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Database: UniProt
Entry: G3JCH4_CORMM
LinkDB: G3JCH4_CORMM
Original site: G3JCH4_CORMM 
ID   G3JCH4_CORMM            Unreviewed;      1253 AA.
AC   G3JCH4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=HECT domain protein {ECO:0000313|EMBL:EGX94635.1};
GN   ORFNames=CCM_02906 {ECO:0000313|EMBL:EGX94635.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94635.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX94635.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX94635.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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DR   EMBL; JH126400; EGX94635.1; -; Genomic_DNA.
DR   RefSeq; XP_006668121.1; XM_006668058.1.
DR   AlphaFoldDB; G3JCH4; -.
DR   STRING; 983644.G3JCH4; -.
DR   GeneID; 18164933; -.
DR   KEGG; cmt:CCM_02906; -.
DR   VEuPathDB; FungiDB:CCM_02906; -.
DR   eggNOG; KOG0941; Eukaryota.
DR   HOGENOM; CLU_001858_0_0_1; -.
DR   InParanoid; G3JCH4; -.
DR   OMA; PEDFHTP; -.
DR   OrthoDB; 1820836at2759; -.
DR   Proteomes; UP000001610; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR   Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR   InterPro; IPR032353; AZUL.
DR   InterPro; IPR042556; AZUL_sf.
DR   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700:SF8; HECT DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   Pfam; PF16558; AZUL; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001610};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          903..1253
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        292..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1221
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1253 AA;  142292 MW;  C8A03440BF4A7B8C CRC64;
     MSAQALRLPQ RRPSDSNGHH DGPDDGNDRY DVFDSLWQEA LFARLPPDAP PQLTPFVREI
     ENPRRVYAIH RASRRHDFQL LVQLLIHQLR DGCGSDTCHT STCFSCRKRL AGKAPIRRYN
     PTSARTLAIY LASQDNPERG ICPSLRRPKD VTPAVNNLVF SKCSVPKSAS QNPSDGDAQR
     TVRRTASKSQ SKSRSPSESE DAQVQGKETI DTTLQPESLR DSTEICISER PVARDYRSFA
     ATTFGTIAFK MIEWLTPSSL DALSRKICDI RSSSPSNPKP TPVPSPDPQP ITGKEARDRD
     HDDTRDASSS PHKSSPHIDP HSIAESRSKR DQPAPKRNSK PALRSKPTVE TTRRKSIEPV
     CVTAEADNAT LHRPTRMNGY HPDKLSRRTK SPTTITFKPA FFENVPIPPA VADEVTVTSS
     DGEESTKEEM TEPPRPGGNH EHRQKQHSAE EVHDEDLDHA TAMEYPLPQT LSQLNIQIID
     FICDVYVDDH TSEDQLHGNI DVGHNYPEPQ ERQGHLVRTP QPRDAACKKL WKDFHEQTLF
     SVLSDPAALI LSFSKDGILY DSHSLWYCMV RLMRASPSLV LHSLWLSAAS LFSLPEANVR
     KEKGKSRCLS PHQVESVMSI CLHALVALVP VVPDSRLLYD LSRIRSHGLA LSNPSASYRR
     PSGLCLKYDD AFSNSLALRL ARRLFLAITI RQKHGNAPLS SLLEQLDLRN TSLERMLKFT
     QEERLLHETR VPTLLLDWAR AVLLHEWDGK AQFYKDGTFH GALSFMDTLY KNRNVLLLGE
     MQFRVEYFSE RLDAMRVPVQ WTTTNSTDHV GNILDYPYLF QSETLVTYFR SINFACMSRT
     FEEASSLKRR MSAIVDPGSL ITNPHHKVVL KDMLRTAASK YLVLDIGRTT VLRDAFDQLW
     RRQKRELLRP LKIHLGEDAG EEGFDSGGVQ QEFFRLAVAQ CLDPVYGAFT VDERNHMAWF
     KPQPAVEDWK FELMGLLLSL AVYNGLTLPV NFPKAFYRKL LKQPVDQLYH IADGWPELTN
     GLTKLLEWDE KDGLIEDIFA RTYEFSVPGV GKDVTIHMLE DKHKEQPGSP VSADTDVPEA
     PYVTNENRDE YVNDYIRYLT DYSVRRQFDS FRRGFVACLP EQSLTLLTPS ILQSVVEGVQ
     EIDISELRRY ARYVGWDTSH HTVRDFWSIV KRYDDRMKRK LLEFVTASDR VPVSGLKNVQ
     FVIQKNGEEN EGGHLPTAYT CYGTLLLPEY RDKEVLRERL GMALENAQGF GFA
//
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