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TOM1_ASHGO
ID   TOM1_ASHGO              Reviewed;        3258 AA.
AC   Q756G2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase TOM1;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT-type E3 ubiquitin transferase TOM1;
GN   Name=TOM1; OrderedLocusNames=AER304C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 2812.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Probable ubiquitin ligase protein, which may be involved in
CC       mRNA export. E3 ubiquitin ligase proteins mediate ubiquitination and
CC       subsequent proteasomal degradation of target proteins. Participates in
CC       mRNA export from the nucleus by regulating the transport of hnRNP
CC       proteins. {ECO:0000250|UniProtKB:Q03280}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.26;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q03280}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016818; AAS52985.2; -; Genomic_DNA.
DR   RefSeq; NP_985161.2; NM_210515.2.
DR   SMR; Q756G2; -.
DR   STRING; 33169.AAS52985; -.
DR   PRIDE; Q756G2; -.
DR   EnsemblFungi; AAS52985; AAS52985; AGOS_AER304C.
DR   GeneID; 4621374; -.
DR   KEGG; ago:AGOS_AER304C; -.
DR   eggNOG; KOG0939; Eukaryota.
DR   HOGENOM; CLU_000215_0_1_1; -.
DR   InParanoid; Q756G2; -.
DR   OMA; HGLLFQI; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000591; Chromosome V.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd00078; HECTc; 1.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR025527; HUWE1/Rev1_UBM.
DR   Pfam; PF06012; DUF908; 1.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF14377; UBM; 2.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   mRNA transport; Nucleus; Reference proteome; Transferase; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN           1..3258
FT                   /note="Probable E3 ubiquitin-protein ligase TOM1"
FT                   /id="PRO_0000120345"
FT   DOMAIN          2922..3258
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          1582..1603
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1945..1981
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2036..2074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2254..2298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2411..2436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1582..1596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1956..1981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2254..2285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3225
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3258 AA;  372401 MW;  0751CA476D9646A2 CRC64;
     MVVTLTKLER LQKAEKSRTF KPLIDELINC EDAVFVGKLE AIREWDRPKD DLFLWIPVLD
     RMDDMLGKVV AKYKYHTTDC KRHPVKLIEM AKPDEDWVAT LLFFTCRLLN NTSNRSLYSS
     LDMMSDLLNC PNFRVKLGAM KVIATIGERH VVARHRIENS SVLASQHLKK RSLSLALALP
     SSTTDDNSDH FSLVDLFFDK RKYPSKWSQL QYTYYITKKQ AGQQSTQKPS QVSSMKRFVL
     NNEELRFLSL QQIFDRAMND LPSEFWFDFS LQASIAKAFS DDSFENIQLR SLIIQTKFAA
     IAFANAIYIP PQVSSKLFEM DPYAFNNLTD FISLSETKIP KDLRTDALFA LECISLKHVW
     CSDIVRNLGG NMSHGLLFQI LRYIAKVLRE GDEDAVDEEY NVRFFYLISN LADVKALQES
     LISAGLISSL LEIVSTQNSK YKRTLASAAH LLEDVISDAD ATAEFINNNG FNILIQTVTY
     EVNFAVQNPS SAEPPKYSVV YYSISFRQLG FIRSLLKLVL KLLKTDSGDR IRNLIDSPIL
     LAFNKILENR PVFGYTLVSH ALDVVQTIIN TEPTIYQVLV ESGTIPYILQ NFDQFLGPTS
     DLLCMLPEVI SAICLNTDGL KQVKEKNLLK YLFQVIKTPE FAKILSWEDQ AVNYGVALDE
     LARHYPELKP LIEDYFAATV KELPSLTSYT HSYLYESTAG NGEFYLSENE TIIDNEDGAD
     ELAFWEVQES SPIIDCFSGV FYSMASENIS WANLTEKIAF QDFLSVAIPE KPTFDYINSQ
     TLLNFTDVLK MFDDERRSYA LPELLTILDS KFADLEDFLS YDFTKSYVLN EPKDRVVATL
     NKLNVLNVIL YIMTDIYINI TTLFPVRVIQ MMEFFEKNGF NLITNLRKMF QRCVLEEMYI
     RSRLPPAVAE ETISPGISFV PPILIHKDVP LKTEAKQEKT SAKFKNTLET RHLFQKVQSW
     TSMLFRCFLR LTHARKMNVE RYDRALEIRI FDKVVNEIVE MLNLDYLDSH LSYFLVVLDF
     NTHIFTCPKA SLTISDGIVQ TVPTFLFYQA GGFAIYHELI KKLSTRLLGF DGIEAIEKVE
     YVKDQDDILT VGVLMNSIAF MNRCIQLETM ENIRSIAEYY PYDDIYYNLT RALIVPVKIL
     SLGAISEIFS QGEVFDTDRR RIPYSVFKQI LSLLKNIYNS TFELEEGTDV YELRWDLMPI
     SHRKVEMLKS CGISHDVAVG YLEEEKDELP IHVKPDVFSD SEWQRYQEER SSGSWRTNIE
     LLPPQYNGSS TRETLSKMRT EFYQNGFESG ILKILQHYPK LINAISHMFF EMYGELGFSH
     TTMLEDLQDM MNTIPIENTN KLAPVIHLFG IFLNDKNIYD QAKKEIFKFV SYLSMNLHPE
     NVNYSWFSKA LYVYEIIFAK SETPEASPLP ENVTVSFSSI PIIYRISQKD KDIIFNLLIR
     ANEVTDFYSA LAISRILILY TREERYAQEV TQSGILSKLL KVIGANQKFD KINYLESSYL
     LLVRRCFETK EIVTSLIDYE LTRAFTTRAI GDHKEKPRDL PALVNEKASI VMRDPEVFVN
     RISETARFED FNSSKELASL SVRRHMDEKD EEMTSKPLSS EGSNSPITGI VHLLLSQLMA
     AHKRDWVSET PLTPEEENQK NKKKKDEVKV SKNPVCAYMI FLLKVLTELV SSYKQSKFEF
     LTYNKKNVYN ETPKPRATAL NFFLYQLLDT NFQDMDKHEG KRRAMISGLA RDTIIGFVSS
     VQDSETKKVD PKIVDSDMTY IRKFTIEAIS KAIKEAGVSA KTIDANAGKL FGWFHLISSL
     LVVDKGYIFS VLDSNKSSND KYQLCKLLIE MNTPGTITDC MASLDLNYPL TKKLFNSAVE
     PLNALNEVRN NFADLFKLEN NEDEDVEDVE SDKDDVPDMF KNSALGMYDI EDVEDDHDDD
     ENESLIGDDE DIAFVHDEDG LEVVFSEDED ANEDTTDASN SIGSDSEGNS DFGGSGPNVT
     LEVYTDSEDA IEDVNTAAIR ITSGNSAEHS YYSEGEDSAE IEIYEEEYDS EIDIDMDDDS
     ELGSSNWESG LSDLSDSEAY SDEERTNNTG DGFVRWYSDD GVEFEDDTDE EGRGLFTGIQ
     HVFPTEEQLF RVHASGAARS TGRHHHRHGA APFTTSTITL GASQRRPHSI LSNPLGPSGL
     EEVENDIVSH YLGNVETSDR IGLSSIPRLP RVLLFDGELF DDKSSSGILL KSTTARWNDI
     YEMFYDSKVY SNNVVTTIIS RIFEPSAELY LKEQEENAVK ESSRINEPTR RQDERKRKLH
     EIDSDEEHIE EEEEHDEVVE PIEAPGINSP QARAPQEPVY VTIDGEAVNI AGTDMDAEFL
     NALPDDIRAE VFAQHIREYR TQFQGSEGSS RELDAGFLNT IPETLRQEIL AQEVPLERNA
     RPSILGLRNR EGEEFSEVED ESPRFNEQRT ESSKTKTDRV HFAPLLDRSG IAAIMKAVFI
     PQPYLSREIY HELFYRLCSS KQNRSDIMNM LLLILMDGIN DQHSLERVYN LLSNRAASSN
     SGTSKTPQRQ LPPDCTPLIV TNQCIEILQS MVDADSKLKY FFITEHENLL INKSPLKNKK
     DIFSKNMKWP INCILALLEK KVITDEAVLM DLLTRILQVC SKPISSIVKS SKDGKKKKFE
     VPDIEKKYLA SIVSIIKLDS CNTKVFQQTL NLMTNLFAIK DAHETFTTEL CNLAKETIEV
     LVTDLDALAK EVPAVDSGTE VSSEIIQKFT VPSSDQSKLL KVLTAIDYIY VNRKKEEEQV
     VDQLLPLYNK MELGHIWVSL SNCLTRFEEK PRMSTSATIL LPLIESLMVV CKHSKVRETK
     DALLKYEAKK CDFARTPVEN LFFAFTDLHK KLLNEMIRSN PKLMSGPFSL LVKNPKILDF
     DNKRYYFTAQ LRAITHDRPK LSISVRREHV FLDSYRSLFF KSNEDIKISK LEISFKGEAG
     VDAGGITREW YQVLSRQMFN PDYALFIPVA SDKTTFRPNR TSGINPEHLS FFKFIGMIIG
     KAISDQCFLD CHFSREVYKN ILGKPVALKD MESLDLDYYK SLIWILENDI TDIIEETFSV
     ETDDYGEHKV IELIENGAHV AVTEQNKHDY VKKIVEYKLQ TSVKDQMENF LQGFYAIIPK
     DLISIFDEQE LELLVSGLPD IDVDDWKNNT IYVNYTPTCK QINYFWRAVR SFDKEERAKL
     LQFVTGTSKV PLNGFKELSG VNGISKFSIH RDYGSIDRLP SSHTCFNQLD LPAYDSYETL
     RGSLLLAINE GHEGFGIA
 
 
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