ID   V9CZR8_9EURO            Unreviewed;      1235 AA.
AC   V9CZR8;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=G647_09352 {ECO:0000313|EMBL:ETI19518.1};
OS   Cladophialophora carrionii CBS 160.54.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1279043 {ECO:0000313|EMBL:ETI19518.1, ECO:0000313|Proteomes:UP000030678};
RN   [1] {ECO:0000313|EMBL:ETI19518.1, ECO:0000313|Proteomes:UP000030678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 160.54 {ECO:0000313|EMBL:ETI19518.1,
RC   ECO:0000313|Proteomes:UP000030678};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora carrionii CBS 160.54.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KB822710; ETI19518.1; -; Genomic_DNA.
DR   RefSeq; XP_008731877.1; XM_008733655.1.
DR   AlphaFoldDB; V9CZR8; -.
DR   GeneID; 19987845; -.
DR   VEuPathDB; FungiDB:G647_09352; -.
DR   HOGENOM; CLU_002173_2_4_1; -.
DR   OrthoDB; 1386at2759; -.
DR   Proteomes; UP000030678; 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   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          854..1235
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..66
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1203
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1235 AA;  139839 MW;  13CD534673B9486F CRC64;
     MHQSFTGSAR KARQVNLSGR NTTNPWAALS KSGQGSSPAG TNPVAQAQAD RVKRQQERDR
     LNASRKIQKV WRGHSTRRKE KAVLRQTWDE NERLRLGRDA EVDYRVLVDN EESIPGYENS
     DQLLVQLRLL LQYQEYRRAR VRDEMDTFRL LYFGQALHPT LLSLQGSLVD HVWRFNLSRL
     GLVVSLHLKS ILIDESTSRM TYGPRLLKMI SMIAIYVSDD MVRDSTTYFE TIELALASQK
     GEGWQKGSLE AIWALLRYPT QKQPAYRAFV TRLMSEPSYA DDSAVLARLA TPLDLTQLST
     AITEMLEDED AAKTDALTTT ERLWQLAYLV YFHDAIQRGS ADRAYIEALS ALLGECANEI
     AERYEQADHL MSGDNSKNSS APLPPFVREM ISRIPQQDNL QAVLDEMGSS QSSTEDTGGT
     DFQSAKRLAN FAVALLRAFP AQAQNIRMAL YRGSVKTVGN ADVSTIQYFW NTARGTGVFK
     KITRDHRIVL SLLREAAPPT NQIGQAPVSK AEIGQWRDEW RITLLFLELY TFVLKFMDDE
     DFFSYDKSHA FGATTTSPIS VLSRKGSLPL NDVAQMTIFL KNLAFVLYWN AAELVESNEH
     EEDVGISALF GGSLHSSNRQ PEKKQQTLTG NGVSQGYLKG LVTGLLRMLH ERDSRRSFVP
     PGHWLMTNQV SMAGFIPAVV AEEERRHELG EDEDADDQQD DFDKDAELDE SAGSMPGEML
     LNTMFGIRPS HIPRSRASRM ADRIEKQRLQ ARKKRQLESL APRLEILRNL PFFIPFETRV
     QIFREFVYRD QLRRRDGAID PDTWRMSVVT STQGRGTDGR PRGVDIISRH HAEIRREKVF
     EDAYEAFYGL GEGLKEPIQI TFIDKFGAPE AGIDGGGVTK EFLMSVTSEA FDPDASLAMF
     KENAQRYLYP NPLIYQETAA YLKRAGRKPG TEGFDFPMAE FLRRFQFLGR VVGKCLYEGI
     LIDVSFAGFF LLKWALTGGT TVGSNESAYR ATINDLREYD EELYQGLLKL KNYPGDVEND
     FGLDFTVTDT ITIEDERHNE VHQTITTELI TNGANTPVTN TNRLVYIDRI VRYRLQQQPK
     AVTDAFLKGL GQIIQPMWLA MFNQKELQKL VGGDNSELDI ADLRRNTQYG GLYVIGDDGQ
     EHPTVQLFWK ALQEMSDSDR RKVLKFVTST PRAPLLGFSH LNPRFSIRDS SEDQERLPST
     STCVNLLKLP RYGDIKTMKE KLLYAVNSGA GFDLS
//