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Database: UniProt
Entry: A0A091CI53_FUKDA
LinkDB: A0A091CI53_FUKDA
Original site: A0A091CI53_FUKDA 
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
//
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