ID A0A3Q1EX56_9TELE Unreviewed; 1081 AA.
AC A0A3Q1EX56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000009801.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000009801.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q1EX56; -.
DR STRING; 80966.ENSAPOP00000009801; -.
DR Ensembl; ENSAPOT00000000950.1; ENSAPOP00000009801.1; ENSAPOG00000012231.1.
DR GeneTree; ENSGT00940000156321; -.
DR InParanoid; A0A3Q1EX56; -.
DR OrthoDB; 1386at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0000209; P:protein polyubiquitination; 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 InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 742..1081
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1049
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1081 AA; 123278 MW; DA871B21B6DAFCF3 CRC64;
MFSFEGDFKT RPKVSLGGAS KKEEKASLLH RTQEERRKRE DERKRLKNAI IIQSYIRGYQ
DLKHQYAIQR AKFDECVSKT QAGGGQHVLD GAGLCLLSRQ LIFFYRQSVD AHRLIWLCQN
LVKHNSQFVK LLVGPQKQTC MFQIKRLLGF CCRLLQNCMD DSLNVAVPMR MLEIFSSERT
YLPVIPDANY VASLLEQILH YMVQKGYYRS LYILVNHRLP SSLEYTDAPS IPLASTLLEH
ILKPLHFTYS SCTTGARQFV FAAFTEEFIS APFTEQIFHF FIPALSDFRH SFPFEAFLSS
LKATIDSSSA AQSQAPWLFY FVLSAGENCL GSLSEEGLLL YLRALQTLLP LLPVSESSSR
PEVTSDSEDD DDAGIHPLPM QDDSRISVQL ITEECVHKLD TKQQTNALLN LVWRDSASEE
VFTMMASICH TLMVQHRLMV PKVRLLYSLA FNARFLRHLW HLITSMTTKM ITGSMVPLLQ
LISRGSPMSF EDSNRIIPLF YLFSSLFSHS LISVHDSEFF GHEMEGQTQS SMMPFTLSEL
VTLSRCLRDA CLGIIKLAYP ETKTEHREEY MAAFRSVGVK TNTEVQQRIQ AEQKRWVQLF
KVITNLVKMV KARDIRRPFC PAGHWLSEEV NIRADKVTQL YVPSARHVWR ARRMGRIGPL
QSTLDVGSEP PQLSVSEERH LAILTELPFV VPFEERVKIF QRLIYADKRD VQGDGPFPDG
INVTIRRNYI YEDAYDKLSP ENEPDLKKRI RVHLLNAHGL DEAGIDGGGI FREFLNELLK
SGFNPNQGFF KTTNEGLLYP SPAAEMLVGD SFTRHYYFLG RILGKALYEN MLVELPFASF
FLSKLLGTSA DVDIHHLASL DPEMYRNLLF LKSYEGDVEE LGLNFTVVNN DLGEAQVVEL
KPGGKDIPVT TANRIAYIHL VADYRLNKQI RPHCLAFRQG LANVVNLEWL RMFDQQEIQV
LISGAHVPIC LDDLKNFTNY SGGYSATHPV IQTFWEVVEG FTDEEKRKLL KFVTSCSRPP
LLGFKELYPA FCIHNGGSDL ERLPTASTCM NLLKLPEFCD QHLMRNKLLY AIESSAGFEL
S
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