ID A0A7K6LVP8_9CORV Unreviewed; 282 AA.
AC A0A7K6LVP8;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 08-OCT-2025, entry version 17.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
DE Flags: Fragment;
GN Name=Siah1 {ECO:0000313|EMBL:NWW28947.1};
GN ORFNames=FALFRO_R14264 {ECO:0000313|EMBL:NWW28947.1};
OS Falcunculus frontatus (Eastern shriketit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Corvoidea; Pachycephalidae; Falcunculus.
OX NCBI_TaxID=254539 {ECO:0000313|EMBL:NWW28947.1, ECO:0000313|Proteomes:UP000534626};
RN [1] {ECO:0000313|EMBL:NWW28947.1, ECO:0000313|Proteomes:UP000534626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-029-77 {ECO:0000313|EMBL:NWW28947.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NWW28947.1}.
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DR EMBL; VZRV01010995; NWW28947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K6LVP8; -.
DR SMR; A0A7K6LVP8; -.
DR OrthoDB; 941555at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000534626; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd03829; Sina; 1.
DR FunFam; 2.60.210.10:FF:000002; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.160.60:FF:000665; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000050; E3 ubiquitin-protein ligase; 1.
DR FunFam; 3.30.40.10:FF:000063; E3 ubiquitin-protein ligase; 1.
DR Gene3D; 2.60.210.10; Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2, Chain A; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:NWW28947.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU201113}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000534626};
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 41..76
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 93..153
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWW28947.1"
FT NON_TER 282
FT /evidence="ECO:0000313|EMBL:NWW28947.1"
SQ SEQUENCE 282 AA; 31127 MW; FA07CC94DC1973D5 CRC64;
MSRQTATALP TGTSKCTPSQ RVPALTGTTA SNNDLASLFE CPVCFDYVLP PILQCQSGHL
VCSNCRPKLT CCPTCRGPLG SIRNLAMEKV ANSVLFPCKY ASSGCEITLP HTEKADHEEL
CEFRPYSCPC PGASCKWQGS LDAVMPHLMH QHKSITTLQG EDIVFLATDI NLPGAVDWVM
MQSCFGFHFM LVLEKQEKYD GHQQFFAIVQ LIGTRKQAEN FAYRLELNGH RRRLTWEATP
RSIHEGIATA IMNSDCLVFD TSIAQLFAEN GNLGINVTIS MC
//
