GenomeNet

Database: UniProt
Entry: A0A061E2B6_THECC
LinkDB: A0A061E2B6_THECC
Original site: A0A061E2B6_THECC 
ID   A0A061E2B6_THECC        Unreviewed;      1118 AA.
AC   A0A061E2B6;
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=Transcription factor jumonji domain-containing protein, putative isoform 3 {ECO:0000313|EMBL:EOX99100.1};
GN   ORFNames=TCM_007714 {ECO:0000313|EMBL:EOX99100.1};
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:EOX99100.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX99100.1, 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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CM001880; EOX99100.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061E2B6; -.
DR   EnsemblPlants; EOX99100; EOX99100; TCM_007714.
DR   Gramene; EOX99100; EOX99100; TCM_007714.
DR   HOGENOM; CLU_001811_2_1_1; -.
DR   Proteomes; UP000026915; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; IEA:InterPro.
DR   CDD; cd02208; cupin_RmlC-like; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR045109; JHDM2-like.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR018866; Znf-4CXXC_R1.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR12549; JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN; 1.
DR   PANTHER; PTHR12549:SF72; LYSINE-SPECIFIC DEMETHYLASE JMJ25-LIKE; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF10497; zf-4CXXC_R1; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          363..410
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          807..1103
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1118 AA;  126174 MW;  975D6154AF872938 CRC64;
     MARPRKRLKP ERAPGSCEGV PQSDGEVMGS KENCASAEDQ VEGINGKGQE EEDSEMDGDK
     AGEVEGKEEG IERKDKKCGD LEGDGEGVAL KKPTKRGRKV KQATVSLKRG TMEIVKEENV
     EGSSDFVAEK KEEVGEKLKE NGVQPKGEKK LSFVENLEIS NGEDGVSIKE EVDSGADGNG
     QGNSGAVLKR RLRAVAKKVS YADVQESEDE GFSAKKRSRK GRQKEKVLKS EGQEYGNNEN
     EDIEIPTKKR GRRGRQKRKV SESEDNEGKD VKEGGKVEQG GDLGADDGKK RSRRGAKNDG
     KKMDKEVLGN GKSLEKLEES LGMNTKPTYS LRASRVRKAR EESVPYSKKR NFAKWIAEES
     LMCHQCQRND KGRVVRCKLC KRKRYCIPCL TNWYPKMSED AIADACPVCR DNCTCKACLR
     MTGLLKKLGK TLKLEFSDDE KVQHSRYLLQ ALLPYIEQFS QEQMKEKVIE SKIQGMLPEQ
     IQLKQAVCLE DERVYCNNCR TSIVDFHRSC SNCNYDLCLT CCHEIRDGHL QGGQKEVIME
     YADRGFSYLH GALQCSMSSE VGKSLDSPKE TNSKEHKAAT SRWKANENGS IPCAPKDLDG
     CGNGLLELRC MFTENAIFEL TEKAEKIAKA LNLGNVLEVS NQQCPCYNSM GEVDTGNGKL
     RKAAFREDAT DNYLYCPKAK DIQTGDLKHF QRHWANGEPV IVSDVLENIS GLSWEPMVMW
     RAFRQITHTK HDQQLEVKAI DCLDWSEVMV NIHQFFKGYT DGPFDTKSWP QILKLKDWPP
     SNEFEKLLPR HHVEFLRCLP FKEYTHSLSG ILNMATKLPE KSLKPDMGPK SYIAYGVAEE
     LGRGDSVTRL HCDMSDAVNV LTHTAEVKLT PKELASIDNL KQRHHLQDQW ELFGMGSKVG
     TNMPGDDSFD ISICDKQSSD RSGDQEGDVI VQQDCQDGYS SLNSNNMGRE FEMEKSGKAK
     VDQEKCMENG RLYETSRNKI EEVEAVEGGA IWDIFRRQDV PKLQDYLKKH FGEFRYVHCC
     PVSQVFHPIH DQTFFLTLDH KAKLKKEYGI EPWTFVQKLG EAVFIPAGCP HQVRNIKSCI
     KVALDFVSPE NVGECVRLTE EFRVLPQDHR AREDKLED
//
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