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
|
|---|---|---|---|---|---|---|
Q94CK9
|
LRP1_ARATH
|
Protein LATERAL ROOT PRIMORDIUM 1
|
Arabidopsis
|
MGMVGLRDVFLVAPAYHHQNAGVISGSDHMNSNAAAAAALGVGVIPLLTAGTPQQNVEDSDINFLGNNRRWQNNNNNHETQYLHFKSTNQTTVGTSSNNSGSGSGASGTATCQDCGNQAKKECKQRRCRTCCKSRGFDCSTHVKSTWVSAARRRERQVMPTGANPTAGSSLSTSSGTKKPRIVGSQQQQQQQATSHTSTSNTPPQSFETSSSRQDGGGSREAWPGQVRAAAVFKCVRVTAVEDGDDEYAYQAVVKIGGHVFKGFLYDQGLEPKEGFPSMSDLHLGGSANNHNGVSASAPILDPPNVVYGGGGGSGGGFYS
|
Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influence vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM). Modulates root growth.
|
Q94CK9
|
C3N1A2
|
LEUD_SULIA
|
Isopropylmalate isomerase
|
Sulfolobus
|
MIIEGPVIKFGDKIDTDIIIPARYLKYTDPQYLAQHAMEPLDPEFYKKASKGVIIVAGKVFGMGSSREQAAIALKAAGVKAVVAESFARIFYRNAINNGLPVITLPNSTKEIDESSYVKIDVETGEILVGNKVLKGKGITGMALEILQAGGIMEYLKKMQTVNRN
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
C3N1A2
|
P08058
|
THIO_CERSP
|
Thioredoxin
|
Cereibacter
|
MSTVPVTDATFDTEVRKSDVPVVVDFWAEWCGPCRQIGPALEELSKEYAGKVKIVKVNVDENPESPAMLGVRGIPALFLFKNGQVVSNKVGAAPKAALATWIASAL
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
P08058
|
B2KWH7
|
NIT22_AJECA
|
Siderophore biosynthesis cluster protein NIT22
|
Histoplasma
|
MACPCGARVLVEILTGLLSLKNQSPSTPPESEGEFTRNYILGPKYIIKAIEIFSTMPNTIPPFEYAPVKTTWLKRDVLLFAHSIGCKAGDELHFLYELHPKFQVFPTYPIVLTFKHADIDIVDFLARNAARTLPPGCPVLDWSVAVDGRRRMEFLCPLPPSSEGKTWDIHTKVLGVFDKGAGKGTVMEMEHVLKQRESGQVYTRAWESVFFKGTGGWGGERGPKMNEHVPSTPPRRPDAVSSFQSNAESAHLYRLNGDYNPLHATPEPGKSLGYGGTIMHGLFSWNITARAVLSQFGGSEGRRLRDFEAMFSSPVKPGDKLDILMWDMGLCKRATSAVRNDESLQEVRFMVKVGDRVVLSNGKALLKCEDEGVEVKL
|
Probable dehydratase; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection .
|
B2KWH7
|
O43653
|
PSCA_HUMAN
|
Prostate stem cell antigen
|
Homo
|
MAGLALQPGTALLCYSCKAQVSNEDCLQVENCTQLGEQCWTARIRAVGLLTVISKGCSLNCVDDSQDYYVGKKNITCCDTDLCNASGAHALQPAAAILALLPALGLLLWGPGQL
|
May act as a modulator of nicotinic acetylcholine receptors (nAChRs) activity. In vitro inhibits nicotine-induced signaling probably implicating alpha-3:beta-2- or alpha-7-containing nAChRs.
|
O43653
|
Q4L8A7
|
RL16_STAHJ
| null |
Staphylococcus
|
MLLPKRVKYRRQHRPKTTGRSKGGNYVTFGEYGLQATTTSWITSRQIESARIAMTRYMKRGGKVWIKIFPHTPYTKKPLEVRMGAGKGAVEGWIAVVKPGRILFEVAGVSEEVAREALRLASHKLPVKTKFVKREELGGETNES
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
Q4L8A7
|
Q753J1
|
NCA2_ASHGO
|
Nuclear control of ATPase protein 2
|
Eremothecium
|
MIASRYVASELESVTRKLELQLYERAAISEVLEQTSTDLELAKANEVLQTIKEEADACVAAINGGQKFYTIKYDQILSGLESLSGGQWSVGSPLEPLIRDGISDYLHILLYYALLSKNLAKLPQLLLDQEYYGHVSRCSWFMRLFYGLQIMPVKLIEFFRGHALQELPSKLRQTLRIHNFQLVGLPTQRAWQWTKLPIAMVDTDIIQKTASLDSQLDINVKKFGKLLREFPRQKSDRLEVLSDFLDLKPGSSEFAVVRAVQKWNVDSCAPQPNWIVRYWPTILIALAGGPAGIAAIWNARNDIAAFIKHNLFEFARDLVKNWLVEPLRNIWSTVHHDPTSSIAIMSQGTLDTEINSLQRMLIDFLKEHEYANTVDTSVLMKEIEQGNLTQFMEIYEAQLRKPIRNLVTGDLIRSLLIQIQKGKVDGSLAIHGIDKLLQSQQLVFGIVSISPALLILYVLCNSLTKLVKYGTVWSKGAKYRRSVSVSLNNVERLLNSPIEEFDGDKGNWNLGLLTLEMANLREYGAKLVPHSRTAEWCRDIDEMASSSALSTTGKLNVINRIYHVYGKYF
|
Involved in the mitochondrial expression of subunits 6 and 8 of the F0-F1 ATP synthase.
|
Q753J1
|
B7N0K2
|
GLNE_ECO81
|
Adenylyl transferase
|
Escherichia
|
MKPLSSPLQQYWQTVVERLPEPLAEESLSAQAKSVLTFSDFVQDSVIAHPEWLTELESQPPQADEWQHYAAWLQEALSNVSDEAGLMRELRLFRRRIMVRIAWAQTLALVTEESILQQLSHLAEMLIVAARDWLYDACCREWGTPCNAQGEAQPLLILGMGKLGGGELNFSSDIDLIFAWPEHGCTQGGRRELDNAQFFTRMGQRLIKVLDQPTQDGFVYRVDMRLRPFGESGPLVLSFAALEDYYQEQGRDWERYAMVKARIMGDSDGVYANELRAMLRPFVFRRYIDFSVIQSLRNMKGMIAREVRRRGLTDNIKLGAGGIREIEFIVQVFQLIRGGREPSLQSRSLLPTLSAIAALHLLSENDAEQLRVAYLFLRRLENLLQSINDEQTQTLPFDELNRARLAWAMDFADWPQLTGVLTAHMANVRRVFNELIGDDESETQEESLSEQWRELWQDALQEDDTTPVLAHLSEDDRKQVLMLIADFRKELDKRTIGPRGRQVLDHLMPHLLSDVCAREDAAVTLSRITALLVGIVTRTTYLELLSEFPAALKHLISLCAASPMIASQLARYPLLLDELLDPNTLYQPTATDAYRDELRQYLLRVPEDDEEQQLEALRQFKQAQLLRIAAADIAGTLPVMKVSDHLTWLAEAMIDAVVQQAWVQMVARYGKPNHLNEREGRGFAVVGYGKLGGWELGYSSDLDLIFLHDCPMDAMTDGEREIDGRQFYLRLAQRIMHLFSTRTSSGILYEVDARLRPSGAAGMLVTSAEAFADYQKNEAWTWEHQALVRARVVYGDPQLTAHFDAVRREIMTLPREGKTLQTEVREMREKMRAHLGNKHRDRFDIKADEGGITDIEFITQYLVLRYAHEKPKLTRWSDNVRILELLAQNDIMEEQEAMALTRAYTTLRDELHHLALQELPGHVSEDCFTAERELVRASWQKWLVEE
|
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
|
B7N0K2
|
P49824
|
MYH7_CANLF
|
Myosin heavy chain, cardiac muscle beta isoform
|
Canis
|
MVDAEMAAFGAAAPFLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVASIDDSEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVAYATGALAKAVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHFSLIHYAGTVDYNILGWLQKNKDPLNETVVALYQKSSLKLLSNLFANYAGADAPVEKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVIDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLSRMEYKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEMATMKEEFARIKEALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTSQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSSGKTIHELEKVRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKGLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKGLNEE
|
Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle.
|
P49824
|
Q22592
|
BECN_CAEEL
|
Beclin homolog
|
Caenorhabditis
|
MTTQRSHICLNCQHPLRLDFTQRRPDSADSEKKSETVITEALTGHSRNLMKLISDAQFPSDAPVCNDCSDALRNEMDAQVATLDDEIKTYQTYINYLKENHPTTSIPDLKAKLQNVSDEEKELEQQLKKLLAEEEQLDLDLQTKRRTAEAASEKSGELWKKYRDNLRQVFEDQDELHSLEAERQYAEVQHRKLTDTNVLDLCFHIWVDGIVGEINGFRLGYLKDAPVEFTEINAALGQIVLLLEILLERIGVQHHELMPVAMGSHSYIKLRRNGIDMETYALYGQGTPLSGSSGIDPGIRRFLQLLEFLLKELKDRNKNFKPPYQIHADSLVDNGVKYNAVMTLNTDVRWTRAMALMLTDLKAACAQCDALRSPI
|
Regulates autophagy . Together with phosphatidyl-3-phosphate kinase vps-34, acts as a core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate (PtdIns3P), thereby regulating membrane trafficking . In association with sorf-1 and sorf-2, negatively regulates phosphatidylinositol 3-phosphate in early endosomes to allow for the conversion to late endosomes . Involved in the clearance of engulfed apoptotic cell corpses . Together with ced-9, negatively regulates somatic and germline apoptosis . Plays a role in endosome-to-Golgi retrograde transport of mig-14 . In a daf-18/PTEN- and skn-1/Nrf-dependent manner, promotes germline stem cell proliferation during late and adult stages, probably by ensuring cell survival and cell cycle progression . Required for embryonic development and L3/L4 molting during larval development . Required for normal dauer morphogenesis and lifespan . Plays a role in male tail ray pattern formation . Required for normal survival when exposed to pathogenic bacteria S.typhimurium by promoting autophagic degradation of intracellular S.typhimurium .
|
Q22592
|
B2SYU8
|
SYP_PARPJ
|
Prolyl-tRNA synthetase
|
Paraburkholderia
|
MKASRFFIGTLKEAPADAEIVSHKLMVRAGMIRRVAGGIYNYLPVGLRSIRKVEAIVREEMNRAGGIELLMPAVQPAELWQESGRWEKYGPELLRFKDRRQSDFVIGPTHEEVVTDIARNQIKSYRQLPVNFYQIQTKFRDEIRPRFGVMRGREFIMKDAYSFDKDMDGLRESYRKMYDAYVRIFTRLGLDFRAVAADNGSIGGSGSHEFHVIAETGEDAIAYCPTSDFAANVEAAEALPLYAERAAPTEEMKKTPTPGKAKCEAVAELLNIPLERTIKSIILATENEGAEPTIWLLMLRGDHDLNEIKASKLPGLAEFRMATEAEIIETFGTPPGYLGPIGTKKPIKVVADRTVANMSDFVVGSNEVDYHTTGVNWGRDLPEPVVADIRNVKKGDPSPDGKGVLDICRGIEVGHVFQLGTKYSEAMGATCLDETGKPRPMEMGCYGIGVTRILGAAIEQNFDDKGIIWPESIAPFEVVLCPMGYDRSEAVRAEADKLYAALVEAGIDVILDDRGERPGVMFADWELIGVPHRLVIGDRGLKEGKLEYQGRRDAEATLLPVEDAAQTVIGKVRAALAR
|
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
|
B2SYU8
|
Q6DDK5
|
HACL2_XENLA
|
IlvB-like protein
|
Xenopus
|
MFHLIPFVVAFLLVFLTWFLIKKLRKVIIFELDQNSKHFGGELVADVLKAHDVRFLFTLCGGHISPILVAAERQNIRVIDVRHEASAVFAADAVSRLSGTVGVAAVTAGPGLTNTVTAVKNAQMAESPIVLLAGAAAGLLRGRGSLQDIDQLSLFRPLCKWSGRVNCVKDIVPMLCKAFYLARSGTPGPVLVEFPIDTLYPYSLVRQHLRISDNPQSWRQRFTNWYLRFYLFRLFANGFRIQPCLPGQVPTQIPVEIPSIPWPSTKSIDQLVWLLSQAKRPVIVVSSQALLPPVPATQTAEHVKSLRIPVYLTGMARGLLGRHHPCVFRHARRAALRVADLIILAGSVCDFRMDYGRVLNRKAKIVIINRDKKQLYLNSDIFWRPYLAIRGDVGTALKELSISLNDRFPCLSDFRCPTEWVGELLAREHHRDEEIRQSSLTQPAERINPLSVLWQLEHNGLTDQESIIVADGGDFVGSAAYILRPRGPLSWLDPGPFGTLGVGGGFALGAKLCRPQAHVWVVYGDGSAGYSLAEWDTMARHKAPAIGVIGNDACWSQIARDQLGLFGSNVACGLQSTRYDLVGAAYAGADPLNSTLSVEDSGAFLVTEKNLDNLSDYMAHARELSDRGLPSIINCNIAASGFREGSISL
|
Endoplasmic reticulum 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner. Involved in the phytosphingosine degradation pathway.
|
Q6DDK5
|
Q084G8
|
PLSX_SHEFN
|
Phosphate-acyl-ACP acyltransferase
|
Shewanella
|
MTNLTLALDAMGGDHGPHVTVPAAMQALKFHTSLNIILVGDKTEIEKYLPQAHSADLSRIEIIHTTEVVTMCDRPIHALRSRKNSSMRIALELVRDGKAEACVSAGNTGALMAMAKVLLKTLPGIDRPALVSCLPAMTGKPVYLLDLGANVSCDSETLFQFAIMGSVLCEAVHKKSRPKVALLNVGIEAIKGNDQVQQAGQILQHTEQVNYIGFVEGDEIYTGNVDVIVCDGFVGNITLKTSEGIAKLLVHQLKRGLNDGFFVRLLSKLIAPRIQAVLSKMNPDHYNGASLIGLRGIVVKSHGNADEAAFLQALNLAATEAKRRLPEMIKDRLESILLDINS
|
Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA.
|
Q084G8
|
A7TNS4
|
RTC5_VANPO
|
Restriction of telomere capping protein 5
|
Vanderwaltozyma
|
MGQTPSVESQESKETKNEMPELKSREDILDFFNNRSLSILLPMEIECFKSRLGDKDLSDPLTKDEFNTLLRIADSNSQLQILLWNFFLKISAFPFLSNRSESMTGFGILKGIILLTRERIKKYLGWSNAKLIKLIFIGLTSQEKVGVKTEASVFKIQHVLDTLDGIDLASSTVKDTDMLSFITWLLLLSVHCPTSNCKLNEKSLYDKWKDYEIVASSMVRSMNKKITTTGKGIGISYSDFSHTIVAVSKNVMSPLENIVEHMLYKQDDLLEFPCLDTFLKETKLMTYPLVAQLCTVLPNEIVMSQLQKLYVGRESGYSMRSLQSKVFNWKAATILLVSGTRIVDDIEYSENKNPRYKRFLEEYPKLKDEDQEMDDCHNLKKKVTFAVYIDEPWRVTNKNYFGEKRTSIIELSPRQDKFNSLKVGSVYFNTIGGGIGIGNNQPVTKLNSVRYAPGNVSLTLDNTLEFGVFRHTGYGGTIGPSELLKKNNEENKAFEIRFLIRDVEVWGCGGEKELEEQLREWKWEEAEAKRRQEINLKTMGEDRALLEMAGIIGQHGQSGGSI
|
May be involved in a process influencing telomere capping.
|
A7TNS4
|
Q98R05
|
IF2_MYCPU
|
Translation initiation factor IF-2
|
Mycoplasmopsis
|
MAKKRDKRLSNINEIKTQIINVKTELKNGVFIFSSPMTIGEFAQKINISGTEIVKEYFLKGKMYTLNHILSEEEIADLCFKHGYDFRVEKEINASNFLDNIEFEDKKEDLETRPPIITIMGHVDHGKTTLIDKIRKSNIVSTESSGITQHTGAYQIIYDNKKITFLDTPGHEAFSAMRARGSKVTDIVILVVAADDGVKPQTKEAIAHAQAANVPIIVFVNKMDKPSKDLNRLKNDLSVSGINLEEWGGDTPIVYGSALKGEGIEKLFENINLQAEILDLKFNPKRHPLGVVIESKMDKGVGSLTTVIVQNGTLHKGDFLVAGPRYGRVKAIYDTNKKPLKKVGAGTPVFVIGLNYAPSAGEKFVGINDEKYAKKLSQEREDSEKQEKFLQQTQTISIRRDNDKKIFNIIIKSDTQGTAEAIKDLILQIANDEIEVIVVSYGIGVINNSDLLLAQTSNSEIIGFNSKPNPNIKQQAEDLNIQINSFDVVYKIVDYLNEKINKMVKPKFEKRTIGRAKILKVFFYSKVGNIAGCLMEEGHVKSDSFVKVYRKNKLIHDGRVETLRKGPDEVKKIEKGFEFGLRIKNFDDIKEDDQLEIIEEFRI
|
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.
|
Q98R05
|
O07137
|
ECHA8_MYCLE
|
Probable enoyl-CoA hydratase echA8
|
Mycobacterium
|
MKYDTILVDGYQRVGIITLNRPQALNALNSQMMNEITNAAKELDIDPDVGAILITGSPKVFAAGADIKEMASLTFTDAFDADFFSAWGKLAAVRTPMIAAVAGYALGGGCELAMMCDLLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLILTGRTIDAAEAERSGLVSRVVLADDLLPEAKAVATTISQMSRSATRMAKEAVNRSFESTLAEGLLHERRLFHSTFVTDDQSEGMAAFIEKRAPQFTHR
|
Could possibly oxidize fatty acids using specific components.
|
O07137
|
Q6TEL1
|
RA21A_DANRE
|
64-kDa carboxy-terminal product
|
Danio
|
MFYAHFVLSKRGPLAKIWLAAHWDKKLTKAHVFECNLESSVESIISPKVKMALRTSGHLLLGVVRIYHRKAKYLLADCNEAFIKIKMAFRPGVVDLPEDNREAAYNAITLPEEFHDFDQPLPDLDDIDVAQQFTLNQSRVEEITMREEVGNISLMTDNDFGDFGMDDREMMREENAFGDIIHESSAANLLLEAEPGPAHLPDKTPNLDYDDFGDNNLENSDGGILMDKILSNEDGGGIFDDPPAITDSVMMPQDHGDDDDDFDNFSPAGGPDSPDSGPVEPLPNTTDQTDQTEQTTLVPNEDEAFALEPIDITVKETKAKRKRKLIVDSLKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNGRLLKMFTRCLTPLVPDELRKRRKGGEADSLEDFLKELENPEVPREEVLGHRSDVIDQTIMEEPSMLQASSMEGSRTALDESMMPPPSRQRGLKRKSLETLEKDAVLPPMGVLEQTLQPLDQSVLSHQLEMPQVELPPEDTTNLSRLIPELDLLDEKSKDKDKDDSDEEGEEGQGGDQDQEERRWNKRTQQMLHGLQRVVAKTGAQSISLLELCRNNNKKQAAAKFYSFLVLKKQQAIDLTQTEPYSDIIAAPGPRFHIV
|
May promote apoptosis.
|
Q6TEL1
|
Q87A70
|
EFTS_XYLFT
|
Elongation factor Ts
|
Xylella
|
MEITASLVKELRERTGVGMMECKKALSENAGNIDASVEWLRKSGLVKADKKAGRIAAEGRIVVVHDGCKAVLVEINSETDFVAKDSHFLAFAEAVAQAALVAGAADVEALKHVKLPSGETVEETRAAVIAKIGENVRVRRLARIDSANNVAAYVHGGRIGVLVEVKGGDVELARGIAMHVAAMNPPYNKVADVSAEFLEKEKEIELSKMSEKDKSKPADILEKIISGKINKIVKEVTLYGQPYVLNPDQSVEQVVKAAGADVIGFQRMEVGEGIEKIVEDYASEVMKQAGLS
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
Q87A70
|
Q10WA3
|
PSBY_TRIEI
|
Photosystem II protein Y
|
Trichodesmium
|
MDFDFRLLIVLLPILAAAGWAVFNIGVVAMQQFQKFLNK
|
Manganese-binding polypeptide with L-arginine metabolizing enzyme activity. Component of the core of photosystem II.
|
Q10WA3
|
Q2YTB9
|
HEM3_STAAB
|
Pre-uroporphyrinogen synthase
|
Staphylococcus
|
MRKLVVGSRRSKLALTQSQQFIDKLKAVEPNLEIEIKEIVTKGDRIVDKQLSKVGGKGLFVKEIQHELFEKNIDMAIHSLKDVPSVIPEGLTLGCIPDRELPFDAYISKTHTPLSQLPEGSIIGTSSLRRGAQILSKYPNLEIKWIRGNIDTRLEKLQTEDYDAIILAAAGLRRMGWSDDIVTSYLDIDTLLPAIGQGALGIECRSDDEELLTLLSKVHNDEVAKCVTAERTFLAEMDGSCQVPIAGYATISDQKEIEFTGLIMTPDGKERFEYTMNGTDPVELGKKVSNKLKEQGAYEIIKRLNEQH
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
Q2YTB9
|
P47790
|
MYPR_TAEGU
|
Lipophilin
|
Taeniopygia
|
MGLLECCARCLIGAPFASLVATGLCFFGVALFCGCGHEALTGTEQLIETYFSKNYQDYEFLIDVIHGFQYFIYGTAAFFFLYGALLLAEGFYTTGAVRQIFGDYRTTICGKGLSATVTGGPKGRGARGPQRAHSWQRVCHCLGKWLGHPDKFVGITYVLTIIWLLVFACSAVPVYIYFNTWTTCQSIGNPTKTSASIGTLCADARMYGILPWNAFPGKVCGSNLLSICKTSEFQMTFHLFIAAFVGAAATLVSLVTFIIATTYNFAVLRLMGRGTKF
|
This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.
|
P47790
|
Q4R366
|
MRPP3_MACFA
|
Mitochondrial ribonuclease P protein 3
|
Macaca
|
MTFYLFGIRSFPKLWKSNPYLGLGPGHSYVSLFLSDSCGIRSQQRLFSLKTMSPQNTKATNLIAKARYLRKEEGSNKQVSSVPHFFSAGAAKKRSQMNPQSKDHALPSVRNTIQLPTQPLNSEEWDKLKADFKGKTSFERFIISQMAHSHSSVDVAKSLLAWVAAKNNGIVSYDLLVGYLYLCVFHMQTSEVIDVFEIMKTRYKTLEPGGYSLLIQGLIHSDRWRESLLLLEDIKKVITPSKKNYNDCIQGALLHQDINTAWNLYQELLGHDFVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFAHSIKTWFESVPGKQWKGQFTTVQKSGQCLGCGKTIESIQLSPEEYEFLKGRIMRDVIDGGDQYKKTTPQELKRFENFVKSCPPFDIVIDGLNVAKMFPKARESQVLLNVVSQLAKQNLRLLVLGRKHMLRQSFQWRKDEMAEVQKQASCFFADNISKDDPFLLYATLHSGNHCRFITKDLMRDHKACLPDAKTQRLFFKWQQGHQLAIINGFPGSKLTFQHILSYDTVVQTTGDSWHIPYDEDVVERYSYEVPTKWLCLHQKT
|
Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends.
|
Q4R366
|
Q72NQ7
|
OBG_LEPIC
|
GTP-binding protein Obg
|
Leptospira
|
MESFVDEVAIEVFAGHGGAGSVHFRREKYVEFGGPDGGDGGIGGNVVIRPNLSMYTLDKYLSKRKFKAQAGFPGVGDNCSGKKGEDLVLFVPLGTQIYDEETGDLLFDFVSDSQEFVVARGGRGGKGNAHFKTSTNQTPRFAQPGEEGEYKFLRLSLKLLADVGIVGLPNAGKSTLISKITDAHPKIAGYAFTTLSPNLGVVKRRGDIFRFTIADIPGIIEGASMGIGLGLSFLRHIERVKGILYLFDASSLDIEEDLKMLRNELSTYNPELLNRPYLIVLNKIDIWNDPEFTKDVIAKVSHLGKVVAISADQEVNLEELLENMDEVFFKNEIEKILNPIKDTKPISLDESDIFES
|
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.
|
Q72NQ7
|
A5GTT4
|
DXS_SYNR3
|
1-deoxyxylulose-5-phosphate synthase
|
unclassified Synechococcus
|
MHLSELSHPNELHGLSSSELEDVARQIREKHLKTVSTSGGHLGPGLGVVELTLALYQTLDLDHDRVVWDVGHQAYPHKLITGRFNEFHTLRKKDGVAGYLKRSESSFDHFGAGHASTSISAALGMAIARDRQGQNHKCVAVIGDGALTGGMALEAINHAGHLPKTRLLVVLNDNDMSISPPVGALSNHLNRMRLSPPMQFLTGSAEEAVRHLPFMQGQVPAELNRIKEGMKRLAVPKVGAVFEELGFTYMGPVDGHDIGALVRTFQEAHRSEGPVLVHVATTKGKGYPYAEADQVGYHAQSAFDLTTGKSFPAKKPKPPSYSKVFGQTLVKLCEQDSRIVGITAAMATGTGLDLLQKAVPDQYVDVGIAEQHAVTLAAGMACDGLKPVVAIYSTFLQRAYDQLIHDVGIQKLPVTFVLDRAGIVGADGPTHQGQYDISYLRCVPNFTVMAPKDEAELQRMLVTGLRHNGPIALRIPRGSGEGVPCLEDGWEPLEIGRGELLAEGDDLLIVAYGAMVAPAMATAGLLQEQGIRATVVNARFLRPLDEALLVPLAKRIGRVVTMEEGCLAGGFGAAVMEALHDRDVLVPMLRLGIPDQLVDHASPDESKQALGLTPPQMADRICERFGSAFGDRLQRQTLSV
|
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).
|
A5GTT4
|
Q07PT0
|
MURB_RHOP5
|
UDP-N-acetylmuramate dehydrogenase
|
Rhodopseudomonas
|
MNFPDLIPDLKPAMPELRGRLLANAPLAPLTWFRVGGPAQLLFTPADENDLAYFLARLPKEIPVSIVGVGSNLIVRDGGLPGAVIRLAARGFGETRVDGDVIHAGAAALDKRVAETAAAAGIGGLEFLYGIPGTIGGALRMNAGANGGEIKDVLEEATGIGRDGSLHVFRNAGMRLSYRKSGVDASVIFTSVRLRGAIAPPETIRAKMDEVQKHRETAQPIREKTGGSTFKNPPGQSAWKLIDEAGCRGLRVGGAQVSELHCNFLINTGDATAADIETLGETVRDRVKTHSGIELQWEIKRIGIAA
|
Cell wall formation.
|
Q07PT0
|
C0RJK9
|
RPOC_BRUMB
|
Transcriptase subunit beta'
|
Brucella
|
MNQEVMNLFNPQAPAQTFDSIRISIASPEKILSWSYGEIKKPETINYRTFKPERDGLFCARIFGPIKDYECLCGKYKRMKYKGIICEKCGVEVTLSRVRRERMGHIELAAPVAHIWFLKSLPSRIGTLLDMTLKDIERVLYFENYIVTEPGLTSLKEHQLLSEEEYMIAVDEFGEDQFTALIGAEAIYELLASMELEKIAADLRVDLAETTSDLKQKKLMKRLKIVENFLESGNRPEWMIMKIVPVIPPDLRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLIELRAPGIIIRNEKRMLQEAVDALFDNGRRGRVITGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVTGPELKLHQCGLPKKMALELFKPFIYARLDAKGYSSTVKQAKKLVEKERPEVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPTLIEGKAIQLHPLVCTAFNADFDGDQMAVHVPLSLEAQLEARVLMMSTNNILHPANGAPIIVPSQDMVLGLYYLSIVAEKEPGEGMIFADMGELQHALENKVVTLHTKIKGRFKTVDAEGNPVSKIYDTTPGRMIMGELLPKNVNVPFDICNQEMTKKNISKMIDHVYRHCGQKETVIFCDRIMQLGFAHACRAGISFGKDDMVIPESKAKIVAETEALTTEYEQQYNDGLITQGEKYNKVVDAWGKATDKITEEMMARLKAVEFDPVTGRQKQMNSVYMMSHSGARGSVNQMRQLGGMRGLMAKPSGEIIETPIISNFKEGLTVNEYFNSTHGARKGLADTALKTANSGYLTRRLVDVAQDAIISEVDCGAEIGLTMQPIVDAGQIVASIGQRVLGRTALDPILHPVTGEVIVEAGRMVEEKDVEIIEKAGIQSIRIRSALTCETRNGVCAKCYGRDLARGTPVNQGEAVGVIAAQSIGEPGTQLTMRTFHLGGTAQVVDSSYLEASYEGTVKLRNRNVVRNSDGNLVVMGRNMAVLILDATGKERAVHRVTYGSRLFVDEGDTVKRGQRIAEWDPYTRPIMTEVEGYVEFEDLVDGLSVSETADESTGITKRVVIDWRSTPRGSDLKPAMVIKDKAGKILKLSKGGDARFLLSVESILSVEPGAHVKAGDVIARLPMESAKTKDITGGLPRVAELFEARRPKDHAIIAEIDGTVRFGRDYKNKRRIIIEPNDDTIEPVEYLIPKGKPFHLQDGDVIEKGEYILDGNPAPHDILAIKGVEALASYLVNEIQEVYRLQGVLINDKHIEVIVRQMLQKVEITESGDTGYIPGDHVDRIELEEINERLIEEGKKPGSGNPVLLGITKASLQTPSFISAASFQETTRVLTEAAVAGKMDTLQGLKENVIVGRLIPAGTGGMANQIRRIATARDELIIDERRKTSGSAEANAMLVDMTDNAAE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
C0RJK9
|
Q6FCK9
|
TSAD_ACIAD
|
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
|
Acinetobacter
|
MIVLGLETSCDETGLALYDSEKGLLGQVLYSQIKLHAEYGGVVPELASRDHVRKMIPLLDQLLNDSQVKKSQIDAVAYTRGPGLMGALMTGALFGRTLAFALNKPAIGVHHMEGHMLAPLLSATPPEFPFVALLVSGGHTQLMAAYGIGQYELLGESIDDAAGEAFDKVAKMMGLPYPGGPNIAKLALQGNPETFEFPRPMLHQGLDFSFSGLKTSVSVQLKKLGEENRDADIAASFQEAIVDTLVKKSVKALKQTGLKRLVIAGGVSANQRLRERLEHSLSKIKSQVYYAEPALCTDNGAMIAFAGYQRLKAGQCDDLVVTTTPRWPMTELSRPAEIIE
|
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.
|
Q6FCK9
|
Q3YAT3
|
MPDB_MYCAO
|
2-methyl-1,2-propanediol dehydrogenase
|
Mycolicibacterium
|
MTTSADQTDVLVIGSGPGGAGVTLKLVQAGYKVTCLEQGPWVTPPEHPHYHREWEIEKQRGWAYDPNVRGLPEDYPVTGFTTPYLMNNVGGSTMHYAGHWPRYKPVDFRKGTEHGLEGTIDWPISYEELAPYYDENDAIYGISGMVGDPSYPDRTGVDRDPPVKPGKLGRNFAQALGDLGWHWWPSDNAIITRPREGREADIAAGNELSGSPTGSLSTPTHTHWPTAIALGADLRTHARVEQIHTKNGKATGATYIDTRTGARHEINAKIVVVSASGIGTPRLLLMSAQKGHPDGLANSNGLVGKYLMHHILRVLASVVRTSRMEGYKGAFGAPLYSHEFYHTDTNRGFVNGFGMQVARSFGAAYTAMGSHTGYVAPWGKSHRKFFNEHFGNHLMVFMFGEDLPVETNCVTLDPDAKDSSGLPAARVNWEPHENDIALANYGIDRIFEAARALGAVETNDTGVLNPPPGWHLMGTCRMGNNPEDSVTNKWHQTWDVPNLFVVDGSSLTTGGAVNPTSTIGALAVRAGDYISRRFSDIVDQRTTPSNEDAPAI
|
Involved in the degradation of methyl tert-butyl ether (MTBE). Catalyzes the conversion of 2-methyl 1,2-propanediol (2-M1,2-PD) to hydroxyisobutyraldehyde.
|
Q3YAT3
|
Q5VIY5
|
ZN468_HUMAN
|
Zinc finger protein 468
|
Homo
|
MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMLKTLSSTGQGNTEVIHTGTLHRQASHHIGEFCFHEIEKDIHGFEFQWKEDETNGHAAPMTEIKELAGSTGQHDQRHAGNKRIKDQLGSSFHLHLPEPHIFQSEGKIGNQVEKSINNASSVSTSQRICCRPKTHISNKYGNNSLHSSLLTQKWEVHMREKSFECIQSFKSFNCSSLLKKHQIIHLEEKQCKCDVCGKVFNQKRYLACHRRCHTGEKPYKCNECGKTFGHNSSLFIHKALHTGEKPYECEECDKVFSRKSHLERHKRIHTGEKPYKCKVCDEAFAYNSYLAKHTILHTGEKPYTCNECGKVFNRLSTLARHHRLHTGEKPYKCEECDKVFSRKSHLERHRRIHSGEKPYKCEECCKVFSRKSNLERHRRIHTGEKPYKCKVCDKAFQRDSHLAQHQRVHTGEKPYKCNECGKTFGQTSSLIIHRRLHTGEKPYKCNECGKTFSQMSSLVYHHRLHSGEKP
|
May be involved in transcriptional regulation.
|
Q5VIY5
|
Q5HUK4
|
PURL_CAMJR
|
Phosphoribosylformylglycinamidine synthase subunit II
|
Campylobacter
|
MDKETIKAHKISDEEYTQILEILGREPNLLELGVISAMWSEHCSYKSSKKYLNGFPTKAPWVIQGPGENAGVIDIGQGMAAVFKVESHNHPSFIEPFAGAATGVGGILRDVFTMGARVVAGLNSLKFGNIHNEKCSKHQKYLVKGVVNGISHYGNCMGVPTIGGECAFDECFNGNILVNAFALGVCKSEDIFYAKAEGVGNPVIYVGSKTGRDGLGGAVMASDSFNEESKSLRPTVQIGDPFSEKLLMEACLELFKTDYIVGIQDMGAAGLTSSSFEMAGRSGSGMKLYLDKTPIRESGMTPYELMLSESQERMLICAKKGYEDKVIEIFKKWDLDAVVIGEVTNTGKMELFWHDELVGLIPIEPLSEKAPILSRPISEPKYLSEIKDYKFELKLSIQELFIQMLQNENINNKAFIYDQFDSSVQTNTIKADGRLGASAIRIKENGASVAMAIECNSRLNYVNPKIGAALAVASAGRKVACTGAKPLAISDCLNYGNPQNPEVMWQFAQGCEGIKEACKELNTPVVSGNVSLYNETEGVSIYPSPTIVSVGVLEDANKTLKASFEKENLSVYLLGESLGEFGGSMVMKIQDKKVSGSLKELDYKAEIALWDLLYKANQNSLLECANSVGIGGIAMTLAKMFAISSVGANLTSGFDDEKMIFDESASRAIVGLSKENEEAFLNLAKEFGVKAYKLGVSTSQKHFKLDSIELSKAELDKLYFESFKEQIQ
|
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
|
Q5HUK4
|
A4QUA4
|
LCL2_MAGO7
|
Long chronological lifespan protein 2
|
Pyricularia
|
MQSPVLLQLLLLALMGTVSAQFGGFFDQMFGGGGGGGGGQQQRQEQNVPSDSAWYRSNVDAAVCSNYLCPDTLACVHFPHHCPCPFPDHEDKFELAEGQRICVSRGGFKAGEAARKVELARKGLL
|
Probable component of the endoplasmic reticulum-associated degradation (ERAD) pathway.
|
A4QUA4
|
Q89WN9
|
COAE_BRADU
|
Dephosphocoenzyme A kinase
|
Bradyrhizobium
|
MRILGLTGSIGMGKSTTAKLFAEAGVPVYDADAAVHQLYEGEAAPAIEAAFPGTTANGKVDRPKLSARVVHDPAAIKQLEQIVHPMLGASRQKFFADAEAANAPVVVLDIPLLFETGGEKRVDAVVVVSTSPELQRERVLARGTMDEAKLNAIIAKQTPDAEKRKRADFVVDTSHGLEPVRAQIAHILAEVVKMPQRRA
|
Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
|
Q89WN9
|
P24803
|
IAD1_ENTFA
|
iAD1
|
Enterococcus
|
MSKRAMKKIIPLITLFVVTLVG
|
Acts as a competitive inhibitor of the CAD1 pheromone.
|
P24803
|
Q8VI64
|
HUMMR_MOUSE
|
Ovary-specific acidic protein
|
Mus
|
MYLRRAVSKTLALPRRAPPGPAPLGKDASLRRMSSRKFPGTSGSNMIYYLVVGVTVSAGGYYTYKALTSKQVRRTEHVAEPKEQTKAELQPLPGEKEEHVAEAEQVCSEPGDTAVTEAESVDAEEVPEAAVVLPEESQASAPSEVPAEAAVVEASLSSSEPELKITEASLVETTESVPESTQEVESAAPDQDDVCNEGADTSQEGADTSQEGADTSQEGADTTKEEADNSKEAEGTTTEDPRSISEESAELEESPPLGSEPPAQPESQEEETQVTEETASPQG
|
Plays a role in the trafficking of mitochondria along microtubules . Regulates the kinesin-mediated axonal transport of mitochondria to nerve terminals along microtubules during hypoxia . Participates in the translocation of TRAK2/GRIF1 from the cytoplasm to the mitochondrion . Also plays a role in steroidogenesis through maintenance of mitochondrial abundance and morphology . Plays an inhibitory role during neocortex development by regulating mitochondrial morphology, distribution and motility in neocortical neurons .
|
Q8VI64
|
A7FQP0
|
ENO_CLOB1
|
2-phosphoglycerate dehydratase
|
Clostridium
|
MKNYIEIVDVYARQILDSRCNPTVEVEVELEDGTVGVAAVPSGASTGAFEAVELRDGDKSKYLGKGVLKAVDNVNTIIADELVGMNVLDQVAIDKTMIELDGTDNKAKLGANAMLGVSLACAKAAANSLGMSLYQYIGGVNGKVLPVPMMNIINGGKHADNNVDLQEFMIMPAGAPSFSEALRMCSEVYHALKSTLKAQGYDTGVGDEGGFAPNLKSNEEAIVVIIEAIKKAGYTPGEDIFIALDPASSEIFEDGKYNLAGEGRVLTPEEMANYYVELAEKYPIISIEDGMAEEDWDGWKILTEKIGNKVQLVGDDLFVTNTERLSKGIKLGVANSILIKLNQIGTLTETLNAIEMAERAGYTAVVSHRSGETEDTTIADLVVAVNAGQIKTGAPARSERVAKYNQLLRIEEELNDMGEYRGLKAFYNINK
|
Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
|
A7FQP0
|
A0RWI9
|
RS11_CENSY
|
30S ribosomal protein S11
|
Cenarchaeum
|
MSGTEAGAGEPAAEEPTKEAAQPEAGAPDAGTPEASAPEAGAAQPEAGTQPEAGTAQPEAPPEGTPETTPADEKLGIAHIYSSYNNTIIHMTDLTGAETVSISSGGVHVNADRYESSPFAAMKAANKVIESARAKGFTGFHIRVRAVGGVGSRVPGPGAQAAIRALARGGFRIGRIDDVTPIPHDTTRKKGGKRGRRV
|
Located on the platform of the 30S subunit.
|
A0RWI9
|
A7X232
|
TRPD_STAA1
|
Anthranilate phosphoribosyltransferase
|
Staphylococcus
|
MTLLTRIKTETILLESDIKELIDILISPSIGTDIKYELLSSYSEREIQQQELTYIVRSLINTMYPHQPCYEGAMCVCGTGGDKSNSFNISTTVAFVVASAGVKVIKHGNKSITSNSGSTDLLNQMNIQTTTVDDTPNQLNEKDLVFIGATESYPIMKYMQPVRKMIGKPTILNLVGPLINPYHLTYQMVGVFDPTKLKLVAKTIKDLGRKRAIVLHGANGMDEATLSGDNLIYELTEDGEIKNYTLNATDYGLKHAPNSDFKGGSPEENLAISLNILNGKDQSSRRDVVLLNAGLSLYVAEKVDTIAEGIELATTLIDNGEALKKYHQMRGE
|
Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).
|
A7X232
|
Q02229
|
GVPD_HALMT
|
Protein GvpD
|
Haloferax
|
MPPPNPAYSPTEQQGRVLFPREVSRFFTGDPGHTLLVNGAPGTGKTLFTIRGLDVLERDGDVLYVSTRVDQDTVHEMYFREHSSLDKTHILDLSQDPFELPLDVDVPFEKLGLDSLLEWIQQIKAASKRLTIAFDSWELIYEYLASRHDDSPDIETVTTQLVSLARQENIRLLLVSETADSSPLEYIVDGVVTLQVAEDERGRTRRYLRLEKLRGVRIGNRLQPITLADGQFQAITPVELPTVRTGANNGTWEPRTNTKAKFSTGIGDLDPILSGGYNRGSVIHLDLGTDLSRDAWSVLTLPTIRNFLANEMGVAVVPPREGSPGLLHNDLNSVLTPRVFDTYCHVFETYAGPSRNRGTYEEDGQVETPLDTSQTATPSDAESPVGTETELSEKVETELSEENPPAPGEVVDTERSTTIGKELESPVEGGQLDYEPYMEYVEEVRKQSDGPLLHVISMDTARTAFETRLGDFANYVALHNDLAILITKPGTELRRRADRVADMHFRLERSGEAIMLYGENPLTPLLGIGIDRSQPIPEIILTEMV
|
May play a role in an energy requiring process such as assembly of gas vesicles in addition to a possible structural or regulatory function.
|
Q02229
|
Q31F26
|
SURA_HYDCU
|
Rotamase SurA
|
Hydrogenovibrio
|
MKKIIPTNLFKLISILFILTPFFAWSAPQETLIDRVVAVVNDNIILKSELDAEVNLAKQDLQARNIPVTNPEELASKVLDKIILERLQLQRINQLGIKIADDELFSQIQEIAKQNNLTVIELRDRLNMSQKNGFESFRERIRQQMLFQKLREVEVLSKTQVTEDEVSNFIQRQALVQSDVEYHLGHIMVSLPESATPDQRDASKQKAQEILQKIRTGGDFSQMAVRYSEGSKALQGGDLGWLGIDQIPTFFNDALNQLEIGETSDVIRSPVGFHIIQLQGKRNKNSQIVKQYHLYRFILLSEDAQNKQQPSPTLVKLAESLNSLESFKQLNEKYSDIPASVNANGNLGWQTAKEMSPEYYQAIEALQPGHAAKPFATEKGWVILFLDGIRDQDLSLKDKRKQAMQTLRMKKANESYEIWLRRLKDEALIDIRLEDPEIMKKQPSHEEANAN
|
Chaperone involved in the correct folding and assembly of outer membrane proteins. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation.
|
Q31F26
|
P61913
|
DUT_WOLPM
|
dUTP pyrophosphatase
|
unclassified Wolbachia
|
MQRSKIKVEIKRLSHGEDLSLPCYATTQSAGMDLYAALNDSAVLNPLERLLVPTGIVIAIPNGFEGQIRPRSGLAAKHGITVLNSPGTIDSDYRGEVKICLINLSNQPYEIKRGDRIAQILISPVSQVIWDDREEFCAEETGRNAGGFGSSGR
|
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.
|
P61913
|
Q68W98
|
SECY_RICTY
|
Protein translocase subunit SecY
|
typhus group
|
MGQNFSKKSSNDLVSRIIFTIFMLIICRIGSFIPIPGIDSIALNSVAEKNQFGILGMFNMLSGGSLGRMSIFALAIMPYITASIIIQLMSVAYKPLENLKKEGESGKRKINQLSRYLTVLLASFQAYGVALSLESMVTNTGPVVILAGFFFRVTTVITLVVGTMLLMWLGEQITQRGIGNGTSLIIFIGIISGVPSAIISMFELSRKGALSPLIAITVCIGVVLLIAIIIFFEKAQRKLLVQYPKRQVGNKIYGGEATHMPLKLNTSGVIPPIFASSILLFPTTLANFSNSNSETMSMLSYYLGHGKPVYILLYVVLIMFFSFFYTAIVFNSEETANNLRKYGAYIPGKRPGKNTSDYFDYILTRLTVIGGLYLSIICVIPELLMNKYVISLSLGGTSFLIVVNVVLDTMTQIQTYLFSSKYEGLMKKIKLKN
|
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
|
Q68W98
|
Q5XCA7
|
FOLB_STRP6
|
7,8-dihydroneopterin aldolase
|
Streptococcus
|
MDKIVLESCRFYGYHGAFKEEQTLGQIFLVDLELSVDLQAASLSDQLTDTVHYGMVFDSVRQLVEGGKFILIERLAGAICEQLFNEFPPIEAIKVAIKKENPPIAGHYKAVGIELERQR
|
Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
|
Q5XCA7
|
P74892
|
SCRR_STAXY
|
Scr operon regulatory protein
|
Staphylococcus
|
MKNIADIAKIAGVSKSTVSRYLNNGSVSLKTQQKLDEIIRENDYQPNQFAQSLRARRTNMIGAIIPRMNSFAVDETIKGVKTVCDQLNYSLLLNYTNLNIQLEIDALETFYRSKVDGIVFMATEITDQHLEVINKINVPVIIVGQAHDDLHCIIHNDYQAGYLVGDMLGQQGYNDIKFFGVTESDIAVGVQRKEGLIAGLEAHNIQPEISLTSFNYQEAMVDVVEALQAYPHYDAIVGATDSIALAIHKYNSEHKPHAHEKYIVGFGGDPVTDIVSPSIHTINYNFEYAGSVAMDKLNQMIQHQVIEQRIIIDVEQSFEN
|
Negative regulator of scrB expression.
|
P74892
|
A8G9Z6
|
PIMT_SERP5
|
Protein-beta-aspartate methyltransferase
|
Serratia
|
MVNKRMQTLLTQLRQQGIRDERLLQAIEAVPRERFVDEALEHKAYENTALPIGSGQTISQPYMVARMTELLNLTPTSRVLEIGTGSGYQTAILAHLVQHVCSVERIKGLQWQAKRRLKQLDLHNVSTRHGDGWQGWASRGPFDAIIVTAAPPEIPPALMEQLDDGGILVLPVGEQAQTLKYIRRQGSEFVIDTVEAVRFVPLVKGELA
|
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
|
A8G9Z6
|
Q84P17
|
AEE18_ARATH
|
Probable acyl-activating enzyme 18, peroxisomal
|
Arabidopsis
|
MWKSIGELSCDDYVKAGLTLEDAKEFDKLVSDVITKAIETDPRDQWKALVDESVLKPWHPHPLHQLLYYSVYSNWDSSVHGPPLYWFPSLSQSKSTNLGKLMEYHGPRLLGPSYKNPLESFELFRRFSVEHPEVYWSFVIDELSLVFHTPPRCILNKSKPEGTWLPDAVLNIAECCLMPSSHPKKEDDSVAVVWRNEGFDDSPVNRMTIKELREQVMLVANAISGSFEKGDTIAIDMPMTVDAVIIYLAIILAGCIVVSIADSFAAKEIATRLKISKAKGIFTQDYILRGGRRFPLYSRVVEAAPSKVIVLPASGTELHVQLREQDVSWMDFLSNAKPHSSGENYYRPIYLPVESVINILFSSGTTGEPKAIPWTQLSPIRSACDGWAHLDVQVGHTYCWPTNLGWVMGPTLMFSCFLTGATLALYSGSPLGRGFGKFVQDAGVTVLGTVPSLVKTWKRTNCMEGLNWTKIKFFATTGEASNVDDVLWLSSKADYKPVIECCGGTELASSYIIGSPLQPQAFGAFSTPSMTTRIIIFDENGVPYPDDQPCTGEVGLFPQHLGATDRLLNANHDEVYFKGMPMYKETRLRRHGDIVKRTVGGYYNVQGRADDTMNLGGIKTSSIEIERVCDQADECISETAAVTLTPPNGGPELLVIFAVLKEGFKQQSGEELKMKFSRTIQKDLNPLFKVSFVKIVPEFPRTASSKLLRRVLRDQIKQELLSLRSRI
|
May be involved in the peroxisomal activation of 2,4-dichlorophenoxybutyric acid (2,4-DB), a precursor of active auxins that inhibit root growth.
|
Q84P17
|
P00306
|
PHCA_GALSU
|
C-phycocyanin alpha chain
|
Galdieria
|
MKTPITEAIAAADNQGRFLSNTELQAVNGRYQRAAASLEAARSLTSNAERLINGAAQAVYSKFPYTSQMPGPQYASSAVGKAKCARDIGYYLRMVTYCLVVGGTGPMDEYLIAGLEEINRTFDLSPSWYVEALNYIKANHGLSGQAANEANTYIDYAINALS
|
Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.
|
P00306
|
Q8CSX6
|
MURD_STAES
|
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase
|
Staphylococcus
|
MLNYTELENKNVLVVGLAKSGYEAAKLLLKLGANVKVNDGKDLSQDAHAKDLESMGIEVISGSHPFSLLDDDPIIVKNPGIPYTVSIIKEATNRGLKILTEVELSYLISEAPIIAVTGTNGKTTVTSLIGDMFQKSVLTGRLSGNIGYVASKVAQEVKSDEYLITELSSFQLLGIEEYKPHIAIITNIYSAHLDYHETLENYQNAKKQIYKNQTKDDYLICNYHQRHLIESENLEAKTFYFSTQQEVDGIYIKDGFIVFNGIRIINTKDLVLPGEHNLENILAAVLASIIAGVPVKAIVDSLVTFSGIDHRLQYIGTNRTNKYYNDSKATNTLATQFALNSFDQPIIWLCGGLDRGNEFDELIPYMENVRVMVVFGETQDKFAKLGNSQGKYVIKATDVEDAVDKIQDIVEPNDVVLLSPACASWDQYHTFEERGEKFIDRFRAHLPSY
|
Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
|
Q8CSX6
|
Q12B88
|
RNH_POLSJ
|
Ribonuclease H
|
unclassified Polaromonas
|
MTDTQAGTTTQTQVVIYTDGACKGNPGPGGWGVLLAMGDTEKELFGGEPVTTNNRMEMTAVIEALAALKRPCRVTLYLDSEYVRKGITEWIHGWKARGWRTAAKAPVKNVDLWQRLDALVTSSGHKIDWRWVKGHNGDPGNERADALANQGVERALGRR
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q12B88
|
B0TVI4
|
DAPE_SHEHH
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Shewanella
|
MSQNTDSPVLSLAKDLISRQSVTPLDEGCQQLMADRLADAGFNIESMVFEDTTNMWARRGTQSPVFCFAGHTDVVPVGDLNRWHTPPFEPVVIDDYLHGRGAADMKGSLAAMLVATERFIKKFPDHQGSIAFLITSDEEGPFINGTTRVIDTLEARNEKITWSLVGEPSSTHKLGDIVKNGRRGSLTGNLTVKGVQGHVAYPHLADNPIHKAAPALDELARMKWDNGNEFFPPTSFQIANINGGTGASNVIPGALEVMFNFRYSTEVTAEILIERVLNILDAHGLEYDIDWVFNGLPFLTGDGPLLEATKAAIKKVTGTNTDPQTSGGTSDGRFIAPTGAQVIELGPVNATIHKVNECVKVSDLELLTDCYEAILENLLCK
|
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.
|
B0TVI4
|
Q9LJ85
|
LTG20_ARATH
|
Non-specific lipid transfer protein GPI-anchored 20
|
Arabidopsis
|
MSKIISLVVAMIAVLALPIRGQQQPLSQCTPSMMTTVSPCMGFITNSSSNGTSPSSDCCNSLRSLTTGGMGCLCLIVTGTVPFNIPINRTTAVSLPRACNMPRVPLQCQANIAPAAAPGPAATFGPSMSPGPETDPIVPEPTPAAQTPQSDTTRPFTPSVDGGAPTSDDGGSTSRPSETPSSAYALSPSLLFFSIALVALKFY
|
Probable lipid transfer protein.
|
Q9LJ85
|
Q9M9V6
|
ICS2_ARATH
|
menF-like protein 2
|
Arabidopsis
|
MASLQCSFHFLGTNPKKYNPSSIFQSYSRTSFTKLSSRVSRQRFLRCTLSMNGCEADHKAPLGTVETRTLSTVPSPAAATERLITAVSDLKSQPPPFSSGIVRLQVPIEQKIGAIDWLHAQNEILPRSFFSRRSDSGRPDLLQDFSSDNGSSDHNPVSVAGIGSAVFFRDLDPFSHDDWRSIRRFLSSKSPLIRAYGGLRFDPTGKIAVEWEHFGSFYFTVPQVEFDEFGGSSMLAATVAWDNELSWTLENAIEALQETMLQVSSVIMRLRRESLGVIVVSKNHVPSEGAYYPAVNNALEIIKDKHSPLSKVVLARSSRIITDTDIDPIAWLARLQCEGQDAYQFCLQPPGAPAFIGNTPERLFHRKHLGVCSEALAATRPRGDSKVREMEIERDLLTSPKDDLEFSIVRENIREKLKTICDRVVVKPHKSVRKLARVQHLYSQLAGQLKREDDEFNILTALHPTPAVCGCPVEEARLLIKQIESFDRGMYAGPIGFFGGGESEFSVGIRSALVEKGLGALIYAGTGIVSGSNPSSEWNELELKISQFTKSLEHESALQPIN
|
Isochorismate synthase involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity.
|
Q9M9V6
|
Q96T23
|
RSF1_HUMAN
|
p325 subunit of RSF chromatin-remodeling complex
|
Homo
|
MATAAAAAAVMAPPGCPGSCPNFAVVCSFLERYGPLLDLPELPFPELERVLQAPPPDVGNGEVPKELVELHLKLMRKIGKSVTADRWEKYLIKICQEFNSTWAWEMEKKGYLEMSVECKLALLKYLCECQFDDNLKFKNIINEEDADTMRLQPIGRDKDGLMYWYQLDQDHNVRMYIEEQDDQDGSSWKCIVRNRNELAETLALLKAQIDPVLLKNSSQQDNSSRESPSLEDEETKKEEETPKQEEQKESEKMKSEEQPMDLENRSTANVLEETTVKKEKEDEKELVKLPVIVKLEKPLPENEEKKIIKEESDSFKENVKPIKVEVKECRADPKDTKSSMEKPVAQEPERIEFGGNIKSSHEITEKSTEETEKLKNDQQAKIPLKKREIKLSDDFDSPVKGPLCKSVTPTKEFLKDEIKQEEETCKRISTITALGHEGKQLVNGEVSDERVAPNFKTEPIETKFYETKEESYSPSKDRNIITEGNGTESLNSVITSMKTGELEKETAPLRKDADSSISVLEIHSQKAQIEEPDPPEMETSLDSSEMAKDLSSKTALSSTESCTMKGEEKSPKTKKDKRPPILECLEKLEKSKKTFLDKDAQRLSPIPEEVPKSTLESEKPGSPEAAETSPPSNIIDHCEKLASEKEVVECQSTSTVGGQSVKKVDLETLKEDSEFTKVEMDNLDNAQTSGIEEPSETKGSMQKSKFKYKLVPEEETTASENTEITSERQKEGIKLTIRISSRKKKPDSPPKVLEPENKQEKTEKEEEKTNVGRTLRRSPRISRPTAKVAEIRDQKADKKRGEGEDEVEEESTALQKTDKKEILKKSEKDTNSKVSKVKPKGKVRWTGSRTRGRWKYSSNDESEGSGSEKSSAASEEEEEKESEEAILADDDEPCKKCGLPNHPELILLCDSCDSGYHTACLRPPLMIIPDGEWFCPPCQHKLLCEKLEEQLQDLDVALKKKERAERRKERLVYVGISIENIIPPQEPDFSEDQEEKKKDSKKSKANLLERRSTRTRKCISYRFDEFDEAIDEAIEDDIKEADGGGVGRGKDISTITGHRGKDISTILDEERKENKRPQRAAAARRKKRRRLNDLDSDSNLDEEESEDEFKISDGSQDEFVVSDENPDESEEDPPSNDDSDTDFCSRRLRRHPSRPMRQSRRLRRKTPKKKYSDDDEEEESEENSRDSESDFSDDFSDDFVETRRRRSRRNQKRQINYKEDSESDGSQKSLRRGKEIRRVHKRRLSSSESEESYLSKNSEDDELAKESKRSVRKRGRSTDEYSEADEEEEEEEGKPSRKRLHRIETDEEESCDNAHGDANQPARDSQPRVLPSEQESTKKPYRIESDEEEDFENVGKVGSPLDYSLVDLPSTNGQSPGKAIENLIGKPTEKSQTPKDNSTASASLASNGTSGGQEAGAPEEEEDELLRVTDLVDYVCNSEQL
|
Regulatory subunit of the ATP-dependent RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, which form ordered nucleosome arrays on chromatin and facilitate access to DNA during DNA-templated processes such as DNA replication, transcription, and repair . Binds to core histones together with SMARCA5, and is required for the assembly of regular nucleosome arrays by the RSF-5 ISWI chromatin-remodeling complex . Directly stimulates the ATPase activity of SMARCA1 and SMARCA5 in the RSF-1 and RSF-5 ISWI chromatin-remodeling complexes, respectively . The RSF-1 ISWI chromatin remodeling complex has a lower ATP hydrolysis rate than the RSF-5 ISWI chromatin-remodeling complex . The complexes do not have the ability to slide mononucleosomes to the center of a DNA template . Facilitates transcription of hepatitis B virus (HBV) genes by the pX transcription activator. In case of infection by HBV, together with pX, it represses TNF-alpha induced NF-kappa-B transcription activation. Represses transcription when artificially recruited to chromatin by fusion to a heterogeneous DNA binding domain .
|
Q96T23
|
A6L8V3
|
PTH_PARD8
|
Peptidyl-tRNA hydrolase
|
Parabacteroides
|
MKYLITGLGNIGSEYWGTRHNIGFRVVNHLVESVGGNFTEERYGAIARIRVKNCDLIVLKPNTFMNLSGNAVRYWLQKENIPVENLLIVVDDLALPFGTLRLKPKGSDAGHNGLKNIAQLLNTQEYSRLRFGIGSDFPRGGQIDYVLGKFPPEELQLMPEILDRATEIIKSFCLAGIQITMNQFNNK
|
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
|
A6L8V3
|
A1CL82
|
MCA1B_ASPCL
|
Metacaspase-1B
|
Aspergillus subgen. Fumigati
|
MYHRNSAPPPPGWSGGYPPPQSQWPPHSYQYPPYPPQGPPPPPAHSYSPPPTYGNYPSPYSTPPPHSPSPYQHPQHGHSRSWTNPSLPPRPPRESQSFGKGAPSNYRFQYSECTGRRRALLIGINYIGQPNQLRGCINDVTNMSTFLHERFGYRREDMVILTDDQKNPMSVPTKINILRAMQWLVKDAQPNDSLFIHFSGHGGRTPDLDGDEEDGYDDVIYPVDYRVAGHIVDDEMHNIMVRPLQPGVRLTAIFDSCHSGTALDLPYVYSTQGILKEPNLAKEAAQDLFSALASYGKGDLSGVAMTAIGFLKKAAIGDSARQRTVMTKTSPADVVMFSGSKDTQTSADTFQDGEARGALSWAFIKSQKQRPNQSYLQLLNSIRAELEGKYTQKPQLSCSHPLDVNLLFVM
|
Involved in cell death (apoptosis).
|
A1CL82
|
B5KF96
|
VKT2_CRYNI
|
Kunitz-type serine protease inhibitor nigrescinin-2
|
Cryptophis
|
MSSGGLLLLLGLLTLWEALTPVSSTDRPEFCELPEDSGPCKGLFHVFYYNPDQSQCLEFIYGGCYGNANNFKTIEECKRTCAA
|
Serine protease inhibitor.
|
B5KF96
|
A0A0B4J1N3
|
GP15L_MOUSE
|
Protein GPR15L
|
Mus
|
MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI
|
Has antimicrobial activity against Gram-positive bacteria, including Staphylococcus aureus and Actinomyces spec., and Mycoplasma hominis and lentivirus.
|
A0A0B4J1N3
|
Q6PIY7
|
GLD2_HUMAN
|
Terminal uridylyltransferase 2
|
Homo
|
MFPNSILGRPPFTPNHQQHNNFFTLSPTVYSHQQLIDAQFNFQNADLSRAVSLQQLTYGNVSPIQTSASPLFRGRKRLSDEKNLPLDGKRQRFHSPHQEPTVVNQIVPLSGERRYSMPPLFHTHYVPDIVRCVPPFREIAFLEPREITLPEAKDKLSQQILELFETCQQQISDLKKKELCRTQLQREIQLLFPQSRLFLVGSSLNGFGTRSSDGDLCLVVKEEPCFFQVNQKTEARHILTLVHKHFCTRLSGYIERPQLIRAKVPIVKFRDKVSCVEFDLNVNNIVGIRNTFLLRTYAYLENRVRPLVLVIKKWASHHQINDASRGTLSSYSLVLMVLHYLQTLPEPILPSLQKIYPESFSPAIQLHLVHQAPCNVPPYLSKNESNLGDLLLGFLKYYATEFDWNSQMISVREAKAIPRPDGIEWRNKYICVEEPFDGTNTARAVHEKQKFDMIKDQFLKSWHRLKNKRDLNSILPVRAAVLKR
|
Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs . Does not play a role in replication-dependent histone mRNA degradation . Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs .
|
Q6PIY7
|
C5D8K7
|
TMCAL_GEOSW
|
tRNA(Met) cytidine acetate ligase
|
unclassified Geobacillus
|
MKAVGIIVEYNPFHNGHLYHLEETKKQTGADCIIAVMSGNFLQRGEPALVSKWARTKMALSAGVDIVIELPYAFAVQSAEQFASGAVTLLHSLFCEEICFGSENGNITAFIDAAKTFLEQKQQHDSYVQEALQEGVSYPRANAEAWKRLNATNLDLSKPNNVLGLAYVKAILQKQIPITPRTIRRIASDYHDKTFSHPSIASATSLRKALKGSLAHLETIAPYIPGTTKQTLEQYYDTYGMFHEWEAYFPFLKYRIMTAEEAELRQIAGVDEGIEHRLKQEIVAAPTFSAFMNSIKTKRYTWTRLQRICTHILTNFTKDQRKKTETPTYIRLLGMSSNGRRYLQHVKKHLPLPLVTKVSNLKHDPIYQQEKKASFAYAAIFPEPARTNVLKEEYATPPLLQ
|
Catalyzes the formation of N(4)-acetylcytidine (ac(4)C) at the wobble position of elongator tRNA(Met), using acetate and ATP as substrates. First activates an acetate ion to form acetyladenylate (Ac-AMP) and then transfers the acetyl group to tRNA to form ac(4)C34.
|
C5D8K7
|
B7IDS3
|
MIAA_THEAB
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Thermosipho
|
MKYTIISGPTAVGKTDIVLEIASQINANIISVDSRQIYKLMDIGTAKPSKEEKSKVTHYLIDHIYPDEYYNAFLFRQDALKIRDKLVNEGIVPLFVGGTGLYIDSLVRGFFEGVPKDEKLRKELSEMEKNEPGILRSMLEKYDPQAAQKIHPSDIKRTIRALEVYFKTGKKISQLQTQSEYSKDYKILVLDRYRDELYERINLRVDKMIKEGLVDEVKSLLEKYPKDLNAFQTIGYKEIIRYLENTYDLNTAVHLIKKNTRHYARRQIIWLRRYKQAKWINLSEISRKKAIEEIKKFILEV
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
B7IDS3
|
Q7NAD3
|
DNAA_PHOLL
|
Chromosomal replication initiator protein DnaA
|
Photorhabdus
|
MSLSLWQQCLARLQDELPATEFSMWIRPLQAELSGNTLALYAPNRFVLDWVREKYINNINGLLNDFCGAEVPLLRFEVGNKPVSQNDSPPQRVVTHTPVAPAPQNTSVRPSWDNTAVQPELSYRSNVNPKHTFDNFVEGKSNQLARAAARQVADNPGGAYNPLFLYGGTGLGKTHLLHAVGNSIMARKANAKVVYMHSERFVQDMVKALQNNAIEEFKRYYRSVDALLIDDIQFFANKERSQEEFFHTFNALLEGNQQIILTSDRYPKEINGVEDRLKSRFGWGLTVAIEPPELETRVAILMKKADENEIQLPGEVAFFIAKRLRSNVRELEGALNRVIANANFTGRAITIDFVREALRDLLALQEKLVTIDNIQKTVAEYYKIKVADLLSKRRSRSVARPRQMAMALAKELTNHSLPEIGDAFGGRDHTTVLHACRKIEQLREESHDIKEDFSNLIRTLSS
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q7NAD3
|
A4WE41
|
IDI_ENT38
|
Isopentenyl pyrophosphate isomerase
|
Enterobacter
|
MSIQEHVILVNDQGEVVGTQEKYAAHTSHTSLHLAFSSWLFNDRGQCLVTRRALSKIAWPGVWTNSVCGHPQIGETTEQAIARRCRFEVGVEIAQLTPIAADFRYCEIDPSGIVENEICPVFAAQIVSPLKVNPDEVMDYQWVELTSLLRALEATPWAFSPWMVSEAANASEKLKHFADNVKA
|
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
|
A4WE41
|
P52827
|
RM12_CRICR
|
P2A1
|
Cricetus
|
MLPAAAAAASLWAPRLGLRGARLRLARQQVPGVCAARQLSSSSQRRSEALAGAPLDNAPKEYPPKIQQLVQDIASLTLLEISDLNELLKKTLKIQDVGLMPMGGMMPGAVPAAAAAAPEVAEGEDILKQKERTHFTVRLTEAKPVDKVKLIKEIKNYVQGINLVQAKKLVESLPQEIKANVAKAEAEKIKAALEAVGGTVVLE
|
As a component of the mitochondrial large ribosomal subunit, it plays a role in mitochondrial translation. Associates with mitochondrial RNA polymerase to activate transcription.
|
P52827
|
A3MZ76
|
END4_ACTP2
|
Endonuclease IV
|
Actinobacillus
|
MKYIGAHVSASGGVENAVLRAVEIGANAFALFTKNQRQWKALALKADTIEKFKRFCKAHQFSPEHILPHDSYLINLGNPEAENLAKSREAFIDEMERANQLGLKLLNFHPSAHLNKISESECLARIAESINIAVDKVPNVIAVIENTAGQGSNLGYRFEHLAEIIDQVEDKNRVGVCLDTCHLFSAGYDISSLESCEQTFSEFERTVGFQYLRGMHLNGSKTPLGSRVDRHHTLREGTIGTDFCKFIMQDDRFDNIPLILETIQPEIWTEEIKFLRTLAK
|
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.
|
A3MZ76
|
Q9UBC7
|
GALP_HUMAN
|
Galanin-like peptide
|
Homo
|
MAPPSVPLVLLLVLLLSLAETPASAPAHRGRGGWTLNSAGYLLGPVLHLPQMGDQDGKRETALEILDLWKAIDGLPYSHPPQPSKRNVMETFAKPEIGDLGMLSMKIPKEEDVLKS
|
Exhibits potent and dose-dependent vasoconstrictor and anti-edema activity in the cutaneous microvasculature, a physiologic effects which does not appear to be mediated via GALR1 or GALR2. Exhibits antimicrobial activity against Gram-negative bacterias, inducing bacterial membrane blebbing .
|
Q9UBC7
|
P45891
|
ACTY_DROME
|
Actin-like protein 53D
|
Sophophora
|
MSSEVDSNSHHAAVVIDNGSGVCKAGFSPEDTPRAVFPSIVGRPRHLNVLLDSVIGDSVIGEAAARKRGILTLKYPIEHGMVKNWDEMEMVWQHTYELLRADPMDLPALLTEAPLNPKKNREKMTEIMFEHFQVPAFYVAVQAVLSLYATGRTVGIVVDSGDGVTHTVPIYEGFALPHACVRVDLAGRDLTDYLCKLLLERGVTMGTSAEREIVREIKEKLCYVSMNYAKEMDLHGKVETYELPDGQKIVLGCERFRCPEALFQPSLLGQEVMGIHEATHHSITNCDMDLRKDMYANIVLSGGTTMFRNIEHRFLQDLTEMAPPSIRIKVNASPDRRFSVWTGGSVLASLTSFQNMWIDSLEYEEVGSAIVHRKCF
|
Required for optimal embryo development, particularly under heat stress conditions . Also appears to have a role in negatively regulating spermatocyte cyst development . Under heat stress conditions, required for the correct organization and migration of nuclei during early embryogenesis, and therefore possibly functions by regulating embryonic actin networks during the heat stress response .
|
P45891
|
B8DE49
|
ERA_LISMH
|
GTPase Era
|
Listeria
|
MSEPFKSGFVAIVGRPNVGKSTLLNHIIGQKIAIMSDKAQTTRNKVQGVYTTDESQIIFIDTPGIHKPKHKLGDFMVKIALNTFQEVDLIYFVIDASTGFGRGDEFIIEKLKNVQTPVFLLINKIDLIAPEDLFKLIEQYRDLMEFDEIIPISALQGNNVPNLLEQTNANLEIGPMYYPKDQITDHPERFIISELIREQVLQLTREEVPHSVAVVIEGIEKNPKTEKLTINATIIVERSTQKGIIIGKQGQMLKQIGMRARKEIERLLGSKVFLEVWVKVQKNWRDKEHYLQDYGFDREEY
|
An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
|
B8DE49
|
F8S108
|
VM34_CROAD
|
Snake venom metalloproteinase 7
|
Crotalus
|
MIQVLLVTISLAVFPYQGSSVILESGNVNDYEVVYPRKVTALPKGAVQPKYEDTMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPTVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLPDSEAHAVFKYENVEKEDEAPKMCGVTQNWESYEPIKKASQSNLTPEQQRYLNAKKYVKLFLVADYIMYLKYGRNLTAVRTRMYDIVNVITPIYHRMNIHVALVGLEIWSNTDKIIVQSSADVTLNLFGNWRATDLLRRKSHDNAQLLTGINFNGPTAGLAYLGGICNTMYSAGIVQDHSKIHHLVAIAMAHEMGHNLGMDHDKDTCTCGTRPCVMAGALSCEASFLFSDCSQKDHREFLIKNMPQCILKKPLKTDVVSPAVCGNYFVEVGEECDCGSPRTCRDPCCDATTCKLRQGAQCAEGLCCDQCRFKGAGTECRAAKDECDMADVCTGRSAECTDSFQRNGQPCKNNNGYCYNGKCPIMADQCIALFGPSATVSQDACFQFNREGNHYGYCRKEQNTKIACEPQDVKCGRLYCFPNSPENKNPCNIYYSPNDEDKGMVLPGTKCADGKACSNGQCVDVTTPY
|
Snake venom metalloproteinase that impairs hemostasis in the envenomed animal.
|
F8S108
|
A3NTZ5
|
UPPP1_BURP0
|
Undecaprenyl pyrophosphate phosphatase 1
|
pseudomallei group
|
MSLWFLVFLSVLQGVTELFPVSSLGHTLLVPALFGMHIDKHAPQLLPFLVALHLGTALALLWYFRERWIALIAGFFASLNGRKNDEGHLMWALIIGTIPTGLVGLLLEKRIERVFHDLRIVAAALIINGVLLWLGDRIQRARAHRPPEKLTFKQAFFVGLAQVGALIPGFSRSGLTMIAGNAAGLTADKAAEFSFLLGTPIIFAAGLLELPKLFHAPDQLADALLGGVLTAIAAYLSVRFLMRYFEGRGRLASFGLYCVLAGLFCLGWFMFHAQPV
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A3NTZ5
|
Q6WNQ9
|
C81E9_MEDTR
|
Cytochrome P450 81E9
|
Medicago
|
ALFYYSLLSLSFIITIKILLKITSRRLKNLPPGPPTIPIIGNLHHLKHPLHRTFTTLSQTYGDIFSLWFGSRLVVVVSSPSLAHECFTKNDIILANRPRFLTGKYIFYNYTTLGSASYGDHWRNLRRITTIDVLSNNRLNSFLGVRRDETNRLIQKLLKDVVSEGFGFTKVELRPRLTEMTFNAMMRMISGKRYYGDDGDVSDVEEAKQFREIISEMMSLLGANNKGDFLPLLRVVDLDNLEKRCKRIAKRSNAFLEGLIEEHRRGNIHSDGGTMIDHLLKLSESQPEYYSDHLIKGLIQGMLLAGTDTSAVTIEWVMSELLNHPEVLKKAKEELDTQIGKNKLVDEQDLSKLPYLQNIISETLRLHPPAPLLLPHYSSEDCTIGEFNVPKDTIILTNVWGIHRDPKHWNDALSFKPERFEKEEEVNKVMAFGLGRRACPGLSLAQRTVGFTVGLLIQCFEWERESEEKLDMMEGKGITMPMKIPLRAMCKALPIANDVTK
|
Involved in the biosynthesis of the pterocarpin phytoalexins. Acts on isoflavones with a 4'-methoxy group on the B-ring, such as biochanin A, formononetin and 2'-hydroxyformononetin. Has a low activity with daidzein and pseudobaptigenin, and no activity with the 7-O-methylated isoflavonoids isoformononetin and prunetin.
|
Q6WNQ9
|
Q05587
|
POCR_SALTY
|
Regulatory protein PocR
|
Salmonella
|
MISASALNSELINKIAQDFAQATGLAVVVVNIHGDEISELFNFTPFCQLMRQHPQHSTRCRMSDRCGGLEASKSDQPCIYRCHAGLTDFSIPLVIAGHLVGFVLCGQVRLSNDVELVNILNVDDRWQADPELLNEFRNVPEMDYSRVIASADLLKLIVENCLKKQLNFVVIKDNPQQSEANKTTRGPTPHDSKMKKALRYIDAHLSDDLRLEDVASHVYLSPYYFSKLFKKYQGIGFNAWVNRQRMVSARELLCHSDWSIASIARNLGFSQTSYFCKVFRQTYQVTPQAYRQQINENSHPPSL
|
Positive regulatory protein of pdu and cob operons . Positively autoregulates its own expression .
|
Q05587
|
Q6ANB6
|
Y1429_DESPS
|
Nucleoid-associated protein DP1429
|
Desulfotalea
|
MDISKLMQQAKDMQGKMAAIQEDLAKKIITGSAGGGMVEVQVNGQGEILAIKIEDALINTDEKEMLQDLVTAATNDGLRRAKDLSKQEMGQLTGGMNLPDLTNFLS
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q6ANB6
|
A1JRK0
|
AROQ_YERE8
|
Type II DHQase
|
Yersinia
|
MSDKFHILLLNGPNLNLLGTREPEKYGYTTLTEIVSQLEAQAQGMDVVLSHLQSNAEHVLIDRIHQARGNTDFILINPAAFTHTSVALRDALLGVQIPFIEIHLSNVHAREPFRHHSYLSDIAVGVICGLGADGYNFALQAAVNRLSKSN
|
Catalyzes a trans-dehydration via an enolate intermediate.
|
A1JRK0
|
Q82UR9
|
ISPD_NITEU
|
MEP cytidylyltransferase
|
Nitrosomonas
|
MAEFIALIPAAGSGSRMGEDIPKQYRPLASKPMIYHALRTLCSAERIGMVCVVLAPDDTEWARHDWSEFAGKIRVFGCGGATRAESVTNGLKALRAENHVQDQDWILVHDAARPGLSRALVERLLDQLAQDEIGGLLAVPLADTLKRADDTGRVMCTEPRERLWQAQTPQMFRTKLLLEALEKAPTGITDDASAVEALGFSPKLVTGDAYNFKVTYPQDLKLAELILQERTATQN
|
Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q82UR9
|
Q6FVY2
|
MTNA_CANGA
|
Translation initiation factor eIF-2B subunit alpha/beta/delta-like protein
|
Nakaseomyces/Candida clade
|
MNALRAIDFKRDDPNNVSVSVLDQLLLPYTTKYIPIYTIDDGFTVIKKMQVRGAPAIAIVGALSVLMESQLLLSEGFCKTQYYYNLNDWENIRSKIDERLAFLLSSRPTAINLSNALDEIKIVLDSASDLQTFKNNLFDYVCKLIDDDFANNKRMGDNGAEFLLNLLKKENFNEDFAVFTICNTGSLATSGYGTALGVIRSLWNDSKSKTQEGNPNKKVKLTESSPKMVQVFPLETRPYNQGSRLTAYELVHDDIPATLIPDSSIAYKIMTSKIPIKAAFVGADRIVRNGDTANKIGTLQLAIICKQFGIKFFVVAPRTTIDKVTEEGKDIIVEERNANEFKIVTGSAVDMQTNKPILDEKNEPITAKVGIAPENINVWNPAFDITSFEYIDGIVTEVGVFTKNENGNFDLSALH
|
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
|
Q6FVY2
|
Q9H0S4
|
DDX47_HUMAN
|
DEAD box protein 47
|
Homo
|
MAAPEEHDSPTEASQPIVEEEETKTFKDLGVTDVLCEACDQLGWTKPTKIQIEAIPLALQGRDIIGLAETGSGKTGAFALPILNALLETPQRLFALVLTPTRELAFQISEQFEALGSSIGVQSAVIVGGIDSMSQSLALAKKPHIIIATPGRLIDHLENTKGFNLRALKYLVMDEADRILNMDFETEVDKILKVIPRDRKTFLFSATMTKKVQKLQRAALKNPVKCAVSSKYQTVEKLQQYYIFIPSKFKDTYLVYILNELAGNSFMIFCSTCNNTQRTALLLRNLGFTAIPLHGQMSQSKRLGSLNKFKAKARSILLATDVASRGLDIPHVDVVVNFDIPTHSKDYIHRVGRTARAGRSGKAITFVTQYDVELFQRIEHLIGKKLPGFPTQDDEVMMLTERVAEAQRFARMELREHGEKKKRSREDAGDNDDTEGAIGVRNKVAGGKMKKRKGR
|
Involved in apoptosis. May have a role in rRNA processing and mRNA splicing. Associates with pre-rRNA precursors.
|
Q9H0S4
|
P58204
|
FLGI_CERSP
|
Basal body P-ring protein
|
Cereibacter
|
MRRALLLAALLACAPPAFADRLKDLTTVAGVRSNPLVGYGVVVGLSGTGDGNSQLTQQSMQSLISRLGLSVETGDLKAKNAAAVMVTADLPPFLKIGQTLDVTVSTVGQAKSLKGGTLLMTPLMGADGEVYAIAQGNLVVGGLGVEGKDGSSLTVNIPTVGRVPRGGMVEKMVETPFLETDHLVLNLNRGDFSTAAAVAEGVNRTFGPDVAVALDGTSIRVRAPADPAQRVSFMSLLENVEVDPAPPVARVVVNARTGTVVIGGTVKVTPAAVTHGSLTVRVTEDQRVSQGASVVVGNNATVVAPGEPVVTPDSQVQVVEEPAKAFVFDPGVSLSSLVDAINAVGASPSDLVAILEALREAGALRAELVVI
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
P58204
|
A6LJ30
|
CH60_THEM4
|
Chaperonin-60
|
Thermosipho
|
MAKMLRFSEEARRALERGVDAVADAVKITLGPKGRNVVIEKSWGSPTITNDGVSIAKEIELEDKFENLGAQLVKEVASKTNDVAGDGTTTATVLAQAMIKEGIKNVTAGANPILVKRGIDKAVAAAVEKIKDISKKLSNSDDIAHVASISANSEEIGKLIAEAMEKVGEDGVITVEDSKSIDTFVEFTEGMQFDRGYISPYFVTDPEKMEVVYNEPFILITDRKLSNIKPLIPILEKVAQTGKPLVIIAEDVEGEALTTLVLNKLKGTLNTVAVKAPGFGDRRKAMLQDIAILTGGIVASEEVGINLEDLTLNDLGRADVVRVKKDETIIVGGHGDQEEIKKRIAQIKAQIEQTTSEYEKETLQERMAKLAGGVAVIKVGAATETELKEKKHRIEDALSATRAAVEEGIVPGGGITLLRARKPVEKIVEELDGDEKIGAKIVYEALSAPINQIAKNAGYDGAIIIHKVLEQDDPAYGFDALKGEYCDMFERGIIDPAKVTRSALQNAASIAGMLLTTEVLVVEKPEPKNNNPMPEMPEY
|
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.
|
A6LJ30
|
F4JTU7
|
RLP48_ARATH
|
Receptor-like protein 48
|
Arabidopsis
|
MHSCSERRMMTVIWSLCLIFCLSNSILAIAKDLCLPDQRDALLEFKNEFYVQEFDPHMKCEKATETWRNKTDCCSWNRVSCDPKTGKVVELDLMSSCLNGPLRSNSSLFRLQHLQSLELSSNNISGILPDSIGNLKYLRSLSFRTCHLFGKIPSSLGSLSYLTHLDLSYNDFTSEGPDSGGNLNRLTDLQLVLLNLSSVTWIDLGSNQLKGMLPSNMSSLSKLVSFDISENSFSGSIPSSLFMIPSLNFSGPLEIGNISSHSELGYLYMGENNFNGPIPGSLSKLVGLRDLSLSFWNTGRGIVDFSIFLHLKSLCSLDLSYLNTRSMVDLSFFSHLMSLDELDLSGINLKISSTLSFPSATGTLILASCNIVEFPKFLENQTSLFYLDISANHIEGQVPEWLWRLPTLSFVNIAQNSFSGELPMLPNSIYSFIASDNQFSGEIPRTVCELVSLNTLVLSNNKFSGSIPRCFENFKTISILHLRNNSLSGVFPKEIISETLTSLDVGHNWLSGQLPKSLIKCTDLEFLNVEDNRINDKFPFWLRSLSNLQILVLRSNEFYGPIFSLEDSLSFPKLRIFDISENHFTGVLPSDYFAGWSAMSSVVDIFDTTPQVHILGVFQGYYHNSVVLTNKGLNMELVGSGFTIYKTIDVSGNRLEGDIPESIGILKELIVLNMSNNAFTGHIPPSLSNLSNLQSLDLSQNRLSGSIPPELGKLTFLEWMNFSYNRLEGPIPQATQIQSQNSSSFAENPGLCGAPFLNKCGGEEEEEEEATKQEEDEDEEKEEKNQVFSWIAAAIGYVPGVFCGLTIAHILTS
|
Plays a role in root hair development.
|
F4JTU7
|
Q9EQ21
|
HEPC_MOUSE
|
Hepcidin
|
Mus
|
MALSTRTQAACLLLLLLASLSSTTYLHQQMRQTTELQPLHGEESRADIAIPMQKRRKRDTNFPICIFCCKCCNNSQCGICCKT
|
Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma. Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes.
|
Q9EQ21
|
Q3BVV6
|
RNC_XANC5
|
Ribonuclease III
|
Xanthomonas
|
MSNRTFQRGDPIGHAFADPALLARALRHRSAGTPHNERLEFLGDGIVNLLIAEALYQRWPKADEGALTRARAELVREGALAVIGRTLNLGERLTLGPGELKSGGHRRDSILADAVEAIVAAIYLDCGFERCRAVVLPWFEASLAALPVGKAEKDPKTRLQEWLQARQLPLPTYALISESGDEHAKQFHVACILEQPVARAEGQGTSRRLAEQQAATLVIAQLDSNT
|
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.
|
Q3BVV6
|
A7MNZ1
|
RL20_CROS8
|
50S ribosomal protein L20
|
Cronobacter
|
MARVKRGVIARARHKKILKQAKGYYGARSRVYRVAFQAVIKAGQYAYRDRRQRKRQFRQLWIARINAAARQNGISYSKFINGLKKASVEIDRKILADIAVFDKVAFSALVEKAKAALA
|
Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
|
A7MNZ1
|
Q2YSS2
|
GRAR_STAAB
|
Glycopeptide resistance-associated protein R
|
Staphylococcus
|
MQILLVEDDNTLFQELKKELEQWDFNVAGIEDFGKVMDTFESFNPEIVILDVQLPKYDGFYWCRKMREVSNVPILFLSSRDNPMDQVMSMELGADDYMQKPFYTNVLIAKLQAIYRRVYEFTAEEKRTLTWQDAIIDLSKDSIQKGDDTIFLSKTEMIILEILITKKNQIVSRDTIITALWDDEAFVSDNTLTVNVNRLRKKLSEISMDSAIETKVGKGYMAHE
|
Member of the two-component regulatory system GraR/GraS involved in resistance against cationic antimicrobial peptides (CAMPs). Upon phosphorylation by GraS, functions as a transcription regulator by direct binding to promoter regions of target genes such as adhesins, exoproteins, transporters, toxins, and proteins involved in cell wall synthesis. Down-regulates the expression of many genes involved in RNA and amino acid synthesis or glycolysis.
|
Q2YSS2
|
Q6Q883
|
SIRP_LEPMC
|
Sirodesmin biosynthesis protein P
|
Leptosphaeria maculans species complex
|
MHITKDIDTIFHRSLEGLTGDDHSPESRRDFPMSQSSGCRNGTDATVCHIFERIASQFPESVAAEDGGRNITYGELHYASNHLANHLSQIGIQSGQKIVIISNRSLEMIVALLGIMKSGACVVPIDFETWSQDRIQTTLETTQCRYAISTKCIEIPNQELILFQEGDLQHVLDNRRDQPASFSTRGFQLPSADDLAYTIFTSGTTSKPKGVMVPHSAIAHYVQQVSDEAPFNLNVQASSRVLLVFSVAFDACLGVVLSTICNGGTLILATSMNFATVATTCTILPLTPTILSTLRPGAEYDSIKSIFLGGESPSPNLLRPWLNGERRIFNCYGPTETTCTSLIKEVLPDEPNHLRYTVAGSSVVLLDGNLREVSEGEIAISGPGLAVGYFNNQALTAEKFIVYKGVRHYLTGDYGRKTSFGIDFLGRKDRVVKNRGFLINLEAEVEAVITNMKLANSAAALMHEGRLIMFVTPETIDVSSLRSRLLEIRDSFLVPDRIYAICSFPITSNGKVDLASLRQLLQEEKFTGVATHQSSPSSNLYVVLEGFSKVLGLPPSALCGSSSFLDNGGNSLSAVSLASHLRERGLSITVREIFESDTAQRICDTLSATILSTSDSEEADLESLRENVVRAGYPLTPRMEVAYMTAIQVNMIQSTIKMPSMNYIQLSITFDLSSGLFKPEVFRRAWEIIVQRHSILRATFIPALEATVIAADPTMDWREQLVDSSEWDSAVADAREKILCSMAPLDAEYLKPRSIFRLITEPKSRTEFIWTIHHSLVDGWSIAVIMRDLQCILSQEELPKVAQFTSVATVQKALAQRSLSRGKQQSWEEKMQNYIPAPRLRLPKPQGWARAARAERRQLLGVHRSQVQRFVQEYRVSDASIFLASWALVLSKYLSTDRVLFGVVLSGRNLPMAAVDQVVGPLLDTVPFPVNTTSTQSTAEFLRTIHGTLHEMNESPWEMKLQKSSMGPESLETLVALQYDLPDSTWNVDPKTWPSPQSMKHNETTELPLHILIDMQNGGDLEARYLYDCSHFEAAMIDQMLSHFSNMLKAILMHPTVELVKSSMMNQLEINDLLYSSPHMHDAYDGPQSLKQAFEEVVDTWPDAIAVESVSDSISYKELDHRSSAISNALLPLVGPGQIVGILSDGSVSWITAILAVLKAGAAYCPIDIALPEERIKVMLRESRCSLLLCTTEDLCELWANHSDLTCFSIGRLLSETLQTPERLPERCSPHDPAAVIFTSGSTGVPKGILLEHIGILSLLDFPNARLRSGPGRRNAQFLSLGFDCCVNEVFATLCYGATLVLRDPLDPVQHIKRVHATMCTPSFLATLDVNDFPNLELIALAGEPVPQKLVDTWGHNRVLLNVYSPSECTISTVYPQLYPGVQVTLGSPVPRQAIYILDKDLNPVPVGVPGEICISGIQVTRGYLNRPEETLVKFLPNPFQKGWRLYRSGDLGRLTNSHEIEYIGRIDNQVKVRGFRIELEEIESTIAALNPEVRQAAVIVVNDVLIGFVTPSSLDTLAIQAIISRHLPSYCRPSYFVALDNMPMSSNQKIDRKKLVSMKAERNHFTKVPIEGTTERIIQEIWKDLIPELGEVSALDNFLQIGGHSLLQARLTRQLGMALGNRIPLRIVIQNPVLRDLALAIDKHILDGGSEDISRGQPEQNTVLSHLEEEMYTVHMLSSEPSAWNIPYIARLTGPLNLAAFEASWNNIIRSNSILRARYQIKDGILTRSISTSISPVTRRYCKVTDDALLDIVNRAFDLANDQPIRLDLCLDRPTMSYVVLNMSHMIGDRSTMGEILRLLEEEYAQMILNDNFNLHEPLSESLPYSVWTAMRRKREVDAGLTHVLQKSLNPSLINPPLFGTFKQELACSAHRDKRIEGDLFSSLKNLRGRFKASGHQLAIAAIGLTLHRLSHREDFIIAAPIEDRTEAGTENMFGLFLDRLLIPLRFNLHSPHSADDLIHMVKSASEQAMANYIPFADLKNVLGMVGKSHSLCEIMVTYHASDLQGPNLTGVDALGIPVQPKGVKFPLMLEFSEFPESIGIDLAYDSHAIDNATMDEFEVQLMAAFRYLADETCSSTCTTYPPRLFPLIWSQKDTNTVAPISEDQEMIDLVREAMAECVGLNRCDISCSRSFFELGGSSVDCLRLQDRLIKSGVSVSLSSIIHLQTAELIAGAVE
|
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyrosine (L-Tyr) in the presence of dimethylallyl diphosphate (DMAPP) to yield 4-O-dimethylallyl-L-Tyr, and therefore represents probably the first pathway-specific enzyme in the biosynthesis of sirodesmin PL . 4-O-dimethylallyl-L-Tyr, then undergoes condensation with L-Ser in a reaction catalyzed by the non-ribosomal peptide synthase sirP to form the diketopiperazine (DKP) backbone . Further bishydroxylation of the DKP performed by the cytochrome P450 monooxygenase sirC leads to the production of the intermediate phomamide . This step is essential to form the reactive thiol group required for toxicity of sirodesmin PL . The next steps of sirodesmin biosynthesis are not well understood yet, but some predictions could be made from intermediate compounds identification . Phomamide is converted into phomalizarine via oxidation, probably by sirT . Further oxidation, methylation (by sirM or sirN) and reduction steps convert phomalizarine to deacetyl sirodesmin . Finally, acetyltransferase sirH probably acetylates deacetyl sirodesmin to produce sirodesmin PL .
|
Q6Q883
|
Q8K9L5
|
RSMC_BUCAP
|
rRNA (guanine-N(2)-)-methyltransferase RsmC
|
Buchnera
|
MIFSKNSQLILRHQKIFKNKIVFFSGNIEDELPINLLTIKTKIHLQKSQNFLKINNNKNITFYRKLLVSQDTVQDCNILIYYWPKNKSEARFQLFNILSFLPIKSEIFIVGSNSSGVKSAKLILEESIKLKKIDNANHSILMSGILINKTKFKLEKFFKIHIWKNLIIKSLPGVFGHKKIDEGSKFIASTFSEKINGKILDVGCGSGFLSVSILRKSPKCVVTMIDRKLSALESSKATLDANFFKGEVLSSNIYSNIFKKFNMIVSNPPLHDDLKINFDITKKIIFNSKKHLKKNGELRFVTNHCFSYDFYLKKVFSEFHIMKKDNKYKVYQAFLK
|
Specifically methylates the guanine in position 1207 of 16S rRNA in the 30S particle.
|
Q8K9L5
|
Q2JSF1
|
AROA_SYNJA
|
5-enolpyruvylshikimate-3-phosphate synthase
|
unclassified Synechococcus
|
MLTTASSADILTLSPARGLRGQVSIPGDKSISHRALMLGSLAEGETVIHGLSLGEDPRSTAACFRALGADIPELNSECVRIQGVGLDRLQEPAEVLDAGNSGTTLRLMLGILAGQAGRFFAVTGDRSLRSRPMGRVVEPLRQMGANIWGRAGGNLAPLAVQGGSLKGIHYHSPVASAQVKSCLLLAGLLAEGTTQVTEPALSRDHSERMLRAFGAEISVDVAAKTVAVVGGSRLVGQTVQVPGDISSAAFWLVAASIVPESELLLQDVGLNPTRTGVLQVLQEMGADIQVEKRREVAGEPLGDLRVRSARLRGCSIAGDLIPTLIDEIPVLAVAAAFAEGTTVIRDAAELRVKESDRLAAIAQELSRMGAQVTEYPDGLEIKGGIPLQGAEVDSHADHRIAMSLMVAALAAQGSTTLRGADCARISYPDFIPTLQRLINPSSAS
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q2JSF1
|
Q2U696
|
DOT1_ASPOR
|
Histone H3-K79 methyltransferase
|
Aspergillus subgen. Circumdati
|
MVLARFANESTSYNRYNLVVPRDKDDFRPIDDIFQVIETVSQNYIPEDEADYFDNESTGIKRRLRRALAHASEAEFRNVVTDYNEAIERLRRDGSIAQKLDSTHRLNLPLVERILTQIYSRTVSPRVESLRQYENGTDNVYGELLPRFISTIFKETGLKSGQVFVDLGSGVGNVVLQAALEIGCESWGCEMMQNACELAELQQTEFRARCRLWGIAPGKTHLVRGDFLKEQSIIDVLKRADVILINNQAFTPQLNNELINHFLDMKEGCQIVSLKSFVPAAHKIQSRNLNSPINLLKVKQREYWSNSVSWTDVGGTYFIATKDSSRLRAFAESMG
|
Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone.
|
Q2U696
|
Q8HY68
|
CRBA2_MACFL
|
Beta-A2 crystallin
|
Macropus
|
MSGTLSQGSSPARLTLWEEENFQGRRCELMSDCSSIRELSGFRRVRSVKVESGAWVGFEYPDFQGQQFILEKGDYPRSTAWSGSSGYRTDQLLSFRPLLCANHSDSRVTLYEGENFQGCKFELSDDYPSLPAMGWASKDVGSLKVTSGAWVGYQYPGFRGYQYVLEQDRHSGEFRKYSEFGTQAHTNQLQSIRRVQH
|
Crystallins are the dominant structural components of the vertebrate eye lens.
|
Q8HY68
|
Q6NKQ9
|
PDLP8_ARATH
|
Cysteine-rich repeat secretory protein 15
|
Arabidopsis
|
MRRLFLFSLLFLFFYSSSSSRSSSESHIFIYGGCSPEKYTPNTPFESNRDTFLSSVVTSSSDASFNSFAVGNDSSSSSSSSAVFGLYQCRDDLRSSDCSKCIQTSVDQITLICPYSYGASLQLEGCFLRYETNDFLGKPDTSLRYKKCSSKSVENDYDFFKRRDDVLSDLESTQLGYKVSRSGLVEGYAQCVGDLSPSDCTACLAESVGKLKNLCGSAVAAEVYLAQCYARYWGSGYYDFSSDPTNGDHVGKSIAIIVGVIAGFAILVVLLSLCRNSMH
|
Modulates cell-to-cell trafficking.
|
Q6NKQ9
|
Q3AB86
|
DXR_CARHZ
|
2-C-methyl-D-erythritol 4-phosphate synthase
|
Carboxydothermus
|
MKKLVILGSTGSIGRQSLEVIEFFPDKFSVVALAAAKNGKLLLEQCLRFKVKHAFLADEESYKTYYQEFKNHGILLTTGSKELLNLALLPGVDGIITAIPGTICLLPTIEALKAGKIIYLANKETMVAAGEIITPLMKLGENLLPVDSEHSAIFQALRGEKLAWVKKLLITASGGPFREYTLEQLKNVTVAEALKHPRWKMGNKITIDSATLMNKGLEIIEAHFLFQIPYEKIEPVIHPQSVIHSLVEFYDGSVLAQLGLPDMRHPIQYALTYPERFPNNLPGLNLTEIGVLSFEKPDYERFPALKLAIQAGKAGNIYPAVLNAANEIAVEAFLAGKIKFLEIAQIVEKVLNCFSPVKMDLETILEVDFRARELARKFIGGEHQ
|
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
|
Q3AB86
|
O79876
|
COX1_PIG
|
Cytochrome c oxidase polypeptide I
|
Sus
|
MFVNRWLYSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNQAWAKIHFVIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTAWNTISSMGSFISLTAVMLMIFIIWEAFASKREVSAVELTSTNLEWLHGCPPPYHTFEEPTYINLK
|
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
|
O79876
|
A0T0Y7
|
RK6_THAPS
|
50S ribosomal protein L6, chloroplastic
|
Thalassiosira
|
MSRIGKLPIKLPTTVEISHQSDATVQVINVKGKFGSLQRTLPEELKIEQIHNDNGSSLIVSFENQTRTNKSLQGLYRTLINNMVIGVTEQFVIILTLQGVGYRASVQGKSLVLNLGYSHPVEIDIPEGITVEVTQNTTLNIKACDKEQLGLFAAKVRAWRPPEPYKGKGILYKNEQILRKAGKSGKK
|
Binds 23S rRNA.
|
A0T0Y7
|
O08664
|
BCL7C_MOUSE
|
B-cell chronic lymphocytic leukemia/lymphoma 7C protein
|
Mus
|
MAGRTVRAETRSRAKDDIKKVMATIEKVRRWEKRWVTVGDTSLRIFKWVPVVDPQEEERRRAGGGAERSRGRERRGRGTSPRGGGPLILLDLNDENSNQSFHSEGSLQKGAEPSPGGTPQPSRPGSPTGPPEVITEDTQPPQLGQERDPGGTPAGGTDEPPKLTKEEPVPELLEAEAPEAYPVFEPVPSVPEAAQGDTEDSEGAPPLKRICPNAPDP
|
May play an anti-apoptotic role.
|
O08664
|
O59456
|
PYRG_PYRHO
|
UTP--ammonia ligase
|
Pyrococcus
|
MTKFIFVTGGVVSGLGKGITSASIGLLMKARGYKTTNIKIDPYINYDAGTMNPYQHGEVFVLDDGGEVDLDLGNYERFLDTNLTFEHNITTGKVYSTVIEKERRGEYLGATVQVIPHITDEIKRRIREIAKDYDIVVVEIGGTVGDIESMPFLEAARQMQLEEGRENVAFVHVTYVPKLKVVGEQKTKPTQHSVKELRSLGIQPDAIVARSEDPLEEEARKKISLFTNVPREAVVSAYDVEDTYEVPLLLEREGLGKYLIKRLKLEDREPDLREWEKMVAKYKALKETVEIAIVGKYVKLTDSYLSIKEALKHASVSNDVKVKIRWIEAEDIEEHGTKLLEGVDGIIVPGGFGARGAEGKIMTIKYARENDIPFLGICFGFQLTVVEFARNVLGMKGAHSTEIDPQTPYPVVDLMPEQRNLEKLGGTMRLGAYPVKIKKGTLAYRLYKKELVYERHRHRWEVNPDYIEAFEKAGLVFSGVAGDDERRMEILELPDKRYFIATQFHPEFKSRPMRPAPVFHGLVRAAKEYKQEKNATN
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Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
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O59456
|
A1TYJ4
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EFG_MARN8
|
Elongation factor G
|
Marinobacter
|
MARKTPIKRYRNIGICAHVDAGKTTTTERILYYTGRSHKMGETHDGASTTDWMEQEQERGITITSAAVTTFWQGMDKQYPEHRINIIDTPGHVDFTIEVERSLRVLDGAVVVFCGSSGVEPQSETVWRQANKYEVPRMVFVNKMDRAGANFMRVVEQIRNRLGATTVPIQLPIGAEDDFEGIVDLLRMKAIYWNEADQGMTYELRDIPESMKAEAEKAREQMIEAAAEANEEYMDKYLEGEELTYEEIKKGLRDRTIANEIVLATCGSAFKNKGVQAVLDAVIEFLPAPDEVKAIRGEVDDEGTEETRPVDDDAPFAALAFKIATDPFVGTLTFFRVYSGKLESGNAVFNSVKGKKERVGRMVQMHANDREEIKEVLAGDIAAAIGLKNVTTGDTLCDENNKIVLERMEFPEPVISVAVEPKSKADQEKMGVALGKLAQEDPSFRVRTDEESGQTIISGMGELHLDIIVDRMRREFKVEANIGKPQVAYRECIRKPVDVEGKFVRQSGGRGQYGHVKVKLEPLPLDDEDGENFIFVNEIVGGVVPKEYIPAVQQGIEEQMQNGCLAGYPLLGIKATLYDGSYHDVDSNEMAFKIAGSMAMKKGALEANPALLEPIMKVEVVTPEDYMGDVVGDLNRRRGLVQGMDEGPAGKVIRAEVPLSEMFGYATDLRSATQGRASYAMEFSRYMEAPSNIAEAIIKKG
|
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
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A1TYJ4
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B0UWM2
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RNPH_HISS2
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tRNA nucleotidyltransferase
|
Histophilus
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MRPNARAINQPRPIKITRHYTKHAEGSVLVEFGETKVICTATVEDSVPRFLKGQGKGWVTAEYGMLPRSTHSRMQREAAKGKQGGRTMEIQRLIARSLRAMVDLEALGERAITLDCDVIQADGGTRTASITGACVALIDAINFLLQNGTLTTNPIKGLVAAISVGIVNGETVCDLEYVEDSIAETDMNVVMMEDGRMIEVQGTAEGEPFSHAELLTLLDLAKQGCEQLFVAQRVALAE
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
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B0UWM2
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Q9ZPN8
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TBB3_ELEIN
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Beta-3-tubulin
|
Eleusine
|
MREILHIQGGQCGNQIGAKFWEVICDEHGIDHTGKYAGDSDLQLERINVYYNEAGGGRFVPRAVLMDLEPGTMDSLRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLATPTFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRSLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSSVCDIPPRGLTMSSTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATAEEEEEYDDDEEEEVAA
|
Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Q9ZPN8
|
O30338
|
UREE_CUPNH
|
Urease accessory protein UreE
|
Cupriavidus
|
MLKIDKLLSAPHGIAPVLVRRAPKLVLPFAERSKSRLRAVLDNGDEAALFLARGTVLRGGDLLVAEDGSFVEVQAAAEAVLEVRAEDPHALMRAAYHLGNRHTPVEIGRDYLRLEYDAVLADMLQRLGVRAERAELPFEPEAGAYGGGHKHGHDATFAEDYAAAQAVFHEHHGHSHSHSHDHVHDEKCGHKH
|
Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
|
O30338
|
Q5M334
|
ILVD_STRT2
|
Dihydroxy-acid dehydratase
|
Streptococcus
|
MEENIVSENNMKHRSSVYDSMVKSPNRAMLRATGMTDDSFEKPIVGVISTWAENTPCNIHLHGFGQIAKEGVKDAGAWPVQFGTITVADGIAMGTPGMRFSLTSRDIIADSIEAAMGGHNVDAFVAIGGCDKNMPGSMIAIANMDIPAIFAYGGTIAPGNLNGKDIDLVSVFEGIGKWNHGDMTAEEVKNLECNACPGPGGCGGMYTANTMATAIEVMGMSLPGSSSHPAESAEKKADIEEAGRAVVKMLEMGLKPSDILTREAFEDAITVTMALGGSTNATLHLLAIAHAANVDLTLEDFNDFQERVPHLADLKPSGQYVFQDLYNVGGVPAVMKYLLKNGFLHGDRITCTGKTVAENLEAFDDLTPGQKVIMPLENPKRADGPLIILKGNLAPEGAVAKVSGVKVRNITGPAKVFDSEEDAIEAVLSDEIVDGDVVVVRFVGPKGGPGMPEMLSLSSMIVGKGQGDKVALLTDGRFSGGTYGLVVGHIAPEAQVGGPIAYLRTGDMVTVDQDTKEITMHVPDEELAKRKAETELPPLYSRGVLGKYAHIVSSASRGAVTDFWNMDKSGKA
|
Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
|
Q5M334
|
Q60880
|
OL141_MOUSE
|
Olfactory receptor 4B
|
Mus
|
MRNITEATFFVLKGLTDNNELQIILFLLFLAIYIFTLIGNVGLIILVVGDSQLHNPMYCFLSVLSSVDACYSTDITPNMLVGFMSKSKIISFYGCATQMFLAVTFGTTECFLLAAMAYDRYVAIHDPLLYAVSMSPRVYIPLIIASYAGGIVHAIIHTVATFSLSFCRSNEVKHIFCDIPPLLAISCSETYVNELLLFFFVSFIELVTILIVLVSYAFILLSILKMNSSEGRRKVFSTCGAHLTAVSIYYGTILFMYVRPSSNYSLEHDMIVSTFYTIGIPMLNPIIYSLRNKDVKEAMKRVLRKKINIKHRIKKLNDFSVFLMP
|
Odorant receptor.
|
Q60880
|
Q255S2
|
RL25_CHLFF
|
General stress protein CTC
|
Chlamydia
|
MELVVTSRETDKKSLLKKIRQTGGIPAVIYSGGKSVANIVVDAHVFSKFLSGLESGALSSTIFSLSYEGRIIRALVKDIQYQVTTYQVIHLDFEELIEDRDVKLNIPIRCINAVDCVGVKLGGSLRQVIRALRVVCKPKDIVPFLELDVRSLGLSQTRKLSDINIPAGLRPITPLKEVVVTVSRR
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
Q255S2
|
Subsets and Splits
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