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Database: UniProt
Entry: A0A3B4GMR2_9CICH
LinkDB: A0A3B4GMR2_9CICH
Original site: A0A3B4GMR2_9CICH 
ID   A0A3B4GMR2_9CICH        Unreviewed;       833 AA.
AC   A0A3B4GMR2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=ube3a {ECO:0000313|RefSeq:XP_005727205.1};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000024290.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000024290.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_005727205.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_005727205.1; XM_005727148.1.
DR   AlphaFoldDB; A0A3B4GMR2; -.
DR   STRING; 303518.ENSPNYP00000024290; -.
DR   Ensembl; ENSPNYT00000024887.1; ENSPNYP00000024290.1; ENSPNYG00000018338.1.
DR   GeneID; 102199625; -.
DR   CTD; 7337; -.
DR   GeneTree; ENSGT00940000155050; -.
DR   OrthoDB; 5471864at2759; -.
DR   Proteomes; UP000261460; Unplaced.
DR   Proteomes; UP000695023; Unplaced.
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   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   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   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|RefSeq:XP_005727205.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000695023};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          505..833
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          70..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..92
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        801
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   833 AA;  94942 MW;  0B1167FB1F53C260 CRC64;
     MNRATAKLLI ERYFRQLTEG CGNGNCTNEF CASCCDFQPL DNNSAAAKAL ELFKINAKLC
     DYHPSITANA DGRTQEGSEM SDKDPSFTKE DFSEVHHLTE NTVCTILSFC EEEGDYSALV
     RVIGRVFSNA EALMKSFRKD ESNSTDNLES CKPADMNKDE KQSERSSEKT GASSAASLPG
     EALNEVFDAC EVTVDIGAVR RVYDRLLPID QLQVALVNAL IYLTPNVELD LEYLDVYETN
     PDYLNIFIIV MENSNLHSPE YLEVALPQFC KAMSKLPVTA LARLTKLWSK YDLPHIRRMM
     ETFQQLITFT VVSNEYDGEN LVNDDETVVA ATQCLQVVFF ASILGGDVDV EHNEEDEEDS
     DSDELTLHEL LGEERLYKKG PRINPLEKEL GVRPMDSIKP LIPFEDFINE SLNDVIEMDK
     DFTFFKVNAE TKFSFQTCPF ILSVITKNQG LYYDNRIRMY SERRLTALFS MVQGQQPNPY
     LKLKVRRDHI IDDALVRLEM ISMENPSDLK KQLYVEFEGE QGVDEGGVSK EFFQLVLEEI
     FNPDIGMFTY ENDTKLFWFN SSSLETEAQY TLIGIVLGLA IYNNCILDVH FPMVVYRKLM
     GKKGTYLDLS DSHPVLYQSL KGVLEYMGNV EEDMMMTFQI SHTDLFGNPV IHDLKEQGDQ
     IPVTKENRQE FVDVYADYIL NKSVERQFKA FKKGFLMVTN ESPLKYLFRP EEVELLICGS
     RKLDFEALEK TTEYDGGYSK DSQVIKDFWE VVHSFGEDQK KFFLQFTTGS DRAPVGGLGK
     LKMIIAKNGS DTDRLPTSHT CFNALLLPEY SSKEKLRERL LKAITYAKGF GML
//
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