ID A0A091CNQ4_FUKDA Unreviewed; 1093 AA.
AC A0A091CNQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=H920_17990 {ECO:0000313|EMBL:KFO20604.1};
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:KFO20604.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO20604.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO20604.1};
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KN124686; KFO20604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CNQ4; -.
DR STRING; 885580.ENSFDAP00000004196; -.
DR eggNOG; KOG0940; Eukaryota.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd08691; C2_NEDL1-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 2.
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; IPR037795; C2_HECW.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR040524; HECW1_helix.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF18436; HECW1_helix; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 2.
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; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..104
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 318..351
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 505..538
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 758..1093
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1061
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1093 AA; 123995 MW; 736AE7A650C467AE CRC64;
MGLKKGMFFN PDPYLKISIQ PGKHSIFPAL PHHGQERRSK VIGNTVNPIW QAEQFSFVSL
PTDVLEIEVK DKFAKSRPII KRFLGKLSMP VQRLLERHAI GDRVVSYTLG RRLPTDHVSG
QLQFRFEITS SIHPGDAHQS TGSESDSSPR PGGEHSCEGC DASCCSPSCH SSSCYSASCY
SSSCYSASCH SPSCYNGGNR FASHTRFSSV DSAKVSESTV FSSQDDDDDE ENSAFESVPD
SVQSPELDPE ATNGVGPWQD ELATPGGTVA RTAEGLECPV AGPSHRREGE CPILHNSQPV
SQLPSLRPEH HHYPTIDEPL PPNWEARIDS HGRVFYVDHV NRTTTWQRPT AAATPDGMRR
SGSVQQMEQL NRRYQNIQRT IATERPEEDS GSQSCEQVLA GGGGGSDSEA ESSQSSLDLR
REGSLSPVNS QKITLLLQSP AVKFITNPEF FTVLHANYSA YRVFTSSTCL KHMILKVRRD
ARNFERYQHN RDLVNFINMF ADTRLELPRG WEIKTDQQGK SFFVDHNSRA TTFIDPRIPL
QNGRLPNHLT HRQHLQRLRS YSAGEASEVS RNRGASLLAR PGHSLVAAIR SQHQHESLPL
AYNDKIVAFL RQPNIFEMLQ ERQPSLARNH ALREKIHYIR TEGNHGLEKL SCDADLVILL
SLFEEEIMSY VPLQASFHPG YSFSPRCSPC SSPQNSPGLQ RASARAPSPY RRDFEAKLRN
FYRKLEAKGF GQGPGKIKLI IRRDHLLEGT FNQVMAYSRK ELQRNKLYIT FVGEEGLDYS
GPSREFFFLL SQELFNPYYG LFEYSANDTY TVQISPMSAF VENHLEWFRF SGRILGLALI
HQYLLDAFFT RPFYKALLRL PCDLSDLEYL DEEFHQSLQW MKDNNITDIL DLTFTVNEEV
FGQVTERELK SGGANTQVTE KNKKEYIERM VKWRVERGVV QQTEALVRGF YEVVDSRLVS
VFDARELELV IAGTAEIDLN DWRNNTEYRG GYHDGHLVIR WFWAAVERFN NEQRLRLLQF
VTGTSSVPYE GFAALRGSNG LRRFCIEKWG KITSLPRAHT CFNRLDLPPY PSYSMLYEKL
LTAVEETSTF GLE
//
