ID   G3Q031_GASAC            Unreviewed;       491 AA.
AC   G3Q031;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023221.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000023221.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000023221.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   AlphaFoldDB; G3Q031; -.
DR   STRING; 69293.ENSGACP00000023221; -.
DR   Ensembl; ENSGACT00000023266.1; ENSGACP00000023221.1; ENSGACG00000017571.1.
DR   eggNOG; KOG4430; Eukaryota.
DR   GeneTree; ENSGT00530000064170; -.
DR   InParanoid; G3Q031; -.
DR   OMA; PEPNCAI; -.
DR   TreeFam; TF339497; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000017571; Expressed in testis and 11 other cell types or tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd16574; RING-HC_Topors; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR   PANTHER; PTHR46077:SF1; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13923; zf-C3HC4_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          29..68
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          317..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          367..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          457..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        326..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  55276 MW;  0E931AAD370822F6 CRC64;
     MGGDVIRGKP LNAIILQQIS VHVSPDSKCP ICLDQFNNIS YLDVCLHKFC FRCIHEWSKN
     KAECPLCKQS FNSIYHSINS EQDFKKYDLQ PVENASFGTF GGVRFRYRTT LTGVHRQMRG
     RTSPPPDNGV MFEASSNPPQ QPQDRYIRRV MMRLAAKRRA ASEGRAVNSL REQEMVNFRR
     ELYRQGVKIR SVRDGGRSRD TSAEFFQRNP ACLHRLIPWL KRELVVLYGA HGSLVNIVQH
     IIMSRITRYD MEDGAIQEEL RPFLQGRTEH FLHEFISFAK CPFNMEAYDQ HAVYDCPAAS
     SNEDSSASSS VIAISEDEEY SAESNPPGDP ASSLSHSLWD DETPGPSYST TAEQARAECL
     SVLDLDSDSS LEEETREFGA SPQEMSPHNL TEETRGPFEN EESPPYDSDD CVIISVVKPT
     ADRTPELVQL SSDSDESASE DIKAVPLLPQ HIRFSSLSPV ASQSSDPSGA GQSENVETDL
     YHKKHKKKSR K
//