(data stored in ACNUC8465 zone)

SWISSPROT: B6H7J0_PENRW

ID   B6H7J0_PENRW            Unreviewed;       833 AA.
AC   B6H7J0;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   30-AUG-2017, entry version 76.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE            EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN   ORFNames=Pc16g02760 {ECO:0000313|EMBL:CAP92946.1}, PCH_Pc16g02760
GN   {ECO:0000313|EMBL:CAP92946.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP92946.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP92946.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine. {ECO:0000256|PIRNR:PIRNR001569,
CC       ECO:0000256|SAAS:SAAS00628607}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|PIRNR:PIRNR001569}.
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DR   EMBL; AM920431; CAP92946.1; -; Genomic_DNA.
DR   RefSeq; XP_002560646.1; XM_002560600.1.
DR   ProteinModelPortal; B6H7J0; -.
DR   STRING; 500485.XP_002560646.1; -.
DR   EnsemblFungi; CAP92946; CAP92946; PCH_Pc16g02760.
DR   GeneID; 8307057; -.
DR   KEGG; pcs:Pc16g02760; -.
DR   eggNOG; KOG0940; Eukaryota.
DR   eggNOG; COG5021; LUCA.
DR   HOGENOM; HOG000208451; -.
DR   KO; K10591; -.
DR   OMA; PGWEIRK; -.
DR   OrthoDB; EOG092C016J; -.
DR   BioCyc; PCHR:PC16G02760-MONOMER; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000000724; Contig Pc00c16.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 3.
DR   Gene3D; 2.60.40.150; -; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR001202; WW_dom.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 3.
DR   PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 3.
DR   SUPFAM; SSF49562; SSF49562; 1.
DR   SUPFAM; SSF51045; SSF51045; 3.
DR   SUPFAM; SSF56204; SSF56204; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   4: Predicted;
DR   PRODOM; B6H7J0.
DR   SWISS-2DPAGE; B6H7J0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001569,
KW   ECO:0000256|SAAS:SAAS00628615};
KW   Ubl conjugation pathway {ECO:0000256|PIRNR:PIRNR001569,
KW   ECO:0000256|PROSITE-ProRule:PRU00104, ECO:0000256|SAAS:SAAS00593691}.
FT   DOMAIN       10     93       C2. {ECO:0000259|PROSITE:PS50004}.
FT   DOMAIN      231    264       WW. {ECO:0000259|PROSITE:PS50020}.
FT   DOMAIN      348    381       WW. {ECO:0000259|PROSITE:PS50020}.
FT   DOMAIN      411    444       WW. {ECO:0000259|PROSITE:PS50020}.
FT   DOMAIN      500    833       HECT (E6AP-type E3 ubiquitin-protein
FT                                ligase). {ECO:0000259|PROSITE:PS50237}.
FT   ACT_SITE    801    801       Glycyl thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR001569-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00104}.
SQ   SEQUENCE   833 AA;  93593 MW;  C166073A86CC240B CRC64;
     MASNLPAQPN LRVTIIAADG LYKRDVFRFP DPFAVATVGG EQTHTTSVIK KTLNPYWNEP
     FDLRVNEDSI LAIQIFDQKK FKKKDQGFLG VINVRIGDVI DLSMGGDEML TRDLKKSNDN
     LVVHGKLIIN LSSNLTTPHP NQNGLQRQQA QTSTSSGLVP QVAAPTSQSQ AGPSNIDTSP
     AAASSSSLTQ RTSATAPPAG APPSLNGAPT NPPGPGVPSR TNLSSFEDSQ GRLPAGYERR
     EDNLGRTYYV DHNTRTTTWS RPSANYNEHA QRSQREANMQ LERRAHQSRM LPEDRTGANS
     PNLPDAQQIP TPPPGPNAGT SLASGAPAGS NAAAISMMAT GATTAGTGEL PPGWERRVTP
     EGRPYFVDHN TRTTTWVDPR RQQYIRMYGQ GQTTGGANNT TIQQQPVSQL GPLPSGWEMR
     LTNTARVYFV DHNTKTTTWD DPRLPSSLDQ GVPQYKRDFR RKLIYFRSQP ALRIMSGQCH
     VKVRRNNIFE DSYAEIMRQS ASDLKKRLMI KFDGEDGLDY GGLSREFFFL LSHEMFNPFY
     CLFEYSAHDN YTLQINPHSG VNPEHLNYFK FIGRVVGLAI FHRRFLDSFF IGAFYKMMLR
     KKVSLQDMEG VDEDLHRNLA WTLDNDIDGI VELTFSVDDE KFGERRTIDL IPGGRDIPVT
     NENKPQYIEL VTEWKIMKRV EEQFDAFMSG FNELIPPDLV NVFDERELEL LIGGIADIDV
     EDWKKHTDYR GYQEQDEVIQ NFWKIVRTWD AEQKSRLLQF TTGTSRIPVN GFKDLQGSDG
     PRRFTIEKSG DPAALPKSHT CFNRLDLPPY KTHDALEHKM SIAVEETLGF GQE
//

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