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
|
|---|---|---|---|---|---|---|
Q9UQ07
|
MOK_HUMAN
|
Renal tumor antigen 1
|
Homo
|
MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQRFESIEQVNNLREIQALRRLNPHPNILMLHEVVFDRKSGSLALICELMDMNIYELIRGRRYPLSEKKIMHYMYQLCKSLDHIHRNGIFHRDVKPENILIKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPAQKILTKFKQSRAMNFDFPFKKGSGIPLLTTNLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQEQRKTEKRALGSHRKAGFPEHPVAPEPLSNSCQISKEGRKQKQSLKQEEDRPKRRGPAYVMELPKLKLSGVVRLSSYSSPTLQSVLGSGTNGRVPVLRPLKCIPASKKTDPQKDLKPAPQQCRLPTIVRKGGR
|
Able to phosphorylate several exogenous substrates and to undergo autophosphorylation. Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner.
|
Q9UQ07
|
Q73T38
|
Y3881_MYCPA
|
Putative S-adenosyl-L-methionine-dependent methyltransferase MAP_3881
|
Mycobacterium avium complex (MAC)
|
MAATAEVGVTATLGAAARAVATRQGLLNDPYAEPLLGAVGIDYLTRAIADHTFAADESPVGDDPAVTSLLDALAAHTRFVDEFLAEAGRAGIRQVVILASGLDTRPYRLWWPRGTTVYEIDRPRVLDFKAGVLRGLDARLATNRCAVGIDLRDDWPAALRRVGFDAAQPTAWVAEQLLVGYLKPAEQNRLLRRLTAASAAGSRLAADHLPTWDPLQLEAERAFVEGWRRRGLDIDLASLTHLGEYHYVPEYLATHGWEPAARSIADLLGGLGLGPRRGAGSGGAQFIPEYVTATRV
|
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
|
Q73T38
|
P51487
|
ARRB_CALVI
|
Phosrestin I
|
Calliphora
|
MVVSVKVFKKATPNGKVTFYLGRRHFIDHFDYIDPVDGVIVVDPDYLKNRKVFAQLATIYRYGREEDEVMGVKFSKELILCREQIVPMGNSNMEMTPTQEKLVRKLGSNAHPFTFHFPPNSPSSVTLQQEGDDLGKPLGVEYTIRAYVADSEDDRQHKRSMVSLVIKKLQYAPPTRGQRLPSSLVSKGFTFSNGKISLEVTLDREIYYHGGKVAATVQINNNSKKAVKNIKVFIIQHTEITMVNAQFSKHVAQLETKEGCPITPGANLSKTFYLIPLASNNKDRHGIALDGHLKDEDVNLASSTMVQDGKSTGDACGIVISYSVRIKLNCGTLGGEIQTDVPFKLLQPAPGSVEKKRSNAMKKMKSIEQHRNTKGYYQDDDDNIVFEDFAKMRNNNADVMD
|
Directly interacts with light-activated rhodopsin thereby activating the phosphorylation of metarhodopsin. Inhibits the dephosphorylation of metarhodopsin.
|
P51487
|
P86018
|
ES1R_PELRI
|
Esculentin-1R
|
Pelophylax
|
GIFSKLAGKKLKNLLISGLKSVGKEVGMDVVRTGIDIAGCKIKGEC
|
Shows antibacterial activity against representative Gram-negative and Gram-positive bacterial species, and hemolytic activity.
|
P86018
|
Q50799
|
CBIN_METTM
|
Energy-coupling factor transporter probable substrate-capture protein CbiN
|
Methanothermobacter
|
MDKRHTIMLIAVAVIAIAPLVIYSGLGEDQGYFGGADDSASKAISETGYKPWFQPIWEPPSGEIESLLFALQAAIGALIIGYVFGYYRGRGESPE
|
Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import.
|
Q50799
|
Q9SKK4
|
GSL_ARATH
|
Probable 2-oxoacid dependent dioxygenase
|
Arabidopsis
|
MAENYDRASELKAFDEMKIGVKGLVDAGVTKVPRIFHNPHVNVANPKPTSTVVMIPTIDLGGVFESTVVRESVVAKVKDAMEKFGFFQAINHGVPLDVMEKMINGIRRFHDQDPEVRKMFYTRDKTKKLKYHSNADLYESPAASWRDTLSCVMAPDVPKAQDLPEVCGEIMLEYSKEVMKLAELMFEILSEALGLSPNHLKEMDCAKGLWMLCHCFPPCPEPNRTFGGAQHTDRSFLTILLNDNNGGLQVLYDGYWIDVPPNPEALIFNVGDFLQLISNDKFVSMEHRILANGGEEPRISVACFFVHTFTSPSSRVYGPIKELLSELNPPKYRDTTSESSNHYVARKPNGNSSLDHLRI
|
Necessary for the hydroxylation of but-3-enyl glucosinolate to 2-hydroxybut-3-enyl glucosinolate, which is toxic to insects, bacteria and nematodes, inhibits seed germination and produces bitter flavors.
|
Q9SKK4
|
P49435
|
APT1_YEAST
|
Adenine phosphoribosyltransferase 1
|
Saccharomyces
|
MSIASYAQELKLALHQYPNFPSEGILFEDFLPIFRNPGLFQKLIDAFKLHLEEAFPEVKIDYIVGLESRGFLFGPTLALALGVGFVPVRKAGKLPGECFKATYEKEYGSDLFEIQKNAIPAGSNVIIVDDIIATGGSAAAAGELVEQLEANLLEYNFVMELDFLKGRSKLNAPVFTLLNAQKEALKK
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
P49435
|
Q7MAK5
|
KGUA_WOLSU
|
GMP kinase
|
Wolinella
|
MERSKGAILVLSGPSGSGKSSLCKTLFKEIKNAYFSVSTTTRTPREGEIEGKHYHFVSKEKFLEGIEENFFLEWAEVHGNYYGTSKESVESALAQGKLVVFDIDIQGHRNIKESYPELTTSVFITTPTQQELRERLVLRGTDDKETIDLRVMHAYTEMKHIKEFDFVIVNRDLKESEKLLLSIARAALSKRILYDVESLVARWKSKETPKTPNSQ
|
Essential for recycling GMP and indirectly, cGMP.
|
Q7MAK5
|
A0A0H2VG78
|
GLCP_STAES
|
Glucose/H(+) symporter
|
Staphylococcus
|
MKANKYLIFILGALGGLLYGYDNGVISGALLFIHKDIPLNSTTEGIVVSSMLIGAIVGAGSSGPLADKLGRRRLVMLIAIVFIIGALILAASTNLALLIIGRLIIGLAVGGSMSTVPVYLSEMAPTEYRGSLGSLNQLMITIGILAAYLVNYAFADIEGWRWMLGLAVVPSVILLVGIYFMPESPRWLLENRNEEAARQVMKITYDDSEIDKELKEMKEINAISESTWTVIKSPWLGRILIVGCIFAIFQQFIGINAVIFYSSSIFAKAGLGEAASILGSVGIGTINVLVTIVAIFVVDKIDRKKLLVGGNIGMIASLLIMAILIWTIGIASSAWIIIVCLSLFIVFFGISWGPVLWVMLPELFPMRARGAATGISALVLNIGTLIVSLFFPILSDALSTEWVFLIFAFIGVLAMIFVIKFLPETRGRSLEEIEYELRERTGARTE
|
Transporter highly specific for glucose uptake.
|
A0A0H2VG78
|
Q9C9Z9
|
ELD1_ARATH
|
Protein ELONGATION DEFECTIVE 1
|
Arabidopsis
|
MKSTHHHRAPLISASSSSSSSSQNHSFVSRLLLLLTLLPVSLACLAFILQWRGGGLADPASASVRSSTSVPGGSDLNHEVFPGMETVSSVSPKSHQSSSDCSNLARSSSPSFPYYADWKFGVDTSLKPKICITTSTSAGLDQILPWMFYHKVLGVSTFFLFVEGKAATPSISKVLESIPGVKVIYRTKELEEKQAKSRIWNETWLSSFFYKPCNYELFVKQSLNMEMAIVMARDAGMDWILHLDTDELIYPAGAREYSLRRLLLDVPPNVDMVIFPNYESSVERDDIKDPFTEVSMFKKNYDHLPKDTYFGMYKEATRNNPNYFLTYGNGKSVARVQDHLRPNGAHRWHNYMKTPNEIKLEEAAVLHYTYSKFSDLTSRRDRCGCKPTKEDVKRCFMLDFDRSAFIIASTATDEEMLSWYREHVVWGDKDVKTKLLRKGILTRIYSPMVVIQALKESGVFSSVVSSASTNLSKKKFLSSIHKSNSSRSTASESLPSKESKSEGISARHLLEAESAIPPLSPPGMEQARFFTED
|
Involved in the coordination between cell elongation and cellulose synthesis by promoting the expression of genes involved in cell elongation and cellulose synthesis . Acts as a regulator of plasmodesmatal permeability . Mediates abscisic acid (ABA) and sugar responses essential for growth (e.g. seed germination, stomatal regulation and ABA-regulated gene expression) . Required for normal organogenesis by promoting cell elongation, regulating cell differentiation in vascular tissues and maintaining root meristem identity . Regulates crystalline cellulose microfibrils deposition and parallel organization during the elongation phase of the cell . Maybe a glycosyltransferase . Negative factor in light inhibition of hypocotyl elongation through modulating cellulose biosynthesis .
|
Q9C9Z9
|
A1CQZ4
|
SDS23_ASPCL
|
Protein sds23
|
Aspergillus subgen. Fumigati
|
MADQQNVEAITDHSNGSAIASPRSSTDSRSPSTRSQSLRLSHSNHQHRQSFSDSLRAAPGSPRARRQPSLTQAAIQSLIDNPPAPRDVNPAFAGRDWREITIGELVSPDDLKFVEVDTGIEEATNMLIDTNAPVLLIRETPQQKTVVGTFDYSDLNAYLLLAAGLTQPTEELRAPYEQLARKAREGHKIPLQDVKALGRNEPLTTLPASASLMAAVETFGGGVHRVIVVDERKDGEVVGIFSQFRLVKFLWENGRSFPVIDQLYPQYLRDLGIGSREVVSINGDKRLCEVLQLMNSEGISSVAVVDNHANVVGNISTTDVKLLTRSSSLPLLHNSCIHFISVILSARGLVEGKDSFPVFYVNPGSTLAHTVAKLVATKSHRLWVTDPLSPSSSGPPTPSHSSGQLPLAANPIQSPPLSPPPTSAGIPSPNYTTPHLPSPPVGIPHVVAPSIPASALPGARLSGRLVGVVSLTDILNLHARASGLRPADPAENRSRRRRSSSSSVSVRKSGDIGRELFSRRE
|
Involved in DNA replication and cell separation.
|
A1CQZ4
|
Q1C6E5
|
RLMF_YERPA
|
rRNA adenine N-6-methyltransferase
|
Yersinia
|
MLSYAPENAYQRASTMENKKVFPKEKSGLHPRNRHCSRYDFDALSVSCPELIPFLAPTAYGDISVDFADPLAVKMLNKALLKHFYGIEYWDIPADSLCPPIPGRADYVHHLADLLASCNGEVIPKGKNIALLDIGVGANCIYPIIGQREYGWRFTGTDIDSHALSAAKMVVSMNPTLKNTLRLKQQKDPHAIFEGVWAVNERYDATLCNPPFHGSAEEAAATTRRKLHKLGKNEVAAKPVQNFGGKNSELWCEGGEEGFVSRMVAESVAKAQNCFWFTSLISKKTTLPAIYHALRYVKAVEVRTIEMAQGQKVSRFVAWTFLTPEQQAAWVAERWA
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
Q1C6E5
|
Q9S597
|
C27AA_BACUH
|
Insecticidal delta-endotoxin CryXXVIIA(a)
|
Bacillus cereus group
|
MNPYQNKNEYEILDAKRNNCHMSNGYPRHPLANDPQMYLRNAHYKDWLSMCNKNNPVGLIPPESFEWTWLNGTVAALTIVSVIAGILVTAPVSVTAGLITVLGAGAALLAGITPLIWPATTDNTFNKITDATEVLLNKEISEFVRKTANTKIDSLQQLIYYYQNALENWKKNPNDSAARNTVSTRFQIVNAFFVEAMPALSMPGYEVVQLGAYAQAANLHLILLREGIAYADQWNLARDPMHAAGDLHYKEFLDYRNQYINHCSTWYNEGQNEANLKNNGLVYQRTMTLFVLDLIAMFSTYDPRLYTMPIKTEILTRTIYTDGVNRNEPKSIHNPGLFRRLEQMKLHIYEYQGAQFLSGHQNIFRSMNYNHPLIYGPVQGYSSSNINKITTINLGDYDKIYSINTESRNRLVQGSTTFDKINFYGAFNENWLFSVYNQNGPIIKHSNIPGIDAPSTGLNYSNYTHYLSNCIFQSNRNGGSAPDYNTQSYVFGWNHYTIDPTGNYVTDAFEVNKNLPESRYVPQISQVPAVKASDIFNPGRVVNAKVESGPYFTGGDVIVSKAQLDGSGLARTLITFPIIPKRYRASGFRVRMYYAANHTGQVSYGVANINTTGYANFQKTFDGWEYFRARHEHFKYIEFDTTFSLRNSGQLEEHLLHIYYPNTTKISGDQLLIIDKIEFIPVGIPLNQTSEGYNTYDQNTNSYNQNYNNYNQNMDTTYQPNYDNYKQNSSGMYDNPYNQNPKDSYNQNYTDTYDSGYNNSQNVGSNYNQEYNTYNQDTENMYNQSYNNYNSDNNNYNQNSDCMCSPGYNGNYECRCNQRANGNYPK
|
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of insects.
|
Q9S597
|
P07910
|
HNRPC_HUMAN
|
Heterogeneous nuclear ribonucleoproteins C1/C2
|
Homo
|
MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGEDGRMIAGQVLDINLAAEPKVNRGKAGVKRSAAEMYGSVTEHPSPSPLLSSSFDLDYDFQRDYYDRMYSYPARVPPPPPIARAVVPSKRQRVSGNTSRRGKSGFNSKSGQRGSSKSGKLKGDDLQAIKKELTQIKQKVDSLLENLEKIEKEQSKQAVEMKNDKSEEEQSSSSVKKDETNVKMESEGGADDSAEEGDLLDDDDNEDRGDDQLELIKDDEKEAEEGEDDRDSANGEDDS
|
Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles . Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules . Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides . May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing .
|
P07910
|
B0C1E8
|
RL18_ACAM1
|
50S ribosomal protein L18
|
Acaryochloris
|
MKTTRRDATRSRHQRVRRKVVGTAERPRLAVFRSNQHIYAQVIDDAQQHTLAAASTVESDLKSSSGATCDASTAVGKLVAERAIEKGIKAVVFDRGGNLYHGRVKALADAAREAGLEF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
B0C1E8
|
O82380
|
PP175_ARATH
|
Protein ORGANELLE TRANSCRIPT PROCESSING 81
|
Arabidopsis
|
MAIFSTAQPLSLPRHPNFSNPNQPTTNNERSRHISLIERCVSLRQLKQTHGHMIRTGTFSDPYSASKLFAMAALSSFASLEYARKVFDEIPKPNSFAWNTLIRAYASGPDPVLSIWAFLDMVSESQCYPNKYTFPFLIKAAAEVSSLSLGQSLHGMAVKSAVGSDVFVANSLIHCYFSCGDLDSACKVFTTIKEKDVVSWNSMINGFVQKGSPDKALELFKKMESEDVKASHVTMVGVLSACAKIRNLEFGRQVCSYIEENRVNVNLTLANAMLDMYTKCGSIEDAKRLFDAMEEKDNVTWTTMLDGYAISEDYEAAREVLNSMPQKDIVAWNALISAYEQNGKPNEALIVFHELQLQKNMKLNQITLVSTLSACAQVGALELGRWIHSYIKKHGIRMNFHVTSALIHMYSKCGDLEKSREVFNSVEKRDVFVWSAMIGGLAMHGCGNEAVDMFYKMQEANVKPNGVTFTNVFCACSHTGLVDEAESLFHQMESNYGIVPEEKHYACIVDVLGRSGYLEKAVKFIEAMPIPPSTSVWGALLGACKIHANLNLAEMACTRLLELEPRNDGAHVLLSNIYAKLGKWENVSELRKHMRVTGLKKEPGCSSIEIDGMIHEFLSGDNAHPMSEKVYGKLHEVMEKLKSNGYEPEISQVLQIIEEEEMKEQSLNLHSEKLAICYGLISTEAPKVIRVIKNLRVCGDCHSVAKLISQLYDREIIVRDRYRFHHFRNGQCSCNDFW
|
Involved in RNA editing event in chloroplasts. Required for the editing of a single site in rps12 transcript.
|
O82380
|
P92966
|
SRS41_ARATH
|
Serine/arginine-rich splicing factor RS41
|
Arabidopsis
|
MKPVFCGNFEYDARESDLERLFRKYGKVERVDMKAGFAFVYMEDERDAEDAIRALDRFEYGRTGRRLRVEWTKNDRGGAGRSGGSRRSSSGLRPSKTLFVINFDAQNTRTRDLERHFEPYGKIVNVRIRRNFAFIQYEAQEDATRALDATNSSKLMDKVISVEYAVKDDDSRGNGYSPERRRDRSPDRRRRSPSPYRRERGSPDYGRGASPVAHKRERTSPDYGRGRRSPSPYKRARLSPDYKRDDRRRERVASPENGAVRNRSPRKGRGESRSPPPYEKRRESRSPPPYEKRRESRSPPPYEKRRERSRSRSKSSPENGQVESPGQIMEVEAGRGYDGADSPIRESPSRSPPAEE
|
Required for constitutive and alternative pre-mRNA splicing (Probable). Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs .
|
P92966
|
P81482
|
IPSG_MARMT
|
Double-headed protease inhibitor, submandibular gland
|
Martes
|
APPPVGDQAGGRKVDCFKYNTTGSAFACTRHERPVCGTDHRTYSNECMFCMLTQNKGFGVRILQDNECDIECTQYSDMCTMEYLPLCGSDGKNYSNKCLFCNAVMGSRGALFLAKHGQCQSP
|
This inhibitor is composed of two homologous actively inhibiting halves: one which inhibits trypsin, the other which inhibits elastase.
|
P81482
|
A5CSZ4
|
IF2_CLAM3
|
Translation initiation factor IF-2
|
Clavibacter
|
MAKPRVHEIAAEIGVDSKTALAKLKEMGEFVKGPSSSIEPPVARKLKAALEAAGLTGQAAAPAAAPSSAPRPGARSSAPKPGGRPTPGPQPTAAPEVEAPEASDVPVPAKPLTVAERQAQAEASRKAAAEEKAQAEKSAASATPDAPAAETPSAPRPDAGSAPAPSNGIPRPGIPRPAAPRPGNNPFASNQGMGTKPRPGNNPFASNQGMGQRPAAGAAGPRPAAPRPGSPRPGAPRPGGVGQGARPAGFGQRPAGAGRPGGAPGGAGRPGAPAAGGFQRPAGGFAGRPGGGGRGRGPGGGTAGAFGRGGGKSKSRKSKRTKRAEFELREAPSLGGVSVPRGDGNTIVRLRRGASISDFADKIDASPGNLVTVLFHLGEMATATESLDEATFEVLGTELGYKIQVVSPEDEDRELLEGFDIDLDQELEDEDDDVLEIRPPVVTVMGHVDHGKTRLLDAIRNANVIEGEAGGITQHIGAYQVWAPHEGYERAITFIDTPGHEAFTAMRARGAQVTDIAILVVAADDGIMPQTVEALNHAQAANVPIVVAVNKVDKEGANPAKVRQQLTEYGLVAEEYGGDVMFVDVSALTGKGVEDLLEAVLLTADAGLDLRSNPNKDARGVAIEARLDKGRGAVATVLIQSGTLRVGDAIVAGTAYGRVRAMMDENGDAVHEAYPSRPVQVQGLSSVPGAGDTFLVTEEDRTARQIAEKREAVERNAQLAKARKRISLEDFTRALEEGKVESLNLIIKGDVSGAVEALEESLMKIEVDDSVQLRIIHRGVGAVTESDVNLATIDNAIIIGFNVRPDPKARARAAREGVDIRFYSVIYSALEEIESSLTGMLKPEFEEVQSGVAEIREVFRSSKFGNIAGVIVRSGTITRNAKARVIRDGVVVGDSLAIESLRRFKDDVSEVRTDFEAGIGLGKFNDIQIGDEIETIEMKEKPRV
|
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex.
|
A5CSZ4
|
Q5LG28
|
END4_BACFN
|
Endonuclease IV
|
Bacteroides
|
MKYIGAHVSASGGVEFAPVNAHEIGANAFALFTKNQRQWVSKPLTEDSIRLFKENCEKFGFAPEYILPHDSYLINLGHPEEEGLTKSRAAFLDEMQRCEQLGLKLLNFHPGSHLNKISVEECLDRIAESINLALEKTKGVTAVIENTAGQGSNLGNEFWQLKYIIDRVEDKSRVGVCLDTCHTFTAGYDFLNDYDDVFGEFGEVVGFEYLRGMHLNDSKKELGSRVDRHDSIGKGLIGFAFFEKLMKDPRFDNMPLILETIDETLWPEEIAWLREQTQ
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
Q5LG28
|
B7MMD7
|
YQGF_ECO45
|
Putative pre-16S rRNA nuclease
|
Escherichia
|
MSGTLLAFDFGTKSIGVAVGQRITGTARPLPAIKAQDGTPDWNIIERLLKEWQPDEIIVGLPLNMDGTEQPLTARARKFANRIHGRFGVEVKLHDERLSTVEARSGLFEQGGYRALNKGKVDSASAVIILESYFEQGY
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
B7MMD7
|
A9M0W6
|
DAPE_NEIM0
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Neisseria
|
MTETQSLELAKALISRPSVTPDDRDCQKLLVERLYKIGFAAEELHFGDTKNIWLRRGTKVPVVCFAGHTDVVPTGPVEKWDSPPFEPTERDGRLYGRGAADMKTSIACFVTACERFVAEHPDHQGSIALLITSDEEGDALDGTTKVVDVLKARGELIDYCIVGEPTAVDKLGDMIKNGRRGSLSGNLTVKGKQGHIAYPHLAINPVHTFAPALLELTQEVWDEGNKYFPPTSFQISNINGGTGATNVIPGELNVKFNFRFSTESTEAGLKQRVHAILDKHGVQYDLQWSCSGQPFLTQAGKLTDVARAAIAETCGIEAELSTTGGTSDGRFIKAIAKELIELGPSNATIHQINENVRLNDIPKLSAVYEGILARLLAGNAV
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
A9M0W6
|
O08467
|
GLNA_THEKO
|
Glutamine synthetase I alpha
|
Thermococcus
|
MNEIKGIERAVQVEVPRPRFLLLAFTDINGSLKGMEIPMERYEEAVEDGVSFDGSSIPGFEGIEDSDLIFKADPSTYAEIPWEGIGRVYGYIYKGDEPYQADPRGILKRVLERLEKEGLKAHIGPEPEFYIFKKNGTWELHIPDSGGYFDLVGLDKAREIRREIALYMPYLGLKPEVLHHEVGKAQHEIDFRYDEALRTADNIVSFKHVVKAVAELHGYYATFMPKPIYGFPGNGMHLHISLWKDGENVFIGEDGLSDTALHFIGGILKHAKALAALTNPTVNSYKRLVPGYEAPVYISWGYRNRSALIRVPAFKGSGARIEYRCPDPSANPYLALAGILMVGLDGIKKKVEPDSYVETNVYEMDDAERERLGIDTLPGSLGEALEELKKDKTVREALGGAYKNFIDYKEREWEEYIEYLSSRDIPIDTKKVTEWELERYFYV
|
Carries out the ATP-dependent synthesis of glutamine from ammonium nitrogen and glutamate. Exhibits both L-gamma-glutamylhydroxamate synthetase and gamma-glutamyltransferase activities when using hydroxylamine as substrate; in fact, the enzyme possesses low biosynthetic activity, suggesting that the reaction is biased towards the degradation of glutamine under ammonia-rich conditions. Might play some role in ammonia assimilation under ammonia-starvation conditions. Can also use GTP instead of ATP in the synthetase reaction, but not CTP or UTP.
|
O08467
|
Q6MLR5
|
RNC_BDEBA
|
Ribonuclease III
|
Bdellovibrio
|
MIDQGRKSLEERVGHQFKNPALLERALTHKSFANELRNTVEHNEKLEFLGDAVLDLVVGEFLYEKFPTDTEGGLSKKRASIVNEEVLSELALEMGLNKLMQLGKGEALTGGAQKPRLIASSFEAIVGALYLDGGFEVARSFIRQEFVPLADRVCGHEDFERDYKTRLQELVQKSSKETPRYEVLAEEGPPHDREFLVCVKVKEDVWAQGRGRSKKNAEQMAAKNALEMKYKETN
|
Digests double-stranded RNA. Involved in the processing of primary rRNA transcript to yield the immediate precursors to the large and small rRNAs (23S and 16S). Processes some mRNAs, and tRNAs when they are encoded in the rRNA operon. Processes pre-crRNA and tracrRNA of type II CRISPR loci if present in the organism.
|
Q6MLR5
|
Q39C92
|
GLMU_BURL3
|
Glucosamine-1-phosphate N-acetyltransferase
|
Burkholderia cepacia complex
|
MNIVILAAGTGKRMRSALPKVLHPLAGRPLLSHVIDTARTLQPSRLVVVVGHGAEQVQAAVAAPDVQFAVQAEQLGTGHAVRQALPLLDPAQPTLVLYGDVPLTRASTLQRLVDAAREGRYGILTVTLDDPTGYGRIVRDAAGFVTRIVEQKDASPEQLKIAEINTGIIVTPTAQLSMWLGALKNENAQGEYYLTDVVELAIEAGFEVVTAQPDEEWETLGVNSKAQLAELERIHQRNIAEALLVDGVTLADPARLDVRGTLRCGRDVSIDVNCVFEGNVTLADNVTIGANCVIRNASVGAGTRIDAFTHIDGAELGAHTVIGPYARLRPGAQLADEAHVGNFVEVKNAVIGHGSKANHLTYIGDADIGARVNIGAGTITCNYDGANKFRTVIEDDVFVGSDTQLVAPVRVGRGVTIAAGTTIWKDVADGLLALNEKTQTAKSGYVRPVKKKS
|
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
|
Q39C92
|
Q6BJD4
|
EDC1_DEBHA
|
Enhancer of mRNA-decapping protein 1
|
Debaryomyces
|
MMAHELPLSIHTKKSNHNVPPSKAPSAKTNKHKPSKSGSDDRGLPNGGKVDFGNKSGSQTNKKSNKKTSKHTSSNTSNNKGVTRVLPDGSKPNFGNESSHQNGGNHKKQNNEPCLPNGEKPNFGEGSKSHSKKKNNDHVLPNGEKPNFFNEKSSKKATKPKEKKPLITEDTYAGSSFHSSPAALNLPKPSFKTSPKTNDAKQHTTEPNYHVNPQVNTPPQHSVNVPPQHPVTTYPAGNGVPNIPTVPSNPTAFPPRNHYAQPGFSYYATPQGYINYQYPQVPPPPPPQGGVYPMVAPQYQQQPQQHPQQHPQPQPQPQQLPQQHRPHHLPAIAAPQQGHRISFNELLGSSKS
|
mRNA-binding protein which stimulates mRNA decapping.
|
Q6BJD4
|
A7MPG5
|
RL6_CROS8
|
50S ribosomal protein L6
|
Cronobacter
|
MSRVAKAPVVIPAGVDVKLNGQVITIKGKNGELTRTLNDAVEVKHADNALTFGPRDGYADGWAQAGTARALLNSMVIGVTEGFTKKLQLVGVGYRAAIKGNVVNLSLGFSHPVDHQLPAGITAECPSQTEIVLKGADKQLIGQVAADLRAYRRPEPYKGKGVRYADEVVRTKEAKKK
|
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.
|
A7MPG5
|
Q68XP6
|
APBC_RICTY
|
Iron-sulfur cluster carrier protein
|
typhus group
|
MANLHQQQIIDKIQNITFKDGTFLNEVISDIIIKGNNIGFSIDISGKNKLEAEEIRLKAINELNNIKDVNNITIVFTQKKTIDKKAQKPKHFVENVKKIILVASGKGGVGKSTISALIAQQLSLENYQVGIVDADIYGPSIPHIFGINEIPKTVEGRIIPILAQNIQIISIGFFVKAHSAIIYRGPMASKIIYQLLSNTRWNNLDYLIIDMPPGTGDIHLSMLENYHLDGVIVVTTPQKISEIDVIRSIDLYRKLGLPILGIIENMIYMLESDRCGHLSKKYNIPLIAKIPIIPQIANACDKSLPLTNLLTLPLEKYL
|
Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP.
|
Q68XP6
|
B4MY65
|
LIS1_DROWI
|
Lissencephaly-1 homolog
|
Sophophora
|
MVLSQRQREELNQAIADYLGTNGYADSLEAFRKEADLSTEAEKKFGGLLEKKWTSVIRLQKKVMELEAKLTEAEKEVIEGAPTKNKRTPGEWIPRPPEKYSLTGHRASITRVIFHPIFGLMVSASEDATIKIWDFETGEYERSLKGHTDSVQDVAFDAQGKLLVSCSADLSIKLWDFQQSYACVKTMHGHDHNVSSVAFVPAGDYVLSASRDRTIKMWEVATGYCVKTYTGHREWVRMVRVHIEGSLFATCSNDHTIRVWLTNSKDCKVELRDHEHTVECIAWAPEAAASAINEAAGADNKKGHHQGPFLASGSRDKTIRIWDVSVGLCLLTLNGHDNWVRGLAFHPGGKYLVSASDDKTIRVWDLRNKRCMKTLYAHQHFCTSIDFHKAHPYVISGSVDQTVKVWECR
|
Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes.
|
B4MY65
|
P0DKU3
|
PA2B1_NAJNG
|
Phospholipase A2 isozyme I
| null |
NLYQFKNMIHCTVPSRPWWHFADYGCYCGR
|
Snake venom phospholipase A2 (PLA2) that shows weak anticoagulant activity. Is more catalytically active than the strong anticoagulant protein CM-IV found in this venom. Acts by inhibiting the complex composed of tissue factor (F3) and coagulation factor VIIa (F7) (TF-VIIa complex) by only enzymatic mechanism . PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
|
P0DKU3
|
A7H443
|
DAPA_CAMJD
|
4-hydroxy-tetrahydrodipicolinate synthase
|
Campylobacter
|
MDKNIIIGAMTALITPFKNGKVDEQSYARLIKRQIENGIDAVVPAGTTGESATLTHEEHRTCIEIAVEICKGTKVKVLAGAGSNATHEAVDLAKFAKEHGADGILSVAPYYNKPTQQGLYEHYKAIAQSVDTPVLLYNVPGRTGCEISTDTIIKLFRDCENIYGVKEASGNIDKCVDLLAHEPRMMLISGEDAINYPILSNGGKGVISVTSNLLPDMISALTHFALDENYKEAKKINDELYNINKILFCESNPIPIKTAMYIAGLIESLEFRLPLCSPSKENFAKIEEVMKKYKIKGF
|
Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).
|
A7H443
|
A1WRK3
|
RSMH_VEREI
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
Verminephrobacter
|
MSSAPCHTTVLREPAVDALLARAGPAPAGTWVDATFGRGGHTRLILCRLGPQGRLVAFDKDPEAIAEAMRITDARFSIRHQGFGQLGQLPAGSLAGVLMDLGVSSPQIDSPERGFSFRFDGPLDMRMDTTRGLSAADWLATADAGQIAQVLRDYGEERFAGLIAKAIVARRQARGPLARTAELADLVAGAVKTREPGQNPATRTFQALRIFINAELEELQQALAASLLVLQPGGRLVVLSFHSLEDRIVKQFIARHSRQPFDRRVPFAAPQAMQLLALARVRPDAAEVAANPRARSAIMRVAERTQAHGAERSDMRRAERPDARRAEHGEVLPP
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A1WRK3
|
Q493V3
|
RL9_BLOPB
|
50S ribosomal protein L9
|
Candidatus Blochmannia
|
MKIILLDNIDKLGNKGSEVVVRSGYARNFLIPKSKAMLATKKNIEIFKAQQLELQSKAIEAQTQAEFCAKTINRLGSITIKAKSGVEGKLFGSIGSRDIATAITAASGFNISKSQIRLPNHDVLRTIGTYSINIHIYNDIFSKINVIILDEIV
|
Binds to the 23S rRNA.
|
Q493V3
|
Q67NP4
|
SURE_SYMTH
|
Nucleoside 5'-monophosphate phosphohydrolase
|
Symbiobacterium
|
MALVLLTNDDGIFAPGINALRARMEQIPGLEVWAVAPDRERSASGHAITTYRPLFPVRVEIPGAVAPCISVTGTPADSAKLAIEAILPRRPDLVISGINRGANLGTDIFYSGTVAAALEGPILGIPALAVSLDSMTSSDYSAAADFAAQLALKVLEEGLPEGTLLNVNVPALPREAIKGVRVTKVGRRIYRDQWVRRMHPRGQEYYWLAGELAEIHNDRESDVSAVEAGYISVTPVHLDLTRYDQMDRLRQWNLTF
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
Q67NP4
|
Q4QNL2
|
EFP_HAEI8
|
Elongation factor P
|
Haemophilus
|
MATYTTSDFKPGLKFMQDGEPCVIVENEFVKPGKGQAFTRTRIRKLISGKVLDVNFKSGTSVEAADVMDLNLTYSYKDDAFWYFMHPETFEQYSADAKAVGDAEKWLLDQADCIVTLWNGAPITVTPPNFVELEIVDTDPGLKGDTAGTGGKPATLSTGAVVKVPLFVQIGEVIRVDTRSGEYVSRVK
|
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.
|
Q4QNL2
|
Q57GZ7
|
MALK_SALCH
|
Maltose/maltodextrin import ATP-binding protein MalK
|
Salmonella
|
MASVQLRNVTKAWGDVVVSKDINLDIHDGEFVVFVGPSGCGKSTLLRMIAGLETITSGDLFIGETRMNDIPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVMNQRVNQVAEVLQLAHLLERKPKALSGGQRQRVAIGRTLVAEPRVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMNFLPVKVTATAIEQVQVELPNRQQIWLPVESRGVQVGANMSLGIRPEHLLPSDIADVTLEGEVQVVEQLGHETQIHIQIPAIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGSACRRLHQEPGV
|
Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system.
|
Q57GZ7
|
B8ZM89
|
RIMP_STRPJ
|
Ribosome maturation factor RimP
|
Streptococcus
|
MDAIATIVELVREVVEPVIEAPFELVDIEYGKIGSDMILSIFVDKPEGITLNDTADLTEIISPVLDTIKPDPFPEQYFLEITSPGLERPLKTKDAVAGAVGKYIHVGLYQAIDKQKVFEGTLLAFEEDELTMEYMDKTRKKTVQIPYSLVSKARLAVKL
|
Required for maturation of 30S ribosomal subunits.
|
B8ZM89
|
Q2V452
|
CIPK3_ARATH
|
SOS2-like protein kinase PKS12
|
Arabidopsis
|
MNRRQQVKRRVGKYEVGRTIGEGTFAKVKFARNSETGEPVALKILDKEKVLKHKMAEQIRREIATMKLIKHPNVVQLYEVMASKTKIFIILEYVTGGELFDKIVNDGRMKEDEARRYFQQLIHAVDYCHSRGVYHRDLKPENLLLDSYGNLKISDFGLSALSQQVRDDGLLHTSCGTPNYVAPEVLNDRGYDGATADMWSCGVVLYVLLAGYLPFDDSNLMNLYKKISSGEFNCPPWLSLGAMKLITRILDPNPMTRVTPQEVFEDEWFKKDYKPPVFEERDDSNMDDIDAVFKDSEEHLVTEKREEQPAAINAFEIISMSRGLNLENLFDPEQEFKRETRITLRGGANEIIEKIEEAAKPLGFDVQKKNYKMRLENVKAGRKGNLNVATEIFQVAPSLHMVQVSKSKGDTLEFHKFYKKLSNSLEQVVWTNNEVKKETAK
|
Involved in the resistance to some abiotic stresses (e.g. high salt, hyperosmotic stress) in young seedlings, by regulating the expression of several stress-inducible genes (cold- and salt-induced genes but not drought-responsive genes). Required for the ABA response during germination. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. The CBL9/CIPK3 complex acts in the regulation of abscisic acid response in seed germination.
|
Q2V452
|
Q2NVB3
|
RDGC_SODGM
|
Recombination-associated protein RdgC
|
Sodalis
|
MLWFKNVMIYRLNRPIELSVEQIEQQLSAFAFTPCGSQDMAKSGWVPPMGAKSDALTHSIPGHVLLCLRKEEKILPSSVVKQELEGKISKLENDQSRKLRKTDKDALKDELLHQLMPRAFSRFGQTLLWLDLANDLVLVDAGSARKAEDCLAMLRKSIGSLPVVPLTMEKPIEMTLTEWVRSGEPAAGFAIQDEAELKVLLEEGGILRCKKQDLSSDEIAVHIEAGKLVTKLALDWRERVQFLLGDDGTVKRLKFSDTLREQNDDIDREDFAARFDADFLLMTGELTGLIAELIAGLGGEAPRQG
|
May be involved in recombination.
|
Q2NVB3
|
Q9ULR3
|
PPM1H_HUMAN
|
Protein phosphatase 1H
|
Homo
|
MLTRVKSAVANFMGGIMAGSSGSEHGGGSCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGAVTSTPNRNSSKRRSSLPNGEGLQLKENSESEGVSCHYWSLFDGHAGSGAAVVASRLLQHHITEQLQDIVDILKNSAVLPPTCLGEEPENTPANSRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSSYNISGGCTALIVICLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDEDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRIYDLSKYDHGSDDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS
|
Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.
|
Q9ULR3
|
Q9PT08
|
SUMO1_ONCMY
|
Small ubiquitin-related modifier 1
|
Oncorhynchus
|
MSDTDTKPSGQDGGDQKDGEYIKLKVIGQDNSEIHFKVKMTTHLKKLKESYSQRQGVHMSTLRFLFEGQRISDNHTPKELGMEDEDVIEVYQEQTGGLRNN
|
Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex sae1-sae2 and linkage to the E2 enzyme ube2i. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric sumo1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.
|
Q9PT08
|
P08877
|
PTHP_BACSU
|
Histidine-containing protein
|
Bacillus
|
MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAEITISASGADENDALNALEETMKSEGLGE
|
P-Ser-HPr interacts with the catabolite control protein A (CcpA), forming a complex that binds to DNA at the catabolite response elements cre, operator sites preceding a large number of catabolite-regulated genes. Thus, P-Ser-HPr is a corepressor in carbon catabolite repression (CCR), a mechanism that allows bacteria to coordinate and optimize the utilization of available carbon sources. P-Ser-HPr also plays a role in inducer exclusion, in which it probably interacts with several non-PTS permeases and inhibits their transport activity.
|
P08877
|
Q68W91
|
RS14_RICTY
|
30S ribosomal protein S14
|
typhus group
|
MAKVSAIQKNKSRQKKSQRLHNKRSALKSKIYDKSLSLEQRFSLIIALAQLPRNSSSTRIRNRCELTGRPRGVTRKFGISRNKLRELIGRGLVPGVVKASW
|
Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site.
|
Q68W91
|
A7I5F0
|
KDPA_METB6
|
Potassium-translocating ATPase A chain
|
Methanoregula
|
MSVNDWAFLVLIGVILALLLIPTGEFMFRVYTGKKTFLSPLFVPVEAWILKACGAGSDEEMDWKSFAVAMMIFSVIGIVFVFILQEVQQFLPLNPLGATAVPWDLSLNTAVSFATNTNWQFYVPETTVSYLTQMIGLTVQNFMSAAVGMVVLVAFIYGFSRRSSHTIGNFWVLLLRSIWILLPLSFVIALVLVSQGAPQTLSGPVTVPLLNATNDSGGNIITTQLISLGPAASQIAVKMLGTNGGGFFNANSAHPFENPTWFTDLVEIVAILLIPVSLCFMFGKMIGSVKKGIAILIAMMILFVPLLGLGIWSEIGGNPAFTPLGISQAPSHLQSGGNMEGKEVRFGPVQSAAFSVITTVTSCGAVNSMHDSFMPLGGLVQIFDIQLGEIVFGGVGSGLYCMLVFVIIAMFIAGLMVGRTPELYGKKIEPYEMKLSTIHILIPIFLILIGTAIAVSITAGTSMTANPGPHGFSEILYAFSSVSQNNGSAFAGLSSDTFYNLTTAFCMFVGRYAIAIITLALAGAFVAKKIVPPGEGTLQDHRPLFIIWVVFTILIIGALSFLPALSLGPVVEFLIQMGRGVIHV
|
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit binds the extracellular potassium ions and delivers the ions to the membrane domain of KdpB through an intramembrane tunnel.
|
A7I5F0
|
P56452
|
SYA_HELPY
|
Alanyl-tRNA synthetase
|
Helicobacter
|
MDIRNEFLQFFQNKGHAVYPSMPLVPNDATLLFTNAGMVQFKDIFTGIVPRPSIPRAASSQLCMRAGGKHNDLENVGYTARHHTLFEMLGNFSFGDYFKEEAILFAWEFVTKNLGFKPKDLYISVHEKDDEAVKLWEKFVPVDRIKKMGDKDNFWQMGDSGPCGPCSEIYIDQGEKHFKGSEDYFGGEGDRFLEIWNLVFMQYERSNDGVLSPLPKPSIDTGMGLERVQALLEHKLNNFDSSLFAPLMEEISELTSLDYASEFQPSFRVVADHARAVAFLLAQGVHFNKEGRGYVLRRILRRALRHGYLMGLKEAFLYKVVGVVCEQFANTHAYLKESKEMVVKECFEEEEHFLETLESGMELFNLSLKHLNENKIFDGKIAFKLYDTFGFPLDLTNDMLRSHGACADMQGFELCMQEQVKRSKASWKGKQNNADFSAILNAYAPNVFVGYETTECSAKVLGFFDSDFKEITDANPNQEVWVLLEKTPFYAEGGGAIGDRGALFKDNGEVAIVLDTKNFFGLNFSLLEIKKALKKGDQVIAQVSDERFEIAKHHSATHLLQSALREVLGSHVSQAGSLVESKRLRFDFSHAKALNDEELEKVEDLVNAQIFKHLNSQVEHMPLNQAKDKGALALFSEKYAENVRVVSFKEASIELCGGIHVENTGLIGGFRIVKESGVSSGVRRIEAVCGKAFYQLAKEENKELKNAKTLLKNNDVIAGINKLKESVKNSQKAPVSMDLPVEKIHGVNLVVGVVEQGDIKEMIDRLKSKHERLLAMVFKKENERITLACGVKNAPIKANVWANEVAQILGGKGGGRGDFASAGGKDIENLQAALNLAKNTALKALEG
|
Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
|
P56452
|
B7H6P9
|
MRAY_BACC4
|
UDP-MurNAc-pentapeptide phosphotransferase
|
Bacillus cereus group
|
MLEQGLLVTAGVAFLISVALSPLFIPFLRKLKFGQSIRDEGPKSHQKKSGTPTMGGIVIYVSMMVTSLIMAIKFNYLGAEVSLLLLVTFGYGLIGFLDDYIKVVKKRNLGLTSKQKLVGQLVIAIAFFLIGKGQAFHTYIMIPGTDVKFELGWAYFVLVLFMLIGGSNAVNLTDGLDGLLSGTAAIAFGAFSIIAVAQEQFGVAIFCMAVVGAVLGFLVFNANPAKVFMGDTGSLALGGAIAAVAILLKQELLLVIIGGVFVMETLSVIIQVISFKTTGKRVFKMSPLHHHYELCGWSEWRVVVTFWSAGFLLAVLGIYIGVWM
|
Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
|
B7H6P9
|
Q7NLJ1
|
YQGF_GLOVI
|
Putative pre-16S rRNA nuclease
|
Gloeobacter
|
MRVVSVLGLDVGSKRIGVAGCDPTGLIASGLETIVRCNLGADLDAIRHWIERRRAQAVVIGLPRNMNGSLGPQAHRIQHFGQQLARVIDVPIDYVDERLSTVQAGRALQSVSATRRKALIDQQAAAIILQQWLDIRRCQHRPTQESLDERHIDTER
|
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
|
Q7NLJ1
|
C4K7A7
|
RL24_HAMD5
|
50S ribosomal protein L24
|
Candidatus Hamiltonella
|
MAMKIRCNDQIIVLTGKDKGKRTKIKKILKNGKVILEGVNLVKKHQKPVPAQNQPGGIIEKEAPIDFSNVAIFNEDTGKADRIGFKYENGKKVRFFKSSGKAIAKINKS
|
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
|
C4K7A7
|
Q6F0I3
|
RF1_MESFL
|
Peptide chain release factor 1
|
Mesoplasma
|
MNPKTYEALETMQKRVDQIDKDLQSEEIVSDVKKMLELNKERANLIEVVEKFIEYKTIIQSIADAKEILGNEKDAEMIELAKMELSENEDAVEPIVAIIEELLLPKDPNDDKNVIVEIRGAAGGDEANIFAGDLLRMYKLYAETQNWKITMLDANSSEAGGFSQVSFMVKGDRVYSKLKFESGAHRVQRVPKTEAKGRIQTSTATVAVLPEMSDVEIEIKNSDLRIDTYRSSGAGGQHVNTTDSAVRITHIPTGVVAASQDGRSQHDNKDIAMTMLRARIYEAELEKQQAEADATRKNAVGTGARSEKIRTYNYPQNRVTDHRVGLTLNKLDQVMEGKIDDFIIALVNDEQRQKVEAQLQDNE
|
Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
|
Q6F0I3
|
B3H1D9
|
PCKA_ACTP7
|
Phosphoenolpyruvate carboxykinase (ATP)
|
Actinobacillus
|
MLSRIEQELAQLGITNVKEIVRNPSYEQLFEEEMKPELEGFEKGRLTTSGAVAVDTGIFTGRSPKDKYIVYDETSKDNVWWTSDAVKNDNKPMNQATWQSLKELVTHQLSNKRLFVVDAFCGANKDSRVAVRIVTEVAWQAHFVKNMFVRPSEEELLNFVPDFVVMNGSKVTNPNWKEQGLNSENFVAFNLTEKIQLIGGTWYGGEMKKGLFSLMNYWLPLKGIASMHCSANVGAKGDVAVFFGLSGTGKTTLSTDPKRKLIGDDEHGWDDDGVFNYEGGCYAKTINLSEENEPDIYRAIRRDALLENVVVREDGSVDFADGSKTENTRVSYPIHHIDNIVEPVSKAGHAKKVIFLTADAFGVLPPVSKLTPEQTKYYFLSGFTAKLAGTERGITEPTPTFSACFGAAFLSLHPTKYAEVLVKRMEEAGSQAYLVNTGWNGSGKRISIKDTRGIIDAILDGSIEKAETKELPIFNLAIPTALPNVDPAILDPRDTYADKAQWQTKAEDLAGRFVKNFEKYTTNDEGKALVAAGPKL
|
Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA.
|
B3H1D9
|
Q39Z75
|
ARGB_GEOMG
|
NAG kinase
|
Geobacter
|
MQHLIEKANTLMEALPYIRRFSGKTIVIKYGGHAMSDEALKKSFALDVILLKSLGINTVVVHGGGPQINETLKRYGIVSEFVRGMRVTDAATMQVVEMVLTGQVNKEVVGYLNQHGGRAVGLSGKDGSLLLCRKLLQEVKQGDGSLEKVDIGFVGDVVKVNQELIQTLEHGKFIPVIAPVGVGEDGESYNVNADLVAGRVAGALKAEKLILLTDVEGVKDKAGELIPGIVLDDVPRLIDGGVITGGMIPKVTCCVDAIEEGVKKASIIDGRVLHAVLLEIFTDVGVGTEIRR
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q39Z75
|
P0CF51
|
TRGC1_HUMAN
|
T cell receptor gamma constant 1
|
Homo
|
DKQLDADVSPKPTIFLPSIAETKLQKAGTYLCLLEKFFPDVIKIHWQEKKSNTILGSQEGNTMKTNDTYMKFSWLTVPEKSLDKEHRCIVRHENNKNGVDQEIIFPPIKTDVITMDPKDNCSKDANDTLLLQLTNTSAYYMYLLLLLKSVVYFAIITCCLLRRTAFCCNGEKS
|
Constant region of T cell receptor (TR) gamma chain that participates in the antigen recognition . Gamma-delta TRs recognize a variety of self and foreign non-peptide antigens frequently expressed at the epithelial boundaries between the host and external environment, including endogenous lipids presented by MH-like protein CD1D and phosphoantigens presented by butyrophilin-like molecule BTN3A1. Upon antigen recognition induces rapid, innate-like immune responses involved in pathogen clearance and tissue repair . Binding of gamma-delta TR complex to antigen triggers phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the CD3 chains by the LCK and FYN kinases, allowing the recruitment, phosphorylation, and activation of ZAP70 that facilitates phosphorylation of the scaffolding proteins LCP2 and LAT. This lead to the formation of a supramolecular signalosome that recruits the phospholipase PLCG1, resulting in calcium mobilization and ERK activation, ultimately leading to T cell expansion and differentiation into effector cells . Gamma-delta TRs are produced through somatic rearrangement of a limited repertoire of variable (V), diversity (D), and joining (J) genes. The potential diversity of gamma-delta TRs is conferred by the unique ability to rearrange (D) genes in tandem and to utilize all three reading frames. The combinatorial diversity is considerably increased by the sequence exonuclease trimming and random nucleotide (N) region additions which occur during the V-(D)-J rearrangements .
|
P0CF51
|
A0A2H5AIX5
|
4CL1_NARPS
|
4-coumarate-CoA ligase 1
|
Narcissus
|
MGSIPSEKETIFRSKLPDIYVPDHLPLHSYCFQNLHQFSDRPCLIDGFTNKTLTYAEVELASKRVGAGLHRLGLRQGHVVMLLLPNSIEFVLSFIGASLLGAMSTTANPFYTSAEIHKQAAAAGAKIIVTESCHVSKLQGLEGISRIVVIDDAVRVPENVMHFSELESTDEAELPRIDVHPDDVVALPYSSGTTGLPKGVMLTHNGLVTSVAQQVDGENPNLHFSEDDVLLCVLPLFHIYSLNSVLLCGLRAGAAIVLMRKFEIVRLMELVEKYRVTIAPFVPPIVVEMVKNEAVDRYDLSSIRVVMSGAAPMGKELENKLREKLPNAKLGQGYGMTEAGPVLSMCLAFAKEPFEVKSGSCGTVVRNAELKIIDPETGFSLSRNQPGEICIRGNQIMKGYLNNPEATKQTIDEEGWLHTGDIGFVDDDDEIFIVDRLKELIKYKGFQVAPAELEAMLITHPNMADAAVVSIKDDSCGELPVAFIVRSNGSEITEDEIKKYISKQVVFYKRIHRVFFIEAIPKAPSGKILRKELRARLAAECPNGRQL
|
Produces CoA thioesters of a variety of hydroxy- and methoxy-substituted cinnamic acids, which are used to synthesize several phenylpropanoid-derived compounds, including anthocyanins, flavonoids, isoflavonoids, coumarins, lignin, suberin and wall-bound phenolics.
|
A0A2H5AIX5
|
A5VWX3
|
HEM3_PSEP1
|
Pre-uroporphyrinogen synthase
|
Pseudomonas
|
MSTREIRIATRKSALALWQAEYVKARLEQAHTGLQVTLVPMVSRGDKLLDAPLAKIGGKGLFVKELETALLDNEADIAVHSMKDVPMDFPEGLGLYCICEREDPRDAFVSNTFDSLETLPAGSIVGTSSLRRQAQLLARRPDLQIRFLRGNVNTRLAKLDAGEYDAIILAAAGLIRLGFEDRITSTISVDDSLPAGGQGAVGIECRSADVEIHALLAPLHHVDTADRVIAERALNKRLNGGCQVPIACYAVLEGDQLWLRGLVGQPSGGTLLVADARAPRAAAEALGVQVAEDLLGQGAEAILKEVYGEAGHP
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
A5VWX3
|
B8DA62
|
HIS6_LISMH
|
ImGP synthase subunit HisF
|
Listeria
|
MLTKRIIPCLDVTAGRVVKGVNFVSLTDVGDPVEIAKAYNEAGADELVFLDITATVELRQTMIDVVERTAEQVFIPLTVGGGISSVSDMKELLQAGADKISLNSAAIKRPDLIQEGADKFGNQCIVVAIDAKWNGTNWSVFTRGGRNDTGLDAITWAKKAVQLGAGEILLTSMDGDGTKNGYDIPLTKAISEAVSVPVIASGGCGNAAHMAEVFEKQTQPPHSPQVFFTTAN
|
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.
|
B8DA62
|
P06710
|
DPO3X_ECOLI
|
DNA polymerase III subunit gamma
|
Escherichia
|
MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPAALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFHPRMPLPEPEVPRQSFAPVAPTAVMTPTQVPPQPQSAPQQAPTVPLPETTSQVLAARQQLQRVQGATKAKKSEPAAATRARPVNNAALERLASVTDRVQARPVPSALEKAPAKKEAYRWKATTPVMQQKEVVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAQVSQLSLPKLVEQVALNAWKEESDNAVCLHLRSSQRHLNNRGAQQKLAEALSMLKGSTVELTIVEDDNPAVRTPLEWRQAIYEEKLAQARESIIADNNIQTLRRFFDAELDEESIRPI
|
Interacts with the delta and delta' subunits to transfer the beta subunit on the DNA . Interacts with ATP, drives ATP-induced conformational changes in the gamma complex that opens the beta sliding clamp ring. After loading of primed DNA ATP is hydrolyzed and the beta sliding clamp ring closes .
|
P06710
|
B8D966
|
CLSA_BUCA5
|
Cardiolipin synthase A
|
Buchnera
|
MDIFYNLIKCLIFSTYWLLIANITFRVLIKRRNIPYSMSWLLTIYIIPFIGISIWFFFGELYLGKRQKKIANRIWSISNKWLHELKSCTYIFQIKNSEVATSIFQLCKNRQGLHGIKSKKIKLLTNTKKIMQILIRDIYLARKNIEMVFYIWKPGGMADDVAIALIDSAKRGIHCRLMLDSAGSIEFFQSPWVEIMRKSGIQVVEALKVNLLRVFLRRVDVRQHRKIILIDNYIAYSGSMNLVDPYLFKKSSGIGQWIDLMTRIEGPIATTMGIIYSCDWEIETGLKILPQLPNKKMLENQSNKNASIQVIASGPGFLKNMIHQALLTAIYSAKRELIITTPYLVPSEDLLEAICTAAQRGVEVSIIIPLYHDSILVKWASRVFFSELLEAGVKIFQFQKGLLHSKSILVDQQLSLIGTVNLDMRSLWLNFEITLVIDDSDFGRNLFCIQNKYISDSQLIDKKAWSMRAYWKRILEKIFYFLSPLL
|
Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
|
B8D966
|
Q88BD3
|
DUT_PSESM
|
dUTP pyrophosphatase
|
Pseudomonas
|
MHALQAKILDPRIGNEFPLPAYATVGSAGLDLRAMLKEDTLLEPGQTLLIPTGLSIYIGDPGLAALILPRSGLGHKHGIVLGNLVGLIDSDYQGELMVSCWNRGQTAFTIAVGERIAQLVLVPVVQARFELVEEFDESQRGTGGFGHSGSH
|
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.
|
Q88BD3
|
P0ADY0
|
RSMD_ECOL6
|
rRNA (guanine-N(2)-)-methyltransferase
|
Escherichia
|
MKKPNHSGSGQIRIIGGQWRGRKLPVPDSPGLRPTTDRVRETLFNWLAPVIVDAQCLDCFAGSGALGLEALSRYAAGATLIEMDRAVSQQLIKNLATLKAGNARVVNSNAMSFLAQKGTPHNIVFVDPPFRRGLLEETINLLEDNGWLADEALIYVESEVENGLPTVPANWSLHREKVAGQVAYRLYQREAQGESDAD
|
Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle.
|
P0ADY0
|
B6Q4Z5
|
SCONB_TALMQ
|
Sulfur metabolite repression control protein B
|
Talaromyces sect. Talaromyces
|
MHNENSVLRDAKESLFNPTPRKQGLPEDNTMTPYNGVRSIFDNSSDSHQLTDDHTHQERAISKAKLANENIAPFLAKHIPSQYAPLGTGISKSAGPPPRPDLKCRRQADEPSMDHLQWELQSLPQSDQQGIAHVWSLFSAAPAKQRELMLRGILAQCCFPQLSLISSSVRDLIRIDFITALPPEISFKILSYLDTASLCRAAQVSRGWKCLADDDVVWHRMCEQHIHRKCTKCGWGLPLLERKRLRASKEQIEKRALGVSVIPEASVTVQSVDATSGVKRTAEDLEASDSQTVKRQRLPIEEDTNIYKTNFRPWKDVYKDRFKVGTNWKYGRCSVKVFKGHTNGVMCLQFEDNILATGSYDTTIKIWDMETGEELRTLTGHTSGIRCLQFDETKLISGSIDRTLKVWNWRTGECISTYTGHLGGIIGLHFQNSILASGSTDKTVKIWNFEDKSTFLLRGHSDWVNAVRVDSCSRTVLSASDDCTVKLWDLDSKQCIRTFQGHVGQVQQVIPLPREFEFEEGHDASHEEDSNASVSGDESPSSQVSCSPTAAFFEGDRPAPPRYILTSALDSTIRLWETYTGRCLRTFFGHLEGVWALSADTLRIVSGAEDRMVKIWDPRTGKCERTFTGHSGPVTCVGLGDSCFVTGSEDCEVRIYSFKN
|
Component of the SCF(sconB) E3 ubiquitin ligase complex involved in the regulation of sulfur metabolite repression, probably by mediating the inactivation or degradation of the metR transcription factor.
|
B6Q4Z5
|
A6SXA4
|
RNH_JANMA
|
Ribonuclease H
|
Janthinobacterium
|
MDKIDIYSDGACKGNPGRGGWGALLVMGEREKEIFGGELDTTNNRMELKAVIEALNLLTRPCEVVVHTDSQYVQKGISEWIHGWKARGWKTAAKAPVKNVDLWQALDAAQARHKIEWRWVRGHNGHAGNERADALANRGVEVAA
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
A6SXA4
|
A5V626
|
PTH_RHIWR
|
Peptidyl-tRNA hydrolase
|
Rhizorhabdus
|
MQIWVGLGNPGAQYAMHRHNVGFMAVDTIAEVHRFDPWKKQFQGWSATGRIGNVKVLLLKPATFMNESGRSVGEAMRFFKRETGDVTVFHDELDLAPFKVKVKTGGGTAGHNGLRSTEAHIGNAFRRVRIGIGHPGHKDRVTGYVLGNYVKAELDPLAGMLGAIASEADWLASGDDARFMSEIALRLAD
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
A5V626
|
Q4JXL9
|
PANC_CORJK
|
Pantoate-activating enzyme
|
Corynebacterium
|
MTFTPGQAEVFTEIEKIGQLTRAMRKAGRPVALVPTMGALHEGHLSLVQAAQQIPGALVVVSIFVNPLQFAEGEDLDAYPRTLDEDVAKLKAAGVDAVFAPSPREMYPNGPRTTIHPGEAGRILEGAHRPTHFAGVLTVVNKLFTITHCDHAFFGEKDYQQLLLIQQIVTDLNMEVQVHGVPIVREADGLAKSSRNVYLSDEERELALTLSAALTAGAFVAEQGPAAVLQTAGSILDAASGIDVDYLELRGTDLSDTPEDGEARLLVAARVGTTRLIDNVGVPLGTGFKGLDDGGEGSAPADNAGE
|
Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
|
Q4JXL9
|
Q1LI37
|
RL3_CUPMC
|
50S ribosomal protein L3
|
Cupriavidus
|
MSLGLVGRKVGMTRIFTDDGDSIPVTVVEVGDNRVTQIKTDETDGYTAVQVTFGSRRASRVTKPLAGHLAKAGVEAGEVIKEFRIDAAKAAELQAGSSLSVDLFQVGQKIDVQGVSIGKGYAGTIKRHHFASGRATHGNSRSHNVPGSIGMAQDPGRVFPGKRMTGHLGDATRTVQNLEIAKIDAERKLLLVKGAIPGSKGGKVIVTPAVKAKA
|
One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
|
Q1LI37
|
Q5GTA4
|
DXR_WOLTR
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
unclassified Wolbachia
|
MKKISVLGSTGSIGKKTVDLLLKRKEEYQVEALSTCSNFALLACQAKLLNARYVAISNKRFYKDLKESLLGTGIKVEVGTEGLMNVASLPVDLSVVAVVGIAGLEPVMHVIESGTKVIALANKESIVCGGKLLLKKTEEKNVQIVPIDSEHNAIFQVLQNGNKCVEKIILTASGGSFLNYSLEQLRNVTVGQALSHPTWNMGKKISVDSATMMNKALEIIEAHNLFNISPNRIEAIVHPESIIHGIVIYKDGFNFAVLAEADMAIPISYALSWPERSALSYKLDLTKQKLTFQEPDHKRFPALKLSMEVLNSSSPHTNSIVLNAANEVAVDKFLKSRIDFLEIIKVVKLTVENFDSYTDINSLSDIINIDLESRAIAKEIIKNKVLAYS
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q5GTA4
|
Q4ZMP8
|
RS19_PSEU2
|
30S ribosomal protein S19
|
Pseudomonas syringae
|
MPRSLKKGPFIDLHLLKKIEVAAEKNDRKPVKTWSRRSMILPQMVGLTIAVHNGRQHVPVLVNEDMVGHKLGEFAGTRTYRGHVADKKAKR
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q4ZMP8
|
Q0A7K7
|
ISPF_ALKEH
|
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
|
Alkalilimnicola
|
MIRVGQGFDAHRFGEPGTPLILGGVQVPHERGLAAHSDGDVLMHAVTDGLLGAAGEGDLGTHFPDSDDAYKGIDSRILLRDALQRVRAGGWRVVNVDATLIAQAPRMNPHVGAMRDHLAADLEVAPSAVNVKATTTERMGFPGRGEGIAAMAVVLIARDGFFEH
|
Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP).
|
Q0A7K7
|
B3PZ93
|
FPG_RHIE6
|
DNA-(apurinic or apyrimidinic site) lyase MutM
|
Rhizobium
|
MPELPEVETVKRGLAPAMEGARVARLELRRQDLRFPFPEALADRVSGRTIVGLGRRAKYLLVDLDDGNTLVSHLGMSGSFRIEEGAASAMPGEFHHARTKDEKHDHVVFHLEGQGGPRRVVYNDPRRFGFMDMVRRADLAAHPFFRDLGPEPTGNDLGAAYLAERFRDKAQPLKSALLDQKNIAGLGNIYVCEALWRSHLSPIRAAGTLVTPGGKPKEKLGLLVASIRDVIADAIAAGGSSLRDHIQTDGSLGYFQHSFSVYDREGQACGTPGCGGTVARIVQAGRSTFYCAACQK
|
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.
|
B3PZ93
|
P05657
|
RL27_BACSU
|
BL30
|
Bacillus
|
MLRLDLQFFASKKGVGSTKNGRDSEAKRLGAKRADGQFVTGGSILYRQRGTKIYPGENVGRGGDDTLFAKIDGTVKFERFGRDRKKVSVYPVAQ
|
Plays a role in sporulation at high temperatures.
|
P05657
|
Q726D3
|
MURA_DESVH
|
UDP-N-acetylglucosamine enolpyruvyl transferase
|
Desulfovibrio
|
MDKLVIEGGVPLTGTINVSGSKNAALPILMASILAEEPVTYTNVPRLRDIHTTNKLLSILGCPAEFEGDTVSVRPCDLKPEAPYDLVKTMRASVLCLGPLLARLGEARVALPGGCAIGARPVDLHLTALEKMGARFELEEGYIIGRCRKLKGAHIYFDFPTVGGTENLLMAATLAEGETILENAAREPEVVDLARFLIACGAKIEGHGTSVIRVQGVPRLHGCEYAIMPDRIEAGTFLVAAGITGGELLLTGCPWEELDAVIVKLNAMGMHIEKTSEGVLAKRRNGGLRGTDVTTQPFPGFPTDMQAQVMSLMCLAEGTSVVQENIFENRFMHVLELVRMGADIRISGRSAVVRGVKRLTGAPVMASDLRASASLVLAGLAARGTTHVQRIYHLDRGYERIELKLNAVGARIRREAE
|
Cell wall formation. Adds enolpyruvyl to UDP-N-acetylglucosamine.
|
Q726D3
|
Q6IM82
|
DVL19_ARATH
|
Small polypeptide ROTUNDIFOLIA LIKE 10
|
Arabidopsis
|
MAGLKRKFNKGHAFTSKCVSLVKEQRARLYILRRCATMLCCWYIHGDE
|
Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
|
Q6IM82
|
Q3AUM0
|
GCSP_SYNS9
|
Glycine dehydrogenase (aminomethyl-transferring)
|
unclassified Synechococcus
|
MTSPFLQRHLGPSETEQHQMLQTLGYQHLDDFIKDVVPDDILDAAPPRNVLPAGCGEAEALADLGTIAAKNLVQRSLIGLGYHGTATPALIQRHVFENPAWYTAYTPYQAEIAQGRLEALLNFQTLISELTGLPIANASLLDEATAAAEAMGLSFGVCRRPEANRFLVDCHVLPQTWAVLQTRAEPLGIELERVDPEQMAFDTRVFGVLLQLPGADGLLWDPTTLIERAHDAGALVTVAIDPLAQTLFAPVADFGADIAVGSAQRFGVPMGFGGPHAAFFATREAYKRQIPGRLVGESKDAEGNPALRLALQTREQHIRRDKATSNICTAQVLLAVIASFYAVHHGPDGLRAIAERLVGLRLQFEAGLRTLDVAVEEADRFDTVTVTTTHAPAVHAAAAEAGFNLRVLPDGVPASQATGFGVSFDEFSDQKEVAHLLEAVARAVGKPVSTAPASAANTALLSLPSRIRPWLTQPAFHRYRSETELMRYIQRLVSRDLSLVHGMIPLGSCTMKLNAAAELLPVSWPEFARLHPFAPLDQALGYRHLADDLERWLAALTGFAAVSLQPNAGSQGEYAGLLVIRAWHRSRGDNHRDICLIPTSAHGTNPASAVMAGLKVVAVACDAEGNIDQDDLAARATEYADRLAALMVTYPSTHGVFETGIRHICEVVHRHGGQVYLDGANLNAQVGLSRPGAFGADVCHLNLHKTFCIPHGGGGPGVGPIGVAAHLAPFLPGHPFENQTASAIGPVSAAALGSASILPISWMYLRMMGADALRQASAVALLSANYLAHRLDDHFPVLFRGATGRVAHECILDLRPLKRDAGIDVDDIAKRLMDYGFHAPTVSWPVAGTVMVEPTESESLSELDRFADALIAIRDEVRAIETGAMDALNNPLKRAPHTMAAVMAEVWDRPYSRQQAAFPLPDQTQNKVWPAVARIDNAFGDRNLICTCPSVEAVAIAA
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
|
Q3AUM0
|
B8GQT0
|
THIG_THISH
|
Thiazole synthase
|
Thioalkalivibrio
|
MSQTETQDLLTIAGRDYRSRLLVGTGKYKDLDETRAAVEASGAEIITVAIRRTNIGQNPGEPNLLDVLPPDRYTYLPNTAGCYSAEDAVRTCRLARELLDGHTLVKLEVLGDEKTLYPDVVQTLAAAETLVKDGFQVMVYTSDDPILAKRLEEIGCVAVMPLAAPIGSGLGIQNRYNILEIVENAQVPILVDAGVGTASDAAIAMELGCDGVLMNTAIAAAKNPVLMASAMKKAIEAGREAFLAGRMPRKRYASASSPVEGTFF
|
Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
|
B8GQT0
|
Q7NR81
|
DNLJ_CHRVO
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Chromobacterium
|
MTIPGAGFAGPFAVREFPMTANELRAAELRELLNRYGHEYYVLDAPTVPDAEYDRLFRELQALEEAHPELAVSDSPTRRVGGAPLDEFVSVVHAVPMLSLSNAFSDMQLTDPAERHSELIQFDERVRKGLDAAEVEYATEPKFDGLAISLLYENGVLTRAATRGDGVAGEQVTENVRTIRAIPLKLDGANPPALLEVRGEVLMLKRDFERLNADQIARGDKTFANPRNAAAGSLRQLDSRITAQRRLSFFAYSIAQVGGADWPATHAGEMAWLKTLGFPVVMDSLRPVVSGAAGLAGYYEAVLTARAGLPFEIDGVVYKVNRRDQQEALGFVSRAPRWAIAHKFPAEEALTCVEAIEEQVGRTGAITPVARLKPVFVGGVTVTNATLHNEDEVRRKDVRVGDTVVVRRAGDVIPEVVSVVLAQRPMQPAEGGDLFSAGEEPRYPAYRLPTACPVCGSHVVREEGEAIARCSGGLSCRAQRSQAIQHFAGRRMMDIDGLGERYIDKLVEYGYVQGVADLYRLKLEDLLEMKRRADEDEGVTPETVKAGKVASKWAENLIEAIDASRAPPLARLLFALGIRHVGESTAKTLADWLGTMALIRRCPAALFAALPDIGGVVADSLADFFAEDNNEKALDALLAEVKPADEHAPSPKLRERLDDASLLARLAIPRLTEVRSQQLAAQRSLAWLGQSERRALLALELPAEVVNALADWLDEPGRRAALASLAGLRDEILASLPAAAEAAALPLEGKTLVLTGTLPTLSRDQAKALIEAAGGKVSGSVSKKTHYVVAGEEAGGKLAKAQELGVAILDEAGLQALLAGN
|
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
|
Q7NR81
|
A9VT78
|
RL19_BACMK
|
50S ribosomal protein L19
|
Bacillus cereus group
|
MQQLITEITKGQLKTDLPSFRPGDTLRVHVKVVEGTRERIQLFEGVVIKRRGGGISETFTVRKISYGVGVERTFPVHTPRIANIEVLRRGKVRRAKLYYLRNLRGKKARIKEIR
|
This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
|
A9VT78
|
P70278
|
STRA8_MOUSE
|
Stimulated by retinoic acid gene 8 protein
|
Mus
|
MATPGEGNQPSDDGAPQPLAQLQKLEPRVVRRRLSQARHRATLVGLFNNLRKAVYSQSDITASKWQVLNRTKIHIQEQEESLDKLLKLKASFNLQDGNPNSLEEVKEEYARMYSENDSVFLNSFLQDSPPEWFPSEAVGPDAEEEGEEEGEEEGEEGEEEEEGDEEGEEEEENGEEREVEEYQEEEEEEEEEEKKVDLSHSSSTLLPDLMEFERYLNFYKQTMDLLTMNSIISAHEVTLPIVSAAISHLWQTLSEEKKARLLQVWEQQHSAFADLTEACLELAGVEGSMKDSGVDSQGASCSLESTPEEILFEDAFDVASFLDKSEAQHMSNISAMFATCNSENPEEKFQLYIQIIEFFKSLGCVNTPLNQEPEPPDDDDAMLLKCLETFDDL
|
Meiosis-inducer required for the transition into meiosis for both female and male germ cells . In female germ cells, acts downstream of ZGLP1 as a key effector of the meiotic program: required for premeiotic DNA replication and subsequent events in meiotic prophase . During spermatogenesis, next to its role in meiotic initiation, promotes (but is not required for) spermatogonial differentiation . In complex with MEIOSIN, directly activates the transcription of a subset of critical meiotic genes playing a central role in cell-cycle switching from mitosis to meiosis .
|
P70278
|
A2BTH1
|
PANCY_PROMS
|
Cytidine monophosphate kinase
|
Prochlorococcus
|
MKKLIIRKTEEIENWRKDIDSEINFIPTMGNLHDGHIKLISTAKNDNSNINLVSIFINPLQFDNKLDLENYPKTIDNDINISFSNGADAIFIPSNEDIYPPNNNISFLKAPIELSSALCGLNRIGHFDGVCTVVYRLLNLIKPKNLYLGEKDWQQLLILKNLVLRKKLNIAIKSIPTQRDFDGIPLSSRNVHLSKNERKLISFFSRELLEAKKNFQKEKKINLKEIIKKLSEKKISIEYLEHLHPYTLQKAKIEDNISLLAGAIRCGETRLIDHVFLMKRRPIIAIDGPAGSGKSTVTKLIAKKLKLLYLDTGAMYRALSWLIIKENIDFKKENKLQNILKDISIVFKSNTSSHQDVYVNNYCVTEEIRSQKISSIVSKISSIKEVREFLVEEQRKIGESGGLVAEGRDIGTTVFPHAELKIFLTASIDERAKRRKSDKNSKDLQEIDLHKLKELIKQRDSEDSNRKISPLIKANDAIEIITDGYSINEVVDKIIDLYNDKIPKESEIK
|
Catalyzes the transfer of a phosphate group from ATP to either CMP or dCMP to form CDP or dCDP and ADP, respectively.
|
A2BTH1
|
Q7VJ08
|
IF3_HELHP
|
Translation initiation factor IF-3
|
Helicobacter
|
MSKEEVLLNEEIDFKEVRCVSDNGEVYGIISSKEALNLAHKAGLDLVLISPNAKPPVCKIMDYGKFRYQAEKKQKEARKKQKQIEIKEIKLSTQIAQNDINYKVKHAIEFLESGKHVKFKVFLKQRELNIPDAGMDTLGKVAVMLEDIAIAEKEPKLEGKHLNVLYVPKKKEKH
|
IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins.
|
Q7VJ08
|
Q7VP95
|
RPIA_HAEDU
|
Phosphoriboisomerase A
|
Haemophilus
|
MTQQEMKKIAAQAALQFVKPDTIIGVGSGSTVNCFIDALASIKDEIKGAVAASKASEDQLRAMGIEVFNANEVAGLDVYIDGADEITPQGAMIKGGGAALTREKIVSSLAKQFICMVDSSKQVDVLGSSFPLPVEVIPMARSYVARQLVALGGSPEYREGVVTDNGNVILDVHNFNIYEPLKMEHTINNIAGVVTNGIFAQRYANIIIVGTAEGAKIIK
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q7VP95
|
I6LDA6
|
GPMI_ONCVO
|
Cofactor-independent phosphoglycerate mutase homolog
|
Onchocerca
|
MSEVKNRVCLVVIDGWGISNESKGNAILNAKTPVMDELCALNSHPIEAHGLHVGLPEGLMGNSEVGHLNIGAGRVVYQDIVRINLAVKNKTLVENKHLKEAAERAIKGNGRIHLCGLVSDGGVHSHIDHLFALITALKQLKVPQLYIHFFGDGRDTSPTSGVGFLQQLIDFVNKEQYGEIATIVGRYYAMDRDKRWERIRVCYDALIAGVGEKTTIDKAIDVIKGRYAKDETDEFLKPIILSDKGRTKDGDTLIFFDYRADRMREITECMGMERYKDLKSDIKHPKDMQVIGMTQYKAEFTFPALFPPESHKNVLAEWLSVKGLTQFHCAETEKYAHVTFFFNGGVEKQFENEERCLVPSPKVATYDLEPAMSSAGVADKMIEQLNRKAHAFIMCNFAPPDMVGHTGVYEAAVKAVEATDIAIGRIYEACKKNDYVLMVTADHGNAEKMIAPDGGKHTAHTCNLVPFTCSSLKFKFMDKLPDREMALCDVAPTVLKVLGLPLPSEMTGKPVVIEV
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
I6LDA6
|
Q5FUV0
|
COAX_GLUOX
|
Pantothenic acid kinase
|
Gluconobacter
|
MLLVIDAGNTNIVFAVHDGESWLGQWRISTNEARTADEYAAWLLTLFDRVGVNAKAITRAIIGTVVPVALYELRRFCREWLDVVPLVANARLDWGIDVLVDNPNELGADRRLNGLAGRELFGAPLIVVDFGTATTFDVVNSAGQFCGGAIAPGVNLSIDALHRAAARLPRMSIGRPTAAIGRNTSVAMRSGLFWGYVGLVEGLIHRISDEMDAKPTVIATGGLAPLFSEGTPLFDVLAPDLTLDGLRLLADRNTGPPLSYSPERSQGIGQ
|
Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
|
Q5FUV0
|
Q6YXN1
|
PSBH_PHYPA
|
Photosystem II 10 kDa phosphoprotein
|
Physcomitrium
|
MATQIIDDTPKTKGKRSGLGDILKPLNSEYGKVAPGWGTTPLMGVAMGLFAVFLVIILELYNSSVLLDGVPVSW
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q6YXN1
|
A7HH59
|
RSMH_ANADF
|
rRNA (cytosine-N(4)-)-methyltransferase RsmH
|
unclassified Anaeromyxobacter
|
MSGEFVHASVLAREVVEVLRPAPGKLLLDGTLGGGGHSELLLERGARVIGLDKDPRALAAATARLARWGEAFRAVRADFRDAKNVLSALGLTGVDGTLVDLGVSSPQLDQADRGFSFSRPGPLDMRMGDEGERLEDLLRRIDERELARILREYGEEPFARPIARAVKRAVESDEALDTARLADIVAKAIPRKAWPRRIHPATRTFQALRIAVNDELGALAAWLDGLPATLNVGGRAAAISFHSLEDRMVKERFRALTQACTCPPDLPVCACGARASFAAITRKAVVASEAEVAENPRARSAKLRAVEKIR
|
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
|
A7HH59
|
A1W1W9
|
LEUD_CAMJJ
|
Isopropylmalate isomerase
|
Campylobacter
|
MQKFIIHKGIACPLEYANIDTDQIIPKQFLLAVSKQGFGKHLFHDLRYLDDKESVLNMDFNLNKKEYQNSSILVSFENFGSGSSREHAPWALVDYGIRAIIAPSFADIFKNNALGNGLLTIELAKDEVLGIVDELKKSQDKNIEISLLEKRVFFKDKIFSFDLDDFHRICLLEGLDNIALTLKHEAQIKAYEKNSKSFLV
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
A1W1W9
|
Q2JDQ8
|
CLPP2_FRACC
|
Endopeptidase Clp 2
|
Frankia
|
MRHEQARQAAAQPQGRYVLPNIIEKTSRGEYGMDPYSKLLKERIVFLGVQIDDVSANDVMAQLLFLESEDPDRDISIYINSPGGSFTSLTAIYDTMQFVRPDISTICMGQAASAAAVLLAAGTPGKRFALENSRILIHQPSAQGEGQSSDIEIQAREILRMRSLLERMLAVHTGKKEEDIRKDIERDKIFSADEAKEYGLIDEVIKTRKSSRLATAR
|
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.
|
Q2JDQ8
|
A6VLS0
|
MLTC_ACTSZ
|
Murein lyase C
|
Actinobacillus
|
MKITLKKLLILAIVPFLYACSSDRANYDDVFAKDTHGLDLLTGQFSQNIDQIWGVNELLVASRKDYVKYNDSYYTRSHISFDEGMITIETLADVNRLHSAIVHTLLMGSDAKGIDLFASGDTPISSRPFLVGQVVNNFGQSITNVNVANNFATYLIQNKLQQRRLNNGRTVQFVSIQMIANHVNIRARKYLPFVRKASRQYGIDESLILGIMQTESSFNPYAISYANAIGLMQVVPHSAGRDIFKMKGRSGQPSKSYLFDPAKNVDAGTSYLWLLRNEYLAGIQNPTSMRYAMISAYNSGAGAVLRVFSDDPDEAIYIINRMQPEQVYRILTTGHPSAQARNYLVKVDKAQRSYRRVR
|
Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division.
|
A6VLS0
|
Q9TF14
|
CYB_SPEAI
|
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
|
Otospermophilus
|
MTNIRKTHPLMKIVNHSFIDLPTPSNISTWWNFGSLLGLCLTVQILTGLFLAMHYTPDTMTAFSSVTHICRDVNFGWLIRYIHANGASMFFICLFLHVGRGLYYGSYTYFETWNVGIILLFVVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGNTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALVMVHLLFLHETGSNNPSGLISDSDKIPFHPYYTIKDILGALLLILILMILVLFSPDLLGDPDNYTPANPLSTPPHIKPEWYFLFAYAILRSIPNKLGGVLALVSSILILLTLPLLHLSKQRSMMFRPLSQLMFWLLVADLLTLTWIGGQPVEYPFIIIGQLASILYFTIILLILPAVSLIENKLLKW
|
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.
|
Q9TF14
|
P27815
|
PDE4A_HUMAN
|
PDE46
|
Homo
|
MEPPTVPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYSDSAERAERERQPHRPIERADAMDTSDRPGLRTTRMSWPSSFHGTGTGSGGAGGGSSRRFEAENGPTPSPGRSPLDSQASPGLVLHAGAATSQRRESFLYRSDSDYDMSPKTMSRNSSVTSEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPVPSNKRSPLGGPTPVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISTTFLDKQNEVEIPSPTMKEREKQQAPRPRPSQPPPPPVPHLQPMSQITGLKKLMHSNSLNNSNIPRFGVKTDQEELLAQELENLNKWGLNIFCVSDYAGGRSLTCIMYMIFQERDLLKKFRIPVDTMVTYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEDNCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQEILDTLEDNRDWYYSAIRQSPSPPPEEESRGPGHPPLPDKFQFELTLEEEEEEEISMAQIPCTAQEALTAQGLSGVEEALDATIAWEASPAQESLEVMAQEASLEAELEAVYLTQQAQSTGSAPVAPDEFSSREEFVVAVSHSSPSALALQSPLLPAWRTLSVSEHAPGLPGLPSTAAEVEAQREHQAAKRACSACAGTFGEDTSALPAPGGGGSGGDPT
|
Efficiently hydrolyzes cAMP.
|
P27815
|
Q01958
|
CPP2_ENTHI
|
Histolysin
|
Entamoeba
|
MFAFICLLAIASAIDFNTWASKNNKHFTAIEKLRRRAIFNMNAKFVDSFNKIGSFKLSVDGPFAAMTNEEYRTLLKSKRTTEENGQVKYLNIQAPESVDWRKEGKVTPIRDQAQCGSCYTFGSLAALEGRLLIEKGGDANTLDLSEEHMVQCTRDNGNNGCNGGLGSNVYDYIIEHGVAKESDYPYTGSDSTCKTNVKSFAKITGYTKVPRNNEAELKAALSQGLVDVSIDASSAKFQLYKSGAYTDTKCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGDKGYINMVIEGNTCGVATDPLYPTGVQYL
|
Involved in the destruction of human tissue by E.histolytica. Can abolish adhesion and degrade matrix proteins such as collagen, laminin and fibronectin. May play an important role in pathogenicity.
|
Q01958
|
A5UEC2
|
RECX_HAEIE
|
Regulatory protein RecX
|
Haemophilus
|
MSSLAFNYIVNLLSRREYSEFELRNKMQEKNFSEEEIDEALSRCQAKNWQSDRRFSENYLNSRVQKGYGVGRIRQELRQLKGVSSDIIDEVLMESEIDWYEMAENLLRKKFPNYNEQQTPKMKQKIWQYMLSHGFRSDEFADLIGQNQSEWD
|
Modulates RecA activity.
|
A5UEC2
|
Q06J23
|
PSBT_BIGNA
|
Photosystem II reaction center protein T
|
Bigelowiella
|
MEALVYTFLLVGTLGIIFFSIFFREPPRLLK
|
Seems to play a role in the dimerization of PSII.
|
Q06J23
|
Q9LTC0
|
PBL19_ARATH
|
PBS1-like protein 19
|
Arabidopsis
|
MNCLFLFKSKKPRKQQKDNNKNKRKGKELLQNSAPELTNRSETSSFNLQTPRSLPSPRSIKDLYTEREQNLRVFSYEELSKATYVFSRKLVIGEGGFGIVYKGKILSNGDSSDPPLVVAIKKLNRQGLQGHKQWLAEVQFLGVVNHPNVVKLIGYCSEDGETGIERLLVYEYMSNRSLEDHLFPRRSHTLPWKKRLEIMLGAAEGLTYLHDLKVIYRDFKSSNVLLDDQFCPKLSDFGLAREGPDGDNTHVTTARVGTHGYAAPEYVQTGHLRLKSDVYSFGVVLYEIITGRRTIERNKPVAERRLLDWVKEYPADSQRFSMIVDPRLRNNYPAAGARSLAKLADLCLKKNDKERPTMEIVVERLKKIIEESDSEDYPMATTTTKESSQVRRRQVAKPEKQSLRGVSVRG
|
May be involved in plant defense signaling.
|
Q9LTC0
|
Q2FT98
|
RS11_METHJ
|
30S ribosomal protein S11
|
Methanospirillum
|
MSEGKEKWGVAHIYASFNNTIITVTDLTGAETITKSSGGMVVKQDRNESSPYAAMQMAGNVAQAAREKGIVGLHVKVRAPGRGKQRSPGPGAQAAIRALARAGMRIGLIEDVTPVPHDSIRPKGGRRGRRV
|
Located on the platform of the 30S subunit.
|
Q2FT98
|
Q556J8
|
AP3B_DICDI
|
Clathrin assembly protein complex 3 beta large chain
|
Dictyostelium
|
MDTVLNNINQSRYFNDSTANTKIEEIKKHLDSPSDADKLESMKKLIAMLSKGRDVSEAFPQVVKNVIVKNLEIKKLVYMYLVHYAESQNDSALLSINTIQKSLNDQSQVIRASALRVMSSIRVIDIIEVIILAIEKSVKDTSPFVRKAAAFAIAKVHKLDCDKQEPLIDLLEILLNDTSTMVLGAAIVAFNELCPQRFDLLHQHYRKICQLLADFDEWSQVIVLDILTKYARSQFRCPDSTMNDKNIKQFKKKSKSFYSDEEDQEDDEPENSLYKKKPLERDMFDSSEEIDMDHRLLLKSTLPLLQSRNNAVVMAVSSLYFYCAPSIEAQKVGKSLVRILRSGPEVQYITLTNISTMVTLRPSMFEPHLSEFFIHSSDPEYSIKLKLEILTRLATPENIGKILKEFKEYVKNEDKKFVAATIQAIGSCASTVPDVTESCIYGLMSLLSNQSTVVVAESVIVLKRLLQLNATNEKLEKLEKEKEKEKDVKENQSTISKHSSSNNSIKYDNIILHLSKLLDTLQVPSARASIVWVIGEYCYRVPLVAPDVFRKLVKSFSDEHESVKLETLNLGSKLYVQFTDNNSTTTTDNSIPNEFKNERTKEKITLMFQYVLNLAKFDQNYDIRDNSRMLKHFYFNTENTQSINSNIKQIVINQKPIPTETSISEDRQRFTLGSLSHIVNHTALGYTALPDFPDVAPDPSVREPIQRWIPNQQSQQQQHQQQQLNNIFVDTPFYSDEEEEDEEEYDEEEEEEEYEEQNEYEDFFGEEKKNKKKNRKQQNYDEDEYNQDIDDGEYDGEGEVQAEDEDDFDELFGITNDDNNQTANGIGGGGSGEEEMDKFDFENYINSTTKSVKKILLKPTISGGLSIDYCFIRIRDNEEFSCQPRYNIIQLNIKNQSDETFTDISIINKNLIDGADISEFDPIESIEPNQAIQKQIYVLFNSTSQSCKFEISFNKGNFPVTLTPIIGELLIPIVPIYESISQWKDEFEEVGEFKQVDDQFEFGDQCLDKLNNNNNNNNNNNNESGDENIGLMPILPIVLEGINLIPIASNKLKSKIQFASKTLLKDENIYVQIQLLKQQPPTVNCIIRSNDQVVSALLLKKLKDVLQK
|
Part of the AP-3 complex, an adaptor-related complex which is essential for the compartmentalization of the endocytic pathway.
|
Q556J8
|
B9E009
|
MINC_CLOK1
|
Probable septum site-determining protein MinC
|
Clostridium
|
MIDNNILVKGNKEGINIVININKFKDFEEMLEALVKRLSVGKMFYKGCNLKIITDLKNINEKQSVRLKQVLFEKFLIKDCIFEDSNEKPSKIFSGIYEGRTKFLRKTIRGGQVVNYPGNIVIIGDVNAGSEIYVGGNIVVFGALRGYAHAGFGGNSKAIVAAISLEPEMLQIADLVTRSPDNMKPQYPEVAKIRGNIIIVEPYLPNKFI
|
Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization.
|
B9E009
|
C3M930
|
HGD_SINFN
|
Homogentisicase
|
Sinorhizobium
|
MLGKAEKRSEALAAEALAYMPGFGNDFETESLPGALPQGQNSPQKCNYGLYAEQLSGSPFTAPRGTNERSWLYRIRPSVRHTGRFAKIDYPHWKTAPHIAEHALALGQLRWNPLPEPTGELNFLQGIRTMTTAGDVLTQVGMAAHAYVFNADMVDDYFFNADGELLIVPEMGALQVFTELGKMDVAPSEICLVPRGTMFKVARLGEEKAWRGYICENYGAKFTLPDRGPIGANCLANPRDFKTPVAAFEDKETPCRVQVKWCGSFHTVEIGHSPLDVVAWHGNYAPYKYDLKTFSPVGAILFDHPDPSIFTVLTAPSGEEGTANVDFVLFPPRWLVAEHTFRPPWYHRNIMSEFMGLIHGRYDAKEEGFVPGGMSLHNMMLAHGPDTSGFEKATNGELKPVKLDNTMAFMFETRFPQQLTRFAAELETLQDDYIDCWAGLRKRFNGTPEGDWS
|
Involved in the catabolism of homogentisate (2,5-dihydroxyphenylacetate or 2,5-OH-PhAc), a central intermediate in the degradation of phenylalanine and tyrosine. Catalyzes the oxidative ring cleavage of the aromatic ring of homogentisate to yield maleylacetoacetate.
|
C3M930
|
P10385
|
GLTA_WHEAT
|
Glutenin, low molecular weight subunit
|
Triticum
|
MKTFLVFALLALAAASAVAQISQQQQAPPFSQQQQPPFSQQQQPPFSQQQQSPFSQQQQQPPFAQQQQPPFSQQPPISQQQQPPFSQQQQPQFSQQQQPPYSQQQQPPYSQQQQPPFSQQQQPPFSQQQQQPPFTQQQQQQQQQQPFTQQQQPPFSQQPPISQQQQPPFLQQQRPPFSRQQQIPVIHPSVLQQLNPCKVFLQQQCIPVAMQRCLARSQMLQQSICHVMQQQCCQQLRQIPEQSRHESIRAIIYSIILQQQQQQQQQQQQQQGQSIIQYQQQQPQQLGQCVSQPLQQLQQQLGQQPQQQQLAHQIAQLEVMTSIALRTLPTMCNVNVPLYETTTSVPLGVGIGVGVY
|
Glutenins are high-molecular weight seed storage proteins of wheat endosperm. Thought to be responsible for the visco-elastic property of wheat dough.
|
P10385
|
Q9JHP7
|
PLGT2_MOUSE
|
Protein O-xylosyltransferase POGLUT2
|
Mus
|
MFSISLLSCLFLGTVPALAQTGGERRLSPEKSEIWGPGLKAHVVLPARYFYIRAVDTSGEQFTSSPGEKVFQVKISAPDEQFTRVGVQVLDRKDGSFIVRYRMYASYRNLKIEVKHHGQHVAESPYVLRGPVYHENCDCPLEDSAAWLREMNCSETISQIQKDLAHFPTVDPEKIAAEIPKRFGQRQSLCHYTLKDNKVYIKTHGEHVGFRIFMDAILLSLTRKVRMPDVEFFVNLGDWPLEKKKSNSNIQPIFSWCGSTESRDIVMPTYDLTDSVLETMGRVSLDMMSVQANTGPPWESKNSTAVWRGRDSRKERLELVKLSRKHPELIDAAFTNFFFFKHDESLYGPIVKHISFFDFFKHKYQINIDGTVAAYRLPYLLVGDSVVLKQDSIYYEHFYNELQPWKHYIPVKSNLSDLLEKLKWAKEHDAEAKKIAKAGQEFARNNLMGDDIFCYYFKLFQGYANLQVSEPQIREGMKRVEPQSEDDLFPCTCHRRKAKDEL
|
Protein glucosyltransferase that catalyzes the transfer of glucose from UDP-glucose to a serine residue within the consensus sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of xylose from UDP-xylose but less efficiently. Specifically targets extracellular EGF repeats of proteins such as NOTCH1, NOTCH3, FBN1, FBN2 and LTBP1. May regulate the transport of NOTCH1 and NOTCH3 to the plasma membrane and thereby the Notch signaling pathway.
|
Q9JHP7
|
Q11QL8
|
QUEA_CYTH3
|
Queuosine biosynthesis protein QueA
|
Cytophaga
|
MKLSEFKFALPAELVAQHPAANRDEAKMMVINRATGTIEHKIFKDIINYFDEGDIMVMNNTKVFPARLYGNKEKTGAKIEVFLLRELNAELHLWDVLVDPARKIRVGNKLYFGESDLVAEVVDNTTSRGRTIRFLFDGNSEDFSKIIETIGETPLPRYIKRPIEEADKDRYQTIFAENKGAVAAPTAGLHFTKQVMKRMEIKGVNFAPLTLHVGLGSFRTVDVEDLTKHKMDSENFIIESTTADVVNKALDNKKRVCAIGTTSMRALESSVSANNRLKQNAGWTDRFIFPPYDFKIANCMLTNFHMPESTLYMMACAFGGYELMTKAYKTAIKEKYNFLSYGDVMLII
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q11QL8
|
Q7UFN6
|
NADD_RHOBA
|
Nicotinate mononucleotide adenylyltransferase
|
Rhodopirellula
|
MSASETTPQSNHGIGILGGSFDPVHVGHLWMAESALEQLPIEHVRWIPAATSPLKPHGPVASNEHRLQMLRLALSGQSGLVIDDWELRQDSVSYTLLTLEYLQEQFPDRPLYLIIGADSLASFDRWREPEQILKRCHLAVIARGGDPPPDYSILDGMTDETQIQRIRESQIQMPQIEISSSDLRNRIATGRSIRFRVPHPVATLIDNEKMYRVR
|
Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
|
Q7UFN6
|
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