
Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable).
|
A0A096P8D3
|
P29295
|
HRR25_YEAST
|
Casein kinase I homolog HRR25
|
Saccharomyces
|
MDLRVGRKFRIGRKIGSGSFGDIYHGTNLISGEEVAIKLESIRSRHPQLDYESRVYRYLSGGVGIPFIRWFGREGEYNAMVIDLLGPSLEDLFNYCHRRFSFKTVIMLALQMFCRIQYIHGRSFIHRDIKPDNFLMGVGRRGSTVHVIDFGLSKKYRDFNTHRHIPYRENKSLTGTARYASVNTHLGIEQSRRDDLESLGYVLIYFCKGSLPWQGLKATTKKQKYDRIMEKKLNVSVETLCSGLPLEFQEYMAYCKNLKFDEKPDYLFLARLFKDLSIKLEYHNDHLFDWTMLRYTKAMVEKQRDLLIEKGDLNANSNAASASNSTDNKSETFNKIKLLAMKKFPTHFHYYKNEDKHNPSPEEIKQQTILNNNAASSLPEELLNALDKGMENLRQQQPQQQVQSSQPQPQPQQLQQQPNGQRPNYYPEPLLQQQQRDSQEQQQQVPMATTRATQYPPQINSNNFNTNQASVPPQMRSNPQQPPQDKPAGQSIWL
|
Protein kinase which phosphorylates serine and threonine residues . Can use casein as a substrate . Phosphorylates elongator complex member ELP1/IKI3 on 'Ser-1198' and 'Ser-1202' which promotes the tRNA modification function of the complex . Associated with repair of damaged DNA and meiosis .
|
P29295
|
Q3Z6W5
|
COAE_DEHM1
|
Dephosphocoenzyme A kinase
|
Dehalococcoides
|
MKIVGITGGIGSGKTTVCRYLKELGVNIIDADEIGHRVLQNKGIRTRITDVFGNEVMNPDGSINRKILGELVFGYPERLEHLNKITHPLIEQAIASLLEEYRQKGIKAVAIEAPLLVEAGWLKLVNEVWLITAPKESIFKRLRNRMGLSREQVMARIQSQATDNERLKYASIVINNNCRFEDLKSCVQLLAKERLELA
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
Q3Z6W5
|
P0CB10
|
O162_CONAJ
|
Omega-conotoxin-like Ai6.2
|
Cylinder
|
MKLTCVMIIAVLFLTAWTFATADDSGNGLENLFSKAHHEMKNPKASKLNKRCTQSGELCDVIDPDCCNNFCIIFFCI
|
Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels (Cav).
|
P0CB10
|
O69753
|
PHZB1_PSEAE
|
Phenazine biosynthesis protein PhzB1
|
Pseudomonas
|
MPDTTNPIGFTDANELREKNRATVEKYMNTKGQDRLRRHELFVEDGCGGLWTTDTGSPIVIRGKDKLAEHAVWSLKCFPDWEWYNINIFGTDDPNHFWVECDGHGKILFPGYPEGYYENHFLHSFELEDGKIKRNREFMNVFQQLRALSIPVPQIKREGIPT
|
Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule. PhzB1 (operon phzA1B1C1E1F1G1) has a role in the biosynthesis of the phenazine during planktonic growth.
|
O69753
|
D7BAR0
|
GGAP_MEISD
|
Glucosylglycerate phosphorylase
|
Meiothermus
|
MSSLTPELRQSILEHLGFLYGERAPAVLGRLEEICSGFPAQRREGGWSEKDALLITYGDQIHAEGEPPLQTLYDFLYERLRGVFSGVHLLPFYPSTSDDGFSVVDFQRVDPELGTWTDIRIIAQDFRLMADLVCNHVSASSPWFQGFLQDDPQYQGFFITVDPGTDLSTVFRPRALPLLTPFQTPSGEKLVWTTFSPDQTDLNYANPEVLLEVIEALLCYVRNGAGLIRLDAVGFIWKEIGTSCMHLEGAHRIVKLMRLVLDAVAPHVLLVSETNAPHRENISYFGNGHDEAQLVYQFPLPPLVMHTFRTGDASKLAGWAAGLTLPSERTTFFNFLASHDGIGVVPAGGILQPEEIAALVRQALEHGGRVNHKDTPDGPVPYELCLTLFDALSNPNSDEAEDLKIARFLAANVILLSLQGIPGVYIHSLFGSPSDHAGFEESGIPRRLNRHKFTKAELEERLADPASRAAKILAAYSHLLRVRSMHPAFHPNAPQRILPSTEVLRIVRGEGDQAVGCYINVTDRPQVVSRIGKNLITGQWFTGVLKPYQAAWIID
|
Catalyzes the reversible phosphorolysis of glucosylglycerate into alpha-D-glucose 1-phosphate (Glc1P) and D-glycerate. May be a regulator of intracellular levels of glucosylglycerate, a compatible solute that primarily protects organisms facing salt stress and very specific nutritional constraints. Has a very strict substrate specificity. Cannot catalyze the phosphorolysis of sucrose or synthesize sucrose from Glc1P and D-fructose.
|
D7BAR0
|
B2UFK5
|
ERPA_RALPJ
|
Putative iron-sulfur cluster insertion protein ErpA
|
Ralstonia
|
MNAVAQAATPDVNEVPAPLVFTDSAADKVKQLIEEEGNPELKLRVFVQGGGCSGFQYGFTFDEETNEDDTTMTKNGVSLLIDSMSYQYLVGAEIDYKEDINGAQFVIKNPNASTTCGCGSSFSV
|
Required for insertion of 4Fe-4S clusters.
|
B2UFK5
|
P82951
|
HEPC_MORCS
|
Hepcidin
|
Morone
|
MKTFSVAVAVAVVLAFICLQESSAVPVTEVQELEEPMSNEYQEMPVESWKMPYNNRHKRHSSPGGCRFCCNCCPNMSGCGVCCRF
|
Antimicrobial activity against Gram-negative bacteria such as E.coli.
|
P82951
|
M1V4Y8
|
CFA73_CHLRE
|
Modifier of inner arms 2 protein
|
Chlamydomonas
|
MDEEGSATARAKMMPQTLVLDHVSPATRLLEKRRQMFEVQEALEAQKQDFNRKEEVFKRREEALKLKDLELQESLIRFSKFLQENDSKRARAEKKANDEIKARIQKEKEIEQLTEVLEELKSEKERILEVLEKNMRYQHYLESVLEVADEYQEVADLLLRHATLSATNADLKDHQRKCSELAEKVRTELQIYVKQKTDEILNLNNQVAKLKTELEGYEAEAMVQEAKKDSSLQIASQRTLEYGQVVLSADNIFNRCRSKSSIGHPAESNPLHQLDVIGNFVSDLGSIIKQFKQEQAKRASLASRAEIE
|
As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of inner dynein arm.
|
M1V4Y8
|
C5D764
|
ARGC_GEOSW
|
N-acetyl-glutamate semialdehyde dehydrogenase
|
unclassified Geobacillus
|
MNIAIIGATGYGGVELLRFLQHHPHVHHCSLYSSSQDGIHFSESFPHVGEIEGAILQKIDVEQMADECEVVFFATPPGVSSTLAPTLIDKGVKVIDLSGDFRLKDRSVYEMWYKRQTASDHYLQQAVYGLTEWNKEDIQKAQLLSNPGCYPTAALLGLAPLVKERLIEEDSIIVDAKSGVSGAGRKASLNTHFSEVNENVKIYKVNSHQHIPEIEQMLKAWNERIQPITFSTHLIPMTRGIMATIYAKAKKELSLETLLDLYKTSYEDSKFVRVRKPGQFPATKEVYGSNYCDIGVAYDERTGRVTVVSVIDNLVKGAAGQAIQNLNVMMGWDEESGLMLAPIYP
|
Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
|
C5D764
|
C3L3F3
|
ERA_CLOB6
|
GTPase Era
|
Clostridium
|
MFKSGFVTIVGRPNVGKSTLLNAIMKEKLSIVSCRPQTTRNNIQTILTEDNYQLVFVDTPGIHKPKHKLGEYMVKSASDAMKDVDLVLFLINPDEKPGRGDLFIIEQLKEVKVPVFLVLNKIDENPQEKVAETLKTYSELMEFEEIIPISALKGKNIDLLKELMFKYIPEGPQYYPEDMIIDQNERFIVAEIVREKALRLLSEEVPHGIAVEILQMKKNEKGTYHIEGNILCEKNSHKPIIIGKGGSKLKKISQYARQDIEAFLQSKVYIRLWVKVKEEWRDNQSLLKELGYKNMK
|
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
|
C3L3F3
|
Q07276
|
KLK1_MACFA
|
Tissue kallikrein
|
Macaca
|
MWFLVLCLALSLGGTGRAPPIQSRIVGGWECSQPWQAALYHFSTFQCGGILVHPQWVLTAAHCISDNYQLWLGRHNLFDDEDTAQFVHVSESFPHPGFNMSLLKNHTRQADDYSHDLMLLRLTQPAEITDAVQVVELPTQEPEVGSTCLASGWGSIEPENFSFPDDLQCVDLEILPNDECAKAHTQKVTEFMLCAGHLEGGKDTCVGDSGGPLTCDGVLQGVTSWGYIPCGSPNKPAVFVKVLSYVKWIEDTIAENS
|
Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin.
|
Q07276
|
B2VIT0
|
AROL_ERWT9
|
Shikimate kinase 2
|
Erwinia
|
MSLPIYLIGARGCGKTTVGQALALALGYDFCDTDHYLQQARQQTVADIVAIEGWAGFRAREAESLKAVTAASKVIATGGGMVLAEENRLYMREHGRVIYLNANALVLAARLEAYPLADQRPTLTGRPVAEEMVEVLAARDALYQLAAHHIIDAMQTPDAVVNQIVSSLSLARAS
|
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
|
B2VIT0
|
O25488
|
ACPS_HELPY
|
4'-phosphopantetheinyl transferase AcpS
|
Helicobacter
|
MIGIDIVSIARIEKCVKRFKMKFLERFLSPSEIVLCKDKSSSIAGFFALKEACSKALQVGIGKELSFLDIKISKSPKNAPLITLSKEKMDYFNIQSLSASISHDAGFAIAVVVVSSSNE
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
O25488
|
B3EHV0
|
RISB_CHLL2
|
6,7-dimethyl-8-ribityllumazine synthase
|
Chlorobium
|
MQIKQIEGSLSAKDIRFALVVSRFNDFIGQKLVEGAIDCILRHGGSEEQITVYRCPGAFELPMVAKKVAMSGSADAVIALGVIIRGSTPHFDVIAAEATKGIAQVSLDTMIPVSFGVLTTENLEQAIERAGTKAGNKGFDAAMTAMEMVNLYRQF
|
Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.
|
B3EHV0
|
A7ZPW0
|
RLMN_ECO24
|
tRNA m2A37 methyltransferase
|
Escherichia
|
MSEQLVTPENVTTKDGKINLLDLNRQQMREFFKDLGEKPFRADQVMKWMYHYCCDNFDEMTDINKVLRGKLKEVAEIRAPEVVEEQRSSDGTIKWAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIVGAAKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDEIRDEIVPINKKYNIETFLAAVRRYLEKSNANQGRVTIEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVLMSYGFTTIVRKTRGDDIDAACGQLAGDVIDRTKRTLRKRMQGEAIDIKAV
|
Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity.
|
A7ZPW0
|
B0G143
|
UCPB_DICDI
|
Uncoupler protein B
|
Dictyostelium
|
MTSQESIGIKFLFGGLSCMGAAVVSNPVDVLKTRFQIHGEGIDSKSLGLVNGTIKIIKNEGISAMYKGLTPSLLREATYSTLRMGGYDVIKNYFIDSNGKTNLLSKVTSGALSGALGACITSPTDLIKVRMQASSKGVKYDSISSAFKEIIAKEGIKGLWKGVGPTTQRAALLTASQIPSYDHIKHMILDHGIIQVDGLQVHIVSSIFAGLIASITTSPVDLVKTRIMNQPFDSNGVGLIYKSSYDCFKKTFQSEGISGLYKGFLPNWFRIGPHTIVTFILYEYLRKVSGIKPI
|
Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane.
|
B0G143
|
Q97R61
|
FPG_STRPN
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Streptococcus
|
MPELPEVETVCRGLEKLIIGKKISSIEIRYPKMIKTDLEEFQRELPSQIIESMGRRGKYLLFYLTDKVLISHLRMEGKYFYYPDQGPERKHAHVFFHFEDGGTLVYEDVRKFGTMELLVPDLLDVYFISKKLGPEPSEQDFDLQVFQSALAKSKKPIKSHLLDQTLVAGLGNIYVDEVLWRAQVHPARPSQTLTAEEATAIHDQTIAVLGQAVEKGGSTIRTYTNAFGEDGSMQDFHQVYDKTGQECVRCGTIIEKIQLGGRGTHFCPNCQRRD
|
Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). 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.
|
Q97R61
|
P58427
|
TXHP3_HETVE
|
Toxin AU5C/KJ7
|
Heteropoda
|
ECGTLFSGCSTHADCCEGFICKLWCRYERTW
|
Blocks transient outward voltage-gated potassium channels in rat ventricular myocytes (thus prolonging action-potential duration) and rat Kv4.2/KCNA4 channels expressed in Xenopus oocytes. Is also a weak blocker of calcium channels in rat cerebellar granule cells.
|
P58427
|
Q1GPB8
|
RL15_SPHAL
|
50S ribosomal protein L15
|
Sphingopyxis
|
MTIKLNELRDNNGARKGRMRVGRGIGSGKGKTAGRGQKGQKARSGVAINGFEGGQMPLHMRIPKRGFNNIFGKDFAIVNLGMVQKLIDAKKLDAKATIDHAALKAAGVARGGKDGVRLLAKGELTAKVTFAVAGASKGAIEAVEKAGGKVELPEARPEGDGKKATRKAEAAAKNA
|
Binds to the 23S rRNA.
|
Q1GPB8
|
O08603
|
RAE1B_MOUSE
|
Retinoic acid early-inducible protein 1-beta
|
Mus
|
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKDPTPADPLWYEAKCFVGEILILHLSNINKTMTSGDPGETANATEVKKCLTQPLKNLCQKLRNKVSNTKVDTHKTNGYPHLQVTMIYPQSQGRTPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWKDDGEFVKQLKFLIHECSQKMDEFLKQSKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
|
Acts as a ligand for KLRK1.
|
O08603
|
Q3A668
|
RIBB_SYNC1
|
3,4-dihydroxy-2-butanone 4-phosphate synthase
|
Syntrophotalea
|
MSQSLLDRFGTPLERVHLAIDRLRQGRGVLLVDDENRENEGDLIFPAETITPAQMAMMIRECSGIVCLCLTEDKLKQLELPQMVSDNTSANQTAFTLSIEARQGVTTGVSAADRVTTIRTAVADDCRPDDLARPGHVFPLRARPGGVLTRRGHTEGTVDLMRMAGYKPAGVLCELTNEDGTMARLPEIITFAERHYLSVVSIEDLALALESHMEKSA
|
Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
|
Q3A668
|
Q5P4R1
|
METXS_AROAE
|
Homoserine transsuccinylase
|
Aromatoleum
|
MIQPQSVGAVVPQRAHFAEPLPLRSGDALPEYELLYETYGELNAARSNAVLVCHALSGSHHVAGHYADDPGNIGWWDNLVGPGKPLDTRKFFVIGVNNLGGCHGTTGPASINPASGKPWGADFPFVTVEDWVAAQARLADRLGIERFAAVVGGSLGGMQALSWTLQYPERIGHAVLVASAPRLTAQNIAFNEVARQAILSDPDFHGGHYYEHGVVPARGLKLARMLGHITYLSDDAMADKFGRTLRHGKAVYSYDVEFEIESYLRYQGDKFAGFFDANTYLLTTKALDYFDPAFEHGGILRAALARASADFLVVSFSTDWRFSPARSREIVYSLLHNRRNVSYAEIESDAGHDSFLLDDAHYHELLAAYFDRIEV
|
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine.
|
Q5P4R1
|
A1A4L0
|
SNX4_BOVIN
|
Sorting nexin-4
|
Bos
|
MEQAAPDPERLWQPAPLEPLSHPDAGLESMVGEETKGARDEGPGDGTMTENNFSLKKIEISVSEAEKRTGRNAMNMQETYTAYLIETRSVEHNDGQSVLTDSLWRRYSEFELLRNYLLVYYPHIVVPPLPEKRAEFVWHKLSADNMDPDFVERRRIGLENFLLRVASHPILCRDKIFYLFLTQEGNWKETVNETGFQLKADSRLKALNATFRVKNPDKRFIELKHYSDELQSVISHLLRVRARVADRLYGVYKVHGNYGRVFSEWSAIEKEMGDGLQSAGHHMDVYASSIDDILEDEEHYADQLKEYLFYAEALRAVCRKHELMQYDLEMAAQDLASKKQQCEELATGTVRTFSLKGMTTKLFGQETPEQREARIKMLEEQIKEGEQQLKSKNLEGREFVRNAWADIERFKEQKNHDLKEALISYAVMQISMCKKGIQVWTNAKECFSKM
|
Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Plays a role in recycling endocytosed transferrin receptor and prevent its degradation. Involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A.
|
A1A4L0
|
O29285
|
AMT1_ARCFU
|
Af-Amt1
|
Archaeoglobus
|
MSDGNVAWILASTALVMLMVPGVGFFYAGMVRRKNAVNMIALSFISLIITVLLWIFYGYSVSFGNDISGIIGGLNYALLSGVKGEDLLFMMYQMMFAAVTIAILTSAIAERAKVSSFILLSALWLTFVYAPFAHWLWGGGWLAKLGALDFAGGMVVHISSGFAALAVAMTIGKRAGFEEYSIEPHSIPLTLIGAALLWFGWFGFNGGSALAANDVAINAVVVTNTSAAVAGFVWMVIGWIKGKPGSLGIVSGAIAGLAAITPAAGFVDVKGAIVIGLVAGIVCYLAMDFRIKKKIDESLDAWAIHGIGGLWGSVAVGILANPEVNGYAGLLFGNPQLLVSQLIAVASTTAYAFLVTLILAKAVDAAVGLRVSSQEEYVGLDLSQHEEVAYT
|
Involved in the uptake of ammonium/ammonia (NH(4)(+)/NH(3)) . Transport is electrogenic . Transport the ammonium and methylammonium cation with high specificity .
|
O29285
|
Q21IR9
|
UBIG_SACD2
|
3-demethylubiquinone 3-O-methyltransferase
|
Saccharophagus
|
MTTQELNVDSAEIAKFERLAARWWDLEGEFKPLHDLNPLRANYIDERAQVAEKKLLDVGCGGGILCEAMAQRGAIVTGIDMGDAPLEVAKLHSLESGVNVDYIKTTAEEFAAKHPQSYDVVTCLEMLEHVPDPAQTIAACAQLVKPGGDIFFSTINRNPKAYLFAVVGAEYVLKMLPKGTHDYNKFIRPSELAQWMRNAGLELQEMCGMTYNPITKHYKLNAKDVSVNYIMHARKI
|
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
|
Q21IR9
|
B1HVD8
|
HEM1_LYSSC
|
Glutamyl-tRNA reductase
|
Lysinibacillus
|
MHTIVVGLNYKTAPVEIREKLSFIESELPQAMEALQKQKSILENVIVSTCNRTEIYAVVDQLHTGRHFVKQFLADWFDLPVETFSSYLTIREEDEAVEHLFKVTAGIDSMVLGETQILGQVKKSFLSGQEIGTTGTVYNQLFKQAVTFAKRAHNETAIGENAVSVSYAAVELAKKIFGSLQRKHVAILGAGKMGELAIENLYGSGVGKVTVINRTFEKAESLAAKFHGQAKSMKELQCSLLEADILITSTGATDYVIDYELMQFVERLRKGKPLFMVDIAVPRDIDPRVGDLPNVFLYDIDDLQGIVEANLAERERAAADITDMIGHEVIQFKDWVSTLGVVPVISALRKKANRIQEETMTSIENKMPDLTERERKILSKHTKSIINQLLKEPILQAKEMANSPKANEQLRLFQQIFGIEEAVEAEVQEMTKQELERKERAQATQTSAEPKYSF
|
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
|
B1HVD8
|
Q9FA05
|
RS10_BRAPL
|
30S ribosomal protein S10
|
Brachyspira
|
MKEQKIRVKLKAFDIELIDQSAQSIVASVKKTGARVSGPIPLPTSIRKVTVIRSPHVNIKSREQFEMRVYKRLIDIFDVTPQTTESLKKLALPAGVDVQLK
|
Involved in the binding of tRNA to the ribosomes.
|
Q9FA05
|
Q96G91
|
P2Y11_HUMAN
|
P2Y purinoceptor 11
|
Homo
|
MAANVSGAKSCPANFLAAADDKLSGFQGDFLWPILVVEFLVAVASNGLALYRFSIRKQRPWHPAVVFSVQLAVSDLLCALTLPPLAAYLYPPKHWRYGEAACRLERFLFTCNLLGSVIFITCISLNRYLGIVHPFFARSHLRPKHAWAVSAAGWVLAALLAMPTLSFSHLKRPQQGAGNCSVARPEACIKCLGTADHGLAAYRAYSLVLAGLGCGLPLLLTLAAYGALGRAVLRSPGMTVAEKLRVAALVASGVALYASSYVPYHIMRVLNVDARRRWSTRCPSFADIAQATAALELGPYVGYQVMRGLMPLAFCVHPLLYMAAVPSLGCCCRHCPGYRDSWNPEDAKSTGQALPLNATAAPKPSEPQSRELSQ
|
Receptor for ATP and ADP coupled to G-proteins that activate both phosphatidylinositol-calcium and adenylyl cyclase second messenger systems. Not activated by UTP or UDP.
|
Q96G91
|
B0S0S7
|
GUAA_FINM2
|
Glutamine amidotransferase
|
Finegoldia
|
MKHQLVIVVDFGGQYNQLIARRVRDLNVYCEVVPYKKALDVIKEKQPIGIIFTGGPNSVYEENSPQIEKEIFELNIPILGMCYGMQLISKDFGGVVEKAKNREFGKTNAKISNQSSILKGMSDESIVWMSHTDFVSEKPEGFDIIQTTDSCPVAAIANEDKKIFAVQYHPEVNHTVEGKTLIKNFLYEICKADGDWTMENFLEEQIQKIRKTVGDKKVLLALSGGVDSSVCAALLSRAIGKNLTCVFVDHGLMRKNEGDEVEAAFKNDELNFVRVNAKDRFLNKLKGVSDPEQKRKIIGEEFIRVFEDEAKKIGSVDFLAQGTIYPDVIESGQGDASVIKSHHNVGGLPDVVDFKDLIEPLRDLFKDEVRRLGLELEMPEYLVYRQPFPGPGLGIRVMGEITEEKLEVLREADFIFRDEVAKAGIDKDINQYFAVITNNRTVGVMGDFRTYDYTLALRAVTTTDFMTADWARIPYEVLDKTSVRIINEVDHINRIVYDITSKPPATIEWE
|
Catalyzes the synthesis of GMP from XMP.
|
B0S0S7
|
Q660M8
|
POTA_BORGP
|
Spermidine/putrescine import ATP-binding protein PotA
|
Borreliella
|
MDNCILEIRNLSHYYDNNGNKTLDNINLKIKKNEFITLLGPSGCGKTTLIKILGGFLSQKNGEIYFFSKEISKTSPNKREINTVFQNYALFPHMNVFDNISFGLRMKKTPKDIIKEKVKTSLSLIGMPKYAYRNINELSGGQKQRVAIARAMVMEPKLLLLDEPLSALDLKMRQEMQKELKKIQRQLGITFIYVTHDQEEALTMSDRIVVMNEGIILQVGTPEEIYNEPKTKFVADFIGESNIFDGTYKKELVVSLLGYEFECLDKGFEAEEAVDLVIRPEDIKLLPKGKGHLSGIITSAIFQGVHYEMTLEIQKTNWIVQSTRLTKVGEEVDIFLEPDDIHVMHKE
|
Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
|
Q660M8
|
O75843
|
AP1G2_HUMAN
|
Gamma2-adaptin
|
Homo
|
MVVPSLKLQDLIEEIRGAKTQAQEREVIQKECAHIRASFRDGDPVHRHRQLAKLLYVHMLGYPAHFGQMECLKLIASSRFTDKRVGYLGAMLLLDERHDAHLLITNSIKNDLSQGIQPVQGLALCTLSTMGSAEMCRDLAPEVEKLLLQPSPYVRKKAILTAVHMIRKVPELSSVFLPPCAQLLHERHHGILLGTITLITELCERSPAALRHFRKVVPQLVHILRTLVTMGYSTEHSISGVSDPFLQVQILRLLRILGRNHEESSETMNDLLAQVATNTDTSRNAGNAVLFETVLTIMDIRSAAGLRVLAVNILGRFLLNSDRNIRYVALTSLLRLVQSDHSAVQRHRPTVVECLRETDASLSRRALELSLALVNSSNVRAMMQELQAFLESCPPDLRADCASGILLAAERFAPTKRWHIDTILHVLTTAGTHVRDDAVANLTQLIGGAQELHAYSVRRLYNALAEDISQQPLVQVAAWCIGEYGDLLLAGNCEEIEPLQVDEEEVLALLEKVLQSHMSLPATRGYALTALMKLSTRLCGDNNRIRQVVSIYGSCLDVELQQRAVEYDTLFRKYDHMRAAILEKMPLVERDGPQADEEAKESKEAAQLSEAAPVPTEPQASQLLDLLDLLDGASGDVQHPPHLDPSPGGALVHLLDLPCVPPPPAPIPDLKVFEREGVQLNLSFIRPPENPALLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGGLPITQLFRILNPNKAPLRLKLRLTYDHFHQSVQEIFEVNNLPVESWQ
|
(Microbial infection) Involved in MVB-assisted maturation of hepatitis B virus (HBV).
|
O75843
|
Q9KGM3
|
RECR_HALH5
|
Recombination protein RecR
|
Halalkalibacterium (ex Joshi et al. 2022)
|
MQYPEPIAKLIEGFMRLPGIGPKTASRLAFFVLEMKEDDVLDFAKALVNVKRKLTYCSVCHNITDTDPCRICEDSKRDESVICVVQDAKDVIAMEKMKEYHGKYHVLHGAISPMDGIGPEDIKIPELIKRLQDDTIQEVIVATNPTIEGEATAMYISRLVKPTGIKVTRIAHGLPVGGDLEYADEVTLSKAMEGRREL
|
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.
|
Q9KGM3
|
Q61233
|
PLSL_MOUSE
|
pp65
|
Mus
|
MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKVFHGLKSTEVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMINLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPKGDEEGIPAVVIDMSGLREKDDIQRAECMLQQAERLGCRQFVTATDVVRGNPKLNLAFIANLFNKYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPRVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNKPPYPKLGGNMKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNILEDIGGGQKVNDDIIVNWVNTTLKEAQKSSSIASFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV
|
Actin-binding protein. Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. Modulates the cell surface expression of IL2RA/CD25 and CD69.
|
Q61233
|
A5UAH8
|
RUVB_HAEIE
|
Holliday junction ATP-dependent DNA helicase RuvB
|
Haemophilus
|
MIEADRIISGQAKVDEDVIDRAIRPKLLADYVGQPQVREQMDIFIKAAKLRQDALDHLLIFGPPGLGKTTLANIVANEMGVNIRTTSGPVLEKAGDLAAMLTNLEPHDVLFIDEIHRLSPAIEEVLYPAMEDYQLDIMIGEGPAARSIKLDLPPFTLVGATTRAGSLTSPLRDRFGIVQRLEFYSVEDLTSIVARSAGCLNLELEQQAAFEVARRSRGTPRIANRLLRRVRDYADVRNGGVISVDVAKQALSMLDVDDAGFDYLDRKLLSAVIERFDGGPVGLDNLAAAIGEERDTIEDVLEPYLIQQGFLQRTPRGRIATSKTYRHFGLQKLSD
|
The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing.
|
A5UAH8
|
Q8L202
|
ENO_BARHE
|
2-phosphoglycerate dehydratase
|
Bartonella
|
MTIIVDIIGREVLDSRGNPTVEVEVHLENGALGRALVPSGASTGAHEAVELRDGGTRYQGKGVKKAIAAINGEILEELGGRDARNQIGIDQAMIALDGTPNKARLGANALLGVSLAVAKAAAESLSLPLYRYIGGTQAHILPTPMMNIINGGVHADNPIDFQEFMIIPVGASTLKEAIRYGAEIFHTLKKRLKDAGYNTNVGDEGGFAPQFKSAEQAIDFIMESIIACGYKPGEQIALGLDCAATEFYKNGSYFYEGEGKYRDVGEQVDYLAQLIKTYPIITIEDGMAEDDWEGWKLLTDSIGKKCQLVGDDLFVTNSARLRDGIKMGAANSILIKVNQIGTLSETLDAVETAHKAGYRAIISHRSGETEDSFIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEMLGLQACYAGNWYC
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
Q8L202
|
Q8MR62
|
VIAF1_DROME
|
Viral IAP-associated factor homolog
|
Sophophora
|
MQDPNEDTEWNDVLRAKGIIGPKAKEAEITEDQIQKLMDDAIQRRTDLPLNEGQRDKKIDDMSLDELDELEDSEDEAVLEQYRQRRIAEMRATAEKARFGSVREISGQDYVNEVTKAGEGIWVVLHLYANGVPLCALIHHHMQQLAVRFPQTKFVRSVATTCIPNFPEKNLPTIFIYHEGALRKQYIGPLELRGDKLTAEELEFMLGQAGAVPTEITEDPRPQIRDKMLADLEDKSSDFY
|
Modulates the activation of caspases during apoptosis.
|
Q8MR62
|
A0A0K8R374
|
EV675_IXORI
|
Evasin P675
|
Ixodes
|
MEVKTFAFLQIAVIIALGLHLAPAGSNQLSGPQSSANSNDAVFCDTNCTQGTDGAWSGCRGDCFCVHVGNSTEGRCIELIGDFDYSTPGAED
|
Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL10, CXCL11 and CXCL13.
|
A0A0K8R374
|
P77744
|
ABGR_ECOLI
|
HTH-type transcriptional regulator AbgR
|
Escherichia
|
MAFQVKIHQIRAFVEVARQGSIRGASRMLNMSQPALSKSIQELEEGLAAQLFFRRSKGVTLTDAGESFYQHASLILEELRAAQEDIRQRQGQLAGQINIGMGASISRSLMPAVISRFHQQHPQVKVRIMEGQLVSMINELRQGELDFTINTYYQGPYDHEFTFEKLLEKQFAIFCRPGHPAIGARSIKQLLDYSWTMPTPHGSYYKQLSELLDDQAQTPQVGVVCETFSACISLVAKSDFLSKLPEEMGCDPLHGQGLVMLPVSEILPKAAYYLIQRRDSRQTPLTASLITQFRRECGYLQS
|
Could be the regulator of the abg operon.
|
P77744
|
A0A1D8PCI6
|
RS4_CANAL
|
40S ribosomal protein S4
|
Candida
|
MARGPKKHLKRLAAPSHWMLDKLSGTYAPRPSAGPHKLRESLPLVVFLRNRLKYALNGREVKAIMMQQHVQVDGKVRTDTTYPAGFMDVITLEATNEHFRLVYDVKGKFAVHRISAEEAAYKLGKVKKVQLGKKGVPYVVTHDGRTIRYPDPLIRANDTVKIDLATGKIDDFIKFDTGRLVMVTGGRNLGRVGVIVHREKHEGGFDLVHIKDALENTFVTRLSNVFVIGTEAGKPWVSLPKGKGIKLSISEERDRRRAQQGL
|
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
|
A0A1D8PCI6
|
Q4FMU2
|
SELO_PELUB
|
Protein adenylyltransferase SelO
|
Candidatus Pelagibacter
|
MTIGWHFDNSYSRLPKTFKENINPVAVNAPEILILNKDLANKLDLDFSNINDDDLSKIFSGNLLPEGSNSIAQAYAGHQFGHFTMLGDGRAVLIGEHLTKNNERFDIQFKGSGRTPFSRSGDGRAVLGPMLREYIISEAMHFLKIPTTRSLAVVKTGEDVVREQISQGAILTRVALGHLRVGTFQYIAAKQNISDLEILINYTIEKYYPNIKSSKNKALDLLNVLIEKQTQLVIDWMRVGFIHGVMNTDNMSISGETIDYGPCAFMDVYDPKTVFSSIDQLGRYAYENQPKITKWNLTRFAECLIPLISTNEDEAIKLATEALDKFEQNYETKWLNMMRDKLGLYGEDKEDKNLIMELLNWMKEKKADYTNTFIFLMNKTIKNSEVYDNADFDLWKTKWMKRLVMFGNTHDKSVDLMSSCNPMVIPRNHKIEEALMLANNGDLTLFNKLIKILKNPYLVNNGDLELMSPAPHSDEKYQTFCGT
|
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
|
Q4FMU2
|
Q975U2
|
PAN_SULTO
|
Proteasome regulatory particle
|
Sulfurisphaera
|
MSDELDSYRAKHYNSDDPIVRLLEEKIESLTKELEKLRQDLNWYKGELEKLLAPPYIEAIVLDILPDGKVIVRSSSGPNLIVNVSSNIDIKKLKPGSLVALTQRGSTIVEVLPEREDAYVKSFEVIEKPNVHYSDIGGLNEQINEIREVIELPLKNPELFKEIGIDPPKGVLLYGPPGTGKTLLAKAVATESNATFIQVVASEFAQKFVGEGARIVREVFELARRKAPSIVFIDEIDAIGAKRVDMGTSGEREIQRTLMQLLAEIDGFKPLDNVKIIAATNRLDILDPALLRPGRFDRLIEVPLPNFEGRKEIFRIYLQKMKTDGNIRYDILASMTEGFSGAEIKNVCTEAGYIAIRNGRKYVNMTDLITAIEKIKAKNNKAKNTDRTEKYV
|
ATPase which is responsible for recognizing, binding, unfolding and translocation of substrate proteins into the archaeal 20S proteasome core particle. Is essential for opening the gate of the 20S proteasome via an interaction with its C-terminus, thereby allowing substrate entry and access to the site of proteolysis. Thus, the C-termini of the proteasomal ATPase function like a 'key in a lock' to induce gate opening and therefore regulate proteolysis. Unfolding activity requires energy from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S proteasome association which triggers gate opening, and supports translocation of unfolded substrates.
|
Q975U2
|
Q9LWN0
|
GSK1_ORYSJ
|
Shaggy/GSK3-like kinase 21
|
Oryza sativa
|
MEAPPGPEPMELDAPPPPAAVAAAAATAGISEKVLQKKEEGGGDAVTGHIISTTIGGKNGEPKRTISYMAERVVGTGSFGIVFQAKCLETGETVAIKKVLQDRRYKNRELQLMRAMEHPNVICLKHCFFSTTSRDELFLNLVMEYVPETLYRVLKHYSNANQRMPLIYVKLYIYQLFRGLAYIHTVPGVCHRDVKPQNVLVDPLTHQVKLCDFGSAKVLVPGEPNISYICSRYYRAPELIFGATEYTTSIDIWSAGCVLAELLLGQPLFPGESAVDQLVEIIKVLGTPTREEIRCMNPNYTEFKFPQIKAHPWHKIFHKRMPPEAIDLASRLLQYSPSLRCTALDACAHSFFDELREPNARLPNGRPFPPLFNFKHELASASPELIHRLIPDHIRRQHGLNFAHAGS
|
Probable serine-threonine kinase that may act as a negative regulator of brassinosteroid (BR) signaling during flower development. May have physiological roles in stress signal-transduction pathways . Phosphorylates LIC in response to BR perception .
|
Q9LWN0
|
Q9X1X6
|
ASPD_THEMA
|
L-aspartate dehydrogenase
|
Thermotoga
|
MTVLIIGMGNIGKKLVELGNFEKIYAYDRISKDIPGVVRLDEFQVPSDVSTVVECASPEAVKEYSLQILKNPVNYIIISTSAFADEVFRERFFSELKNSPARVFFPSGAIGGLDVLSSIKDFVKNVRIETIKPPKSLGLDLKGKTVVFEGSVEEASKLFPRNINVASTIGLIVGFEKVKVTIVADPAMDHNIHIVRISSAIGNYEFKIENIPSPENPKTSMLTVYSILRTLRNLESKIIFG
|
Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate. Does not show aspartate oxidase activity. Is also able to catalyze the reverse reaction, i.e. the reductive amination of oxaloacetate.
|
Q9X1X6
|
Q16665
|
HIF1A_HUMAN
|
PAS domain-containing protein 8
|
Homo
|
MEGAGGANDKKKISSERRKEKSRDAARSRRSKESEVFYELAHQLPLPHNVSSHLDKASVMRLTISYLRVRKLLDAGDLDIEDDMKAQMNCFYLKALDGFVMVLTDDGDMIYISDNVNKYMGLTQFELTGHSVFDFTHPCDHEEMREMLTHRNGLVKKGKEQNTQRSFFLRMKCTLTSRGRTMNIKSATWKVLHCTGHIHVYDTNSNQPQCGYKKPPMTCLVLICEPIPHPSNIEIPLDSKTFLSRHSLDMKFSYCDERITELMGYEPEELLGRSIYEYYHALDSDHLTKTHHDMFTKGQVTTGQYRMLAKRGGYVWVETQATVIYNTKNSQPQCIVCVNYVVSGIIQHDLIFSLQQTECVLKPVESSDMKMTQLFTKVESEDTSSLFDKLKKEPDALTLLAPAAGDTIISLDFGSNDTETDDQQLEEVPLYNDVMLPSPNEKLQNINLAMSPLPTAETPKPLRSSADPALNQEVALKLEPNPESLELSFTMPQIQDQTPSPSDGSTRQSSPEPNSPSEYCFYVDSDMVNEFKLELVEKLFAEDTEAKNPFSTQDTDLDLEMLAPYIPMDDDFQLRSFDQLSPLESSSASPESASPQSTVTVFQQTQIQEPTANATTTTATTDELKTVTKDRMEDIKILIASPSPTHIHKETTSATSSPYRDTQSRTASPNRAGKGVIEQTEKSHPRSPNVLSVALSQRTTVPEEELNPKILALQNAQRKRKMEHDGSLFQAVGIGTLLQQPDDHAATTSLSWKRVKGCKSSEQNGMEQKTIILIPSDLACRLLGQSMDESGLPQLTSYDCEVNAPIQGSRNLLQGEELLRALDQVN
|
(Microbial infection) Upon infection by human coronavirus SARS-CoV-2, is required for induction of glycolysis in monocytes and the consequent pro-inflammatory state . In monocytes, induces expression of ACE2 and cytokines such as IL1B, TNF, IL6, and interferons . Promotes human coronavirus SARS-CoV-2 replication and monocyte inflammatory response .
|
Q16665
|
P81078
|
CYC31_DESAC
|
Cytochrome c3, 10 kDa
|
Desulfuromonas
|
ADSLTQFDGIKGRYSHEAFYEEKACDSCHLNK
|
Participates in sulfate respiration coupled with phosphorylation by transferring electrons from the enzyme dehydrogenase to ferredoxin.
|
P81078
|
Q39027
|
MPK7_ARATH
|
Mitogen-activated protein kinase 7
|
Arabidopsis
|
MAMLVEPPNGIKQQGKHYYSMWQTLFEIDTKYVPIKPIGRGAYGVVCSSINRETNERVAIKKIHNVFENRVDALRTLRELKLLRHVRHENVIALKDVMLPANRSSFKDVYLVYELMDTDLHQIIKSSQSLSDDHCKYFLFQLLRGLKYLHSANILHRDLKPGNLLVNANCDLKICDFGLARTSQGNEQFMTEYVVTRWYRAPELLLCCDNYGTSIDVWSVGCIFAEILGRKPIFPGTECLNQLKLIINVVGSQQESDIRFIDNPKARRFIKSLPYSRGTHLSNLYPQANPLAIDLLQRMLVFDPTKRISVTDALLHPYMAGLFDPGSNPPAHVPISLDIDENMEEPVIREMMWNEMLYYHPEAEISNA
|
MKK3-MPK7 module acts as a positive regulator of PR1 gene expression.
|
Q39027
|
A4QJB9
|
NDHK_AETCO
|
NADH-plastoquinone oxidoreductase subunit K
|
Aethionema
|
MNSIKFPVLDRTTKNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDAITKLRKKIAREIYKDKIRPQQGNRCFTTNHKFFIVRSTDTGNSDQELLYPPSSTSEISTETFFKYKSPVSSHELVNSGGF
|
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.
|
A4QJB9
|
B7J3V1
|
MURC_ACIF2
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Acidithiobacillus
|
MRNWVRQIHMVGIGGSGMRGIAEVLLNLGYAVSGSDLRPGNSTLRLTDLGARIFSGHEAANVRGADVVVISSAIPESNPEVQAARELRIPVIRRAEMLAELMRFKQGIAIAGTHGKTTTTSLVASILGAGGLDPTFVIGGRLKSAGTHAALGSGEYLVAEADESDASFLYLSPVMAVVTNIDADHMETYGGSLDNLRGAFLQFLQRLPFYGLAVLCTDEAVVAGLIPELRTPVLRYGFGADADLQARDVTVQGIGSRFAVWRRVDSDYVHWLDVELGIPGRHNVLNALAAIGIASKVGIPESTIATALADFRGVGRRFELVGTFDGITVVDDYGHHPREIAATIAAARSVWPERPLVVAFQPHRYSRTQALFADFVSSLAAADRVILTDIYSAGEKALPGVTGRALAEAMAAQGMSVRFLPDLLTAPQQIRAELPAGAVLLTLGAGSIASLAAQWPQVFGEDPS
|
Cell wall formation.
|
B7J3V1
|
P19108
|
ARRB_DROMI
|
Phosrestin I
|
Sophophora
|
MVVSVKVFKKATPNGKVTFYLGRRDFIDHLDYCDPVDGVIVVEPEYLKNRKVFGQLATTYRYGREEDEVMGVKFSKELILSRDEIVPMTNPNMEMTPMQEKLVRKLGSNAHPFTFHFPPNSPSSVTLQQEGDDNGKPLGVEYTIRAFVGDSEDDRQHKRSMVSLVIKKLQYAPLNRGQRLPSSLVSKGFTFSNGKISLEVTLDREIYYHGEKTAATVQVSNNSKKSVKSIKCFIVQHTEITMVNAQFSKHVAQLETKEGCPITPGANLTKTFYLIPLAANNKDRHGIALDGHLKDEDVNLASSTMVQEGKNTGDACGIVISYSVRIKLNCGTLGGEMQTDVPFKLLQPAPGTIEKKRSNAMKKMKSIEQHRNVKGYYQDDDDNIVFEDFAKMRMNNVNMAD
|
Undergoes light-induced phosphorylation, probably plays an important role in the photoreceptor transduction.
|
P19108
|
B6QAR7
|
DRE2_TALMQ
|
Anamorsin homolog
|
Talaromyces sect. Talaromyces
|
MPSLPVLIDTTPDFDFAPAQDATQKRTLLLAPPSIAAHEEKLRDIFATFDRSVTDLQMLDRLSAGFVTLPASAYDLVLVLTDTNGARRNEALGLLTRDVFNVLTPAMKPSAQLKLQDGPFQATEGREAILAGLVENNGAFEKPQYQEAAVPLRFGLKKKNKVAPEPVKVESVGFVDNYDDDELIDEDDLLAEEDLGRPVQQPAECKPDIAKKRRRACKDCTCGLAAQLEAEDAERREKANAELNVLKLKTDELNDEVDFTVQGKTGSCNSCSLGDAFRCEGCPFIGLPAFKPGEEVRIMNDMAQL
|
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex cfd1-nbp35. Electrons are transferred to dre2 from NADPH via the FAD- and FMN-containing protein tah18. Tah18-dre2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit rnr2.
|
B6QAR7
|
Q49539
|
DNAK_MESH2
|
P65
|
Mesomycoplasma
|
MAKEIILGIDLGTTNSVVAIIENQKPVVLENPNGKRTTPSVVAFKNNEEIVGDAAKRQLETNPEAIASIKRLMGTDKTVRANERDYKPEEISAKILAYLKEYAEKKIGHKVTKAVITVPAYFDNAQREATKNAGKIAGLQVERIINEPTAAALAFGLDKTEKEMKVLVYDLGGGTFDVSVLELSGGTFEVLSTSGDNHLGGDDWDNEIVNWLVKKIKEVYDFDPKSDKMALTRLKEEAEKTKINLSNQSVSTVSLPFLGMGKNGPINVELELKRSEFEKMTAHLIDRTRKPIVDALKQAKIEASDLDEVLLVGGSTRMPAVQSMIEHTLNKKPNRSINPDEVVAIGAAIQGGVLAGEISDVLLLDVTPLTLGIETLGGIATPLIPRNTTIPVTKSQIFSTAEDNQTEVTISVVQGERQLAADNKMLGRFNLSGIEAAPRGLPQIEVSFSIDVNGITTVSAKDKKTGKEQTITIKNTSTLSEEEINKMIQEAEENREADALKKDKIETTVRAEGLINQLEKSITDQGEKIDPKQKELLEKQIQELKDLLKEDKTDELKLKLDQIEAAAQSFAQATAQQANTSESDPKADDSNTIDAEIKQD
|
Acts as a chaperone.
|
Q49539
|
Q9LK29
|
CYC1A_ARATH
|
Ubiquinol-cytochrome c reductase complex cytochrome c1 subunit 1
|
Arabidopsis
|
MVGGGVIQQILRRKLHSQSLATPVLSWFSSKKAHEDAGSSGVRALALLGAGVTGLLSFSTVASADEAEHGLESPEYPWPHDGILSSYDHASIRRGHQVYQQVCASCHSMSLISYRDLVGVAYTEEEAKAMAAEIEVVDGPNDEGEMFTRPGKLSDRFPQPYANESAARFANGGAYPPDLSLITKARHNGPNYVFALLTGYRDPPAGISIREGLHYNPYFPGGAIAMPKMLNDEAVEYEDGVPATEAQMGKDIVSFLAWAAEPEMEERKLMGFKWIFLLSLALLQAAYYRRLKWSVLKSRKLVLDVVN
|
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
|
Q9LK29
|
B2SLC0
|
MURB_XANOP
|
UDP-N-acetylmuramate dehydrogenase
|
Xanthomonas
|
MSDTTQVGWQLSEHAPLRALNTFHVEATARWLLSVHTPEALPQALAAPEIADQPLLVLGSGSNVLLAGDPPGCVLCFENRDTAIIAHHADHAIVRAGAGVNWHALVLYSLQQGLSGLENLALIPGTVGACPIQNIGAYGAQVGDFIHVVEAFDRHHQQFVRLDAAACALGYRDSVFKQQPERYLIVAVEFNLPLLCELRLDYAGIREELASMGAELARAADVAQAVINIRQRKLPDPDVLGNAGSFFKNPLLPNEQIAALQASFADMPVYPGEHAGLGKLSAAWLIEQCGWKGRREGDAGVSPEHALVLVNYGTASGAQLLDFARRIAESVRERYSVILEPEPRIIGAHW
|
Cell wall formation.
|
B2SLC0
|
Q8BZN4
|
NUAK2_MOUSE
|
Omphalocele kinase 2
|
Mus
|
MESVALLQRPSQAPSASALASESARPLADGLIKSPKPLMKKQAVKRHHHKHNLRHRYEFLETLGKGTYGKVKKARESSGRLVAIKSIRKDKIKDEQDLLHIRREIEIMSSLNHPHIIAIHEVGRSRLVTVFENSSKIVIVMEYASRGDLYDYISERPRLSERDARHFFRQIVSALHYCHQNGIVHRDLKLENILLDANGNIKIADFGLSNLYHKGKFLQTFCGSPLYASPEIVNGKPYVGPEVDSWSLGVLLYILVHGTMPFDGQDHKTLVKQISNGAYREPPKPSDACGLIRWLLMVNPTRRATLEDVASHWWVNWGYTTGVGEQEALREGGHPSGDFGRASMADWLRRSSRPLLENGAKVCSFFKQHVPGGGSTVPGLERQHSLKKSRKENDMAQNLQGDPAEDTSSRPGKSSLKLPKGILKKKSSTSSGEVQEDPQELRPVPDTPGQPVPAVSLLPRKGILKKSRQRESGYYSSPEPSESGELLDASDVFVSGDPVEQKSPQASGLLLHRKGILKLNGKFSRTALEGTTPSTFGSLDQLASSHPAARPSRPSGAVSEDSILSSESFDQLDLPERLPETPLRGCVSVDNLRGLEQPPSEGLKRWWQESLGDSCFSLTDCQEVTAAYRQALGICSKLS
|
Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Phosphorylates LATS1 and LATS2. Plays a key role in neural tube closure during embryonic development through LATS2 phosphorylation and regulation of the nuclear localization of YAP1 a critical downstream regulatory target in the Hippo signaling pathway.
|
Q8BZN4
|
P83409
|
FABPL_RHIAE
|
Liver-type fatty acid-binding protein
|
Rhinella
|
MAFNGTWNVYAQENYENFLRTVGLPEDIIKVAKDVNPVIEIEQNGNEFVVTSKTPKQTHSNSFTVGKESEITSMDGKKIKVTVQLEGGKLICKSDKFSHIQEVNGDEMVEKITIGSSTLTRKSKRV
|
Involved in intracellular lipid transport. Binds free fatty acids and their coenzyme A derivatives, lysophospholipids, prostaglandins, retinoids, bilirubin and some other small molecules.
|
P83409
|
Q2G870
|
KUP2_NOVAD
|
Probable potassium transport system protein kup 2
|
Novosphingobium
|
MQTITRTSRNSLASLTLGAIGVVYGDIGTSPLYAFREALGQAARDGIVQAEIVGVLSLALWALIIVVTLKYVIFLSRMDNNGEGGVLSLMALAQRATGGGWVAVTLLGATGAALFYGDAIITPALSVLSAAEGLKTIPGLDGMSQTAIIGVTVGILAALFMFQSRGTASVATLFGPVCLVWFVALAGLGLWHIADAPEVLTAFNPLHAVTFLVSHGVTGLFVLGAVFLTVTGAEALIADMGHFGRRPIQLGWLSFVWPALTLNYLGQGALALKALAAAEAIGQPLANADWFFIMAPDVLRAPLVILATLATIIASQAVITGAYSLTHQAISLGLLPRLTIRQTSEHQMGQIYMPGVNWLLLGGVLLLVLGFKSSSAMAAAYGIAVTGTMVVTTCMAFLIAWKYWNWEPVWTALLIAPFLALDLFFFGANILRVSEGGWVPLLVAGLVGLVIFTWLKGRRTALARASEQGVSLNETVMALHARPPTRIEGTAVFLTQDLDVTPSALLHNLKHNKALHRNNIVLKVEIQARPYVAPEQRVVVDRIDESFLKARLRYGYMDTIDVPSDLARADGLLVGPGGTSFFVGRSAIRFAARPVLPRWMTVVYMFLHRNAADPTAYFSIPSNRVVELGSQIEL
|
Transport of potassium into the cell.
|
Q2G870
|
I3BN39
|
METAS_THINJ
|
Homoserine transsuccinylase
|
Thiothrix
|
MPLVAHTRLPTFERLKQEGQTVLSEDYAFQQDIRELHIGFLNMMPDAALAATERQFLRLVNESNLIAQFHIHPFTLGTLPRGDKAQAHIAQYYDKFEDLQEQGLDALIITGANPAAPHLEDEPFWDGLCEVVAWAQENVTSTLCSCLASHALVQHLWGIRRRPLGFKRWGVYSHAVTMPEHPLVNDLNTRFDVPHSRFNQIDREPLEAVGVQVLVESTEAGVHMAVSPDLFRMVFMQGHPEYDTVSLLKEYRREVTRWFDGTRADYPPFPQNYLRPKAKAILNEYRLEQEKAKRLGKPLPDFPEKLLLPMLHNTWCDTAKVFYSNWIGKVYQLTNNDRRKPFMEGVNPDDPLGLRQQLGI
|
Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine. In vitro, can also use glutaryl-CoA as acyl donor.
|
I3BN39
|
A1WW05
|
HIS6_HALHL
|
ImGP synthase subunit HisF
|
Halorhodospira
|
MTAKRIIPCLDVDAGRVVKGVRFVDIRDAGDPVEIARRYDAMGADELTFLDITASHEERETIYDVVEAVAGQVFIPLTVGGGVRSVADVRRLLNAGADKVAINTAAVHRPDFVREAAERFGSQCIVVAVDAKQVEDDPPRWEVFTHGGRNPTGLEVVSWCQRLVALGAGEILLTSMDRDGTRAGFDLGLTRAVADAVSVPVIASGGVGELEHLADGVDDGGADAVLAASIFHFGDHTVGEAKAHMAERGIEVRR
|
IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.
|
A1WW05
|
B3EUM2
|
RL4_AMOA5
|
50S ribosomal protein L4
|
Candidatus Amoebophilus
|
MELSVLQYTGKDTGRKVVLSDTIFGITPNDHAIYLDVKNILANKRQGTHKSKERGEIAGSTKKIKKQKGTGTARAGSIKSPIFRGGGRVFGPKPRDYGFKLNKKLKKLARKSALTYKAQQGNISVLEDFSFEMPKTKMYLEMLQNLNMADQKTLLILPAVDKNLVLASRNLPNTSVALVEQINTYDLLYSKKILISETALSKLTENFNNA
|
Forms part of the polypeptide exit tunnel.
|
B3EUM2
|
A1VMW5
|
RNH_POLNA
|
Ribonuclease H
|
Polaromonas
|
MTDSAAEPTISQPQHVVIYTDGACKGNPGPGGWGALLASGGTEKEIFGGEMGTTNNRMEMTAVIEALAALKKPCTVTLYLDSQYVLKGITEWIHGWKARGWRTAAKAPVKNVDLWQRLDALLVSSGHSIDWRWVRGHNGDPGNERADALANKGVERALGRL
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
A1VMW5
|
A0T0X8
|
RK22_THAPS
|
50S ribosomal protein L22, chloroplastic
|
Thalassiosira
|
MSNGQSVKAVAKYVRISPHKVRQVLDQIRGRSYQEALMILEFLPYDAGSPIWQVVHSVAANAKNNYNLDKKKLVISEIFADEGPKLKRIRPRAQGRAYKILKPTCHITVVVKSIS
|
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
|
A0T0X8
|
Q15RL2
|
RNFD_PSEA6
|
Rnf electron transport complex subunit D
|
Pseudoalteromonas
|
MNYKLASSPHQHVRRNTGQVMRMVIYALIPGILLQTWFFGFGVLVQIALAVITAVVTEATILEMRKRNFERAIKDYSAILTAILLAISIPPFAPWWVIVIGTFFAIAMVKQLYGGLGFNVFNPAMAAYVMLLVSFPVQMTQWLPAQSLTAHQPGLIDAIYAVFTGFSADGFSLAQLQGAADGHTMATPLDAIKTGLAQGLTYEEGLQSAIFDGSLGIGWWWVSTGYLLGGLYLIRAKIINWHIPGGMLAGAALCAGVMFLVDADRFASPLFHIFNGSLILGAFFIATDPVSASTTNKGRIIFGAAIGFWVYVIRTWGGYPDAIAFSVLIMNMAVPLIDYYTRPRTYGHTKRTKGEPK
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q15RL2
|
Q7MZX9
|
EFP_PHOLL
|
Elongation factor P
|
Photorhabdus
|
MATYSTNEFRSGLKIMLDGEPCAILESEFVKPGKGQAFARVRIRKLISGKLLEKTFKSTDSVESADVMDMNLTYLYNDGEFWHFMNNETFEQLAADEKAVGDNAKWLVEQAECILTLWNGQPISVTPPNFVELEITDTDPGLKGDTAGTGGKPATLNTGAVVKVPLFVQIGEVIKVDTRSGEYVSRVK
|
Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation.
|
Q7MZX9
|
Q9UBZ4
|
APEX2_HUMAN
|
Apurinic-apyrimidinic endonuclease 2
|
Homo
|
MLRVVSWNINGIRRPLQGVANQEPSNCAAVAVGRILDELDADIVCLQETKVTRDALTEPLAIVEGYNSYFSFSRNRSGYSGVATFCKDNATPVAAEEGLSGLFATQNGDVGCYGNMDEFTQEELRALDSEGRALLTQHKIRTWEGKEKTLTLINVYCPHADPGRPERLVFKMRFYRLLQIRAEALLAAGSHVIILGDLNTAHRPIDHWDAVNLECFEEDPGRKWMDSLLSNLGCQSASHVGPFIDSYRCFQPKQEGAFTCWSAVTGARHLNYGSRLDYVLGDRTLVIDTFQASFLLPEVMGSDHCPVGAVLSVSSVPAKQCPPLCTRFLPEFAGTQLKILRFLVPLEQSPVLEQSTLQHNNQTRVQTCQNKAQVRSTRPQPSQVGSSRGQKNLKSYFQPSPSCPQASPDIELPSLPLMSALMTPKTPEEKAVAKVVKGQAKTSEAKDEKELRTSFWKSVLAGPLRTPLCGGHREPCVMRTVKKPGPNLGRRFYMCARPRGPPTDPSSRCNFFLWSRPS
|
Functions as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also displays double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes.
|
Q9UBZ4
|
P39701
|
COBC_SALTY
|
Alpha-ribazole-5'-phosphate phosphatase
|
Salmonella
|
MRLWLVRHGETEANVAGLYSGHAPTPLTEKGIGQAKTLHTLLRHAPFDRVLCSELERARHTARLVLEGRDVPQHILPELNEMYFGDWEMRHHRDLTHEDAESYAAWCTDWQNAVPTNGEGFQAFTRRVERFISRLDAFSDCQNLLIVSHQGVLSLLIARLLTMPAASLWHFRVEQGCWSAIDICEGFATLKVLNSRAVWRPE
|
Catalyzes the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole.
|
P39701
|
G1FE62
|
NDB4A_CHATC
|
Non-disulfide-bridged peptide 4.10
|
Chaerilus
|
MDSKYLFVFLIFNVIVIDLCQGFLWGLIPGAISAVTSLIKKGRRRRELGSQYDYLQDFRKRELDLDDLLSKFPDY
|
Antimicrobial peptide that acts by breaking the cell wall. Is active against Gram-positive bacteria, fungi and antibiotic-resistant pathogens: S.aureus (MIC=5 ug/ml), M.luteus (MIC=5 ug/ml), B.thuringiensis (MIC=10 ug/ml), B.subtilis (MIC=10 ug/ml), C.albicans (MIC=20 ug/ml), methicillin-resistant S.aureus (MIC=5-10 ug/ml), and penicillin-resistant S.epidermidis (MIC=10 ug/ml). Is efficient in curing staphylococcal skin infection in mice, when externally applied.
|
G1FE62
|
A7ZD37
|
HEM3_CAMC1
|
Pre-uroporphyrinogen synthase
|
Campylobacter
|
MKEIKIATRKSILALWQSEHIKARIEAQHKGMKVVLEGMKTKGDVILDTPLAKIGGKGLFTKELEDSMLKGETDIAVHSLKDVPVVFPEGLRLAAICSREDTRDAMISEKFAKFSDLPHGAKVGTTSLRRKMQLLIMRPDLEIISLRGNVQTRLRKLKEGEFDAIILAMAGINRLNIKAEVAHIYTFGFDEMIPAMGQGALGIEARDEKQILDETSFLNDENAVIETTIERDFVSVLEGGCQVPIGISARLKGDEISIDAIVGLPDGSEYIKDSLKTSKDKFQSVGKELAHKFIEKGARELLKRAEEMA
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A7ZD37
|
P22433
|
RBS2_NICSY
|
Ribulose bisphosphate carboxylase small subunit, chloroplastic 2
|
Nicotiana
|
MAFLIMSSAAAVATGTNAAQASMIAPFTGLKSATSFPVSRKQNLDITSIASNGGRVQCMQVWPPINKKKYETLSYLPDLSEEQLLREVEYLLKNGWVPCLEFETEHGFVYRENNKSPGYYDGRYWTMWKLPMFGCTDATQVLAEVEEAKKAYPQAWIRIIGFDNVRQVQCISFIAYKPEGY
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate. Both reactions occur simultaneously and in competition at the same active site. Although the small subunit is not catalytic it is essential for maximal activity.
|
P22433
|
Q9UT86
|
APC11_SCHPO
|
20S cyclosome/APC complex protein apc11
|
Schizosaccharomyces
|
MKVKILRYHAIANWTWDTPKDDVCGICRVPFDGCCPQCTSPGDNCPIVWGKCKHIFHAHCIQNWLATSGSQGQCPMDRQTFVVADSTNEKSETQ
|
Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome.
|
Q9UT86
|
A0L4J3
|
GLMM_MAGMM
|
Phosphoglucosamine mutase
|
Magnetococcus
|
MVQNRAIFCFLSTIKSEETMTSESQPQVTQTRKFFGTDGIRGMANIHPMTPDLVLKLGRAAGHVFRVGDKRHTVIIGKDTRLSGYMFESALLAGLTSMGIHCLQVGPLPTPAIAFLTRALRADAGIMISASHNPFHDNGIKFFGPNGMKLPDELELEIERVLLSDEDLPMPTPHHLGRAHRIDDALGRYIEFAKTSFPKDLRLDGLRVVVDCAHGAAYKVAPAVLWELGAEVVTLGNHPNGTNINDGVGSLYPQEMVKRVQEVRADVGIAFDGDADRVVICDERGEILDGDVILAMSALEMKRKGVLRGDGVVATVMSNLGLERALAAEGLTLARTKVGDRYVLEHMLAHGFNLGGEQSGHLIFLDHNTTGDGLISALSVLALMTTQAQPLSKLANVMQRVPQVLQNVTIARGSDPMDDSRVVAAIAEAEAQLGTRGRILVRKSGTEPKVRVMVEGDDTAHITALASGVCEAIKRASNGFGEG
|
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
|
A0L4J3
|
B2GGG9
|
SYS_KOCRD
|
Seryl-tRNA(Ser/Sec) synthetase
|
Kocuria
|
MIDINELRADPDTYRASQTARGADAGLVDRILEADSRRRSAITDFESLRAEQNAFGKKVARAQGEEKQQLLAQVKQLAADVKAAQAAADEAQATQQQLVTQFPNLIVEGIPAGGEDDFVQLRTEGTPRDFAAEGFEPRDHLELGELLDGIDMERGAKVSGSRFYFLKRDVARLETALLMAAQDLALDNGFIPMTTPNLVRPGIMNGTGFDVEHDDEIYRVGKDDLYLVGTSEVALAGYHSDEILDLSGGPLRYAGWSSCYRREAGSAGKDTRGIIRVHQFNKLEMFVYCHPEDAAAEHERLLAWEEQMLQACGLAYRVIDTAAGDLGTSAARKFDCEAWIPTQGKYRELTSTSNCTTYQARRLNIRERLPETTDAHGKVKKGGTRAVATLNGTLATTRWLVALLETHQQADGSVTVPELLRPYLRGQEVLRPVA
|
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
|
B2GGG9
|
A7I1B2
|
ATP6_CAMHC
|
F-ATPase subunit 6
|
Campylobacter
|
MLKDIFLFWGSLFGYDHTAIYIFHFLLVVAITMFIAVAVTKSMRLVPRGLQNIIEAYLSGVIALGKDAMGSEKLARKYMPLIATIGFIVFLSNIIGLIPGFEAPTASLNLTLSLTLCVFFYYHFEGIREKGFIKYFAGFCGPVKAIAPFMFVIEVISHLSRIISLSFRLFGNIKGDDLFLLVMLTLAPVLVPMIPYALLSFMAILQAFIFMVLSYVYLAGAVVVDEEH
|
Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.
|
A7I1B2
|
B4SPV3
|
NFUA_STRM5
|
Fe/S biogenesis protein NfuA
|
Stenotrophomonas maltophilia group
|
MIQISDTAQTHFRKLIEREGAPGMGVRLSAVDPGTPRADARLEFAEPSDLLGDEWAVDCDGFTLYVDAASVGWLDGAEIDIVAGTAGAQQLTIKAPRIKGEAPGDAASLVERVHWVVENEINPQLASHGGKVAVQEVSAEGVVLLRFGGGCQGCGMADVTLKQGIEKTLMGRVPGVTAVRDATDHDSGHAPYIPRGNAA
|
Involved in iron-sulfur cluster biogenesis. Binds a 4Fe-4S cluster, can transfer this cluster to apoproteins, and thereby intervenes in the maturation of Fe/S proteins. Could also act as a scaffold/chaperone for damaged Fe/S proteins.
|
B4SPV3
|
Q3JAN0
|
UVRC_NITOC
|
Excinuclease ABC subunit C
|
Nitrosococcus
|
MANFDIDDFLRNLTPCPGVYRMLDAKGKVLYVGKAKNLKRRIKSYFRNSKLAPKIHVLVKQICDIKITVTHTENEALILESNLIKALQPRYNVLLRDDKSYPYIFLSADDFPRLGFHRGVKQVSGQYFGPYPNIRSVWQTLKLLQRVFPVRQCEDNFYRNRSRPCLQYQIKRCTAPCVGLISKKDYSQDIQHVVMFLKGRDQQVINELVIRMEEASGQLAFEQAAYYRDRIASLRQIQARQYISGEKKDIDVLGVALTEKMACVEVFFIRGGHNLGNKTFLPKLEGNLTPEELLSTFIAQYYLNRETPPILILSHQPKDMGLLTEVLSKQAGRKIALIKPVRGPKVQWIKMALANAKINLNQHLAEKSNITARFKSLQQLLSLANFPQRIECFDVSHIQGTATVASCVVFDREGPRKADYRRFNITGIIPGDDYGALRQALMRRFKKKEGVFPDLLVIDGGKGQINQSLRVLKEIGITEITVLGIAKGPERKAGNETLFLAGYENPVMVTSDSPALHILQHIRDEAHRFAIVSHRKRRAKGGKLSLLEGISGLGPKRRRKLLIQLGGLQEITRAGVEDLAQIEGISLELAQRIYDVFHR
|
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.
|
Q3JAN0
|
P04991
|
RBL_MEDSA
|
Ribulose bisphosphate carboxylase large chain
|
Medicago
|
MSPQTETKATVGFKAGVKDYRLTYYTPDYETKDTDILAAFRVSPQPGVPAEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEETQFIAYVAYPLDLFEEGSVNYMFTSIVGNVFGFKALRALRLEDLRIPAAYVKTFQGPPQGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAVFARELGVPIVMHDYLTVGFTANTTLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIFFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREATKWSPELAAACEVWKEIKFEFPAMDN
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P04991
|
Q8AA76
|
YIDC_BACTN
|
Membrane protein YidC
|
Bacteroides
|
MDKNTITGLVLIGILLVGFSYLSRPSEEQIAAQKKYYDSIAVVQQQQEALKAKTEAALANENKGAAAAADSSALFFNAMHGTDSKVSIQNSVAEITFTTKGGRVYSAMLKEYKGQDKTNPVVLFDGDDATMSFNFYNKQGAIQTKDYYFEAVNKTDSSVTMRLAADNASYIDFIYTLKPNSYLMNFEIKATGMEGKLASTEYVDIDWTQRARQLEKGFTYENRLSELTYKVKGDNVDNLSAAKDDEKDLGNTAIDWVAFKNQFFSSVFIADQDFNKVSVKSRMEQQGSGYIKDYSAEMSTFFDPSGKQPTEMYFYFGPNHFKTLKALDKGRTEKWELNRLVYLGWPLIRWINQFITINVFDWLSGWGLSMGIVLLILTIMVKVVVYPATWKTYMSSAKMRVLKPKIDEINKKYPKQEDAMKKQQEVMSLYSQYGVSPMGGCLPMLLQFPILMALFMFVPSAIELRQQSFLWADDLSTYDAFITFPFHIPFLGNHLSLFCLLMTVTNILNTKYTMTMQDTGAQPQMAAMKWMMYLMPIMFLFVLNDYPSGLNYYYFVSTLISVGTMILLRKTTDETKLLAILEAKKKDPKQMKKTGFAARLEAMQKQQEQLQQQKQNKR
|
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
|
Q8AA76
|
P86265
|
HS74L_MESAU
|
Osmotic stress protein 94
|
Mesocricetus
|
SVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTPACISLGSRSQIVTNVRNTIHGFKKIRLPYELQKMPNGSTGVKVRLKVLATTFDPYLGGRVEPPLKSVMDQANLQREDINSIEIVGGATRIPAVKEQVTRFFLKDISTTLNADEAVARNHPAPFSKSIDLPIQSSLYRNAVEEYVYDFRDKFITPEDMNKYGQPIQMKYVEHEERPK
|
Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase.
|
P86265
|
Q2G8Y1
|
RS10_NOVAD
|
30S ribosomal protein S10
|
Novosphingobium
|
MEAQNIRIRLKAFDHRVLDQATGEIADTARRTGALIRGPIPLPTRIEKFCVNRGPHIDKKSREQFEVRTYKRLLDIVQPNAATVDALMKLDLAAGVNVEIKLA
|
Involved in the binding of tRNA to the ribosomes.
|
Q2G8Y1
|
Q6T269
|
VKT3_BITGA
|
Two-Kunitz protease inhibitor
|
Bitis
|
PLRPGTEKHTFPFPAEFCNLPADLGPCKNYTGRFYYDSASNKCEVFIYGGCPGNANNFKTREECRKTCVEICILPAELGPCDEYTGRFYYDSASNKCEVFIYGGCQGNANNFKTRDECRKTCVEICILPAELGPCDEYTGRLLLRLGIKQM
|
Serine protease inhibitor.
|
Q6T269
|
Q96QA5
|
GSDMA_HUMAN
|
Gasdermin-A, C-terminal
|
Homo
|
MTMFENVTRALARQLNPRGDLTPLDSLIDFKRFHPFCLVLRKRKSTLFWGARYVRTDYTLLDVLEPGSSPSDPTDTGNFGFKNMLDTRVEGDVDVPKTVKVKGTAGLSQNSTLEVQTLSVAPKALETVQERKLAADHPFLKEMQDQGENLYVVMEVVETVQEVTLERAGKAEACFSLPFFAPLGLQGSINHKEAVTIPKGCVLAFRVRQLMVKGKDEWDIPHICNDNMQTFPPGEKSGEEKVILIQASDVGDVHEGFRTLKEEVQRETQQVEKLSRVGQSSLLSSLSKLLGKKKELQDLELALEGALDKGHEVTLEALPKDVLLSKEAVGAILYFVGALTELSEAQQKLLVKSMEKKILPVQLKLVESTMEQNFLLDKEGVFPLQPELLSSLGDEELTLTEALVGLSGLEVQRSGPQYMWDPDTLPRLCALYAGLSLLQQLTKAS
|
Pore-forming protein that causes membrane permeabilization and pyroptosis . Released upon cleavage in vitro of genetically engineered GSDMA, and binds to membrane inner leaflet lipids . Homooligomerizes within the membrane and forms pores of 10-15 nanometers (nm) of inner diameter, triggering pyroptosis . Binds to membrane inner leaflet lipids, such as phosphatidylinositol (4,5)-bisphosphate . The functional mechanisms and physiological proteases that cleave and activate this pore-forming protein are unknown .
|
Q96QA5
|
Q05085
|
PTR7_ARATH
|
Protein CHLORINA 1
|
Arabidopsis
|
MSLPETKSDDILLDAWDFQGRPADRSKTGGWASAAMILCIEAVERLTTLGIGVNLVTYLTGTMHLGNATAANTVTNFLGTSFMLCLLGGFIADTFLGRYLTIAIFAAIQATGVSILTLSTIIPGLRPPRCNPTTSSHCEQASGIQLTVLYLALYLTALGTGGVKASVSGFGSDQFDETEPKERSKMTYFFNRFFFCINVGSLLAVTVLVYVQDDVGRKWGYGICAFAIVLALSVFLAGTNRYRFKKLIGSPMTQVAAVIVAAWRNRKLELPADPSYLYDVDDIIAAEGSMKGKQKLPHTEQFRSLDKAAIRDQEAGVTSNVFNKWTLSTLTDVEEVKQIVRMLPIWATCILFWTVHAQLTTLSVAQSETLDRSIGSFEIPPASMAVFYVGGLLLTTAVYDRVAIRLCKKLFNYPHGLRPLQRIGLGLFFGSMAMAVAALVELKRLRTAHAHGPTVKTLPLGFYLLIPQYLIVGIGEALIYTGQLDFFLRECPKGMKGMSTGLLLSTLALGFFFSSVLVTIVEKFTGKAHPWIADDLNKGRLYNFYWLVAVLVALNFLIFLVFSKWYVYKEKRLAEVGIELDDEPSIPMGH
|
Dual affinity nitrate transporter. Involved in proton-dependent nitrate uptake and in the regulation of the nitrate transporter NRT2.1. Acts also as a nitrate sensor that trigger a specific signaling pathway stimulating lateral root growth and seed germination. The uptake activity is not required for sensor function. Displays an auxin transport facilitation inhibited by high nitrate concentration. Required to prevent auxin accumulation in preemerged lateral root primordia and young lateral roots when external nitrate concentration is low or null. May be involved in the basipetal transport of auxin out of the lateral root tips. Acts as a bidirectional transporter involved in root-to-shoot nitrate translocation. Recognizes specifically nitrate and chlorate, but not nitrite, alanine, sulfate, phosphate or the di-peptide Ala-Ala.
|
Q05085
|
Q9UBU6
|
FA8A1_HUMAN
|
Autosomal highly conserved protein
|
Homo
|
MAEGPEEARGHPPGQDDGGGDHEPVPSLRGPPTTAVPCPRDDPQAEPQAPGRPTAPGLAAAAAADKLEPPRELRKRGEAASGSGAELQEQAGCEAPEAAAPRERPARLSAREYSRQVHEWLWQSYCGYLTWHSGLAAFPAYCSPQPSPQSFPSGGAAVPQAAAPPPPQLGYYNPFYFLSPGAAGPDPRTAAGISTPAPVAGLGPRAPHVQASVRATPVTRVGSAAPSRSPSETGRQAGREYVIPSLAHRFMAEMVDFFILFFIKATIVLSIMHLSGIKDISKFAMHYIIEEIDEDTSMEDLQKMMVVALIYRLLVCFYEIICIWGAGGATPGKFLLGLRVVTCDTSVLIAPSRVLVIPSSNVSITTSTIRALIKNFSIASFFPAFITLLFFQHNRTAYDIVAGTIVVKRNGVR
|
Plays a role in the assembly of the HRD1 complex, a complex involved in the ubiquitin-proteasome-dependent process of ER-associated degradation (ERAD).
|
Q9UBU6
|
Q6CMQ1
|
TVP18_KLULA
|
Golgi apparatus membrane protein TVP18
|
Kluyveromyces
|
MVSVGFLKSMFNVSGMVADLKSSNFSIYGQWISYLNIIFCLAFGIANIFHFSAVIVFSIIAIVQGLIILFIEVPFLLKICPLSDNFIGFVSKFDTNLRRALFYLVMCAIQWCSIIVQSTSLIVVAVGLSITATVYALGAAAGQEFKNSAILSDRGRVAASVTNEAVVRDML
|
Golgi membrane protein involved in vesicular trafficking.
|
Q6CMQ1
|
Q12996
|
CSTF3_HUMAN
|
Cleavage stimulation factor 77 kDa subunit
|
Homo
|
MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFALDKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEKSNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEGIKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKETALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPNTVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR
|
One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs.
|
Q12996
|
Q0APP7
|
HFQ_MARMM
|
RNA-binding protein Hfq
|
Maricaulis
|
MSHDKKQNLQDVFLNSVRKTKTPLTIFLVNGVKLQGVVTWFDNFCVLLRRDGLSQLVYKHAISTIMPAAPVSLFEDDKADDDAAEESATD
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
Q0APP7
|
C6Y4D3
|
ECL1_SCHPO
|
Extender of the chronological lifespan protein 1
|
Schizosaccharomyces
|
MDLDFCTVCGATTQDGSLYCSSECHLLDFTKLDTQTTSNISVSSEYQFLVSEHLAHFHRKSMTSADFPTPRFSAYTKLHA
|
Involved in chronological cell aging. Extends cell viability after entry into the stationary phase probably through affecting the Pka1-dependent pathway negatively.
|
C6Y4D3
|
B6I335
|
TUSA_ECOSE
|
tRNA 2-thiouridine synthesizing protein A
|
Escherichia
|
MTDLFSSPDHTLDALGLRCPEPVMMVRKTVRNMQPGETLLIIADDPATTRDIPGFCTFMEHELVAKETDGLPYRYLIRKGG
|
Sulfur carrier protein involved in sulfur trafficking in the cell. Part of a sulfur-relay system required for 2-thiolation during synthesis of 2-thiouridine of the modified wobble base 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) in tRNA. Interacts with IscS and stimulates its cysteine desulfurase activity. Accepts an activated sulfur from IscS, which is then transferred to TusD, and thus determines the direction of sulfur flow from IscS to 2-thiouridine formation. Also appears to be involved in sulfur transfer for the biosynthesis of molybdopterin.
|
B6I335
|
P68193
|
SRA_ECO57
|
30S ribosomal protein S22
|
Escherichia
|
MKSNRQARHILGLDHKISNQRKIVTEGDKSSVVNNPTGRKRPAEK
|
Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein.
|
P68193
|
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