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Database: UniProt
Entry: A0A1Y2DPW4_9PEZI
LinkDB: A0A1Y2DPW4_9PEZI
Original site: A0A1Y2DPW4_9PEZI 
ID   A0A1Y2DPW4_9PEZI        Unreviewed;      1702 AA.
AC   A0A1Y2DPW4;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=BCR38DRAFT_347380 {ECO:0000313|EMBL:ORY61300.1};
OS   Pseudomassariella vexata.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Pseudomassariaceae; Pseudomassariella.
OX   NCBI_TaxID=1141098 {ECO:0000313|EMBL:ORY61300.1, ECO:0000313|Proteomes:UP000193689};
RN   [1] {ECO:0000313|EMBL:ORY61300.1, ECO:0000313|Proteomes:UP000193689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 129021 {ECO:0000313|EMBL:ORY61300.1,
RC   ECO:0000313|Proteomes:UP000193689};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC   -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC       {ECO:0000256|ARBA:ARBA00006331}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ORY61300.1}.
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DR   EMBL; MCFJ01000010; ORY61300.1; -; Genomic_DNA.
DR   STRING; 1141098.A0A1Y2DPW4; -.
DR   InParanoid; A0A1Y2DPW4; -.
DR   OrthoDB; 1093891at2759; -.
DR   Proteomes; UP000193689; Unassembled WGS sequence.
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   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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR045322; HECTD1/TRIP12-like.
DR   PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000193689};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1349..1702
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          899..1003
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1038..1084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..40
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..575
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..611
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..939
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..978
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1047..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1669
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1702 AA;  187368 MW;  893906E39193B211 CRC64;
     MAGTEEHEKE ADPPPPPPPP AHDPDDDSDD DDDDDDEPHR HYDDDDPFGG FGGPPGSGLS
     STLRALTGMM SGMPSRLREL LNNLRMKEDP SMQMIALQEL SEILLVSNED NLAGHFSPDS
     FVKELVVLMQ PNEITGEENP DMMLIACRCL ANLMEALPAS AANVVYGGAV PVLCQKLLEI
     QFIDLAEQSL STLEKISVDY PTSIVREGGL TACLSYLDFF ATSTQRTAVT TAANCCRNIP
     EDSFPVIKDV MPILLNVLGS NDQRVVEQAS LCVTRIIESF KYQSSKLEEL VSVDLLKAIL
     RLLVPGTTNL IRANIHTQFL RVLAITARAS PRLSAELFKL NVVETLYQIL TGVSPPDETE
     DVASKLDSVV IMQALIHRPR DQIIETLNVV CELLPGLKWI DLSTPQIPTG LDVSEPITPS
     SVGGPRKKSS NEKRLEFLDE CKDQVRRFAL ILFPTLTDAF SSTVNLSVRQ KVLTAQLKML
     SNLDKDILVD ALKSVPYASF LAAILSQQDH PSLVMSAIQT TELLLTRLDD IYRYQIYREG
     VISEIAKLAE DQETAEPKGA ETTPMESNTE PSMGSADGGG SDRVSIHNDS EEEEEDDEDE
     EDNDDEDHEN DHHDDDMSGS PVSSDGSTMS LDGPPRTFLA DIPSIKSRIA EVAKKFLEAH
     ETEKQGKSMK KKALKILTDL QSLASDIESF YLQRTAKNLA PEQGTALFER LSAYFDADVL
     ESVTSAELLA SGLVRVLEEV FSNPDEALAN AARSAFLEVF MGRSVKSRPK TTSADSPATP
     FSVMVHKMQD LLSRSEHFEV LTVHQNTFDG NRSSAASMLA KQIRLKLVAD DDSDIPRSYR
     NIMVSIHAIA TFKALDDYLR PRISLHERPR GPRPRDGLSR ALAAMAGSAG LPPERLAERL
     GYSSTPAPPP PVPAQSSSSR PAKKPRPKSS GQTDAPATPN PPAGSAREKV SLRRSTRRNP
     APPSESQAPP PPPPPEEEDD LQNALECADE KQLSDDDEDE VPDSSALDAI VGDLDEDMED
     APVPDPSAVN LEVAAGGKIT ARKEDGTRIP TPSQSGLGNV PNRSVAHPPS GLSQQSTPTP
     AMAPSRPLSY AAAIQAVPQD WHIEFSLDTR VIPNETTIYR AVHRTSPPAD EHFSRSVWSA
     VHAIKFRRVP GPPPAEPIGF ATSTDESTDI NGTPASLANN PTTASILRLL KMLHDLNANI
     DDILIEDKTA LRLNVEPLSQ FVNTKLTAKL NRQLEEPLIV ASNCLPGWSE DLARLYPFLF
     PFETRHLFLQ STSFGYARSM SRWQNAQQEE TSRRDRRDER PFLGRLQRQK VRISRTKILE
     SAVKVMELYG ASQSILEVEY FEEVGTGLGP TLEFYSTVSK EFSKKKLKLW REMDSNDSEV
     FISGPHGLFP RPMAKDDVNS ERILQLFKML GKFVARSMID SRIIDLNFNP IFFRIGDGTT
     GVKPSLGAVK IVDAGLANSL KHIKKFASAK KEIDEDPNRD AAQKVADTEQ IVIDNIKIED
     LALDFTLPGF PDIELIPNGS HSPVTIYNVD MYLDKVVDMT LGSGVKRQVD AFRAGFSQVF
     PYSALSAFTP DELVALFGRV DEDWSLETLM DSIKADHGFN MDSKSVKNLL QTMSELTAAQ
     RRDFLQFTTG SPKLPIGGFK SLTPMFTVVC KPSEPPYTSD DYLPSVMTCV NYLKLPDYTT
     IDSMRRQLFT AIKEGQGAFH LS
//
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