ID A0A091CI53_FUKDA Unreviewed; 764 AA.
AC A0A091CI53;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|PIRNR:PIRNR001569};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR001569};
GN ORFNames=H920_20531 {ECO:0000313|EMBL:KFO18079.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18079.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18079.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18079.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) 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; KN125550; KFO18079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CI53; -.
DR STRING; 885580.ENSFDAP00000007112; -.
DR eggNOG; KOG0940; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028990; 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:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 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; 3.
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; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transferase {ECO:0000256|PIRNR:PIRNR001569};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR001569}.
FT DOMAIN 11..135
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 173..206
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 267..300
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 313..346
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 430..764
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 732
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 764 AA; 88043 MW; 9201E644D4A2DB00 CRC64;
MCPLPPKHVI TLEENPVPIE LHISPCCHQF ILYFMLLLNY LIAINQGLPD PFAKVVVDGS
GQCHSTDTVK NTLDPKWNQH YDLYIGKSDS VTISVWNHKK IHKKQGAGFL GCVRLLSNAI
NRLKDTGYQR LDLCKLGPND NDTVRGQIVV SLQSRDRIGT GGQVVDCSRL FDNDLPDGWE
ERRTASGRIQ YLNHITRTTQ WERPTRPASE YSSPGRPLSC FVDENTPISG TNGATCGQSS
DPRLAERRVR SQRHRNYMSR THLHTPPDLP EGYEQRTTQQ GQVYFLHTQT GVSTWHDPRV
PRDLSNINCE ELGPLPPGWE IRNTATGRVY FVDHNNRTTQ FTDPRLSANL HLVLNRQNQL
KDQQQQQVVS LCPDDTECLT VPRYKRDLVQ KLKILRQELS QQQPQAGHCR IEVSREEIFE
ESYRQVMKMR PKDLWKRLMI KFRGEEGLDY GGVAREWLYL LSHEMLNPYY GLFQYSRDDI
YTLQINPDSA VNPEHLSYFH FVGRIMGMAV FHGHYIDGGF TLPFYKQLLG KSITLDDMEL
VDPDLHNSLV WILENDITGV LDHTFCVEHN AYGEIIQHEL KPNGKSIPVT EENKKEYVRL
YVNWRFLRGI EAQFLALQKG FNEVIPQHLL KTFDEKELEL IICGLGKIDV SDWKVNTRLK
HCTPDSNVVK WFWKAVEFFD EERRARLLQF VTGSSRVPLQ GFKALQGAAG PRLFTIHQID
ACTNNLPKAH TCFNRIDIPP YESYEKLYEK LLTAIEETCG FAVE
//