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TOM1_NEUCR
ID   TOM1_NEUCR              Reviewed;        4076 AA.
AC   Q9P4Z1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 4.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=E3 ubiquitin-protein ligase TOM1-like;
DE            EC=2.3.2.26;
DE   AltName: Full=HECT-type E3 ubiquitin transferase TOM1-like;
GN   ORFNames=B11B22.010, NCU08501;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB92704.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL356834; CAB92704.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002237; EAA34194.3; -; Genomic_DNA.
DR   PIR; T49799; T49799.
DR   RefSeq; XP_963430.3; XM_958337.3.
DR   SMR; Q9P4Z1; -.
DR   STRING; 5141.EFNCRP00000008460; -.
DR   PRIDE; Q9P4Z1; -.
DR   EnsemblFungi; EAA34194; EAA34194; NCU08501.
DR   GeneID; 3879570; -.
DR   KEGG; ncr:NCU08501; -.
DR   VEuPathDB; FungiDB:NCU08501; -.
DR   HOGENOM; CLU_000215_0_1_1; -.
DR   InParanoid; Q9P4Z1; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; 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   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; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   Coiled coil; mRNA transport; Nucleus; Reference proteome; Transferase;
KW   Transport; Ubl conjugation pathway.
FT   CHAIN           1..4076
FT                   /note="E3 ubiquitin-protein ligase TOM1-like"
FT                   /id="PRO_0000120346"
FT   DOMAIN          3740..4076
FT                   /note="HECT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT   REGION          225..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          748..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          921..970
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1571..1646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1988..2041
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2067..2110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2275..2295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2356..2551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2581..2634
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2782..2817
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2858..2955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3037..3066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3105..3132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3216..3241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3353..3444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          2851..2929
FT                   /evidence="ECO:0000255"
FT   COILED          3341..3375
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        237..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..343
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..765
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..954
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..970
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1643
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1998..2017
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2018..2041
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2082..2096
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2403..2451
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2468..2551
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2581..2596
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2597..2624
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2858..2912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3353..3372
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3375..3416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3417..3438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4043
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   4076 AA;  453670 MW;  0ED7E2C532706D5D CRC64;
     MGKITKTMQQ KHRDTLSPWL KEFVDTASSA PLPLILQRLD EFPRRWMFPR GDLYHWIPLL
     NRFDNILESI CATYELSKGP QTRDFGRDVL LNNGGPSLEY RDEPWTVERL AEAGYKEDGD
     CQLLVAILKF TRMLLEHCGN RSIYASSHHI DRLLNSPYLE VQAAALEVGL ELAQRYNASV
     KRMPSPPRSV NPTLLANHYN IDLEKVQLLA RPFVRTPIVK SLEASSAAPA VSAGSTAKAK
     DKEKEKEKAT GPKNVASMYA NDLKALASSR PDEEDLWKSW GDLKMSYYPD TTNGEPSARD
     SKDAQPVEPR TTSSPAAPTP LRRSSTMNVS QSSRTQRVGS SEEGSPLKPS GAATDDRDGP
     KVVEIPRSVI ESKRIYDLYD MCPSDMPATM KFEFTSRLRT CKALLGTHRE RQLALAVRLL
     AITNLAYILP EAVFVDKVLK YDKDEPRTFQ LVYQLAELIA PSPDGNPSEV PKWLQSITLA
     LLEAISHQQE KHSDVLAALN VNVNHGILLY VIRIAVAEMK EDAPVDDQDE LDADNWRGNL
     FGLTLQIAMA TRIGQEMMTA GLMDCLVEIL NLRTAVASRH YSMVLAFLDS LTYAYQTAFS
     QLNSAGGLDA ITNLIVHTVG ESKTLTEAGL GTKPELHASL VDYSIPFYHQ QTLKWLLKFI
     HHVMANTYSF DGTNTERLLR NLVDNSSLLG SLCTIARQNR FFGTVVWSNA TTLLSDFINN
     DPTSFAAISE SGWIQAFLES VTNRPVSIPA EQPSLEPSQS RANDGSEGND ADDDSEDDGS
     AHDAAPDSDG QAATQPHPPT QEMLEAPRDF PPAHGILPSS ESMNIIPTVL NSISLNNRGM
     KMVLSSGAIQ SYMEIFESAT HVQCMAHDPE LASTIGSSLD ELSRHHPALR PAIANAIIDM
     IARVTHLVKT MDATKACGAR LEAPESSASP VAEPAQATEV KGKGKEKATD DTDVEMAEAS
     SSSSGNNKPA QAPSIPYIQV LSTFLQPIIS NSHLKGALIS AGVIEILLDL AESPSLPHDF
     GETPACRMLV AAISQLIESA QIVGLPSLLF RMENTVKVLQ PRINPTTTEP FFAPFLTLNS
     SVSPVQDEEP ASEKRTPDVS SGTETVKALL NIQTMIKILY HCFPFSNRSQ MVSMPAVNVY
     DYYIRLIQSL GPLLRGVLKE EAAVNGAVPH HWTLKNKPYQ TNSLGSRTDV QDLLTDSAAQ
     DSSANGKKLT PEEQSTAEYK NFQTLRVLLH SFMPSIFPFF QTIGKALLPR RNNNDPYIRS
     RHLAIAEASA ETLIQQLQQS KAELTVRDIH NWIIMIHTFG EMVVDTNHRT ASGGAFLILP
     VITAFKELGG FEALNVMLKR LADMVSTGAT EGQEATKAKL SMIGMKKVLD IYCFIISGKN
     LSDSMAQIAL APKPTERTTR EFSHQLVVEL RMSILPVVRE IWASNIIEKS TGTVVSKIID
     IIKTIAAGDL ESNAQSRSDK ESLPHLFKNR ESVPFKWISR KDAETLATEQ GVDVDLALEA
     LYRANGKESD TKEYIKYQKA HLVRNRNPVP AEDAFKEVPS PNLSSSAGMS LSNLLNTPTF
     PVSDLLGAEP MALDPVPNQP LGEASGETAL GHATESSEDG SDEGQPGTSR ETNVGASTTA
     PQQLPVLPSQ QPATESQSNT PRITREDLVE ERAKLYDTLI DRSLEVISSH PEAVFEVADL
     IQNTILKTDN EDRRVEVGEI LANALMSFAS DDADELKENG SSIAAYAHLL ALLLQQTAFM
     RTTVDMLRDY VGDYLGFLKL PPASSNDSLP PWIPYILLIF EIMLFKDAQP PDIKWKQPVK
     EDDPIEESVI EVKEPNFLAE HRSSLLTTLL DFLPRIGKEE SLAVSVLRIL VVLTRDHAVA
     KIVGEKKNLQ RLFVMAKQLC GAGSTRLKQT HISEHIRQIL RHIIEDEETL RQIFETDIRH
     LMTSRQRPSA APGLEPQAYL RTQAHLALRS PKTFVEVSTE LLKLNRAVSH LGDGTLRSTP
     FLVLKERPAD ASVSPKESSV EPAVQATEDL TISDVKPSTE VTDKDMHDAP KNPAQDLKRP
     ILEHPDGVVH FLLTELLNYK DVDERENVPA PPAAASKPES DATAANEATP SPSGDEQNSE
     SKEKEKKLAK SPFKAEDHPI FIYRCFLLDC LAELLQSYNR AKVEFINFKR SAPVQANAPV
     KPRSSVLNYI LNDLLCFSPA SGVPESIAMK KKAATAVPAR AVLVALVSKT GEKPQNRTHE
     PFEYDDEPDL LFIRRFVLDT ILRAYKDASV SGEPADIRYG KMNALAELMA QMIGEGDKDS
     RPNNPRGTDP SIGRSQAQLK RLMYEKGYLT SLTASIADID LTFPHNRAPL KPILAVIKTL
     SKTAVSMSQL GLIPASGTAG TDQAEDEFLS DGSSVSEDLT DDREETPDLY RNSTLGMLEP
     GRDDEFSDED EDDDEDMYDD EQYDDELDYG DDMSQDNEDN PSDEEDDLGE MGEMGGMPGQ
     PGVVEVLMGE NDDEEDNDDM DDMDEDDEMD EDDEQELSDE DEDEEVGSED MDDLEDDIHI
     VDEEGNAIDD DGASWDDGTD EDEEDEEELD YEAEAQNMQE AQLHNRRTFP EIMRAAMENA
     GDDLDAEPIR DFDGHYIDDD EDGEEDDDED EGEDDMDDDM YFDGDGLHDD LLAPNMPSGL
     GWDIAIEPNH RHRPSRSPWP NSPFVVGRHR DAIDFQNFFR RPAHLSRHLP PPADVMSGTN
     PLLLPQSRRE VPRHAHSQLV RLGITPNMIG GLGMGMGVEP LAFISDLVQH LPDVRLSAGG
     GPLALHFTAD GPGGIIRELN AIPIPPPHSR ESRPTEARRD TYQEPHQAVQ FSPESTHERW
     QQEVKMIFGF GYQDKAQKLA PLILSKLTPA AIQAEKEEKA RKAEADRKAE EERKKRQEEE
     RKKREAKEAE EKAAREKKEA EERERLERER AEAAAQAAAQ AAADQEANAV SQEAHPMEGV
     ETQGPGENAE QQAEDERPRV YYTLRNQQID ITELGIDAEY LEALPEEFRD EVIAQAISTR
     RSQAREQVSQ EGENTEVFQE FLEALPEELR NEILHQEQHE QRRRERQNAA GGQDLGPADM
     DPASILLTFP PGLRQQVLLD QGEDIMEHLG PELAAEARTL VARHRQLHAQ QGGQAASRSR
     DAQRPTEAGA GTVQKIQKRT VVQMLDKQGI ATLLRLMFVS QQGSIRSSLF SIFANLCENR
     QNRLDVISSL LQILQDGCAN MDAVERSFAQ ISHKAKQLKE KDAKTPHPLK RSLTGGTNNN
     GQFPASSEVS PLLIVQQCLD LLVELSKLNP HIPSVFLTEH ETVASTLKRS LSRKGKGKDV
     NGKAQKFAIN SLLTLLDRSL VMESSAVMQV LADLLNKVTI PLQAIERRRK EAEEQAKKKK
     EAEEKAATER EAANAPEEQA STSTEQTPAQ QEATQQPSES TPAAASGQQP AQQDQENKEL
     EAPKEKADEK DVQSDEKKIR QLTPPTIPEH NLKLVINIFV ARECSSKTFQ NTISTIKNLS
     NIPGAKKVFG DELVRQARVL SENILSDLDN LLPHILKAES GTQIQGVALA KFSPGASEQN
     KLLRVLTALD HLFDSKSKKQ DKPAEGENTK EDLLGSLYWN PTFGKMWDKL SACLSAIRQR
     DNMLNVATIL LPLIESLMVV CKNTTLSDAS AVSNANSQKE MLLTSPPPED RIAGLFFTFT
     EEHRRILNEL VRHNPKLMSG TFSLLVKNPK VLEFDNKRNY FNRSVHSKYQ QTRHSFPPLQ
     LQVRREHVFH DSFRSLYYKK ADELKFGKLN IRFQGEEGVD AGGVTREWFQ VLSRQMFDPN
     YVLFVPVSSD RTTFHPNKLS PINDEHLPFF KFIGRIIGKA LYEGRLLECY FSRAVYKRIL
     GKPVSVKDME SFDPDYYKSL VWMLENDITD IITETFSVED DVFGEVKVVD LIENGRNIPV
     TEENKHEYVR LIVEHKLITS VKDQMKAFLT GFHEIIPEEL IAIFNEQELE LLISGLPDID
     IDDWKANTEY HNYSAGAPQI QWFWRAVRSF DKEELAKLLQ FVTGTSKVPL NGFKELEGMN
     GVSRFNIHRD YGSKDRLPSS HTCFNQLDLP EYENYETLRS QLLKAITAGS DYFGFA
 
 
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