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Database: UniProt
Entry: A0A1S3E1B8_CICAR
LinkDB: A0A1S3E1B8_CICAR
Original site: A0A1S3E1B8_CICAR 
ID   A0A1S3E1B8_CICAR        Unreviewed;       295 AA.
AC   A0A1S3E1B8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC101489285 {ECO:0000313|RefSeq:XP_012569540.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_012569540.1};
RN   [1] {ECO:0000313|RefSeq:XP_012569540.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012569540.1};
RG   RefSeq;
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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family.
CC       {ECO:0000256|ARBA:ARBA00038033}.
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DR   RefSeq; XP_012569540.1; XM_012714086.2.
DR   AlphaFoldDB; A0A1S3E1B8; -.
DR   STRING; 3827.A0A1S3E1B8; -.
DR   PaxDb; 3827-XP_004494919-1; -.
DR   GeneID; 101489285; -.
DR   KEGG; cam:101489285; -.
DR   eggNOG; ENOG502QQHB; Eukaryota.
DR   OrthoDB; 901818at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087171; Chromosome Ca3.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR   GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd23127; RING-HC_BAH1-like; 1.
DR   CDD; cd14482; SPX_BAH1-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR033326; BAH1.
DR   InterPro; IPR004331; SPX_dom.
DR   InterPro; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR46764; E3 UBIQUITIN-PROTEIN LIGASE BAH1; 1.
DR   PANTHER; PTHR46764:SF2; E3 UBIQUITIN-PROTEIN LIGASE BAH1-LIKE-RELATED; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51382; SPX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          1..152
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   DOMAIN          219..268
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   295 AA;  33815 MW;  9C55F779E614B8BE CRC64;
     MKFGYTFKEY LQEEREWLVD ENCAHIEYNR LKNVLKSCQN CKDTSSDKDQ LCQCQSCPVC
     DQKFFSELMK EASDIAGYFS SRVQHLLHLH IAKGLQRYVL SLRQCFKNDR QALAQEGRIL
     IEYITMNAIA MRKILKKYDK VHSSMNGENF KSKMHAEHIE LLHSPWLIEL GAFYLNSSGQ
     DGCELDGVRG HFSCDFDVTN AVMTLILPDS IKLEYDLNCA ICLDFVFNPY ALGCGHFFCK
     SCACSAASVM TFQGLKAASP ESKCPICREG GVYSKAVRML ELDLLMKRRC KDYWN
//
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