ID A0A087QJ00_APTFO Unreviewed; 883 AA.
AC A0A087QJ00;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=AS27_09405 {ECO:0000313|EMBL:KFM01204.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM01204.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM01204.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM01204.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KL225647; KFM01204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QJ00; -.
DR STRING; 9233.A0A087QJ00; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 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 Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR017134; UBE3A.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:KFM01204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053286};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 555..883
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 92..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 851
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM01204.1"
FT NON_TER 883
FT /evidence="ECO:0000313|EMBL:KFM01204.1"
SQ SEQUENCE 883 AA; 101375 MW; 5144C92D061EA610 CRC64;
CHRMATACKR SPGEPHSENI ETSRMKRAAA KHLIERYYHQ LTEGCGNEAC TNEFCASCPT
FLRMDNNAAA IKALELYKIN AKLCDPHPSK KGTSSAYLEN NSKGAHNNSC TDRKMNKKEM
QGPRDDFKDV TFLTEDKIYE ILELCREKED YSPLIRVIGR VFSSAEALVQ SFRKAKQHTK
EELKSLQGKD EDKDEDEKEK AACSAAAMEE DSGASSSSSS RIGDNTQGDN NLQKLGPDEV
SVDIEAVRRV YDRLLSNEKI ETAFLNALVY LSPNVECDLT YHNVYSRDPN YLNLFIIVME
NGNLHSPEYL EMALPLFCKA MSKLPLAAQA KLVRLWSKYR ADQIRRMMET FQQLITYKVI
SNEFNSRNLV NDDDAVVAAS KCLKMVYYAN VVGGDVDTDH NEEEDEEPIP ESSELTLQEL
LGEERRNKKG PRVDPLETEL GVKTIDCRKP LIPFEEFINE PLNDVLEMDK DYTFFKVETE
NKFSFMTCPF ILNAVTKNLG LYYDNRIRMY SERRITVLYS LVQGQQLNPY LRLKVRRDHI
IDDALVRLEM IAMENPADLK KQLYVEFEGE QGVDEGGVSK EFFQLVVEEI FNPDIGMFTY
DESTKLFWFN PSSFETEGQF TLIGIVLGLA IYNNCILDVH FPMVVYRKLM GKKGTFRDLA
DSHPVLYQSL RDLLEYEGSV EDDMMITFQI SHTDLFGNPM MHDLKENGDK IPITNENRKE
FVNLYADYIL NKSVEKQFKA FRRGFHMVTN ESPLKYLFRP EEIELLICGS RNLDFQALEE
TTEYDGGYTR DSLIIREFWE IVHSFTDEQK RLFLQFTTGT DRAPVGGLGK LKMIIAKNGP
DTERLPTSHT CFNVLLLPEY SSKEKLKERL LKAITYAKGF GML
//
