ID A0A2N1J7M9_9BASI Unreviewed; 802 AA.
AC A0A2N1J7M9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=MVES_003433 {ECO:0000313|EMBL:PKI82567.1};
OS Malassezia vespertilionis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=2020962 {ECO:0000313|EMBL:PKI82567.1, ECO:0000313|Proteomes:UP000232875};
RN [1] {ECO:0000313|EMBL:PKI82567.1, ECO:0000313|Proteomes:UP000232875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWHC:44797-103 {ECO:0000313|EMBL:PKI82567.1,
RC ECO:0000313|Proteomes:UP000232875};
RA Lorch J.M., Palmer J.M., Vanderwolf K.J., Schmidt K.Z., Verant M.L.,
RA Weller T.J., Blehert D.S.;
RT "A novel species of cold-tolerant Malassezia isolated from bats.";
RL Submitted (OCT-2017) 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 ECO:0000256|PIRNR:PIRNR001569};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|PIRNR:PIRNR001569}.
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DR EMBL; KZ454994; PKI82567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1J7M9; -.
DR STRING; 2020962.A0A2N1J7M9; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000232875; 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; cd08382; C2_Smurf-like; 1.
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; IPR000008; C2_dom.
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; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
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:UP000232875};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..115
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 238..271
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 322..355
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 380..413
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 469..802
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 147..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 770
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 802 AA; 90129 MW; 81DAB5866F00CDBB CRC64;
MVSAAAPGRL ARKVRITVVA SDGLTKRDVF RLPDPFAIVT VDGEQTHTTS VIKKTLNPYW
NDSFDITVTD ASIVAVQIFD QKKFKKRDQG FLGVVNIRVA EVIDLELGGK ALLTRDLKRS
NDNLVVHGKL IIDLNTNVST PLPHDAAAGG ASLATPASAP APAPAESAAA STAPAVAALQ
PNAASEPDVA RAQTSAHRPS VADSIPAVIA SDTDAHSNTS APISAPQPRP EGNSDEYGLL
PVGWERRTDH LGRTYYVDHN MRSTTWTRPT GEAPQDTIEI DRARMNSTAV ADDFLGVENS
SVNSPSATPV GAASNATSAG AGPLPSGWEQ RTTADGRAYF VDHNTRTTTW VDPRRQQILR
VMGPNGNNLS LQPQSVSQLG PLPSGWEMRL TSTARVYFVD HNTKTTTWDD PRLPSSLDQN
VPQYKRDFRR KLIYFRSQPA LRPVPGQCHV KVRRTHIFED SYAEIMRQQP NDLKKRLMIK
FEGEDALDYG GVSREFFFLL SHEMFNPFYC LFEYSAHDNY TLQINPHSGI NPEHLNYFKF
IGRVLGLAIF HRRFLDAHFI VSFYKMILKK KILLSDMESV DADYYRSLQW MLDNPIDGVM
EETFSAIEDK FGEMITVELK PGGEHIDVTD DNKREYVERM VEWRIMKRVE EQFRAFISGF
SELIPLDLIN VFDERELELL MGGMSEIDVD DWKRFTDYRG FTEQDDVVQW FWQCVQKWPA
EQRSRLLQFA TGTSRIPVNG FKDLQGSDGP RRFTIEKSGE VNHLPKSHTC FNRIDLPPYP
SMEVLESKLV LAIEEGMRFG NE
//
