ID A0A091NZ53_HALAL Unreviewed; 876 AA.
AC A0A091NZ53;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=N329_08087 {ECO:0000313|EMBL:KFP98514.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFP98514.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFP98514.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFP98514.1};
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}.
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DR EMBL; KK645342; KFP98514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NZ53; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000054379; 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; 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; 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:SF310; E3 UBIQUITIN-PROTEIN LIGASE NEDD4-LIKE; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 4.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 2.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 4.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 4.
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:UP000054379};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 94..127
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 286..319
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 398..431
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 449..482
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 541..875
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 843
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:KFP98514.1"
FT NON_TER 876
FT /evidence="ECO:0000313|EMBL:KFP98514.1"
SQ SEQUENCE 876 AA; 100809 MW; 025E6F0406D06CE7 CRC64;
TRDDFLGQVD VPLSHLPTED PTMERPYTFK DFLLRPRSHK SRVKGFLRLK MAYLPKNGGQ
EEENNDQRDE SEHGWDVVDP NDSASQRQEE LPPPPLPPGW EEKVDNLGRT YYVNHNNRTT
QWHRPSLIDV GSDSDNNIRQ INQEAAHRRF RSRRHISEDL EPEPMESGDI PEPWETISEE
ASASGDSLSL SLPPPPASPV SRTSPQELSE ELSRRLQVTP DSNGEQLSSL IQRDPSSRLR
SCSVTDTVAE QSQLSLQSGP SRRARSSTVT GGEEPTPSVA YVHTTPGLPS GWEERKDAKG
RTYYVNHNNR TTTWTRPIMQ LAEDGMVGST ANSSNHLSEP QIRRPRSLSS PTVTLSAPLE
GIKDSPVRRA VKDTLSNPQS PQPSPYNSPK PQHKIAQSFL PPGWEMRIAP NGRPFFIDHN
TKTTTWEDPR LKFPVHLRSK ASLNPNDLGP LPPGWEERIH LDGRTFYIDH NNKITQWEDP
RLQNPAITGP AVPYSREFKQ KYDYFRKKLK KPADIPNRFE MKLHRNNIFE ESYRRIMSVK
RPDVLKARLW IEFESEKGLD YGGVAREWFF LLSKEMFNPY YGLFEYSATD NYTLQINPNS
GLCNEDHLSY FTFIGRVAGL AVYHGKLLDG FFIRPFYKMM LGKPITLKDM ESVDSEYYNS
LKWILENDPT ELDLMFCIDE ENFGQTYQVD LKPNGSEIMV TNENKREYID LVIQWRFVNR
VQKQMNAFLE GFTELLPIDL IKIFDENELE LLMCGLGDVD VNDWRQHTIY KNGYCPNHPV
IQWFWKAVLL MDAEKRIRLL QFVTGTSRVP MNGFAELYGS NGPQLFTIEQ WGSPDKLPRA
HTCFNRLDLP LYESFEDLRE KLLMAVENAQ GFEGVD
//
