ID   A0A3Q2E0W6_CYPVA        Unreviewed;       286 AA.
AC   A0A3Q2E0W6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000025831.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000025831.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. {ECO:0000256|RuleBase:RU201113}.
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,
CC         ECO:0000256|RuleBase:RU201113};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}.
CC   -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC       ligase activity. {ECO:0000256|RuleBase:RU201113}.
CC   -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC       interaction with substrate proteins. It is related to the TRAF family.
CC       {ECO:0000256|RuleBase:RU201113}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_015239290.1; XM_015383804.1.
DR   AlphaFoldDB; A0A3Q2E0W6; -.
DR   Ensembl; ENSCVAT00000000625.1; ENSCVAP00000025831.1; ENSCVAG00000010927.1.
DR   GeneID; 107090431; -.
DR   CTD; 6477; -.
DR   GeneTree; ENSGT00940000154837; -.
DR   OMA; HSNTGCT; -.
DR   OrthoDB; 222086at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; 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; cd03829; Sina; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR004162; SINA-like_animal.
DR   InterPro; IPR049548; Sina-like_RING.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR45877:SF7; E3 UBIQUITIN-PROTEIN LIGASE SIAH1; 1.
DR   PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF03145; Sina_TRAF; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU201113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU201113};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU201113};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00455}.
FT   DOMAIN          45..80
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          97..157
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  31645 MW;  60E225A8AF2B3CE9 CRC64;
     MDEEMSRQTA TALPTGTSKC PPSQRVPTLS GTNASNSDLA SLFECPVCFD YVLPPILQCQ
     SGHLVCSNCR PKLTCCPTCR GPLGSIRNLA MEKVANSVLF PCKYASSGCE VTLPHTDKTE
     HEELCEFRPY SCPCPGASCK WQGSLDAVMP HLMHQHKSIT TLQGEDIVFL ATDINLPGAV
     DWVMMQSCFG FHFMLVLEKQ EKYDGHQQFF AIVQLIGTRK QAENFAYRLE LNGHRRRLTW
     EATPRSIHEG IATAIMNSDC LVFDTSIAQL FAENGNLGIN VTISMC
//