ID A0A0D1ZUP7_EXOME Unreviewed; 1299 AA.
AC A0A0D1ZUP7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN ORFNames=PV10_07794 {ECO:0000313|EMBL:KIV90493.1};
OS Exophiala mesophila (Black yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=212818 {ECO:0000313|EMBL:KIV90493.1, ECO:0000313|Proteomes:UP000054302};
RN [1] {ECO:0000313|EMBL:KIV90493.1, ECO:0000313|Proteomes:UP000054302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 40295 {ECO:0000313|EMBL:KIV90493.1,
RC ECO:0000313|Proteomes:UP000054302};
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 Exophiala mesophila CBS40295.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847524; KIV90493.1; -; Genomic_DNA.
DR RefSeq; XP_016222067.1; XM_016372735.1.
DR STRING; 212818.A0A0D1ZUP7; -.
DR GeneID; 27325639; -.
DR VEuPathDB; FungiDB:PV10_07794; -.
DR HOGENOM; CLU_001858_0_0_1; -.
DR OMA; MDVISHR; -.
DR OrthoDB; 1820836at2759; -.
DR Proteomes; UP000054302; 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; 3.30.2410.10; 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; 2.
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:UP000054302};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 882..1299
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1267
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1299 AA; 146317 MW; 4DEEBB2599043A35 CRC64;
MHYAQPTSKS GTHDDHVPEP HDSKFSRASK ISADLGFHVP DHFLSDIIPL PDPKLDYVAH
HAQRDRTLRL LIRRYTNQVQ YGCRNVNCAT PTCLSYRKRN CASPLRRYTD VSARALACHL
IDDFVKSGAD ARGGLCQNDP VVPWYEDPAL SKKRRSNVER HARLPSNASE NGHAAKSFPS
SNTHRLKDTR KLSPLTEHPM RRSSQEDIVQ AGRRLRNPDM STGATRLNMD HASDPLSLPA
DDLKELDTST LDTLRHAQSF DHATISPPAK TKDLASFTQT LFDLLPLRML NWLPSVKPMA
TQQPPQSHEH TSAQSSIGGA EDKAPTHDLK QANVDETQPC KLQAKQHELA PTMTAACPPT
YTLRNLEFGH LVWLQSFTKS SSSQGTYDRQ VLPFLQQSLI YCLSDPERLV TTVKTLQATY
GRSTQSTRPD DLNQVEEVSQ GDIDPTPSKD APKSLLRRSL PTPWPAFKSS TRTEVKSLVK
SLAHLDQLEQ RDLVINSIFT ALQYSYALPT WLQKSTRLSS PACSTGGDRS PKPAKRFNLD
NATKSASLDI LHNILSQDIE NPRPALKDIQ VCELCLVGLM TIASLITADN YWAHKFTFTQ
LRILRNKDRA HSHWPKLANR GPESYSTDVL RFAGLMIRSI DTFDDWNILR LLKAVMDVIS
HRLTVSKWAA AVKGANLPKE RKTTIVDLLV ARLDRVALTD DESDYGDSLS WMGTAIVEMV
RTVMLRIWDR KPVIQRAGSV SGALELLAGI YRARLSLNLD EQVFTMPFIA DSFDDIAMPN
DWLAFRPDTR QTHLLSFSFL FEPATLVKYF RAINVEIMRK SHEQATLVYT ETRHFMSASS
IPLYGGKEIL SHLRPHMAKY FVLTIRRDDI LKDAIDQIWH RERMELLRPL RVRLGQNEGE
DGLDHGGVQQ EFFRVVFAEA LDKNLGMFTI DDTTRMAWFQ PGSLEPLYSF EALGVLMSVA
VYNGITIPVT FPLAFYRKLL NLKAKSLDHI SDGWPELTKG LRTLLEWSDG DVGDVIARTY
EFSYEVYGSA VTIDLSRVGR EDPWPQLHGV NGTSALKKRT KSTSFELPPP TNRFGPTPHL
SPPHQCTLDT GLAHVSRAAS LNLKGCGTPN SLEESDMPTS PQDDEAPLVT NANREQYVLD
YIYWLVHKSV APQFTAFARG FYTCLDRNAL SIFTPEALKL VIEGHSKIDI NELERTATYD
DFERDSEYMH WFWAIVRNMS PEQHKHLLEF VTASDRVPVN GLGSVTFVIQ KNGDGDVDGR
LPSSSTCYGR LLLPVYRQRA VLEEKLTKAI ENHVGFGIL
//
