ID A0A091IL39_EGRGA Unreviewed; 917 AA.
AC A0A091IL39;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=E3 ubiquitin-protein ligase HACE1 {ECO:0000256|ARBA:ARBA00040370};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE AltName: Full=HECT domain and ankyrin repeat-containing E3 ubiquitin-protein ligase 1 {ECO:0000256|ARBA:ARBA00042378};
DE AltName: Full=HECT-type E3 ubiquitin transferase HACE1 {ECO:0000256|ARBA:ARBA00041409};
DE Flags: Fragment;
GN ORFNames=Z169_00111 {ECO:0000313|EMBL:KFP09032.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP09032.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP09032.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP09032.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|ARBA:ARBA00037859}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
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DR EMBL; KK500575; KFP09032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091IL39; -.
DR STRING; 188379.A0A091IL39; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF363; E3 UBIQUITIN-PROTEIN LIGASE HACE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00632; HECT; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT REPEAT 39..71
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 72..104
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 105..137
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 138..170
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 171..196
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 582..917
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 884
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP09032.1"
FT NON_TER 917
FT /evidence="ECO:0000313|EMBL:KFP09032.1"
SQ SEQUENCE 917 AA; 103159 MW; 413A9258D5FB71EA CRC64;
DNETAVYTLM PMVMADQHRS VSELLSNSKF DVNYAFGRVK RSLLHIAANC GSVECLVLLL
KKGANPNYQD ISGCTPLHLA ARNGQKKCMS KLLEYSADVN ICNNEGLTAI HWLAVNGRTE
LLHDLVQHVS NVDVEDAMGQ TALHVACQNG HKTTVQCLLD SGADINRPNV SGATPLYFAC
SHGQRDTAQI LLMRGAKYLP DKNGITPLDL CVQGGYGETC EVLIQYHPRL FQTIIQMTQN
EDLRENMLRQ VLEHLSQQSE SQYLKILTSL AEVATTNGHK LLSLSSNYEA QMKSLLRIVR
IFCHVFRIGP SSPSNGNDMG YNGNKTPRSQ VFKVRKVYDV VRKIDVKEMN FTKHAFINQT
SHEQEPLELL WHSLDEWLVL IATELMKNKR DSANITSILL KQKGPDHQDA TPTPAFAAAG
TEGRKELSTD DGELKAYDVA GKQEACADCQ DVISMTANRL SAVIQAFYMC CSCQMPQGMT
SPRFIEFVCK HDDVLKCFVN RNPKIIFDHF HFLLECPELM SRFMHIIKAQ PFKDRCEWFY
EHLHAGQPDS DMVHRPVNEN DILLVHRDSI FRSSCEVVSK ANCAKLKQGI AVRFHGEEGM
GQGVVREWFD ILSSEIVNPD YALFTQSADG TTFQPNSNSS VNPDHLNYFR FAGQILGLAL
NHRQLVNIYF TRSFYKHILG IPVNYQDVAS IDPEYAKNLQ WILDNDISDL GLELTFSVET
DVFGAMEEVP LKPGGASILV TQENKAEYVQ LVTELRMTRA IQPQINAFLQ GFHMFIPPSL
IQLFDEYELE LLLSGMPEID VNDWLKNTEY TSGYERGDQV IQWFWDVVEE LTQEERVLLL
QFVTGSSRVP HGGFAHIMGG SGLQNFTIAA VPYTANLLPT SSTCINMLKL PEYPSKEILK
DRLLVALHCG SYGYTMA
//
