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Database: UniProt
Entry: A0A1U8IX46_GOSHI
LinkDB: A0A1U8IX46_GOSHI
Original site: A0A1U8IX46_GOSHI 
ID   A0A1U8IX46_GOSHI        Unreviewed;       369 AA.
AC   A0A1U8IX46;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-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=LOC107899318 {ECO:0000313|RefSeq:XP_016680489.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016680489.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016680489.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016680489.1};
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};
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DR   RefSeq; XP_016680489.1; XM_016825000.1.
DR   AlphaFoldDB; A0A1U8IX46; -.
DR   STRING; 3635.A0A1U8IX46; -.
DR   PaxDb; 3635-A0A1U8IX46; -.
DR   GeneID; 107899318; -.
DR   KEGG; ghi:107899318; -.
DR   OMA; HAESHCA; -.
DR   OrthoDB; 469114at2759; -.
DR   Proteomes; UP000189702; Chromosome 17.
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:UP000189702};
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          190..231
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          60..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..354
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   369 AA;  41208 MW;  42F7262A76A6D430 CRC64;
     MESIRSPYWC YRCNRFIRIR VRSPHDSLNC PDCGGGFIEE IETPSRSPIH HRFPVAAMYS
     DTPSPALSPS PTATPHFRRT RRNAGDRSPF NPVVVLRGPT SESDGIVTER GNRNFELYYD
     DGSGSGLRPL PASMSEFLMG SGFDRLLDQL SQLEANGVGR FEQPPASKAA IESMPVIKIL
     GSHVRSESHC AVCKEPFELD SEAREMPCKH IYHSDCILPW LSIRNSCPVC RHELPTENNG
     NNFAENEAVR DEEAVGLTIW RLPGGGFAVG RFTGGTRAAE REFPLVFTEM DGGFNNAGAA
     PRRISWAPRG RRSQESRGLG RVFRSFVSFF GRFRSSPRSG SDSGFTRRSR SSSVFGRSSR
     RDSDWDFED
//
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