ID A0A9P0Q5R3_ACAOB Unreviewed; 416 AA.
AC A0A9P0Q5R3;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ACAOBT_LOCUS32505 {ECO:0000313|EMBL:CAH2011936.1};
OS Acanthoscelides obtectus (Bean weevil) (Bruchus obtectus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Acanthoscelides.
OX NCBI_TaxID=200917 {ECO:0000313|EMBL:CAH2011936.1, ECO:0000313|Proteomes:UP001152888};
RN [1] {ECO:0000313|EMBL:CAH2011936.1}
RP NUCLEOTIDE SEQUENCE.
RA Sayadi A.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
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:CAH2011936.1}.
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 EMBL; CAKOFQ010008127; CAH2011936.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P0Q5R3; -.
DR OrthoDB; 620422at2759; -.
DR Proteomes; UP001152888; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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 FunFam; 3.30.40.10:FF:000041; E3 ubiquitin-protein ligase SINAT3; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR004162; SINA-like_animal.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR PANTHER; PTHR45877:SF2; E3 UBIQUITIN-PROTEIN LIGASE SINA-RELATED; 1.
DR Pfam; PF21362; Sina_RING; 1.
DR Pfam; PF21361; Sina_ZnF; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 2.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP001152888};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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:PRU00455}.
FT DOMAIN 69..130
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT DOMAIN 270..305
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 322..380
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
SQ SEQUENCE 416 AA; 48412 MW; 920DDB9418748162 CRC64;
MAEQSMSSFV DEILEMNCLS CVICKEVLRP PIMLTQNLGN VCSTCYEEKC ELSQMTSLPN
EPMEKILKLM KLPCRYKQKG CEETLSYEDL LTHQNSCRYR TKLCALFRFT GCDWEGNRND
FATHFKECHG DHVINFENNI FFLETSLRDL NLVKLLIMNK KVYILRMQTN PTKKKLFYMI
CNVKDEHSSF CEYSVKHKGS SDNYIKTKSK ILSSYNIYNE FDENIAVQVD LEALKQISQI
SDTITNIFKI KAEESRAEHL DEKILHFFEC PVCKNYMKPP IYQCQSGHSI CNSCRPRLEK
CPTCRAIFGS TRNYSLEGLT SGVQYPCLYH DLGCPETAIA NVISRHEREC QFKPYSCPFT
NCTSTGNYHT MINHLIAFHS ESVIYNGATG MHLILFLYHT EYFKNREGRF KRWYGL
//
