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Database: UniProt
Entry: A0A068U3F4_COFCA
LinkDB: A0A068U3F4_COFCA
Original site: A0A068U3F4_COFCA 
ID   A0A068U3F4_COFCA        Unreviewed;       369 AA.
AC   A0A068U3F4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, 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   ORFNames=GSCOC_T00039434001 {ECO:0000313|EMBL:CDP02138.1};
OS   Coffea canephora (Robusta coffee).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC   Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX   NCBI_TaxID=49390 {ECO:0000313|EMBL:CDP02138.1, ECO:0000313|Proteomes:UP000295252};
RN   [1] {ECO:0000313|Proteomes:UP000295252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DH200-94 {ECO:0000313|Proteomes:UP000295252};
RX   PubMed=25190796; DOI=10.1126/science.1255274;
RA   Denoeud F., Carretero-Paulet L., Dereeper A., Droc G., Guyot R.,
RA   Pietrella M., Zheng C., Alberti A., Anthony F., Aprea G., Aury J.M.,
RA   Bento P., Bernard M., Bocs S., Campa C., Cenci A., Combes M.C.,
RA   Crouzillat D., Da Silva C., Daddiego L., De Bellis F., Dussert S.,
RA   Garsmeur O., Gayraud T., Guignon V., Jahn K., Jamilloux V., Joet T.,
RA   Labadie K., Lan T., Leclercq J., Lepelley M., Leroy T., Li L.T.,
RA   Librado P., Lopez L., Munoz A., Noel B., Pallavicini A., Perrotta G.,
RA   Poncet V., Pot D., Priyono X., Rigoreau M., Rouard M., Rozas J.,
RA   Tranchant-Dubreuil C., VanBuren R., Zhang Q., Andrade A.C., Argout X.,
RA   Bertrand B., de Kochko A., Graziosi G., Henry R.J., Jayarama X., Ming R.,
RA   Nagai C., Rounsley S., Sankoff D., Giuliano G., Albert V.A., Wincker P.,
RA   Lashermes P.;
RT   "The coffee genome provides insight into the convergent evolution of
RT   caffeine biosynthesis.";
RL   Science 345:1181-1184(2014).
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   EMBL; HG739092; CDP02138.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A068U3F4; -.
DR   EnsemblPlants; CDP02138; CDP02138; GSCOC_T00039434001.
DR   Gramene; CDP02138; CDP02138; GSCOC_T00039434001.
DR   InParanoid; A0A068U3F4; -.
DR   OMA; HLKSSWI; -.
DR   PhylomeDB; A0A068U3F4; -.
DR   Proteomes; UP000295252; Chromosome 7.
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:SF18; RING-H2 FINGER PROTEIN ATL18-RELATED; 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:UP000295252};
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        55..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          144..186
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   369 AA;  40765 MW;  394822D4A84C163E CRC64;
     MSWIQHQLNQ KDGILTYPPP FPLSASSPPY VTGDNFHKES SHPTSSSSGT RISPAVLFII
     VILAVLFFIS GLLHLLVRFL IKHPSSSASS QSSRYPEVST SDALQRQLQQ LFHLHDSGLD
     QSFIDALPVF VYKEIVGAKE PFDCAVCLCE FSEKDQLRLL PMCSHAFHIN CIDTWLLSNS
     TCPLCRGTLF NPGFSIENPV YDFDDLREDD GYPVSTENGI STRQKAVEIE EVAVEKGVFP
     VRLGKFRKLS GEEGEAGGET SSSNLDARRC YSLGSYQYVV GDSHLRVALS HDHIGRDVSL
     LKDRGQSNPP VSEDGAGKKI DIGAKTDSYS VSKIWLWPRK GKFASSADTP SEDVSFAADL
     PWMRRAEGM
//
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