ID   A0A1S2YTX1_CICAR        Unreviewed;       333 AA.
AC   A0A1S2YTX1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=LOC101496698 {ECO:0000313|RefSeq:XP_004509846.1};
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_004509846.1};
RN   [1] {ECO:0000313|RefSeq:XP_004509846.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004509846.1};
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. ATL subfamily.
CC       {ECO:0000256|ARBA:ARBA00024209}.
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DR   RefSeq; XP_004509846.1; XM_004509789.3.
DR   AlphaFoldDB; A0A1S2YTX1; -.
DR   PaxDb; 3827-XP_004509846-1; -.
DR   GeneID; 101496698; -.
DR   KEGG; cam:101496698; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   OrthoDB; 400239at2759; -.
DR   Proteomes; UP000087171; Chromosome Ca7.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45768; E3 UBIQUITIN-PROTEIN LIGASE RNF13-LIKE; 1.
DR   PANTHER; PTHR45768:SF54; RING-H2 FINGER PROTEIN ATL47; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          93..135
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   333 AA;  37188 MW;  FED52863542607B6 CRC64;
     MTPAIVFIIV ILAIVFFITG ILQLLVRFII RKRSSSTVSQ SNNYPQISES DPYQRQLQQL
     FNLHDSGLDQ AFIDALPLFL YKEIIGLKEP FDCAVCLCQF TEQDMLRLLP LCNHAFHVDC
     IDTWLLSNST CPLCRGSLYE HGFAFENPVF YDFESLREET GVSCSVVGDA GSVNKHAENH
     IMSGKRVFSV RLGKFRSSNN AEGESSNSNS TTCTSVVDVR RCYSMGSYKY VVDDSDLVVA
     LCPNRGEEVG TSVSMRQQLK GGFVPNENSS IDGGDVEGKR INIARKGESF SISKIWLWSR
     KDKVSSSSSQ SHLVNSNVNS TLPWMNRELK EAT
//