ID A0A137Q5L5_9AGAR Unreviewed; 761 AA.
AC A0A137Q5L5;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=AN958_02351 {ECO:0000313|EMBL:KXN82500.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN82500.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN82500.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN82500.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KQ962949; KXN82500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137Q5L5; -.
DR STRING; 1714833.A0A137Q5L5; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF429; E3 UBIQUITIN-PROTEIN LIGASE SU(DX); 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 178..211
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 282..315
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 339..372
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 428..761
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 98..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 729
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXN82500.1"
SQ SEQUENCE 761 AA; 85080 MW; 374C0F2DAB8C729C CRC64;
ITVGESSVIA VQIFDQRKFK RRDQGFLGVV NIRVSDELDL ELDSHQMLTL DLKKSNDNLV
VHGKLIVYLT TNINQPITNP GPGTSSSLTA GVAGLSLDGS SPAASSSNVA LQPATEQQSS
TQQPTTTPGS ASASGSVVSP TTSSAPAASA SAQGASAAAT SPQNPNMRNF NPNVDQYGPL
PPGWERRIDP LGRTYYVDHN TRSTTWNRPS PSAAVNHNTQ DTETNAAREQ NSRRILADDL
LEASNPSYRG GDATSASAAT ASTTNTTPAQ ISTGGATTAG SGSLPHGWEE RYTPEGRPYY
VDHNTRTTTW VDPRRQTIIR VVGANGQGSV QPQTISQLGP LPSGWEMRLT STARVYFVDH
NTKTTTWDDP RLPSTLDANV PQYKRDFRRK LIYFRSQPSM RAQPGNCQIK VRRNHIFEDS
YAEIMRQTPN DLKKRLMIKF DGEDGLDYGG LSREFFFLLS HEMFNPFYCL FEYSAHDNYT
LQINPVSGVN PEHLNYFKFI GRCLGLGIFH RRFLDAYFIV SFYKMILKKK VTLSDLESVD
AELHRGLTWM LENDITDVID ETFTTTEDRF GEMVTVDLKP GGADTPVTEE NKKEYVDLVV
EYRISKRVKE QFDAFMSGFS ELIPQDLITV FDERELELLI GGMSEIDVDD WTKYTDYRGY
EQTDEVIQWF WKCVRSWPPE RKSRLLQFVT GTSRIPVNGF KDLQGSDGPR RFTIEKSGDP
SQLPKSHTCF NRIDLPPYKD YASLEQKLTL AVEETVGFGQ E
//
