ID   A0A178E8U8_9PLEO        Unreviewed;      1204 AA.
AC   A0A178E8U8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=IQ07DRAFT_562955 {ECO:0000313|EMBL:OAL52430.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL52430.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL52430.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL52430.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KV441641; OAL52430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E8U8; -.
DR   STRING; 765867.A0A178E8U8; -.
DR   InParanoid; A0A178E8U8; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000077535; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:UniProt.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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   InterPro; IPR000048; IQ_motif_EF-hand-BS.
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.
DR   PROSITE; PS50096; IQ; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          824..1204
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          681..728
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1172
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1204 AA;  137027 MW;  DB59047DDD4F0DAD CRC64;
     MFTSFTGNTR RPRQVNLGGR KTNPFGTSGG SGSQATLDRA QQERVQRQRE RDVLNAARNI
     QRVWRGHSSR RHVSDELRRA WDAAESTLQP THYPSEAEAL RALQRLLRFA SPRCEQDLDR
     IRHHGARLVE TMSASIGQPT GSWPSAYLRL EEILLVALER QGKAATCWDH SCQLLSLLRF
     VADRIPAQTA RNAEKYYRSL ACVALKLISD LDIPGATSLN TWTVLFDTVI LPLKTVASYT
     LDAYEAFAYT FLPLPPLSSD SATPPTRRFR DSLADSINYK LLANALSNLL RGLGLRLDLG
     LDDAISRLRV LGLFIYFHRY AHNFDTPEAY SVHRDFVIVI SALLNSLPVN IIVDTQRSVD
     FSEDKALAPT HGLVTEFLKE QLLSLVNQEG IGSLLAQPSQ STETSADEKM EEARQLANYA
     LALLRFFPRR GDEIRMWLYM GPSDPALGKE VQKSPAIKYF WEASKCSSVF ATVFRDSRAA
     IGLLKPRTST VHGSDHPRAQ GHLRQSLWQP AQQEIDRNAV LTDEWRVILV FLELYTFVLK
     VTDDEEFFSA GKYDTHANQF RDSGLPLNEV KDLTTFLKNL GFTLYFNSSE ITTTEDDPDN
     SKPSLTYFNP NLAESPAPKE TFEPSIGGVA GLKIDYVKGL ITGLLRMIYE RDSRRKFLPS
     DHWLMTSRFD MTGFIPAVVE EEESRHKIQE EDADDMDDHE EDDEETPQLI GTSRTQQQRR
     LERLQRQQRK ASRRRYLQAV APRLEILQNM PFFIPFATRV QIFREFVHLD MTKRRGSSDA
     EAWRLRVMQW PDAVRQFEKH AANIRRENEF EDAFEQFFSL GQGLKEPIHI TFMDQFGAAE
     AGIDGGGVTK EFLTSVTNRA FMPTDHINMF IENDQHLLYP NPSAVEEHKE ALRQGGLREN
     SPEFRLQVVE LLQRYEFLGR IIGKCLYEGI LVDVNFAPFF LRKWALTGGA GSAPNESGYR
     PTLNDLRDLD EELYQGLHKL KTYNGDVEDF SLNFTVTDTV IVDHTTNPKK TRAITKELKP
     DGANTPVTNQ NRLVYISYMA RHRLQNQPYL QTTAFLRGLS TMVQPSWLSM FNQSELQTLI
     SGTRTSIDVE DLRRNTSYGG TYVIGDDNLE HPTIQLFWKI MREMSDDERR AVLKFVTSTP
     RAPLLGFGTL NPRFSIRDAG GDQERLPSTS TCVNLLKLPM YRDEGVLKKK LLYSIFSGAG
     FDLS
//