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Database: UniProt
Entry: A0A067EMA6_CITSI
LinkDB: A0A067EMA6_CITSI
Original site: A0A067EMA6_CITSI 
ID   A0A067EMA6_CITSI        Unreviewed;       374 AA.
AC   A0A067EMA6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=CISIN_1g017269mg {ECO:0000313|EMBL:KDO52347.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO52347.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO52347.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) 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};
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DR   EMBL; KK785035; KDO52347.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067EMA6; -.
DR   PaxDb; 2711-XP_006480869-1; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd16667; RING-H2_RNF126-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR010543; DUF1117.
DR   InterPro; IPR039525; RNF126-like_zinc-ribbon.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF256; E3 UBIQUITIN-PROTEIN LIGASE RHC2A-RELATED; 1.
DR   Pfam; PF06547; DUF1117; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   Pfam; PF14369; zinc_ribbon_9; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
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          188..229
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          63..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   374 AA;  41633 MW;  734AB5ABABEB819E CRC64;
     MSSIGLSYWC YRCNRIIRIQ SRTEDAIVCP DCHTGFIEQI ETIQRPSNER YPAAEMYLED
     TQNPETFPTT RFGRTRRNGG DRSPFNPVIV LRGPQTPDSG GGNEGTAMER GNFELFYDDA
     TGAGLRPLPA SMSDFLMGSG FDRVLDQLTQ LDFNGVTRFV NPPASKAAIE SMPVVTIAES
     HVAKESHCAV CKEPFQLNSE AREMPCKHIY HGECILPWLS MRNSCPLCRR ELPNEANDRG
     SNVGGGPDET LGLTIWRLPG GGFAVGRFNG SRRAAERELP VVFTEMDGGF NAPIGAPRRI
     SWVPSRRRAR EGNGFARAFR GFTSLLGRIR LPTSRATAEF NRRSPFLDVI YGRSSDTATA
     NYFSQFHVGG RRLY
//
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