ID A0A2G7FRM5_9EURO Unreviewed; 870 AA.
AC A0A2G7FRM5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE AltName: Full=HECT ubiquitin ligase A {ECO:0000256|ARBA:ARBA00029870};
DE Flags: Fragment;
GN ORFNames=AARAC_009444 {ECO:0000313|EMBL:PIG82925.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG82925.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG82925.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG82925.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:PIG82925.1}.
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DR EMBL; NEXV01000472; PIG82925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7FRM5; -.
DR STRING; 656916.A0A2G7FRM5; -.
DR OrthoDB; 5480520at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:PIG82925.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 47..167
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 284..317
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 388..421
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 448..481
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 537..870
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 189..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 838
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:PIG82925.1"
SQ SEQUENCE 870 AA; 98646 MW; EBCCFF224CD1785D CRC64;
CGGCARRELP FRLVLIGRFT PGGVYCQLPF YSTGWVPICP QTRRQAPWVE KRGCANESMT
CSQPNLRVTI IAADGLYKRD VFRFPDPFAV ATVGGEQTHT TSVIKKTLNP YWNEMFDLRV
NEDSILAIQI FDQKKFKKKD QGFLGVINVR IGDVIDLQMG GDEMLTRDLK KSNDNLVVHG
KLIINLSTNL STPNTNQANG LHRSHMQPST SSGLVPQVSA STPQPSPGPS QADPTASNPS
LHPQRVPSTT RPSSTIVPAN GPPAPPNGQQ GSRTNLSSFE DSQGRLPAGW ERREDNLGRT
YYVDHNTRTT TWTRPSNNYN EQTSRTQREA SMQLERRAHQ SRMLPEDRTG ASSPNLQENQ
QQAQTPPAGG SASAVSMMAT GATTAGTGEL PPGWEQRSTP EGRPYFVDHN TRTTTWVDPR
RQQYIRMYGQ NANGTNTTIQ QQPVSQLGPL PSGWEMRLTN TARVYFVDHN TKTTTWDDPR
LPSSLDQGVP QYKRDFRRKL IYFRSQPALR IMSGQCHVKV RRNNIFEDSY AEIMRQSASD
LKKRLMIKFD GEDGLDYGGL SREFFFLLSH EMFNPFYCLF EYSAHDNYTL QINPHSGVNP
EHLNYFKFIG RVVGLAIFHR RFLDSFFIGA FYKMMLRKKV SLQDMEGVDE DLHRNLTWTL
DNDIEGIIEL TFAVDDEKFG ERRTIDLKPG GRDIPVTNEN KGEYVELVTE WKIVKRVEEQ
FNAFMSGFNE LIPADLVNVF DERELELLIG GIADIDVDDW KKHTDYRGYQ ESDEVIQNFW
KIVRTWDAEQ KSRLLQFTTG TSRIPVNGFK DLQGSDGPRR FTIEKSGDPG ALPKSHTCFN
RLDLPPYKTN DVLEHKLSIA VEETLGFGQE
//
