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Database: UniProt
Entry: A0A0D2DJT4_9EURO
LinkDB: A0A0D2DJT4_9EURO
Original site: A0A0D2DJT4_9EURO 
ID   A0A0D2DJT4_9EURO        Unreviewed;      1231 AA.
AC   A0A0D2DJT4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PV04_10799 {ECO:0000313|EMBL:KIW62642.1};
OS   Phialophora macrospora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX   NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW62642.1, ECO:0000313|Proteomes:UP000054266};
RN   [1] {ECO:0000313|EMBL:KIW62642.1, ECO:0000313|Proteomes:UP000054266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW62642.1,
RC   ECO:0000313|Proteomes:UP000054266};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN846963; KIW62642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D2DJT4; -.
DR   STRING; 5601.A0A0D2DJT4; -.
DR   HOGENOM; CLU_002173_5_1_1; -.
DR   OrthoDB; 5471864at2759; -.
DR   Proteomes; UP000054266; Unassembled WGS sequence.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR   CDD; cd00078; HECTc; 1.
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   InterPro; IPR044611; E3A/B/C-like.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR   PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          870..1231
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..132
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1199
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1231 AA;  138398 MW;  374D8FAE63FD8FCD CRC64;
     MASLPSSASH HHHFGRPRPR NPQLTRSASH DQPPPTADLN RPLPPPPPPP LATAAAETYE
     IPTLRRKPVP DELPDPGAAK LNHSRSFSHP FPSIFGSRKS EKKNKHGGDF DGTRDSRHDE
     VGSKHPAAES SSFRDDRQPV TGRCMTCDST VRWPQGLKVF RCTTCLTIND LEFNPDKRPD
     TQGPAIGPAP QRKILPLSVE RTRSLLDRCL TQYLESRVGR DEPVTPAHPV PVENDSLADD
     SFLVDGSPPE GILYNQLADE QESPPPSPLP RVNPRSPSEE STLSTHHSGR NAGPPFVQDH
     SIDPFSSATS LSVRPRDARA RQPSEPGPTT SPNPGPRWDI FYLVEDYIAG CFVGCAALNH
     SFLTPRPPQE PNPKPRSSSG TRQRRQLSET ISAPSFDNDV FLSELDAKTL LLGDVAENGS
     WWLGAPSGRM TTGKDVNHQR DKSPDKNRSI ASARHHRINW LELAEWYRLI IYAGDLWEER
     WHELLPKLSD ARAQQCWRST PLENIQRDII ESRIHLQRSL LKVSENLLKR PRQPLKHPED
     CRFLLILLAN PLLTPARLEA GKMFGTTMPH PPIPPARLQV DGKARDSPSK RIPSSGRRPG
     SLGHHSGIIK RILGLMANLS NENHQYLVSW FSRYADGHFQ RTVEMVGSFV SYRLSRQQKN
     PTHEPVNPTE GLVPSFSDAG THHASQIHAA LGGYRPASTA AGKSQEKPRL SAYGEDWQIR
     VAARVMALLF QANVGHVARK RDASAAHEQR LHSPGLNAKY RAYLHGQIVP ISNFYNTMLD
     YADLVADFET WENTKTKFTF CQYPFFLSIY AKIHILEHDA RRQMEVKARE AFFDSILSRR
     AVSQYLILKV RRDCLVEDSL RGVSEVVGSG GSDIKKGLRI DFQGEEGVDA GGLRKEWFLL
     LTREIFDPYH GLFVYDDDSQ YCYFNPFCFE SSEQFFLVGV LLGLAIYNST ILDVSFPPFV
     FKKMLASAPS TGDKLTSTPK VPHGYTLEDL AELRPLLAKG LRHLLEFEGD VEETFCRDFV
     AEMDRYGEIV QIPLCPGGEK RAVTNSNRRE FVDLYVHYLL DTAVARQYEP FKRGFFTVCG
     GNALSLFRPE EIELLVRGSD EPLDIASLRA VATYEGWPKA DGPPEQQPQV IWFWEFFARV
     SPTDQRKILS FITASDRIPA MGAANLVIKI QLIREREEVD SVGTPTNKPI ERFPIARTCF
     NTLSLYRYAS RQKLEEKLWM AVQCSEGFGL K
//
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