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
|
---|---|---|---|---|---|---|
A5CR32
|
OBG_CLAM3
|
GTP-binding protein Obg
|
Clavibacter
|
MATFVDTVTLHLRAGNGGNGCVSVRREKFKPLAGPDGGNGGNGGDIVLVADPQVTTLLAYHRGPHRSSRNGGPGMGDHRHGTLGEALELHVPVGTVVKDADGNELADMATPGMRFIAAEAGQGGLGNASLATTKRKAPGFALLGTRGYEGDVVLELKVVADVALVGYPSAGKSSLVAAISAAKPKIADYPFTTLHPNLGVVEVADSRYTVADVPGLIEGASEGKGLGLEFLRHVERCSALLHVLDCATLDPGRDPISDLDIILTELAAYPVPDGQVPLLDRPQLIALNKIDVPEARELAELVRPELEARGYRVFDISTVSHDGLRQLSFALAELVEDARTKAAEEPEAPRIVLRPRAVNEKPFTIRVDGGSYGDIYRVIGTKPERWVQQTDFTNDEAVGYLADRLAKLGVEDGLFKAGAVAGSSVVIGEGDGIVFDWEPTLTSTAELITSPRGADARVDPISRRTNQARREDYFARMDAKAEARAQLVREGEAGLWADEDGTDEDASSDAKA
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
A5CR32
|
O54457
|
PPSA_ENTAG
|
Pyruvate, water dikinase
|
Pantoea agglomerans group
|
MSSKGEQPLVLWYNQLGMHDVDRVGGKNPSLGEMITNLSSLGVSVPNGFATTSYAFNLFLD
|
Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate.
|
O54457
|
Q0TC49
|
MALT_ECOL5
|
ATP-dependent transcriptional activator MalT
|
Escherichia
|
MLIPSKLSRPVRLDHTVVRERLLAKLSGANNFRLALITSPAGYGKTTLISQWAAGKNDIGWYSLDEGDNQQERFASYLIAAVQQATNGHCAICETMAQKRQYASLTSLFAQLFIELAEWHSPLYLVIDDYHLITNPVIHESMRFFIRHQPENLTLVVLSRNLPQLGIANLRVRDQLLEIGSQQLAFTHQEAKQFFDCRLSSPIEAAESSRICDDVSGWATALQLIALSARQNTHSAHKSARRLAGINASHLSDYLVDEVLDNVDLATRHFLLKSAILRSMNDALITRVTGEENGQMRLEEIERQGLFLQRMDDTGEWFCYHPLFGNFLRQRCQWELAAELPEIHRAAAESWMAQGFPSEAIHHALAAGDALMLRDILLNHAWSLFNHSELSLLEESLKALPWDSLLENPQLVLLQAWLMQSQHRYGEVNTLLARAEHEIKDIREGTMHAEFNALRAQVAINDGSPDEAERLAKLALEELPPGWFYSRIVATSVLGEVLHCKGELTRSLALMQQTEQMARQHDVWHYALWSLIQQSEILFAQGFLQTAWETQEKAFQLINEQHLEQLPMHEFLVRIRAQLLWAWARLDEAEASARSGIEVLSSYQPQQQLQCLAMLIQCSLARGDLDNARSQLNRLENLLGNGKYHSDWISNANKVRVIYWQMTGDKAAAANWLRHTAKPEFANNHFLQGQWRNIARAQILLGEFESAEIVLEELNENARSLRLMSDLNRNLLLLNQLYWQAGRKSDAQRVLLDALKLANRTGFISHFVIEGEAMAQQLRQLIQLNTLPELEQHRAQRILREINQHHRHKFAHFDENFVERLLNHPEVPELIRTSPLTQREWQVLGLIYSGYSNEQIAGELEVAATTIKTHIRNLYQKLGVAHRQAAVQHAQKLLKMMGYGV
|
Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto-oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box.
|
Q0TC49
|
P31415
|
CASQ1_HUMAN
|
Calsequestrin, skeletal muscle isoform
|
Homo
|
MSATDRMGPRAVPGLRLALLLLLVLGTPKSGVQGQEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEVDSMYVFKGDEVIEYDGEFSADTIVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKSKDSEHYKAFEDAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGFEFLETLKAVAQDNTENPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDDDDD
|
Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle . Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions . Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity .
|
P31415
|
Q8A749
|
NTPPA_BACTN
|
Nucleotide pyrophosphatase
|
Bacteroides
|
MLGNLDKYQIILASNSPRRKELMSGLGVDYVVRTLPDVDESYPADLAGAEIPEYISREKADAYRSIMQPGELLITADTIVWLDGKVLGKPEGREGAVEMLRSLSGKSHQVFTGVCLTTTEWQKSFTAASDVEFDVLSEEEIRYYVDKYQPMDKAGAYGVQEWIGYIGVKSISGSFYNIMGLPIQKLYGELKKL
|
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
Q8A749
|
Q3ZBJ8
|
MFRN1_BOVIN
|
Solute carrier family 25 member 37
|
Bos
|
MELRRGGVGSQARARRMDGDSRDGGGGCKDAGSEDYENLPTSASLSTHMTAGAMAGILEHSVMYPVDSVKTRMQSLNPDPKAHYTSVYGALKKIIRTEGFWRPLRGLNVMMMGAGPAHAMYFACYENMKRTLNAVFHHQGNSHLANGICKRLSGVRKVSPSTDPSPGFSSL
|
Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis.
|
Q3ZBJ8
|
Q9LXZ8
|
TRH10_ARATH
|
Putative thioredoxin H10
|
Arabidopsis
|
MGNRCARTSCCRKLWSCICCCSNNNNNSYGQTRSQHGSKGKVHPVSRIEKWEEKITEANNHGKILVVNFSAPWCVPCKKIEPVFRDLASRYPSMIFVTVDVEELAEFSNEWNVEATPTVVFLKDGRQMDKLVGAETSELQKKTAAAADLFLRKP
|
Probable thiol-disulfide oxidoreductase that may be involved in the redox regulation of a number of cytosolic enzymes.
|
Q9LXZ8
|
O57774
|
DTDA_PYRHO
|
D-tyrosyl-tRNA(Tyr) deacylase
|
Pyrococcus
|
MKVIMTTKVDKASMNIMNKLIENFGFKETEYVFDGNPVYKRGDVLILTTNDEMIYYDYLDREIENQLGFKPEIIAFASRHSSKQKLPALTTHVTGNWGKAMYGGKDESFAVAIPSAMKLSLLKMSELNDLGWTVCYEATHHGPTELEVPSFFIEIGSSEEEWINDRAGEIIAETIIYVLDNYEKGRSKFKVALGIGGGHYAPKQTKRALEGDLAFGHILPKYAQPVSRDVMIKALNRFGEKVEAIYVDWKGSRGETRQLAKSLAQELGLEFIKD
|
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
|
O57774
|
Q6D1T5
|
LUXS_PECAS
|
Autoinducer-2 production protein LuxS
|
Pectobacterium
|
MPLLDSFTVDHTRMAAPAVRVAKTMKTPHGDNITVFDLRFCRPNIEVMPERGIHTLEHLFAGFMRDHLNGDGVEIIDISPMGCRTGFYMSLIGTPDEQRVAESWKAAMSDVLKVTDQRKIPELNEYQCGTYDMHSLKEAQEIAQHIVDHDIGINQNDDLALPKDKLAELHI
|
Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
|
Q6D1T5
|
G9FRD7
|
HDHA_CLOSR
|
NADP-dependent 7alpha-hydroxysteroid dehydrogenase
|
Clostridium
|
MKRLEGKVAIVTSSTRGIGRASAEALAKEGALVYLAARSEELANEVIADIKKQGGVAKFVYFNAREEETYTSMVEKVAEAEGRIDILVNNYGGTNVNLDKNLTAGDTDEFFRILKDNVQSVYLPAKAAIPHMEKVGGGSIVNISTIGSVVPDISRIAYCVSKSAINSLTQNIALQYARKNIRCNAVLPGLIGTRAALENMTDEFRDSFLGHVPLNRVGRPEDIANAVLYYASDDSGYVTGMIHEVAGGFALGTPQYSEYCPR
|
7alpha-hydroxysteroid dehydrogenase that catalyzes the NADP(+)-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as cholate, chenodeoxycholate, glycochenodeoxycholate and taurochenodeoxycholate, to the corresponding 7-oxosteroids . Is also able to catalyze the reverse reduction reactions . Together with 7beta-HSDH encoded in the adjacent gene, is likely involved in the epimerization of the hydroxy group at C-7 of primary bile acids through 7-keto bile acid intermediates .
|
G9FRD7
|
Q4K629
|
PANB1_PSEF5
|
Ketopantoate hydroxymethyltransferase 1
|
Pseudomonas
|
MSSHTRTQRLSVPQLVAMKGRQKIVSLTAYTSHMARLMDPFVDFILIGDSTAMVGYGRTSTLDMSLAEIIAHTRAVVAGSRLACVIADMPFGSYQESPQQAYRNCAEVMARTGCAALKLEGGRALAPTVEFLVQRGIPVMAHIGLMPQFVNQMGGFKAQGLDSEAARKIEEDARAHLEAGAFSLLLEGVAEPLARRISDFSPMPTIGIGASPACDGQVLVTEDLLGLGGPQVPRFVKQYADAGALISQACERFAAEVREQAFPQLQHCYGVVQEA
|
Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
|
Q4K629
|
B1Y500
|
BIOF_LEPCP
|
8-amino-7-ketopelargonate synthase
|
Leptothrix
|
MLIEHLNRQLREREAQSLRRRRRIAETPCAPHQRVSLDGQTASEARELLAFCSNDYLGLANHPALIGALAEGARLWGAGAGASHLISGHTRAHAALEDTLAEWAAPNIPGAKALSFCTGYMANLALLTALGDAEATLFADKLNHASLVDGALLAKAKLQRYAHRQFDVLERQLAACTTPIKLIVTDAVFSMDGDLAELDQLLSLAERFDAWLVIDDAHGFGVLGPKGRGSLAHFGLRSERLILMGTLGKAAGLGGAFVAAHPSVIDWLVQSARAYIYTTAAPPAIAHALSASLALIAGDEGEARRQHLRELIAALRCQLAALIAAQPQLGWRLAESDTAIQPLIVGSNDSALALAAALDAQGLWVPAIRPPTVPVGTARLRITLSAAHSQADVTRLVAALATTARELA
|
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
|
B1Y500
|
Q8BWQ4
|
CMTR2_MOUSE
|
FtsJ methyltransferase domain-containing protein 1
|
Mus
|
MSKRRKLPARQPACLETFSPDVLNDVSELFAKSFSYRKPLDNEWQLPAPTESFSCGHLEFRALLDLKNSLNEVKNLLSDKKLDEWHRHTAFTNKAGKIISHVKKAVNAELCTQAWCKFQEILCSFPLIPQEAFQSGRLNSLHLCEAPGAFIASLNHYLKSHRFPCEWSWVANSLNPYHEANDNLRMITDDRLMANTLHCWYFGPDNTGDIMTLKYLTGLQDFLSGMSPIHLVTADGSFDCQGNPGEQEALVSSLHYCEAVTALITLGDGGSFVLKMFTLFEHCSVNLMYLLNCSFDQVHVFKPATSKAGNSEVYVVCLRYKGREAVQPLLSRMVLNFGTEMTRKALFPHHVIPKSFLERHEECCTFFHRYQLETISENIRLFESMGTGEQERLNNLRDCAVQYFMQKFQLKPLSRNHWLVKKSNIGCSMNTKWFGQRNKYFKTYNERKMMETLSWKDKVAKGYFNSWAEEHTVYHPGQNSLLEGTASSLEYQSWQVLEGKKLPKVKCSPFCDGEILKTLNEAIEKSLGEALSVDAKVSSKQQYRCCPVFSEESVLSELLRLTKCLPDEQGAEPSGPVKCLLVGSPAVCDLQMPAPLEIQLVESVELTAFSCSLLHDGDPAYQHLFLDCLLHSLRRLHRGDVMVLPILSCFTRFMAGLTFVLHGCFRFITFSCPTSLEPLRTCAVLLCIGYQNLPDAVFQFLQNVHDLLSKLLHPSAPRQILQFLPMEALLQGTLLDFLWDLNAAIAKRHLHLIIQGERDQAIGSLEL
|
S-adenosyl-L-methionine-dependent methyltransferase that mediates mRNA cap2 2'-O-ribose methylation to the 5'-cap structure of mRNAs. Methylates the ribose of the second nucleotide of a m(7)GpppG-capped mRNA and small nuclear RNA (snRNA) (cap0) to produce m(7)GpppRmpNm (cap2). Recognizes a guanosine cap on RNA independently of its N(7) methylation status. Display cap2 methylation on both cap0 and cap1. Displays a preference for cap1 RNAs.
|
Q8BWQ4
|
P01848
|
TRAC_HUMAN
|
T cell receptor alpha chain constant
|
Homo
|
IQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESSCDVKLVEKSFETDTNLNFQNLSVIGFRILLLKVAGFNLLMTLRLWSS
|
Constant region of T cell receptor (TR) alpha chain . Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens . Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn, ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation . The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity .
|
P01848
|
B3TN47
|
ATPF_BRADI
|
ATPase subunit I
|
Brachypodium
|
MKNVTHSFVFLAHWPSAGSFGLNTDILATNLINLTVVVGVLIFFGKGVLKDLLDNRKQRILSTIRNSEELRRGTFEQLEKARIRLQKVELEADEYRMNGYSEIEREKENLINATSISLEQLEKSKNETLYFEKQRAMNQVRQRVFQQAVQGALGTLNSCLNTELHFRTIRANIGILGSMEWKR
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
B3TN47
|
P35861
|
CH602_BRADU
|
Chaperonin-60 2
|
Bradyrhizobium
|
MSAKEVKFGVDARDRMLRGVDILHNAVKVTLGPKGRNVVLDKSFGAPRITKDGVTVAKEIELEDKFENMGAQMVREVASKSADAAGDGTTTATVLAAAIVREGAKSVAAGMNPMDLKRGIDMAVEAVVADLVKNSKKVTSNEEIAQVGTISANGDAEIGKFISDAMKKVGNEGVITVEEAKSLETELEVVEGMQFDRGYISPYFVTNADKMRVEMDDAYVLINEKKLSQLNELLPLLEAVVQSGKPLVIIAEDVEGEALATLVVNRLRGGLKVAAVKAPGFGDRRKAMLQDIAILTGGQAISEDLGIKLENVTLNMLGRAKKVMIDKENTTIVSGAGKKADIEARVAQIKAQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKERKDRVDDAMHATRAAVEEGILPGGGVALLRASEHLKGIRTKNDDQKTGVEIVRKALSYPARQIAINAGEDGSVIVGKILEKDQYSYGYDSQTGEYGNLVSKGIIDPTKVVRVAIQNAASVAALLITTEAMVAEVPKKNTGAGGMPPGGGGMGGMGGMDF
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
P35861
|
A1AHD0
|
SELA_ECOK1
|
Selenocysteinyl-tRNA(Sec) synthase
|
Escherichia
|
MTTETRSLYSQLPAIDRLLRDSSFLSLRDTYGHTRVVELLRQMLDEAREVIRDSQTLPAWCENWAQEVDARLTKEAQSALRPVINLTGTVLHTNLGRALQAEAAVEAVTKAMRSPVTLEYDLDDAGRGHRDRALAQLLCRITGAEDACIVNNNAAAVLLMLAATASGKEVVVSRGELVEIGGAFRIPDVMRQAGCTLHEVGTTNRTHANDYRQAVNENTALLMKVHTSNYSIQGFTKAIDEAELVALGKELDVPVVTDLGSGSLVDLSQYGLPKEPMPQELIAAGVSLVSFSGDKLLGGPQAGIIVGKKEMIARLQSHPLKRALRADKMTLAALEATLRLYLHPEALSEKLPTLRLLTRSAEVIQIQAQRLQAPLAAHYGAEFAVQVMPCLSQIGSGSLPVDRLPSAALTFTPHDGRGSHLESLAARWRELPVPVIGRIYDGRLWLDLRCLEDEQRFLEMLLK
|
Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
|
A1AHD0
|
Q039F7
|
TYSY_LACP3
|
Thymidylate synthase
|
Lacticaseibacillus
|
MLEQPYLDLAQKVLDEGHFKPDRTHTGTYSIFGHQMRFDLSKGFPLLTTKKVPFGLIKSELLWFLRGDTNIRFLLQHKNHIWDEWAFEKWVASPDYHGPDMTDFGHRSQKDPEFAASYREQMAKFDERILTDESFAAKYGDLGLVYGSQWRAWHTSRGDTIDQLGDVIEQIKTHPYSRRLIVSAWNPEDVPTMALPPCHTLFQFYVNDGKLSLQLYQRSADIFLGVPFNIASYALLTHLVAHECGLQVGDFIHTFGDAHLYVNHLDQIKEQLTRTPRQAPTLVLNPDKHDIFDFDMQDIKLLNYDPYPAIKAPVAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
Q039F7
|
A1VUV0
|
BPHD_POLNA
|
2,6-dioxo-6-phenylhexa-3-enoate hydrolase
|
Polaromonas
|
MTALTESSTSKFVKINEKGFSDFQIHYNEAGNGETVIMLHGGGPGAGGWSNYYRNIGAFVEAGYRVILKDSPGFNKSDAVVMDEQRGLVNARAVKGLMDALDIDRAHLVGNSMGGATALNFALEYPDRIGKLILMGPGGLGPSMFAPMPMEGIKLLFKLYAEPSYETLKQMLQVFLYDQSLITEELLQGRWEAIQRNPEHLKNFLVSAQKAPLSTWDVSARLGEIKAKTFITWGRDDRFVPLDHGLKLVWGINDARLHVFSKCGHWAQWEHADEFNRLVIDFLRHA
|
Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD).
|
A1VUV0
|
B3PY58
|
NUOC2_RHIE6
|
NDH-1 subunit C 2
|
Rhizobium
|
MSVEPSLNRAPIMERFGDTIEDLGTAHGIDVFAVPPERIVEFCRFLKEHPAMQFNFLSDICGVDHYPETPRFEAVYHLYSLPNRWRVRIKCRLGDPPEVPSVTGVWRTANWHEREAWDMYGIRFAGHPDLRRIYMWEGFEGFPQRKDFPLRGYKDKLNPFGAEGPPPTQPDLATRDIPQGRPSTPES
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
B3PY58
|
E1VBK3
|
TEAC_HALED
|
Ectoine TRAP transporter large permease protein TeaC
|
Halomonas
|
MTTIMVATMIGLLLLGFPMMIPLATASIIGFFMMFGGLGQMETLIQQLMAGIRPASLIAVPMFILAADIMTRGQSANRLINMVMAFIGHIKGGLAVSTAASCTLFGAVSGSTQATVVAVGSPLRPRMLKAGYSDSFSLALIINSSDIAFLIPPSIGMIIYGIISGTSIGELFIAGIGPGLMILVMFAIYCVIYAIVRGVPTEPKASWGERFSAVRLALWPLGFPVIIIGGIYGGIFSPTEAAAACVLYAVLLEFVVFRSLKISDIYAIAKSTGLITAVVFILVAVGNSFSWIISFAQIPQAILEAVGINEAGPTGVLIAICVAFFVACMFVDPIVVILVLTPVFAPAIEATGLDPVLVGILITLQVAIGSATPPFGCDIFTAIAIFKRPYLDVIKGTPPFIFMLVLAAALLILFPQIALFLRDLAFR
|
Part of the tripartite ATP-independent periplasmic (TRAP) transport system TeaABC involved in the uptake of ectoine and hydroxyectoine in response to osmotic upshock. Probably functions as a recovery system for synthesized ectoine that leaks out of the cell.
|
E1VBK3
|
A6W5U9
|
RL24_KINRD
|
50S ribosomal protein L24
|
Kineococcus
|
MGKTRIKKGDLVQVITRVRGRRNADGTKTSDLGKQGKVLEVIAETDRVLVEGVNRIKRHTKARPGVEGGIVEREAPIHISNVQLVDPETKKPTRVGIRTEQVERDGRTKTNRIRVAKRSGKDI
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
A6W5U9
|
P15529
|
MCP_HUMAN
|
Trophoblast leukocyte common antigen
|
Homo
|
MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL
|
(Microbial infection) May act as a receptor for pathogenic bacteria Neisseria and Streptococcus pyogenes .
|
P15529
|
Q253V7
|
DUT_CHLFF
|
dUTP pyrophosphatase
|
Chlamydia
|
MTIFCELESGVDLPEYATEGASGADLRANIEEPIAVLPGQRVLVPTGIKMQIPQGYEVQVRPRSGLALKHGIMVVNSPGTIDADYRGEVCIILANFGESTFIIEPKMRVAQAVVAPVVQAKFIVVDQEEGLTTTSRGSRGFGHTGEK
|
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.
|
Q253V7
|
P44305
|
RIMI_HAEIN
|
[Ribosomal protein S18]-alanine N-acetyltransferase
|
Haemophilus
|
MSIISQIEACDFERLYEIEQQAHLVPWSFGTLKNNQGERYLNLKLIENNQIIGFAICQTVLDEATLFNIAILPTYQGCGFGKLLLGKLIFQLKEKGVQTLWLEVRESNSARFLYEKIGFNEVDIRKNYYPKPSGGRENAVVMACYL
|
Acetylates the N-terminal alanine of ribosomal protein S18.
|
P44305
|
B4TJ42
|
KEFC_SALHS
|
K(+)/H(+) antiporter
|
Salmonella
|
MDSHTLLQALIYLGSAALIVPIAVRLGLGSVLGYLIAGCIIGPWGLRLVTDAESILHFAEIGVVLMLFVIGLELDPQRLWKLRASVFGGGALQMVVCGGLIGLFCMFLGLRWQVAELIGMTLALSSTAIAMQAMNERNLTVSQVGRSAFAVLLFQDIAAIPLVAMIPLLAASGASTTLGAFALSALKVAGALALVVLLGRYVTRPALRFVARSGLREVFSAVALFLVFGFGLLLEEVGLSMAMGAFLAGVLLASSEYRHALESDIEPFKGLLLGLFFIGVGMSIDFGTLVENPLRILLLLAGFLAIKIVMLWLVARPLGVPAKQRRWFAVLLGQGSEFAFVVFGAAQMAGVLEPEWAKALTLAVALSMAATPIFLMLLTRMEKTEKGEAREADEIDEEQPRVIVAGFGRFGQIAGRLLLSSGVKMVVLDHDPDHIETLRKFGMKVFYGDATRMDLLESAGAAKAEVLINAIDDPQTNLQLSELVKSHFPHLQIIARARDVDHYIRLRQAGVAMPERETFEGALKSGRQALEALGLGRYEARERADLFRHFNTRMVEEMAKGENDPLSRAAAYKRTSAMLSEIITEDREHLSLIQRHGWQGTAEGKHSGEAADEPEVKPSI
|
Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport.
|
B4TJ42
|
C3K330
|
GLPE_PSEFS
|
Thiosulfate sulfurtransferase GlpE
|
Pseudomonas
|
MSEFKRIPPEHAQALREQGAVVVDIRDQPTYAAGHITGAQHVDNVNIADFIRAADLDAPVIVACYHGNSSQSAAAYLVSQGFSDVYSLDGGFELWRTTYPAEISSGNSQ
|
Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide.
|
C3K330
|
B7HJE9
|
NAMA_BACC4
|
NADPH dehydrogenase
|
Bacillus cereus group
|
MNSKLFSPYTIKNVTLKNRIVMSPMCMYSSGNEDGSVTNFHLIHYGTRAAGQVGLVMVEATAVLAEGRISNKDLGIWDDNLIEGLHKTTTFIHDNGAKAAIQLAHAGRKAELDTNAFAPSAIPFNDKMKIPVEMNIQQIKETILAFQRAALRSKQAGFDVIELHGAHGYLINEFLSPLTNKRTDKYGGSPENRYRFLREIIDSVNEVWDGPIFVRISANDYHPDGLTVQDYVQYTKWMKEQGIDLIDCSSGAVVPAHIDVYPGYQVQYAKHIKEHTKIATGAVGLITTGSQAEQILNNNEADLIFIGRELLRNPYFPRIAANELGFELQEPYQYKRAPGKIHTNK
|
Catalyzes the reduction of the double bond of an array of alpha,beta-unsaturated aldehydes and ketones. It also reduces the nitro group of nitroester and nitroaromatic compounds. It could have a role in detoxification processes.
|
B7HJE9
|
Q5LH44
|
DXS_BACFN
|
1-deoxyxylulose-5-phosphate synthase
|
Bacteroides
|
MKNEPTYSLLNAINYPKDLRQLSVDQLPEVCEELRQDIIKELSCNPGHFAASLGVVELTVALHYVYNTPYDRIVWDVGHQAYGHKILTGRREAFSTNRKLGGIRPFPSPEESEYDTFTCGHASNSISAALGMAVAAERKGEKDRHVVAVIGDGSMSGGLAFEGLNNASSTANNLLIILNDNDMAIDRSVGGMKQYLFNLTTSNRYNQLRFKTSRLLFKMGLLNEERRKALIRLGNSLKSLAAQQQNIFEGMNIRYFGPIDGHDVKNIARILHDIKDMQGPKILHLHTIKGKGFGPAEKQATIWHAPGKFDPVTGKRIVANTDGMPPLFQDVFGHTLVELAEKNKRIMGVTPAMPSGCSMNMLMDRMPDRAFDVGIAEGHAVTFSGGMAKDGLLPFCNIYSSFMQRAYDNIIHDVAIQKLNVVFCLDRAGLVGEDGPTHHGVFDMAYLRPIPNLTISSPMDEHELRRLMYTAQLPDKGPFAIRYPRGRGSLVDWECPLEEIPVGKGRKLKDGNDLAVITIGPIGKLAARAIERAEADTGISVAHYDLRFLKPLDEELLHEVGKKFRHIVTIEDGIIKGGMGCAILEFMADNGYYPEIRRIGVPDQFIEHGSVQQLYHLCGMDEEGIYKVITKNKLRMDAPVESCMATHS
|
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
|
Q5LH44
|
Q72R59
|
FLAB_LEPIC
|
Flagellin class B
|
Leptospira
|
MIINHNLSAVNAHRSLKFNELAVDKTMKALSSGMRINSAADDASGLAVSEKLRTQVNGLRQAERNTEDGMSFIQTAEGFLEQTSNIIQRIRVLAIQTSNGIYSNEDRQLVQVEVSALVDEVDRIASQAEFNKFKLFEGQFARGSRVASMWFHMGPNQNQRERFYIGTMTSKALKLVKADGRPIAISSPGEANDVIGLADAALTKIMKQRADMGAYYNRLEYTAKGLMGAYENMQASESRIRDADMAEEVVSLTTKQILVQSGTAMLAQANMKPNSVLKLLQQI
|
Component of the core of the flagella.
|
Q72R59
|
Q0K634
|
RL6_CUPNH
|
50S ribosomal protein L6
|
Cupriavidus
|
MSRVGKAPIALPKGAEVNVAAGVLSVKGPLGTLSQPIHSLVKVNVENDTLTFSPADESREANALQGTMRALVANMVKGVTTGFERKLNLVGVGYRAQLQGAALKLQLGFSHDVIHEMPEGVKAETPTQTEIIIKGADKQKVGQVAAEVRAYRPPEPYKGKGVRYSDERVILKETKKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
Q0K634
|
Q9M373
|
AGP20_ARATH
|
Arabinogalactan peptide 20
|
Arabidopsis
|
MASRNSVAVIALFAFVFAVISPFAGAQSLAPAPSPTSDGTSIDQGIAYLLMVVALVLTYLIHPLDASSSSYTFF
|
Proteoglycan that seems to be implicated in diverse developmental roles such as differentiation, cell-cell recognition, embryogenesis and programmed cell death.
|
Q9M373
|
Q0RE66
|
MDH_FRAAA
|
Malate dehydrogenase
|
Frankia
|
MSSTPVNVTVTGAAGQIGYALLFRIASGQLLGADTPVRLRLLEIPQAVRAAEGTALELEDSAFPLLAGVDVFDDAKRAFEGTNVALLVGARPRTKGMERGDLLSANGGIFKPQGEAINSGAAEDIRVLVVGNPANTNALIAQTHAPDVPAERFTAMTRLDHNRAIAQLAKKLGVPSAEIRKITIWGNHSATQYPDIFHAQVGGRSGAEAVGDQKWIAEEFIPRVAKRGAEIIEVRGASSAASAASAAIDHVYTWVNGTPEGDWTSAAIPSDGSYGVPEGLISSFPVTAAGGKFEIVQGLELDAFSREKIDASVRELAEEREAVRALGLI
|
Catalyzes the reversible oxidation of malate to oxaloacetate.
|
Q0RE66
|
Q8FQZ4
|
ISPE_COREF
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Corynebacterium
|
MRITARAWGKINLHLGVGPAREDGYHELVTVFQTIDLAETITLTTLEDELVEEGSVVRQLTVTGPRGVPTTPDNLAWRAVDALVGRRREHDRTPLPAVELHIDKGIPVAGGMAGGSADAAAALRAVDAWIGPFGEETLLEVAAELGSDVPFCLLGGTKLGTGRGEQLVDMLSRGTYHWALVVSPKGLSTPEVFAKFDEMSLPSSMDVTPMSQALLDGSAGALAEVLENDLAPAALSLRPDLRKTQLAGLRAGALATMVSGSGPTIALLCDDAQSARDVADALMDEGVGLSVHPATSPVPGPAKNRGAHIVSIESE
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
Q8FQZ4
|
C3PPA3
|
RS19_RICAE
|
30S ribosomal protein S19
|
spotted fever group
|
MARSIWKGPFVDGYLIKKVQKLMESGKSEMIKTWSRRSTILPIFVGFTFSVHNGNKFIPVSVNEEMVGRKLGEFAPTRTFHGHGADKKIKRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
C3PPA3
|
Q69XJ0
|
SPX1_ORYSJ
|
Protein SPX DOMAIN GENE 1
|
Oryza sativa
|
MKFGKSLSSQIVETLPEWRDKFLSYKDLKKRLKLIGGGGGGEERQAKRARVAADGGEEEAAAAAMTPEEAGFMRLLEAELDKFNSFFVEKEEEYIIRQKELQDRVARAAGRESKEELMRVRKEIVDFHGEMVLLENYSALNYTGLVKILKKYDKRTGALIRLPFIQKVLQQPFFTTDLLYKLVKQCEAMLDQLLPSNELSVSSEDGRGDSTNEDKPSNPSSSLVNGGTIPELDEIEYMESMYMKGTVAALRSLKEIRSGSSTVSAFSLPPLQGDSSPEEQQELWNKIPVIEQAAK
|
Involved in plant adaptation to phosphate starvation . Inhibits PHR2 DNA-binding activity via a Pi-dependent protein interaction . Suppresses the regulation on expression of PT2 by PHR2 and accumulation of shoot Pi . Optimizes growth under phosphate-limited conditions through a negative feedback loop of the PSI (phosphate starvation-induced) signaling pathway . Regulates the expression of SPX2, SPX3 and SPX5 . May be an important link between signal transduction pathways related to phosphate starvation and cold stress .
|
Q69XJ0
|
Q12645
|
PID9_FUSVN
|
Cytochrome P450 57A1
|
Fusarium solani species complex
|
MLVDTGLGLISELQAKLGWAVLLQIVPITIVAYNLLWFIYASFFSSLRKIPGPFLARISRVWEMKKTATGNIHEIMMDLHRRHGAIVRIGPRRYDFDTMEALKIIYRIGNALPKADYYKPFGLPSFPNLFDEQNPARHSAIKKQVASLYTMTALLSYEEGVDGQTAILKEQLQRFCDQKQVIDLPRFLQYYAFDVIGVITVGKSMGMMESNSDTNGACSALDGMWHYASMMAYIPNMHAWWLRLSSLLPIEVPIKGLTEYVERRIIQYRLKAAEFGDDAALKGENNFLAKLLLMEKKGTVTPVETQQAVGLNIGAGSDTTANALSTILYYLYTNPRTLHTLREELERYVKDGPISFQQSQSMPYLQAVIKEALRLHPGVGTQLTRVVPKGGLVIEGQFFPEGTEVGVNGWALYHNKAIFGNDASIFRPERWLEANENINIGGSFAFGAGSRSCIGKNISILEMSKAIPQIVRNFDIEINHGDMTWKNECWWFVKPEYKAMIKPRRCCLSRDESLV
|
Can detoxify the phytoalexin pisatin from garden pea. Pisatin is an antimicrobial compound produced by pea in response to infection by plant pathogens.
|
Q12645
|
B8GIX8
|
DTDA_METPE
|
D-tyrosyl-tRNA(Tyr) deacylase
|
Methanosphaerula
|
MKITLVNSRLDPAGVTIREQIQVLLADPEYQREGIDWEFLEIDGRLIHQERIDTGLNSDLLIFLSRHTSRRPVPVLTVHPTGNPGEALLGGEAGSFAPAAPGWMQAVLQNLVRLVPDGYQASYEVTHHGPTTLSTPSFFVEIGSTDHEWSDPVAGAAVAEAVLTAAPVDPISLIGFGGTHYAPRETAVALETRGAFGHILHSREIGGLTGSLLAKIATAAEAEAVYIDRKAIDRPALDHLYALLEETDLPVLGEKELHQIGSLSWQEYRSLRQIAGDAAPGAHLVIGTLPGGGTPVTATVPADLLAQAISADQGRVMTAIGRMPVVGLTGRGGLLLPIIITYERYRSQIIHDLITLCVKTIREEQHAVIDGDRLIIKKERFDPGLAASLGVPPGALFGMLKGGQAVRVGDQVIKPEMVRSCTVTAIHLRGLERYT
|
D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
|
B8GIX8
|
O87940
|
TDIR_THAAR
|
Transcriptional regulatory protein TdiR
|
Thauera
|
MQATKTGNASTVFVVDDEASVRDSLTWLLNSISLDVRTFESAKDFLDADISCTHGCVVLDVRMQNVSGLQLQQALSERGFKLPIIFLSAYGDAQMGAQAVKKGAFDFLQKPYRNQDLLDAVNAALALNREMADKQNEKQKHLDLLATLSQREMEILDKVVAGSSSKEIAKLLGISYKTVEAHRGRIISKLGLKSTGDLMHFVMRGSSHCSDCGRQPLPGSSPCRPAA
|
Member of the two-component regulatory system TdiR/TdiS, which probably regulates transcription of toluene catabolic genes (bss operon). Binds to DNA.
|
O87940
|
C1DCC3
|
ENO_LARHH
|
2-phosphoglycerate dehydratase
|
Laribacter
|
MSSIVDVIAREILDSRGNPTVECDVWLDSGVMGRAAVPSGASTGEKEALELRDGDARRYLGKGVLKAVEHVNNEICEALIGLDPTDQAYIDQTLLELDGTDNKGSLGANAILAVSVAVAKAAALEVGLPLYRYLGGSGPMSLPVPMMNVINGGAHANNTLDIQEFMIMPVGARSFREALRCGAEIFHTLKKICADKGYSTAVGDEGGFAPNLARNEDAIKLILEATDKAGYVPGEDVLIALDCASSEFYKDGKYHLAGENLALSSEEFTNYLATLCDNYPIISIEDGMSEHDWAGWKLLTDKLGDKVQLVGDDVFVTNPAILAEGIKQGICNSLLVKINQIGSLSETLKAVDLAKRSGYTSVMSHRSGETEDSTIADLAVATNCMQIKTGSLSRSDRMAKYNQLLRIEEELGSAASYPGRAAFYHLK
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
C1DCC3
|
B0S0K8
|
RECR_FINM2
|
Recombination protein RecR
|
Finegoldia
|
MSLYPKAMDELIKNLSNLPTIGRKSARRLAYRIIDMDPKKVDELVESIVNVKTNIRPCANCGNLTDKKLCDICSDQKRDNSVITVVEDSMNVISIEKTGEYNGKYHVLGGLLSPRDNIAPQDLNLENLFLRCKKDYVKEVILALSPTTNGDLTTNFIIEVLKNEEYNVKVSRIAMGVPLGANLEYYDEMSLYKAILDRREIK
|
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.
|
B0S0K8
|
Q865X5
|
IL4_LAMGL
|
Lymphocyte stimulatory factor 1
|
Lama
|
MGLTSQLIPTLVCLLVCTSNFAHGHKCDITLQEIIKTLNTLTARKNSCMELTVADVFAAPKNTTEKETFCKAATALRHIYRHHNCLSKHLSGLDRNLSGLANTTCSVNDSKKSTLRDFLERLKKIMKEKYSKC
|
Participates in at least several B-cell activation processes as well as of other cell types. It is a costimulator of DNA-synthesis. It induces the expression of class II MHC molecules on resting B-cells. It enhances both secretion and cell surface expression of IgE and IgG1. It also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes. Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4.
|
Q865X5
|
Q91VZ6
|
SMAP1_MOUSE
|
Stromal membrane-associated protein 1
|
Mus
|
MATRSCREKAQKLNEQHQLILSKLLREEDNKYCADCEAKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTPEQIQCMQDMGNTKARLLYEANLPENFRRPQTDQAVEFFIRDKYEKKKYYDKNAIAITNKEKEKKKDEKKREKEPEKPAKPLTTEKLPKKEEQQLEPKKSTSPKNAAEPTIDLLGLDGPAEAPVTNGNPATAPALSDDLDIFGPMISNPLPAAVMPPAQGTASVPAPATLSTVTSGDLDLFTEQTTKSEEVAKKQLSKDSILSLYGTGAQQSTPGVFMGPTNIPFTSQAPTAFQGFPSMGVPVPAAPGLIGNMMGQNTGMMVGMPMHNGFMGNAQTGVMPLPQNVVGPQGGMVGQMGAPQSKFGLPQAQQPQWNLSQMNQQMAAMNLSSANASAGFGQPPSTTAGWSGSSSGQTLSTQLWK
|
GTPase activating protein that acts on ARF6. Plays a role in clathrin-dependent endocytosis. May play a role in erythropoiesis.
|
Q91VZ6
|
D5EXZ4
|
AXFA_PRER2
|
Ferulic acid esterase
|
Prevotella
|
MYQSTLKTILLASALLILPASMSAQKRKAAPKKAATEQVGKPDPNFYIFLCFGQSNMEGNARPEAQDLTSPGPRFLLMPAVDFPEKGRKMGEWCEASAPLCRPNTGLTPADWFGRTLVASLPENIKIGVIHVAIGGIDIKGFLPDSIQNYLKVAPNWMKGMLAAYDNNPYERLVTLAKKAQKDGVIKGILMHQGETNTGDPKWAGMVKQVYDNLCGDLNLKPEEVNLYAGNIVQADGKGVCIGCKKQIDELPLTLHTSQVISSDGCTNGPDRLHFDAAGYRELGCRYGEAVARHLGYEPKRPYIEMPKQIEVPADAFIAETTVPGNEFPKVDKEGRAYFRIAAPEARKVVLDICNKKYDMQRDGKGNFMAVTDPLPVGFHYYFLNINGVNFIDPSTETFFGCNRESGGIEIPEGSEGDYYRPQQGVPAGQVRSIYYYSNEQQTWRHAMVYTPAEYELAKNAKKRYPVLYLQHGMGEDETGWSKQGHMQHIMDNAIAKGEAVPMIVVMESGDIKAPFGGGNNQAGRSAYGASFYPVLLNDLIPYIDSNYRTKSDRENRAMAGLSWGGHQTFDVVLTNLDKFAWLGTFSGAIFGLDVKTAYDGVFANADEFNKKIHYMYMNWGEEDFIKSGDIVKQLRELGIKVDSNESKGTAHEWLTWRRGLNEFIPHLFKK
|
Involved in degradation of plant cell wall polysaccharides. Bifunctional esterase that possesses both acetyl esterase and ferulic acid esterase activities. Has deacetylase activity towards acetylated xylo-oligosaccharides smaller than xylo-heptaose, as well as from glucose-pentaacetate. Is also able to release ferulic acid from methylferulate, and from the more natural substrates wheat bran, corn fiber, and XOS(FA,Ac), a corn fiber-derived substrate enriched in O-acetyl and ferulic acid esters.
|
D5EXZ4
|
Q0AGN5
|
LEU1_NITEC
|
Alpha-isopropylmalate synthase
|
Nitrosomonas
|
MKERLVIFDTTLRDGEQSPGASMTMEEKVRIARQLERMGVDVIEAGFPAASKGDFEAVKAVAEAVSNSTVCGLSRAIEADINRAGEALQANQNMRIHTFIATSPIHMKNKLRMSPDRVIEQAIKAVKWARQYTDNVEFSPEDAGRSEIDFLCRILEAVIDAGARTLNIPDTVGYTMPDQFGGLIRTLRERIPNSDKAVFSVHCHNDLGLAVANSLSAVMNGARQVECTINGLGERAGNAALEEVVMAVRTRQDYFPCDTRIDTTQIVSTSKLVSGITGFPVQPNKAIVGANAFAHESGIHQDGVLKHRETYEIMRAEDVGWGANKLLLGKHSGRNAFRSRLKELGIELESEEKLNTIFIRFKDLADKKHEIFDEDLHALVSDEAQIPEEHYRLLSLVAHSETGEIPFAQVVIATGNNEQQAESEGSGPVDATFRAIEKILNSKAELQLFSVNNITSGTDALGEVTVRLQKVGRIVNGHGADTDIIAASAKAYLNACNKLHSSLERTHPQV
|
Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
|
Q0AGN5
|
Q6ME32
|
CLPP1_PARUW
|
Endopeptidase Clp 1
|
Candidatus Protochlamydia
|
MTRETSMPKHDKNKSAIPSKMADRIEHAILDSRRIFISDAVDSGSASEIIRKLWYLELTDPGKPILFVINSPGGAVDSGFAIWDQIKMITSPVTTLVTGLAASMGSILSLCASPGRRFATPHSRIMIHQPLLSGVIKGQATDLEIQAKEMLKTRNGLIEIYVQATGKNFAAIEKAIDRDTWMTAQEALEFGLLDKVINSFEEIEST
|
Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
|
Q6ME32
|
Q6D6H3
|
FLGH_PECAS
|
Basal body L-ring protein
|
Pectobacterium
|
MNAKSVIKPLRRPRLLALIAMLALNGCAYIPHDKVVTGPTTAQPGSPVLAGPNGSIFQTVQPMNYGYQPMFEDRRPRNIGDTLTIVLQENVSASKSSSANAARNGSSTFGVATTPRYLEGPLGNNRAALDATGTNDFSGKGGANANNTFSGTITVTVGQVLANGNLNVVGEKQIAINQGTEFIRFSGVVNPRTISGNNSVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNVSPF
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
Q6D6H3
|
A8GCZ9
|
TRHO_SERP5
|
tRNA hydroxylation protein O
|
Serratia
|
MPVLHNRISNEELKARMLAETEPRTTVSFYKYFTIEDPKAFRDSLYVQFDKLKVFGRIYVAKEGINAQISVPQNKFEAFKAALFASHPALDQVRLNIALEDDGKSFWVLRLKVRERIVADGLDDESFNPANVGEYLQADRVNQMIDDPDTLFVDMRNHYEYEVGHFENAIEVPSDTFRDQLPMAVEMLQDNKDKNIVMYCTGGIRCEKASAYMLHNGFKNVYHVEGGIIEYARKAKEQGLPLKFVGKNFVFDERMGERISDDVIANCHQCGAPCDTHTNCLNDGCHLLFIQCPSCAAKFEGCCSEICREELKLPREEQRARRAGRENGIKIFNKSKGLLQTTMHIPAPEEDKDSAN
|
Catalyzes oxygen-dependent 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs.
|
A8GCZ9
|
Q5IS50
|
DPP6_PANTR
|
Dipeptidyl peptidase VI
|
Pan
|
MTTAKEPSASGKSVQQQEQELVGSNPPQRNWKGIAIALLVILVICSLIVTSVILLTPAEDNSLSQKKKVTVEDLFSEDFKIHDPEAKWISDTEFIYREQKGTVRLWNVETNISTVLIEGKKIESLRAIRYEISPDREYALFSYNVEPIYQHSYTGYYVLSKIPHGDPQSLDPPEVSNAKLQYAGWGPKGQQLIFIFENNIYYCAHVGKQAIRVVSTGKEGVIYNGLSDWLYEEEILKTHIAHWWSPDGTRLAYATINDSRVPIMELPTYTGSIYPTVKPYHYPKAGSENPSISLHVIGLNGPTHDLEMMPPDDPRMREYYITMVKWATSTKVAVTWLNRAQNVSILTLCDATTGVCTKKHEDESEAWLHRQNEEPVFSKDGRKFFFIRAIPQGGRGKFYHITMSLSQPNSSNDNIQSITSGDWDVTKILAYDEKGNKIYFLSTEDLPRRRQLYSANTVGNFNRQCLSCDLVDNCTYFSASFSHSMDFFLLKCEGPGVPMVTVHNTTDKKKMFDLETNEHVKKAINDRQMPKVEYRDIEIDDYNLPMQILKPATFTDTTHYPLLLVVDGTPGSQSVAEKFEVSWETVMVSSHGAVVVKCDGRGSGFQGTKLLHEVRRRLGLLEEKDQMEAVRTMLKEQYIDRTRVAVFGKDYGGYLSTYILPAKGENQGQTFTCGSALSPITDFKLYASAFSERYLGLHGLDNRAYEMTKVAHRVSALEEQQFLIIHPTADEKIHFQHTAELITQLIRGKANYSLQIYPDESHYFTSSSLKQHLYRSIINFFVECFRIQDKLPTVTAKEDEEED
|
Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity.
|
Q5IS50
|
Q18KQ9
|
NOP10_HALWD
|
Ribosome biogenesis protein Nop10
|
Haloquadratum
|
MKSNIKICASWQKKHEQPVYTLADTCPKCNSVTKNTAPAPFDPTDAYGEYRRALKQRVRE
|
Involved in ribosome biogenesis; more specifically in 18S rRNA pseudouridylation and in cleavage of pre-rRNA.
|
Q18KQ9
|
O52025
|
ARSM_HALSA
|
Arsenite methyltransferase
|
Halobacterium
|
MELWTHPTPAAPRLATSTRTRWRRTSRCSQPWATTPGTNSSDASRTPTTASASATSKPQSASARARSVRRSPDCTPRAWSRGARKDRGATTNRPRRPKFCSKRSTTCEATMSNDNETMVADRDPEETREMVRERYAGIATSGQDCCGDVGLDVSGDGGCCSDETEASGSERLGYDADDVASVADGADLGLGCGNPKAFAAMAPGETVLDLGSGAGFDCFLAAQEVGPDGHVIGVDMTPEMISKARENVAKNDAENVEFRLGEIGHLPVADESVNVVISNCVVNLAPEKQRVFDDTYRVLRPGGRVAISDVVQTAPFPDDVQMDPDSLTGCVAGASTVDDLKAMLDEAGFEAVEIAPKDESTEFISDWDADRDLGEYLVSATIEARKPARDD
|
Catalyzes the transfer of a methyl group from AdoMet to arsenite, producing methylated arsenicals.
|
O52025
|
Q1I169
|
SCX5_TITDI
|
P*T-beta* NaTx14.4
|
Tityus
|
IGMVVECKDGYLVGNDGCKYSCSTRPGHYCASECSRVKGKDGYCYAWLACYCYNMPNWAPIWNSATNRCRGRK
|
Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
|
Q1I169
|
P29552
|
ABDA_AEDAE
|
Homeobox protein abdominal-A homolog
|
Stegomyia
|
MSNPFDRVVCGDFAGPNGCPRRRGRQTYTRFQTLELEKEFHFNHYLTRRRRIEIAHALCLTERQIKIWFQNRRMKLKKELRAVKEINEQARREREEQDKMKNDSLKSAQQHHNSQKQQEQTIVGSQQSSGGGGGGGGGGGSSSLGSHLHHPSIVAQNDLKLGLGSMGVGVGVGGNLSMMGGLDNKTNQDILKARGSLVRESFFTVNETILRLRWTTREYVIVALFYPVAASSLLLKFRD
|
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
|
P29552
|
Q46DN2
|
SECG_METBF
|
Protein transport protein Sec61 subunit beta homolog
|
Methanosarcina
|
MAKKSGSGLQSSAGLMRYYEADKNAVQVQPKVVLIVGAIVGIAVLFLSAVNGFWP
|
Involved in protein export. The function of the beta subunit is unknown, but it may be involved in stabilization of the trimeric complex.
|
Q46DN2
|
Q39688
|
EP1G_DAUCA
|
52/54 kDa medium protein
|
Daucus sect. Daucus
|
MARFFPLTLTILLFFIQRIDFCHTLVPANETFKFVNEGELGQYISEYFGDYRPLDPFTSPFQLCFYNQTPTAFTLALRMGLRRTESLMRWVWEANRGNPVDENATLTFGPDGNLVLARSNGQVAWQTSTANKGVVGLKILPNGNMVLYDSKGKFLWQSFDTPTDTLLVGQSLKMGAVTKLVSRASPGENVNGPYSLVMEPKGLHLYYKPTTSPKPIRYYSFSLFTKLNKNESLQNVTFEFENENDQGFAFLLSLKYGTSNSLGGASILNRIKYNTTLSFLRLEIDGNVKIYTYNDKVDYGAWEVTYTLFLKAPPPLFQVSLAATESESSECQLPKKCGNFGLCEESQCVGCPTSSGPVLAWSKTCEPPKLSSCGPKDFHYNKLGGWITT
|
May be involved in the limitation of water flow through the outer epidermal cell wall, either by direct modification of wall structure or as a signal instructing the protoplast to restrict water transport across the cell wall.
|
Q39688
|
Q7Z553
|
MDGA2_HUMAN
|
MAM domain-containing protein 1
|
Homo
|
MDLLYGLVWLLTVLLEGISGQGVYAPPTVRIVHSGLACNIEEERYSERVYTIREGETLELTCLVTGHPRPQIRWTKTAGSASDRFQDSSVFNETLRITNIQRHQGGRYYCKAENGLGSPAIKSIRVDVYYLDDPVVTVHQSIGEAKEQFYYERTVFLRCVANSNPPVRYSWRRGQEVLLQGSDKGVEIYEPFFTQGETKILKLKNLRPQDYANYSCIASVRNVCNIPDKMVSFRLSNKTASPSIKLLVDDPIVVNPGEAITLVCVTTGGEPAPSLTWVRSFGTLPEKTVLNGGTLTIPAITSDDAGTYSCIANNNVGNPAKKSTNIIVRALKKGRFWITPDPYHKDDNIQIGREVKISCQVEAVPSEELTFSWFKNGRPLRSSERMVITQTDPDVSPGTTNLDIIDLKFTDFGTYTCVASLKGGGISDISIDVNISSSTVPPNLTVPQEKSPLVTREGDTIELQCQVTGKPKPIILWSRADKEVAMPDGSMQMESYDGTLRIVNVSREMSGMYRCQTSQYNGFNVKPREALVQLIVQYPPAVEPAFLEIRQGQDRSVTMSCRVLRAYPIRVLTYEWRLGNKLLRTGQFDSQEYTEYAVKSLSNENYGVYNCSIINEAGAGRCSFLVTGKAYAPEFYYDTYNPVWQNRHRVYSYSLQWTQMNPDAVDRIVAYRLGIRQAGQQRWWEQEIKINGNIQKGELITYNLTELIKPEAYEVRLTPLTKFGEGDSTIRVIKYSAPVNPHLREFHCGFEDGNICLFTQDDTDNFDWTKQSTATRNTKYTPNTGPNADRSGSKEGFYMYIETSRPRLEGEKARLLSPVFSIAPKNPYGPTNTAYCFSFFYHMYGQHIGVLNVYLRLKGQTTIENPLWSSSGNKGQRWNEAHVNIYPITSFQLIFEGIRGPGIEGDIAIDDVSIAEGECAKQDLATKNSVDGAVGILVHIWLFPIIVLISILSPRR
|
May be involved in cell-cell interactions.
|
Q7Z553
|
Q8ZED3
|
RNFG_YERPE
|
Rnf electron transport complex subunit G
|
Yersinia
|
MLKTMRRHGITLALFAAGATGLTAVVNSLTENTIAHQAALQQKALLDQVVPAENYDNDMQAECYVVTDSALGNMAPHRLYLARKGNQPVAAAIETTAPDGYSGAIQLLVGADFHGNVLGSRVIEHHETPGLGDKIDIRISDWINHFSGQHVTGDDDKRWAVKKDGGSFDQFTGATITPRAVVRAVKNAALYLQTLPPQLSRLPSCGEDQ
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q8ZED3
|
Q9V9I4
|
OR42B_DROME
|
Odorant receptor 42b
|
Sophophora
|
MVFELIRPAPLTEQKRSRDGCIYLYRAMKFIGWLPPKQGVLRYVYLTWTLMTFVWCTTYLPLGFLGSYMTQIKSFSPGEFLTSLQVCINAYGSSVKVAITYSMLWRLIKAKNILDQLDLRCTAMEEREKIHLVVARSNHAFLIFTFVYCGYAGSTYLSSVLSGRPPWQLYNPFIDWHDGTLKLWVASTLEYMVMSGAVLQDQLSDSYPLIYTLILRAHLDMLRERIRRLRSDENLSEAESYEELVKCVMDHKLILRYCAIIKPVIQGTIFTQFLLIGLVLGFTLINVFFFSDIWTGIASFMFVITILLQTFPFCYTCNLIMEDCESLTHAIFQSNWVDASRRYKTTLLYFLQNVQQPIVFIAGGIFQISMSSNISVAKFAFSVITITKQMNIADKFKTD
|
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to ethyl acetate and pentyl acetate.
|
Q9V9I4
|
Q2P0X3
|
TRUB_XANOM
|
tRNA-uridine isomerase
|
Xanthomonas
|
MKPRIAYRPLHGILLLDKPAGLSSNNALQAARRLLRAEKGGHTGSLDPLATGLLPLCFGEATKIAGLLLGSAKAYDAEIVLGVTTDTDDADGEPLRERAVPDVSEADLQVALAAFIGRIQQQAPIYSALKQGGEPLYAKARRGEVIDAPVREVEVQAIEVLGYSAPRLTLRVTCGSGTYIRSLARDLGEVLGCGAHIASLRRLWVEPFRAPQMITLEGLATALEAGAEAQTVLLPIEAGLADFARIVLDAALAARFRMGQRLRDAAFPTGQVAVFGPDGSPSGLGLVDADGRLSPQRLFNGLNEISVC
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q2P0X3
|
P67827
|
KC1A_BOVIN
|
CK1
|
Bos
|
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF
|
Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling. Phosphorylates CTNNB1 at 'Ser-45'. May phosphorylate PER1 and PER2. May play a role in segregating chromosomes during mitosis. May play a role in keratin cytoskeleton disassembly and thereby, it may regulate epithelial cell migration.
|
P67827
|
Q66HY7
|
IF4E3_DANRE
|
Eukaryotic translation initiation factor 4E type 3
|
Danio
|
MAVPAAPNLQLNTARQSSPVNSTENDIHIDERELENITNHVEDGTSLPLHSPWTFWLDRSLPGTTAAECESNLKKIYTVHTVQSFWSVYNNIPPVSCLPLRCSYHLMRGERRPLWEEESNAKGGVWKMKVPKESTLAVWKELLLATIGEQFTDYCASEDEVVGVSVSVREREDVVQVWNGNASFANEANVLGRIYELLPQISFKAVFYKPHEEHHAFEGGRSRH
|
Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis.
|
Q66HY7
|
Q4FNM7
|
RS15_PELUB
|
30S ribosomal protein S15
|
Candidatus Pelagibacter
|
MTKKAEELKMHEKDTGSSEVQIALLTGKIETLSAHIKQFKKDKHSSVGLLRAVNRRKKLLEYLKKNKFDSYKNVLTQLNLRK
|
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
|
Q4FNM7
|
Q9TLU2
|
RK14_CYACA
|
50S ribosomal protein L14, chloroplastic
|
Cyanidium
|
MISVHTRLKVIDNSGGKEIMCIRVLGTNRKYATLGDVIIGVVKNAVPNMPVKKSDVVRAVVVRIKKTINRKNFFSVRFDDNAAVIIGSDGNPKGTRIFGPVARELRDKNFSKIASLAQEVV
|
Binds to 23S rRNA.
|
Q9TLU2
|
A1T5Q3
|
NTPP_MYCVP
|
Nucleotide pyrophosphatase
|
Mycolicibacterium
|
MTRVVLASASKGRLGVLRQAGIDPQVIVSAVDEDTLLAALDPDLPPEAVVAKLATAKALSVAAELPDELLADCVVIGCDSMLFLDGTLRGKPGSAEAARAQWESMAGSAGHLLTGHALLRISGGVITHTEGDTGSTKVHFGKPAEDEITRYVDSGEPIHVAGAFTLNGLGGWFVDRIEGDPSNVIGLSLPLVHRLVRRTGLSISDLWQR
|
Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
|
A1T5Q3
|
Q4WUS1
|
ABCI_ASPFU
|
ABC multidrug transporter I
|
Aspergillus subgen. Fumigati
|
MDEKPAVSESSNGSDVDSLSTASAYEQHRERLRDANPQGVTSHRSGVNVKEAEEEFSELNRQFSTISHQAHCLSKQISRASKPTGKTEDVERSDSPADSDEPWDLETALRGNRDAETAAGIRSKRIGVIWDNLTVRGMGGVKTYIKTFPDAIIDFFNVPETIMHMLGYGKKGKEFEILRNFRGVLQPGEMVLVLGRPGSGCTTFLKTITNQRFGYTSIDGDVLYGIFDADTFAKRFRGEAVYNQEDDVHQPTLTVKQTLGFALDTKTPGKRPLGVSKAEFREKVINMLLKMFNIEHTANTVIGNQFIRGVSGGERRRVSIAEMMITSATVLAWDNSTRGLDASTALDFAKSLRIMTNIYKTTTFVSLYQASENIYKQFDKVLVIDSGRQVFFGPASEARSYFESLGFKERPRQTTPDYLTGCTDPFEREFKEGRSEDDVPSTPDSLVEAFNRSSYSERLAQEMDAYRKKLEQEKHVYEDFEIANQEAKRKFTPKSSVYSIPFHLQIWALMQRQFLIKWQDRFAQTVSWITSTGVAIILGTVWLRLPKTSAGAFTRGGLLFISLLFNGFQAFSELVSTMMGRSIVNKHRQFTFYRPSALWIAQILVDTTFAIARILVFSIIVYFMCGLVLDAGAFFTFILIIVLGYLCMTCFFRVIGCMSPDFDYAMKFASVVITLFVLTSGYLIQWSSEQEWLRWLYYINPFGLGFAALMVNEFKDLTMTCTADSLVPSGPGYDDMASRVCTLAGGEPGSVIIPGASYLAKTFSYFPGDLWRNFGIMVALTVGFLTLNLYHGETLQFGAGGRTVTFYQKENKERRALNGALMEKRTNRESKDQSAANLKITSKSVFTWEDVCYDVPVPSGTRRLLQSVYGYVQPGKLTALMGASGAGKTTLLDVLASRKNIGVISGNILVDGAPPPGSFLRTVSYAEQLDIHEPMQTVREALRFSADLRQPYETPQSEKYEYVEGIIQLLELEDLADAIIGTPETGLSVEERKRVTIGVELAAKPELLLFLDEPTSGLDSQSAFNIIRFLRKLAAAGQAILCTIHQPNSALFENFDRLLLLQRGGECVYFGDIGEDSHVLLDYFRRNGADCPPDANPAEWMLDAIGAGQTRRIGDRDWGEIWRTSSEFEQVKREIIQIKAQRAEEVRQSGGSQIIVREYATPLWHQIKVVCKRTNIVFWRSRNYGFTRLFNHVVIALVTGLAFLNLDDSRASLQYRIFVIFNVTVLPAIILQQVEPRFEFSRLVFFRESACKSYSQFAFALSMVIAELPYSILCAVCFFLPLYYIPGFQAAPSRAGYQFLMVLITELFSVTLGQMISALTPNSFIASQINPPIVIIFSLFCGVAIPRPQMPGFWRAWLYQLDPFTRLISGMVTTELHGRTVSCSPSEFNRFQAPENQTCGEYMLPFFERGGLGYLADNTTQACEYCAYKIGDEFYSAFSMSFNTRWRDLGIFLAFIGSNLIILFLAVSFMSPRCRLRYKLIYDIF
|
ABC efflux transporter that confers resistance to fluconazole (FLC) but shows no resistance to other azoles . Is also able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters .
|
Q4WUS1
|
Q87QY1
|
LFTR_VIBPA
|
Phenyalanyltransferase
|
Vibrio
|
MAIYLTELDSTFNFPSPYEALSDPNGLLAFGGDLDPHRILSGYYQGIFPWYGPGEPILWWSPSPRAVFDPLTFKPSKSLKKFQRKHQYKVTINQATEHVIQLCSSTRPADETWLNEEMQAAYIQLSNLGHCHSVEVWHDNTLVGGLYGISVGQLFCGESMFSLKDNASKIALWYLCTHLASKHGQLIDCQVMNPHLASLGAFELDRDEFIQKLLSLREKQTASDTFTPQVLQDSES
|
Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
|
Q87QY1
|
P13104
|
TPM1_DANRE
|
Tropomyosin-1
|
Danio
|
MDAIKKKMQMLKLDKENALDRAEQAETDKKAAEERSKQLEDDLVALQKKLKATEDELDKYSEALKDAQEKLELAEKKATDAEGDVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIVEGELERTEERAELNEGKCSELEEELKTVTNNMKSLEAQAEKYSAKEDKYEEEIKVLTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
|
Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
|
P13104
|
Q71XT8
|
TSAD_LISMF
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Listeria
|
MGGLMKKNTLILGIESSCDETAASVVKNGNEIISSVVASQIESHKRFGGVVPEIASRHHVEQITLVIEEALKQANVTMDDLDGIAVTEGPGLVGALLIGVNAAKTLAFMHNLPLVGVHHIAGHIYANRFETEFKFPLLSLVVSGGHTELVLMKADNEFEIIGETRDDAAGEAYDKVARTLGLAYPGGVQIDKLAKDGEDTFHFPRAMMDEGSFDFSFSGLKSSFINTLHNLRQRGEEPNPNDMAASFQASVVDVLVSKTIRAAKQYDVKQLLLAGGVAANQGLRERLIQEVKLELPETELIIPPLALCGDNAAMIAAAGTVSFLQGKRSGFDMNANPGLLLEDI
|
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
|
Q71XT8
|
Q03KJ9
|
DEOB_STRTD
|
Phosphodeoxyribomutase
|
Streptococcus
|
MSKFNRMHLIVLDSVGIGAAPDANNFVNAGVPDGASDTLGHISKTVGLNVPNMAKLGLGNIPREQPLKTVPAESNPTGYATKLEEVSLGKDTMTGHWEIMGLNITEPFDTFWNGFPEEILTQIEEFSGRKVIRESNRPYSGTAVIDDFGPRQMETGELIIYTSADPVLQIAAHEDIIPVEELYRICEFARSITLERPALLGRIIARPYVGEPGNFTRTSNRRDLAISPFAPTVLDKLNEAGIDTYSVGKISDIFNGEGINHDMGHNKSNNHGVDNLIKAMTSEDFKHGFSFTNLVDFDALYGHRRNPQGYRDCLHEFDERLPEIIAAMKEDDLLMITADHGNDPTYAGTDHTREYIPFLAYSPSFKCSGLIPVGHFADISATIADNFGVEKAMIGESFLDKLV
|
Phosphotransfer between the C1 and C5 carbon atoms of pentose.
|
Q03KJ9
|
Q29RQ5
|
TRIM9_BOVIN
|
Tripartite motif-containing protein 9
|
Bos
|
MEEMEEELKCPVCGSFYREPIILPCSHNICQACARNILVQTPESESPQSRRASGSGVSDYDYLDLDKMSLYSEADSGYGSYGGFASAPTTPCQKSPNGVRVFPPAMPPPATHLSPALASVPRNSCITCPQCHRSLILDDRGLRGFPKNRVLEGVIDRYQQSKAAALKCQLCEKAPKEATVMCEQCDVFYCDPCRLRCHPPRGPLAKHRLVPPAQGRVSRRLSPRKVSTCTDHELENHSMYCVQCKMPVCYQCLEEGKHSSHEVKALGAMWKLHKSQLSQALNGLSDRAKEAKEFLVQLRNMVQQIQENSVEFEACLVAQCDALIDALNRRKAQLLARVNKEHEHKLKVVRDQISHCTVKLRQTTGLMEYCLEVIKENDPSGFLQISDALIRRVHLTEDQWGKGTLTPRMTTDFDLSLDNSPLLQSIHQLDFVQMKASSPVPATPILQLEDCCTHNNSATLSWKQPPLSTVPAEGYILELDDGNGGQFREVYVGKETMCTVDGLHFNSTYNARIKAFNKTGVSQYSKTLVLQTSEVAWFAFDPGSAHSDIIFSNDNLTVTCSSYDDRVVLGKTGFSKGVHYWELTVDRYDNHPDPAFGVARIDVMKDVMLGKDDKAWAMYVDNNRSWFMHNNSHTNRTEGGITKGATIGVLLDFNRKTLTFFINDEQQGPIAFENVEGLFFPAVSLNRNVQVTLHTGLQVPDFYSSRASIA
|
E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.
|
Q29RQ5
|
P11409
|
MTP2_PROHU
|
N-4 cytosine-specific methyltransferase PvuII
|
Proteus
|
MMTLNLQTMSSNDMLNFGKKPAYTTSNGSMYIGDSLELLESFPDESISLVMTSPPFALQRKKEYGNLEQHEYVDWFLSFAKVVNKKLKPDGSFVVDFGGAYMKGVPARSIYNFRVLIRMIDEVGFFLAEDFYWFNPSKLPSPIEWVNKRKIRVKDAVNTVWWFSKTEWPKSDITKVLAPYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGGSIPPNLLQISNSESNGQYLANCKLMGIKAHPARFPAKLPEFFIRMLTEPDDLVVDIFGGSNTTGLVAERESRKWISFEMKPEYVAASAFRFLDNNISEEKITDIYNRILNGESLDLNSII
|
A beta subtype methylase, recognizes the double-stranded sequence 5'-CAGCTG-3', methylates C-4 on both strands, and protects the DNA from cleavage by the PvuII endonuclease.
|
P11409
|
B5ZB76
|
ENGB_UREU1
|
Probable GTP-binding protein EngB
|
Ureaplasma
|
MAKFIKSAQYFDQYPVDKQFEICVIGRSNVGKSSLINALANEKIARTSNTPGRTQLVNFFDFNSFRLVDLPGYGFARVSKDKQLDLATIIDQYLGYRQNLCAVFQICDINVLTNDDVEMSRYFENQNYAHFVVLNKVDKVNKSHFDNNKQKIAKFLNISVDRLLCVSAQKNTNVATLFALMKKVVIETRQKQLLLKKEEKKSSEEEIK
|
Necessary for normal cell division and for the maintenance of normal septation.
|
B5ZB76
|
C3N652
|
COXX_SULIA
|
Heme O synthase
|
Sulfolobus
|
MSLQQKIKAYLKLGKLGVVSLLDLAAVAGAFLAYKHGISLLPIIPMFIGGTLASMGAMIINSGIEIDRDKVMSRTSKRPTVVGYVNRKEAIIVGSLLAILGTALGFIDNILTAFFIALGVVIYIFVYTILLKPRTWLNIVIGGFAGSAAAWAGYTSLTNSLTLEGFLLGFLIFMWTPGHFWSLALKYREDYVNAHYPMLPAVVGITTSARAIAISNALMIPIVLLLGYYINLIALIAFSILSLFLMFLSYRLILNPTKEEAIKSFIFSNIYLMLILLIMIIVKLI
|
Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
|
C3N652
|
C1FKN5
|
HSLO_CLOBJ
|
Heat shock protein 33 homolog
|
Clostridium
|
MKDKLVKAIAKDGQVRIIGAITTELVNEGVRLHNCAPTAAAALGRMLTAGALMGTTLKSEKDTLTLQIHGGGIAKGVVVTSYADGHVKGYIGNPTADIEPNSKGKLDVSGIIGKNGNLLVIRDMGLKEPYIGQVPIYTGEIGEDLAYYYTVSEQTPSAVGLGVLVDKDLSIKSAGGFIIQMMPGADEMLADLISYRLEEIPSITEMISKGMTIEEILEYIFEDMDLNILESIVPEYRCDCSREKVERALASIGQKDLKEIYDEVKEEELKCHFCNKAYAFSHDEIGNILESYYNEK
|
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
|
C1FKN5
|
A7FP85
|
FDHD_YERP3
|
Sulfur carrier protein FdhD
|
Yersinia
|
MSQIKPSRLSSSAEIRGARQLDVLQRHKLAEPQQDWLAEEVPVALVYNGISHVVMMATPKDLAAFALGFSLSEGIISSPQEIYAIEITPGCNGIEVNIELSSRRFAGLKERRRAMAGRTGCGVCGIEQLDDIFRPITPLPFTQAFNLEHLDTALAQLKQVQPVGQLTGCTHAAAWINPEGELLGGCEDVGRHVALDKLLGIRAKQPWQQGAVLVSSRASYEMVQKTAMCGAEILFAVSAATTLAVEVAERCNLTLVGFSKPGRATVYTHPQRIK
|
Required for formate dehydrogenase (FDH) activity. Acts as a sulfur carrier protein that transfers sulfur from IscS to the molybdenum cofactor prior to its insertion into FDH.
|
A7FP85
|
A8A6R1
|
CYAY_ECOHS
|
Iron-sulfur cluster assembly protein CyaY
|
Escherichia
|
MNDSEFHRLADQLWLTIEERLDYWDGDSDIDCEINGGVLTITFENGSKIIINRQEPLHQVWLATKQGGYHFDLKGDEWICDRSGETFWDLLEQAATQQAGETVSFR
|
Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis.
|
A8A6R1
|
A3GGU2
|
EIF3G_PICST
|
Translation initiation factor eIF3 p33 subunit homolog
|
Scheffersomyces
|
MSTTVIGSWADAGDEFSAPDITTNPDGTKTVITYRTNQDGKKVKITQKIKEVKVQERVHPLIAQRKNWKKYGKESKSPPGPDTSTTQLGEKVELKLGTSWKQQEKEEEEEKAENRAQKLSVQTIRCRTCGGDHYTSKCPFKDTLGATTSSPAAESGAGDNGPGKYVPRHLRADANGNLPSKEGRDDSTTLKVSQLNSFVDEDMLRNELFARFGPLQRVTLVRNRETGDSRGFAYVSFITEDMAQRALDALNGKGYHSLILHLEWSKKKKTV
|
RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. This subunit can bind 18S rRNA.
|
A3GGU2
|
A3DJF7
|
HIS6_ACET2
|
ImGP synthase subunit HisF
|
Acetivibrio
|
MVTKRIIPCLDVHNGRVVKGVNFVNIRDAGDPVEIASYYDKAGADELTFLDITASAEARNIMIDVVRRVAEQVFIPFTVGGGIRTVEDFREILKAGADKVSINSAAVKRPELISEAASRFGSQCVVVAIDAKRRDDNSGWDVYINGGRINTGKDAVEWAVEVEKLGAGEILLTSMDCDGTKKGYDIELTRKVSESVRIPVIASGGAGTMEHFREALVEGKADAVLAASLFHYREIEIMELKKYLKENGIEIRM
|
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.
|
A3DJF7
|
Q9VZI2
|
ACK_DROME
|
Activated Cdc42 kinase Ack
|
Sophophora
|
MTSTSAVDGGLGSETAWLEDLLREVQLEQFLDRIRDDLQVTRLAHFDYVLPDDLERCGLGKPAIRRLMEAVRKKKAHQWRKNILSKLIGGGKQPSSKKQSSAARESSQGNGTQLTCLIHEKDITMGLKLGDGSFGVVRRGEWSASPAGKVIPVAVKVLKSDNLTQPGIIDDFFREVQAMHALDHANLVRLYGVVLSQPMMMITELAERGSLLDTLRKQCRHTSLTIIWNWSVQIVTGMAYLEQKRFLHRDLACRNVLLAAGNKIKIGDFGLMRALPQEDDCYVMSEHKKVPFPWCAPESLRFRQFSHASDTWMFGVTLWEMFSFGEDPWVGLNGSQILRKIDREGERLHQPDACPPDVYAMMLQCWDKTPAERPTFAALKEYLASMSPPVMRASRSHHESKGLQIEPGDTIAIIDGRHELKLIKGQNQRTFDIGIFPRNLLEQRKVGAAGDVVMRSSVGNGSSSSPFGFCWGGAAAMANGDDRQRKCASMTNQPHAKERKSTSSKQFAYNKLVNDSATGLQRRNAVKHKGVVVGPQRPPPPQFQQEGILIDISPDMRPIAEAGTGGAKGAGDSSSLQADSSFCILDAPIDVPTYAGSSGSGDLNVSPTYYNEQPQFDFDPAKMTASPGRLQPPPYQMPPTYSNTMEFVQKRDLHQQQLATPVRERDPFDTTNVETTVALYSNFNQSLEAASPPAPIYNSPSVRKSLFGGSKSNKENIPALESAAMQLNLSNLTLERHDATCIQPVEPVPAPPGDGVLLDKSFIAELEKDMYSNGQNRAQEEYQRNSTQMYASKDMVYKQNLTPLKNGAAPGSVHSNHSSPSSTASPKQNNVEAAAAAAATTQSVVNRIWYEQVASTQSEYYAQPPTEQAEEQIYQNHRHQQQQQQELNHSFVAISNRVVAPKNNAYSSTASLYDAVAASTAGSTYYGQVPNGSGAVLYDEVTQDDYLRPTRPAPLAPPPLSAQQIQRRMEKMRLQQQQQLDGAHQLYAPVPSDYGREQEKLQQLMQELGSSAVEQDVRNALRAASGDVGLATRHYKIDQLARLGVAGRPQCEQALQQTNWSLEVAAELLLNAG
|
Non-receptor tyrosine-protein and serine/threonine-protein kinase that is implicated in diverse biological functions such as cell survival, cell differentiation, cell growth and proliferation . Phosphorylates SH3PX1 and ex . Phosphorylates SH3PX1 predominantly on 'Tyr-56', which likely promotes the recruitment of SH3PX1 to an axonal guidance receptor complex that includes dock and Dscam; because phosphorylation of SH3PX1 increases its interaction with the complex member dock while decreasing its interaction with the actin cytoskeleton modulator WASp . In the wing and eye, promotes tissue growth, and during embryogenesis coordinates cell shape changes required for correct dorsal closure . Functions in the negative regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway by enhancing yki activity thereby promoting cell proliferation and inhibiting apoptosis . This is accomplished, at least in part, by phosphorylating ex thereby reducing its ability to efficiently activate the Hippo signaling cascade . In the eye disk, wing disk and possibly spermatids, inhibits programmed cell death induced by hid and rpr through a mechanism that is independent of the MAP kinase signal transduction pathway . Essential for male and female fertility . During oogenesis required for the correct temporal assembly, and consequently the catalytic activity of long CTPsyn filaments (cytoophidium) in the germline nurse cells, likely by phosphorylating an unidentified substrate that is essential for linking individual CTPsyn filaments into large, catalytically active assemblies .
|
Q9VZI2
|
A1V292
|
HTPG_BURMS
|
High temperature protein G
|
pseudomallei group
|
MTQQTMSFQAEVKQLLHLMIHSLYSNKEIFLRELVSNASDAADKLRFEALENNALYESDPNLRIRLSFDKAARTITIDDNGIGMSRDEAIANLGTIARSGTKEFFSKLSGDQQKDAALIGQFGVGFYSGFIVADRITVETRRAGLPASEGVRWESAGEGDFQVDTIERAARGTTITLHLREGEDELLSSYRLKSIVQKYSDHVALPILMKKEEWDQEKGEMVEKDEDETINQASALWTRAKSEVTDEQYKQFYQHVAHDHQDPLAWTHNRVEGRSEYTQLLFVPSHAPFDLWNRDYRGGLKLYVKRVFIMDDAEQLLPQYLRFIKGVVDSSDLPLNVSREILQESRDVKAIREGVTKRALSMLEELANAEDDAGKEKYKTFWSAFGQVLKEGVGEDHANRERVAKLLRFASTHGDTDAQDVALADYVARMKPEQTKIYYVTADTWQAAKNSPHLEVFRKKGVEVLLLTDRVDEWMLSFLHEFDGKPLASVARGDLDLGALNDDEKKAQEETGEAMKPVVDKMKETLGEKVKDVRVTFRLTDSPSCLVADDNDMSGYLQRMLKAAGQSAPSFQPILEINPEHPLVKALKADGADFGDWCHLLFDQALLAEGGALEDPASFVKRTNALLLSRAA
|
Molecular chaperone. Has ATPase activity.
|
A1V292
|
Q0A7Z2
|
SYS_ALKEH
|
Seryl-tRNA(Ser/Sec) synthetase
|
Alkalilimnicola
|
MLDTRKLRQDPEGVARALARRGYRLDVAHYRALDERRRELQVRTQELQNERNTRSKGIGQAKARGEDIEPLKAEVADLGRQLEAAKGELQAVQDELHDIHVGMPNLPHPDVPEGEDDSENVEVRRWGTPPEFGFRPRDHVELGELLDGGLDFEAAAKLTGARFVVMRGAVARLHRALIQFMLDTHTAEHGYQEIYVPYMVNRDSLFGTGQLPKFAADLFHLDAEQDYYLIPTAEVPVTNMARDEIIADGQLPLKFACHTPCFRSEAGSHGKDTRGMIRQHQFEKVELVQMVRPEASWEALEALTGHAETILQRLDLPYRVVTLCTGDLGFSSAKTYDIEVWLPAQETYREISSCSNFLDFQARRMQARWRNPETGKPEPLHTLNGSGLAVGRCLVAILENYQEADGRVTVPEALRPYMGGITRL
|
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).
|
Q0A7Z2
|
Q3AY05
|
THF1_SYNS9
|
Protein Thf1
|
unclassified Synechococcus
|
MGERQTIADSKRAFHQAFPHVIAPLYRRLADELLVELHLLSHQSSFKTTPLFAVGLCTVFDTFSAGYRPEEHITGLLDALCSSNGYDANTFRKESKRCIDAAKTESVDAMDSHLAGQKLGEGSHYSRLMAIGVLRLFEEAKGDADQPDEADLRKRCKELSTALNFPAERVEKDLSLFASNSERMSAAIELVQETIAAERRKKERRQAEQAQRSES
|
May be involved in photosynthetic membrane biogenesis.
|
Q3AY05
|
P41746
|
RODL_ASPFU
|
Rodlet protein
|
Aspergillus subgen. Fumigati
|
MKFSLSAAVLAFAVSVAALPQHDVNAAGNGVGNKGNANVRFPVPDDITVKQATEKCGDQAQLSCCNKATYAGDVTDIDEGILAGTLKNLIGGGSGTEGLGLFNQCSKLDLQIPVIGIPIQALVNQKCKQNIACCQNSPSDASGSLIGLGLPCIALGSIL
|
Cell wall protein regularly arranged in interwoven fascicules of clustered proteinaceous microfibrils, or rodlets, to form the outer spore coat protein. It is involved in resistance to environmental stress and may well be associated with conidial hydrophobicity. It is important in the morphogenesis of the dispersible conidia.
|
P41746
|
Q8R7W9
|
RL6_CALS4
|
50S ribosomal protein L6
|
Caldanaerobacter
|
MSRIGRLPIPIPKGVEVKVSPDNVVTVKGAKGTLEKKFPPIVNIEVRDGEVVVTRKGDDKEERAMHGTTRAIIANMVKGVTEGFEKALEIVGVGYRAAKQGKKLILNVGYSHPVEIEEEPGIEIIVEGNNRIIVRGADKERVGQVAANIRRVREPDAYQGKGIRYVGEVVRLKEGKTGKK
|
This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center.
|
Q8R7W9
|
P53874
|
UBP10_YEAST
|
Ubiquitin-specific-processing protease 10
|
Saccharomyces
|
MTTQESIKPLVDRILSNPLQFNAAMISNKSNNNDTSAAPENSSYIVIGKQHNNNSNSTAIAATAESKQIKENNLIDRPNGKKTNTVPKSMAEALLLYTSKNDKDAADATGAKKSAELSTELSTEPPSSSSEDDKVGKEEEEEGEIFHEARDYVEPRKASLKERDNADKGDGEDIGEDIGEDIGEDIGEDIGEDIGENLGSPLATIDDSSNENEKEKRKELSTSISSDDEIEDDEDEDDMDYDSSAMEKELPEEEENDSSSKISEGEKKSLYQDLMENSTVEVNRYEPVNNTKENGNRNPKGEEEEEEEEELKHKSRSITPPVTISNLSNFYQFNENINDRGSLNSTRIVKNWGDKFTNLKPRGLLNHGVTCYTNAAVQAMLHIPSIQHYLFDILMGKYDSTISKNSVSYTLAETSKKMWLPVSKNPRKNVSASYINPKHLISRLDDINCMMSEWQQEDSHEYFMSLMSRLQEDSVPKGHKLIESIIYDIFGGLLKQIVTCKSCGSISKTEQPFYDLSLHLKGKKKLDPNSDLSSDSINGTSATTSTTTSNAATKPSLSSSSSVNLNNGSPFAAASDLSSANRRFSIEKSIKDFFNPELIKVDKEQKGYVCEKCHKTTNAVKHSSILRAPETLLVHLKKFRFNGTSSSKMKQAVSYPMFLDLTEYCESKELPVKYQLLSVVVHEGRSLSSGHYIAHCKQPDGSWATYDDEYINIISERDVLKEPNAYYLLYTRLTPKSVPLPLAKSAMATGNVTSKSKQEQAVNEPNNRPLKINSKKNNRKKWKKNKKRKFTK
|
Deubiquitinating enzyme involved in telomere and HM loci silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes . Targets histone H2B for deubiquitination, thus helping to localize SIR2 to the telomere . At silent chromatin, including telomeres and the rDNA locus, not only maintains low H2B 'Lys-123' ubiquitination (H2BK123Ub), but also low H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively) . Controls the proliferating-cell nuclear antigen PCNA/POL30 deubiquitination which is crucial for keeping TLS polymerases in check as well as for down-regulating the error-free bypass . Deubiquitinates and stabilizes RPA190, the largest subunit of RNA polymerase I, to achieve optimal levels of ribosomes and cell growth . Protects also nutrient transporters such as GAP1 from ubiquitin-dependent endocytosis .
|
P53874
|
A1BHM3
|
ISPE_CHLPD
|
4-(cytidine-5'-diphospho)-2-C-methyl-D-erythritol kinase
|
Chlorobium
|
MDHLSVKSFAKINLGLLITGKRKDGYHTLETIFAPINWYDTIGFSDSDVISMSCSNIDLPVDDNNLCIRAARALQQSASCSKGAAMNLQKVVPFGAGLGGGSSDAATVLRVLNELWKINVSSAELHELAVKLGADVPYFLEMKGLAFARGIGDELEDLGLTLPFHVVTVFPEEHISTVWAYKNFYQKFDRPVPDLRLLLQRLCLDGDRSVLGAFENDFEPAVFDHYPKVRVVKESLLDAGSFYASLSGSGSAVFGLFDTLENAAGAVCAMQQKGYRVTLTPPGFSMEAQAGSRL
|
Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
|
A1BHM3
|
Q76MJ5
|
ERN2_HUMAN
|
Endoribonuclease
|
Homo
|
MASAVRGSRPWPRLGLQLQFAALLLGTLSPQVHTLRPENLLLVSTLDGSLHALSKQTGDLKWTLRDDPVIEGPMYVTEMAFLSDPADGSLYILGTQKQQGLMKLPFTIPELVHASPCRSSDGVFYTGRKQDAWFVVDPESGETQMTLTTEGPSTPRLYIGRTQYTVTMHDPRAPALRWNTTYRRYSAPPMDGSPGKYMSHLASCGMGLLLTVDPGSGTVLWTQDLGVPVMGVYTWHQDGLRQLPHLTLARDTLHFLALRWGHIRLPASGPRDTATLFSTLDTQLLMTLYVGKDETGFYVSKALVHTGVALVPRGLTLAPADGPTTDEVTLQVSGEREGSPSTAVRYPSGSVALPSQWLLIGHHELPPVLHTTMLRVHPTLGSGTAETRPPENTQAPAFFLELLSLSREKLWDSELHPEEKTPDSYLGLGPQDLLAASLTAVLLGGWILFVMRQQQPQVVEKQQETPLAPADFAHISQDAQSLHSGASRRSQKRLQSPSKQAQPLDDPEAEQLTVVGKISFNPKDVLGRGAGGTFVFRGQFEGRAVAVKRLLRECFGLVRREVQLLQESDRHPNVLRYFCTERGPQFHYIALELCRASLQEYVENPDLDRGGLEPEVVLQQLMSGLAHLHSLHIVHRDLKPGNILITGPDSQGLGRVVLSDFGLCKKLPAGRCSFSLHSGIPGTEGWMAPELLQLLPPDSPTSAVDIFSAGCVFYYVLSGGSHPFGDSLYRQANILTGAPCLAHLEEEVHDKVVARDLVGAMLSPLPQPRPSAPQVLAHPFFWSRAKQLQFFQDVSDWLEKESEQEPLVRALEAGGCAVVRDNWHEHISMPLQTDLRKFRSYKGTSVRDLLRAVRNKKHHYRELPVEVRQALGQVPDGFVQYFTNRFPRLLLHTHRAMRSCASESLFLPYYPPDSEARRPCPGATGR
|
Induces translational repression through 28S ribosomal RNA cleavage in response to ER stress. Pro-apoptotic. Appears to play no role in the unfolded-protein response, unlike closely related proteins.
|
Q76MJ5
|
B4F103
|
SECM_PROMH
|
Secretion monitor
|
Proteus
|
MSIINFWRQFGRRYFWSHLLLGMVAAGIGMPSLVSAHAENPSQTDTPSSQNRQSQALIAFDNLFLRQSVQNPASSFTFNYWQQHAVKNVIKQLSFAFTIHSPELMVKAKDEPSPVANVAEVMLDTLYALLTQAPSSTLVNLPISRGVLTENRISYHTGLWLAQIRGIRAGPYLTA
|
Regulates secA expression by translational coupling of the secM secA operon. Translational pausing at a specific Pro residue 5 residues before the end of the protein may allow disruption of a mRNA repressor helix that normally suppresses secA translation initiation.
|
B4F103
|
Q5P9M7
|
SSRP_ANAMM
|
Small protein B
|
Anaplasma
|
MEIVAENRKARFDYFVLQEYDAGMVLVGSEVKSLRQRKVNMGDAYVLEKDMELWIHNLHISEYNRADRKNHKPLRVRKLLLRKREIHKIAGNIKVSGLAVVPLMIFFNNKGIAKIKIAIVKGKKLYDKREAIKTRDWQREKSRISRREV
|
Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
|
Q5P9M7
|
Q82M90
|
G6PI1_STRAW
|
Phosphohexose isomerase 1
|
Streptomyces
|
MSDSPRLTRRPEWTELEDHRAGPLLHPALRELFAADPERAERYVVRAGDLRLDYSKHLITDETLALLQELATATDVFGLRDAMFRGEKINVTENRAVLHTALRAPRDAVIEVDGENVVPAVHAVLDRMADFADRVRSGEWTGHTGSRIRTVVNIGIGGSDLGPAMAYEALRAFTDRSLTVRFVSNVDGADLHEAVRDLDPAETLFVIASKTFTTIETITNATSARSWLLAGLDGDEKAVAKHFVALSTNAGKVSDFGIDTANMFEFWDWVGGRYSFDSAIGLSLMIAIGPERFRELLDGFRIVDEHFRTAPAEANAPLLLGLLGVWYGSFFGAQSHAVLPYSHYLSKFTAYLQQLDMESNGKSVDRDGHPVEWQTGPVVWGTPGTNGQHAYYQLLHQGTKVIPADLIGFINPVDGLSDELAAQHDLLMANLFAQGQALAFGKTGDEVRAEGVPEEQVPHRTFRGNHPTTTILAAELTPSVLGQLIALYEHKVFVQGAIWNIDSFDQWGVELGKVLAKRVEPALTEGADVPGLDPSTAALVAAYRTHRKK
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
Q82M90
|
P79875
|
TPG_RANTE
|
Temporin-G
|
Rana
|
MFTLKKSLLLLFFLGTINLSLCEEERDADEERRDDLEERDVEVEKRFFPVIGRILNGILGK
|
Amphipathic alpha-helical antimicrobial peptide with activity against Gram-positive bacteria (M.luteus), Gram-negative bacteria (E.coli), and fungi (S.cerevisiae) . Stimulates insulin release from pancreatic beta-cells in a dose-dependent manner, without increasing intracellular calcium . Does not protects BRIN-BD11 beta-cells against cytokine-induced apoptosis . In vivo, intraperitoneal injection together with a glucose load into mice improves glucose tolerance with a concomitant increase in insulin secretion .
|
P79875
|
B5FP62
|
BIOF_SALDC
|
8-amino-7-ketopelargonate synthase
|
Salmonella
|
MSWQQRVDDALTARRATDTLRRRYVVSQGAGRWLVANGRQYLNFSSNDYLGLSQHPQIIRAWQQAATRFGVGSGGSGHISGYSVAHQALEEELAQWLGYPRALLFISGFAANQAVITALMKKNDRIVADRLSHASLLEAANLSPAQLRRFIHNDTQHLSRLLQSPCVGQQLVVTEGVYSMDGDSAPLAEIQHIARRHHAWLLVDDAHGIGVTGDEGRGTCWQRGGKPELLVVTFGKGFGVSGAAVLCSESVADYLLQFARHLVYSTSMPPAQAQALSASLAVIRSDEGRERREKLAALVQRFRAGVNASRFTLLNAHSAIQPLIVGDNSRALRLAEALRQQGCWATAIRPPTVPVGTARLRLTLTQAHEACDIDRLLEVLHGAGE
|
Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
|
B5FP62
|
Q72L31
|
DCUP_THET2
|
Uroporphyrinogen decarboxylase
|
Thermus
|
MDLVNDLILRAARGEPTPRPPVWFMRQAGRYQKAYRKLRERYTLPEIVQNPEVCAEVTLLPVKALGVDAAILFADITTPLYGMGVDLSLVENKGPVIHNPVRDEKGVEALRPLVPEEAVPFVLETIRILKRELPVPLIGFAGAPFTLASYLVEGGPSRRFLRVKALMYGEEALWHRLMEKLTEAMARYLRAQAEAGADLLQVFDSWVGALSPADYRRYVKPHMERLFQSLRPAGVPVIHFGVGTMGLLEDMKEAGGDVLGLDHHTPLPWARALLGATPVQGNLDPAVLLAPKGVIRREVQRILKENGGKSGHIFNLGHGIVPETPEENVRYVVELIQEVAA
|
Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
|
Q72L31
|
C3PP47
|
RL25_RICAE
|
General stress protein CTC
|
spotted fever group
|
MSEILELEAESRTEFGTGAARALRRAGRVPAIIYGAGKTPVSISLEEKEITKYYRKPAFISQLINLTIDKKKYKVLPKAVELHPVTDIVRHVDFVFLEEKTQKMEVPVVYEGKERALGVKRGGYFNIVKRRVTLLCDVNNIPRNITIDVTNMPMATSLKSSKIELPKGCSFVTKKEFVLATIIGRRGAKTEAEGEQQAAEAGK
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
C3PP47
|
Q9S4Z0
|
METN_SALEN
|
Methionine import ATP-binding protein MetN
|
Salmonella
|
MIEIEKVCVDFTAGRGTSGAGKSTLLRTLNALTRPSQGRVNVNGVEISALDGKALRQARQRIGMIFQHFNLMHTRTVAQNVAFSLKAAGWERSKIAPRVAEILTLVGLADKANRFPVQLSGGQKQRVGIARAIANHPDVLLCDEPTSALDLETSATILALLRQINAQLGITIVLITHEMNVIKSICDRVAVMSGGKVVESGEVFDEFAHPQHAFTQQLVSHTLNLTLPERLREHLPGQLLKILFIGDSAEQPVLSEVAIKFGVAVNILHGKIEYIGERALGILVVQLTAPHNPTAVAAAVEHIRQRTAQVEVIRG
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q9S4Z0
|
Q15Q18
|
MURC_PSEA6
|
UDP-N-acetylmuramoyl-L-alanine synthetase
|
Pseudoalteromonas
|
MIAPDKVHYHVPEMRRIKNIHFVGIGGAGMGGIAEVLLNEGYQVSGSDRQANGMTDRLSGLGATIFFGHQASNVEKANVVVVSSAIDPTNPEVNAANEMRIPVIRRAEMLAELMRFRHGIAIAGTHGKTTTTSLIATIFAQAELDPTFVIGGLLNSAGTNARLGSSQYLIAEADESDASFVHLQPMVSVVTNIEPDHMETYQGDFQKMQDTYIDFLHNLPFYGLAVLCIDDPVITQLLPRIKRKYLTYGYSEVADVRATHVKHTFNQSEFTLKRKDHQDIQVVVNAPGKHNVLNALAAIAVATDENIEDAAITAALANFSGIGRRFEMLGEFATGEGDVLLVDDYGHHPTEVEATIAVARNNWPDRRLVMAYQPHRYSRTRDLYEDFVRVLSQVDVLLLLDVYSAGEEKIEGADSKSLCRSMRQRGQLEPIYVADKNELPKLLADNLKDQDILLTQGAGNIGQIAKELQEMKLDKGALRTGWSK
|
Cell wall formation.
|
Q15Q18
|
Q86BY9
|
RIG_DROME
|
Protein rigor mortis
|
Sophophora
|
MNSQVMYHNVPTPPGNVSLAAAAPDGGLLYAGIRCINYISAPPANGEQPQVVTMSTRINILALDVSPMWGLGNGGPTKPFAIVGDDLSVQVWDCALGEAVIGHKAHQHQHEARDVRVVHHTTNSVLMSYLANGNILSMDASDLVIYCVASNTYCRRSTFISPRNHQLTMVRCSPYNDNLFAVGTAMGNVLVCDLRKMNIVYKFHGHKAPICGLAWREVPAAEDEKTNNLALSAEEWRSRNGGQEEKPKTKPPPLTKSKAAESDDPFDIYNFDHLEYEFGAPIAERRRKSSEDCGGEFVGLEKPAGAAVLDFVEACESVKAELLASRQEDKTQHVEVTLHDCEPTKPTGPLSDASTISNKNDASDSTEGSLEVIQYSSSSDDAVIVDGEAAKPKREVLHHIYHQAEVHASGTPQTKSEPQSNLQVVPAISAETISLTSVNSTHLETLLVSIDGDEVMMIWNTNTGAHAGKNYSKSKTAGKLNNVYWLNNHVIVSLSRHQLFFWSVEFERKMLRYKISKDKSHSCHLQDIVSFACDSSKEMIWLCRNNRQIGMMNPKTGRMADFYGTVAFGVRAMAECPDDMNKIALGCSDRRVAFFDISKLTTSCLPIDSVYVSSNVYCLAWSPNCLELAFGTFDGTVGILDVERMKVKTHLRTPHKKEVYSLVWQDHFIYFIVNRVLGFFDLRKSKIEPTIVNCISRPSYLSIRDSFLFVGTDDGLLQIHERDSGMEKSWSPFIRQSALFARYVTDIAWCPLDSNKFAVSGNDRSVYVMEFQPTERNWKTLHTFTANTEKASITSMRWSHTQKHLLLTFHIEGKVCLWNCNAPEKPPLTITYHCPMWCGMFLPTNENIIMCSGKALSVELIDIKDALEGDEKSICPKVDALLNVKWASKSLTQPYAPVLTAAEKKRQRRDQRKAAAKLEVDVANKDQKKIQESVTAVIDNPTNDKCTQETPVEEMLEALSLDKEQNNRSAKECPKCKEQSPDSFTHSRTCLYLTQKELNKSALEKLAIVLTEDSAKIDKSVLISKLFSSKVMAKELIATELTNLKHSNTKDIAPLCLAMSTFKLREELEQHIANKTLTERHVSLAPSVSFTLWQDCCRAYAKQMEEKGYIMHAATYLFSQGMQSEAIKLFLANEYYKEALVHARICLPATDPLIKTVINNWLEHLEGTGNFAAAALICVLDNEMLRGYSYLRKYRNCTPEIADLMDQIKRIGQLGGVLDGCAPNEPIHNGSTAEH
|
Nuclear receptor cofactor for the ecdysone-regulated processes of molting and puparium formation. Acts downstream from ecdysone biosynthesis and release to control the expression of specific ecdysone-regulated genes such as Eip74EF (E74).
|
Q86BY9
|
Q9MLJ8
|
CYB_BUNFA
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Bungarus
|
MSNQHILLMSNLLPVGSNISTWWNFGSMLLTCLLLQIMTGFFLAIHYTANINLAFSSVVHILRDVPYGWIMQNIHAIGASLFFICIYIHIARGLYYGLYLNKEVWLSGTALLITLMATAFFGYVLPWGQMSFLAATVITNLLTAIPYLGNTLTIWLWGGFSINDPTLTRFFALHFILPFAIISLSSIHIILLHNEGSNNPLGTNSDIDKIPLHPYHSYKDMLMITIMITMLFITMSFTPNLLNDPENFSKANPLLTPQHIKPEWYFLFAYGILRSIPNKLGGTMALIMSVAILITVPFTHTSHTRSMLFRPLTQILFWTLISTFIIITWTATKPVESPFISISQMTSIIYFSFFIINPLLGWIENKIMMP
|
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.
|
Q9MLJ8
|
Q0V869
|
OTU11_ARATH
|
Deubiquitinating enzyme OTU11
|
Arabidopsis
|
MDENHRNPFANASTSARASGSTSASSNSSFSSSVADTDDDQTIARILAEDESLRREGKLGKRLSHLDSIPHTPRVNREIPDINDATLDHELLSGRLATYGLAELQMEGDGNCQFRALADQLFRNADYHKHVRKHVVKQLKQQRKLYEEYVPMKYRHYTRKMKKHGEWGDHVTLQAAADRFEAKICLVTSFRDQSYIEILPHNKNPLREAWLSFWSEVHYNSLYANGVLALPDVPTRKPRRKHWLF
|
Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation (Probable). Inactive cysteine protease .
|
Q0V869
|
Q986D2
|
ATPF1_RHILO
|
F-type ATPase subunit b 1
|
Mesorhizobium
|
MFVTSAFAEETAPAVTGGDTHSGTGVPAEAHGTFPPFDPATFPSQLLWLAITFGLFYLFLKKVAMPRIGGIIDVRNDRISQDLDQASKLKGEADAAVAAYEQELAEAKKNASSIGQQAADAAKAEAETARKKIEAALDEKLGEAEARISSIKANAMKEVGSIAEDTASAIVEALVGGKASKAEIAAAVKSVAR
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q986D2
|
Subsets and Splits
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