ID A0A061GU96_THECC Unreviewed; 831 AA.
AC A0A061GU96;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=DNA-binding protein with MIZ/SP-RING zinc finge isoform 6 {ECO:0000313|EMBL:EOY33076.1};
GN ORFNames=TCM_041076 {ECO:0000313|EMBL:EOY33076.1};
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:EOY33076.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY33076.1, 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).
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000256|ARBA:ARBA00004718}.
CC -!- SIMILARITY: Belongs to the PIAS family.
CC {ECO:0000256|ARBA:ARBA00005383}.
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DR EMBL; CM001887; EOY33076.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061GU96; -.
DR EnsemblPlants; EOY33076; EOY33076; TCM_041076.
DR Gramene; EOY33076; EOY33076; TCM_041076.
DR HOGENOM; CLU_015870_2_0_1; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000026915; Chromosome 9.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; IEA:UniProt.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR CDD; cd15570; PHD_Bye1p_SIZ1_like; 1.
DR CDD; cd16792; SP-RING_Siz-like; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR031141; SIZ1/2_SP-RING.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10782:SF4; E3 SUMO-PROTEIN LIGASE SIZ1; 1.
DR PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF02891; zf-MIZ; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000313|EMBL:EOY33076.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00452}.
FT DOMAIN 11..45
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 346..429
FT /note="SP-RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51044"
FT REGION 536..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 91121 MW; 4A4FA525765FF4E6 CRC64;
MDLVASCKDK LAYFRIKELK DVLTQLGLSK QGKKQDLVER ILGALSDEQV AKMWAKRTPV
GKEDVAKLVD DIYRKMQVSG ATELASKGQG VSDSSNVKVK GEIDDPFQSD MKVRCPCGSS
LETENIIKCE GPRCQVWQHI RCVIIPEKTM EGNPPVPDLF YCEICRLSQA DPFWITIAHP
LYPLKLAVSN IPNDGTNPVL SAEKTFQITR ADKDLLTKQE YDVQAWCMLL NDKVPFRMQW
PQYADLQVNG LPVRAINRPG SQLLGANGRD DGPIITPCTK DGINKITLTG CDARVFCFGV
RIVKRRTVQQ VLNMIPKETD GERFEDALAR VCRCVGGGTA TDNGDSDSDL EVVADFFGVN
LRCPMSGSRM KVAGRFKPCV HMGCFDLEVF VELNQRSRKW QCPICLKNYS LENIIIDPYF
NRITSKMRNC GEDITEIEVK PDGSWRAKAK SENERRELGD LAQWHSPDGT LCVPGSAEVK
PRAETSKQIK LEGASDGHTG LKLGIKKNSD GLWEVSKPED MNTSSDSRLQ ERFEHHEQKI
IPMSSSATGS VKDGEDPSVN QDGGGTYDFT SNGIELDSMP LNIDSAYEFT DRNSSAPTGN
AEVIVLSDSD EENDILISSA TLYKDNQNDS SGLNFPVAPP GISHPYSEDP ALGPAGNLGL
FPTNDEFDMG LWSLPPGPPE GSGFQLFSTN ADVSDALVDL QRNALNCPQS MNGYTLAPET
TMGSANLVPG SSIGQTDTDI NDRLVDNPLF GAEDPSLQIF LPTRPSDASA QSDLRDQADV
SNGIRTDDWI SLRLGDGATG GHGDSTTVNG LNLRQQIPSR ERTMDSLDDT D
//
