ID   A0A3B4ZUX9_9TELE        Unreviewed;       341 AA.
AC   A0A3B4ZUX9;
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=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN   Name=siah1 {ECO:0000313|RefSeq:XP_008281620.1,
GN   ECO:0000313|RefSeq:XP_008281621.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000012090.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000012090.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008281620.1, ECO:0000313|RefSeq:XP_008281621.1}
RP   IDENTIFICATION.
RG   RefSeq;
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}.
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DR   RefSeq; XP_008281620.1; XM_008283398.1.
DR   RefSeq; XP_008281621.1; XM_008283399.1.
DR   AlphaFoldDB; A0A3B4ZUX9; -.
DR   STRING; 144197.ENSSPAP00000012090; -.
DR   Ensembl; ENSSPAT00000012296.1; ENSSPAP00000012090.1; ENSSPAG00000009177.1.
DR   GeneID; 103358431; -.
DR   CTD; 6477; -.
DR   GeneTree; ENSGT00940000154837; -.
DR   OrthoDB; 222086at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; 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; cd16752; RING-HC_SIAH2; 1.
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:UP000694891};
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          100..135
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          152..212
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
SQ   SEQUENCE   341 AA;  37823 MW;  5BE3215DC828FB74 CRC64;
     MSVVQVKSKP ASVALQAPPW NYLFRLFSCV ATRNVHRTKE VPTFQEKTTA LFGNLMDEEM
     SRQTATALPT GTSKCPPSQR VPTLSGTTAS NSDLASLFEC PVCFDYVLPP ILQCQSGHLV
     CSNCRPKLTC CPTCRGPLGS IRNLAMEKVA NSVLFPCKYA SSGCEVTLPH TDKTEHEELC
     EFRPYSCPCP GASCKWQGSL DAVMPHLMHQ HKSITTLQGE DIVFLATDIN LPGAVDWVMM
     QSCFGFHFML VLEKQEKYDG HQQFFAIVQL IGTRKQAENF AYRLELNGHR RRLTWEATPR
     SIHEGIATAI MNSDCLVFDT SIAQLFAENG NLGINVTISM C
//