ID A0A428P3M8_9HYPO Unreviewed; 814 AA.
AC A0A428P3M8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=CEP53_009872 {ECO:0000313|EMBL:RSL47599.1};
OS Fusarium sp. AF-6.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325737 {ECO:0000313|EMBL:RSL47599.1, ECO:0000313|Proteomes:UP000287544};
RN [1] {ECO:0000313|EMBL:RSL47599.1, ECO:0000313|Proteomes:UP000287544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62590 {ECO:0000313|EMBL:RSL47599.1,
RC ECO:0000313|Proteomes:UP000287544};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-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}.
CC -!- SIMILARITY: Belongs to the RSP5/NEDD4 family.
CC {ECO:0000256|ARBA:ARBA00010334}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSL47599.1}.
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DR EMBL; NKCJ01000262; RSL47599.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428P3M8; -.
DR STRING; 1325737.A0A428P3M8; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000287544; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000287544};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 231..264
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 332..365
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 391..424
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 480..814
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 144..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 782
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 814 AA; 91973 MW; F0ED63A366CE4789 CRC64;
MTSRTDSGLP NRPNLRVTII AADGLYKRDV FRFPDPFAVA TINGEQTKTT TVSKRTLNPY
WNESFDFRSN EDSILAVQVF DQKKFKKKDQ GFLGVINIRV GDVMPELSAD ADDQMLTRDL
KKSTDNLVVH GKLIINLSCN LSAPARGGQA SSTRPSLGAG PSNLSSLSAP PPDNRPGSSM
SGPNGAASSQ VNLPHRPSSI NSVGGASAPG PNVSGQPRQS NQLSPFEDAQ GRLPAGWERR
EDNLGRTYYV DHNTRTTSWN RPTSNGTQEQ RNDREAATQV ERQRHQNRTL PEDRTGSNSP
TLQAQQPQQS SSPTANAGGA VMHTGATSPG SGELPPGWEQ RWTPEGRPYF VDHNTRTTTW
VDPRRQQYIR MYGGQNNANG QIQQQPVSQL GPLPSGWEMR LTNTARVYFV DHNTKTTTWD
DPRLPSSLDQ NVPQYKRDFR RKLIYFRSQP AMRILSGQCH IKVRRSHIFE DSFAEITRQS
ATDLKKRLMI KFDGEDGLDY GGLSREFFFL LSHEMFNPFY CLFEYSAHDN YTLQINPHSG
INPEHLNYFK FIGRVVGLAI FHRRFLDAFF IGALYKMMLG KAVALADMEG VDADFHRSLQ
WMLDNDISGG ILEQTFSTED ERFGVMTTED LIPNGRNIEV TNENKKEYVD LMVKWRIEKR
IAEQFQAFKE GFQELIPQDL INVFDERELE LLIGGIAEID VDDWKKHTDY RGYTESDEVV
QNFWATVRSW DGEQKSRLLQ FTTGTSRIPV NGFKDLQGSD GPRRFTIEKA GEITNLPKAH
TCFNRLDLPA YKSLEMLQQK LTIAVEETMG FGQE
//
