ID A0A061EQU2_THECC Unreviewed; 464 AA.
AC A0A061EQU2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=RING/U-box superfamily protein, putative isoform 5 {ECO:0000313|EMBL:EOY07206.1};
GN ORFNames=TCM_021694 {ECO:0000313|EMBL:EOY07206.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY07206.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY07206.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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DR EMBL; CM001883; EOY07206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061EQU2; -.
DR EnsemblPlants; EOY07206; EOY07206; TCM_021694.
DR Gramene; EOY07206; EOY07206; TCM_021694.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR032010; APD1-4_M.
DR InterPro; IPR032008; APD1-4_N.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46858:SF15; E3 UBIQUITIN-PROTEIN LIGASE APD1-RELATED; 1.
DR PANTHER; PTHR46858; OS05G0521000 PROTEIN; 1.
DR Pfam; PF16041; APD1-4_M; 1.
DR Pfam; PF16040; APD1-4_N; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 101..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..225
FT /note="E3 ubiquitin-protein ligase APD1-4 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16040"
FT DOMAIN 249..355
FT /note="E3 ubiquitin-protein ligase APD1-4 middle"
FT /evidence="ECO:0000259|Pfam:PF16041"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 50652 MW; 63A8743282193D4A CRC64;
MAEPNRSSPS ASASASASSS SSSSSYREDS GGAAGAAASS SGTSSQVREE EEGQDHEYRQ
HLQHFHNPEL ENQHIDLVSY RGNLSGFDDS STVIGDDTWS CIIVVLTFWF FVSMTLILGV
YGAVNIRVGP NCSLLLQPNP IFVQSVKVEE VDDTKPGLKL YGFYKSPSLD VVTTWSETRT
ATVQADSHKE WIHYLNRGSQ VNISYNVNSA GSSVFLIIAQ GSEGLSQWLE DPTYPNTTLS
WNIVRGSGMI QQDIYRSSSY YIALGNLNSE DVEVELNITV RAFIYNTTEA YYRCTFGNGL
CSLSVLFPQG NSVVLTSPGL EQSTSADDWS VRLSYGPRWI IYIVGIGGMT AIMLVAFNFL
NKFQFTRGGE TNLHYGENAS ARAPLLSNKD DDISSWGSSY DSVSSDEADL EDFLAAGSVE
GTSIREGENS NNTRRLCAIC FDAPRDCFFL PCGHCVACFA CGSR
//
