ID A0A093HPX8_STRCA Unreviewed; 887 AA.
AC A0A093HPX8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=N308_02765 {ECO:0000313|EMBL:KFV84703.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV84703.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV84703.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV84703.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL206666; KFV84703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093HPX8; -.
DR STRING; 441894.ENSSCUP00000019555; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000053584; 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; cd04033; C2_NEDD4_NEDD4L; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 4.
DR Gene3D; 2.20.70.10; -; 3.
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:SF282; E3 UBIQUITIN-PROTEIN LIGASE NEDD4; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 4.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
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; 4.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 4.
DR PROSITE; PS50020; WW_DOMAIN_2; 4.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..109
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 177..210
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 334..367
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 409..442
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 460..493
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 552..886
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 164..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 854
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:KFV84703.1"
FT NON_TER 887
FT /evidence="ECO:0000313|EMBL:KFV84703.1"
SQ SEQUENCE 887 AA; 102755 MW; 474A52ADCE4085CB CRC64;
ENTRIVRVKI IAGIGLAKKD ILGASDPYVK VTVYDPVNGV LTSVQTKTIR KSLNPKWNEE
LLFRVNPQKH RLLFEVFDEN RLTRDDFLGQ VDIPLHQLPT ENPSMERPYT FKDFVLHPRS
HKSRVKGHLR LKMTYLPKNN GSEEETTEQA EELEPGWIIL DQPDAASQPQ QQQQESPPLP
PGWEERQDIL GRTYYVNHEF RRTQWKRPTA QDNVAVADIG NIQLEAQHAF AHRRQISEDT
ENLDSRDSPE SWEIITEDEA TMYSNQNLHI PLPQSNCDVQ THLAEELNAR LSTSGSSATG
QSAVYTNHSS RRGSLQTYRI EEQPALPVLL PTSSGLPPGW EERQDEKGRS YYIDHNSRTT
TWIKPVVQIA IEAGQLSTAQ SVSIGRQPQA TSSDSSQQSS KQQPETEQGF LPKGWEVRHA
PNGRPFFIDH NTKTTTWEDP RLKIPAHLRR KTSLDPVDLG PLPPGWEERT HTDGRIFYIN
HNTKRTQWED PRLQNVAITG PAVPYSRDYK RKYEFFRKKL KKQSDIPNRF EMKIHRTTIL
EDSYRRIIAV KRADFLKARL WIEFDGEKGL DYGGVAREWF FLLSKEMFNP YYGLFEYSAA
DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD AFFIRPFYKM MLQKPITLHD
MESVDSEYYN SLRWILENDP AELDLRFIVD EELFGQTHQH ELKSGGSEIV VTNKNKRDYI
HLVIQWRFVS RVQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVADWKLHTK
YKNGYNVNHQ VIQWFWKAVL MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQLFTVE
QWGTPEKLPR AHTCFNRLDL PPYESFEDLW DKLLLAIENA QGFDGVD
//
