ID   E5GCQ3_CUCME            Unreviewed;       265 AA.
AC   E5GCQ3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Cucumis melo subsp. melo.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=412675 {ECO:0000313|EMBL:ADN34252.1};
RN   [1] {ECO:0000313|EMBL:ADN34252.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Young leaves {ECO:0000313|EMBL:ADN34252.1};
RX   PubMed=20509895; DOI=10.1186/1471-2164-11-339;
RA   Gonzalez V.M., Garcia-Mas J., Arus P., Puigdomenech P.;
RT   "Generation of a BAC-based physical map of the melon genome.";
RL   BMC Genomics 11:339-339(2010).
RN   [2] {ECO:0000313|EMBL:ADN34252.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Young leaves {ECO:0000313|EMBL:ADN34252.1};
RX   PubMed=21073723; DOI=10.1186/1471-2229-10-246;
RA   Gonzalez V.M., Benjak A., Henaff E.M., Mir G., Casacuberta J.M.,
RA   Garcia-Mas J., Puigdomenech P.;
RT   "Sequencing of 6.7 Mb of the melon genome using a BAC pooling strategy.";
RL   BMC Plant Biol. 10:246-246(2010).
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; HM854819; ADN34252.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5GCQ3; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15710; E3 UBIQUITIN-PROTEIN LIGASE PRAJA; 1.
DR   PANTHER; PTHR15710:SF239; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 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   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          212..258
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   265 AA;  30863 MW;  552CA408E08EA4E7 CRC64;
     MAEEIFNICR YGSGSYMGMS LRITDPNPRH QPLNQIDQTS SPTLVEQICL KFKVQLKCQH
     FQVWEGGNGH STTLVREHIR SQHSFATFQL PISIFKHGDK TLKRILFREF KMYGDIINIE
     LLANEIIKHW VRKVEEEEDQ ENNSNVLFKK IYPLEIMIRL LVSKMIRAVQ PRLAMIDQPL
     MVPTSDSAVE SMLKRVENEE IMKSGDDESI NCVVCLEEIS KEEKGSETTV LQMPCLHMFH
     EECIRKWLKT SHYCPTCRFS MPIDN
//