ID A0A061GSK3_THECC Unreviewed; 1810 AA.
AC A0A061GSK3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Chromatin remodeling complex subunit isoform 2 {ECO:0000313|EMBL:EOY32820.1};
GN ORFNames=TCM_040842 {ECO:0000313|EMBL:EOY32820.1};
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:EOY32820.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY32820.1, 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; CM001887; EOY32820.1; -; Genomic_DNA.
DR STRING; 3641.A0A061GSK3; -.
DR EnsemblPlants; EOY32820; EOY32820; TCM_040842.
DR Gramene; EOY32820; EOY32820; TCM_040842.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_000315_28_0_1; -.
DR InParanoid; A0A061GSK3; -.
DR OMA; REICQQH; -.
DR Proteomes; UP000026915; Chromosome 9.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18660; CD1_tandem; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 418..506
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 531..595
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 635..807
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 980..1136
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1671..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1752..1810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1178..1205
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 114..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..290
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1755..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1810 AA; 207436 MW; 582442DA363B9350 CRC64;
MAFFRNYSSD TVSHSVLEEK SQGQNIGRIH STVGNEDVDG TYEREFDINM DAQYQSDGEP
DDAVRLHNEV PADNVAGVSN SNFQPAGRRI APGKWGSTFW KDCQPMDRQG GSDSGQDSKS
DHKNLEVLEY NSSDDRDDRL ESDDDEAQKE VGKAQRGHSD VPADEMLSDE YYEQDGEEQS
DTMHYRGFSN SVGLNTRPQS KPVCVSTTVS RGSRALNTRN YDDEDDDVNN DDADADYEEE
EEEDDDDPDD ADFEPDYGVA SGHAGNKDKD WDGEDSEEED NSDGDVDVSD EDDSYYKKKP
KGRQQVKVGR NVKPNKERKS SNRQRRGRSS FEEDEYSAED SDSESDVNFK SMARRGGNLR
KHNARSNMLT SMGRNNEVRT SSRSVRKVSY VESEESEEID EGKKKKTLKD EAEEEDGDSI
EKVLWHQPKG MAEDAIRNNR STEPVLLSHL FDSEPDWNEM EFLIKWKGQS HLHCQWKSFF
ELQNLSGFKK VLNYSKKVME DVRYRKALSR EEIEVNDVSK EMDLDLIKQN SQVERVIVDR
ISKDASGSVM AEYLVKWQGL SYAEATWEKD IDIAFAQDAI DEYKAREAAM AVQGKMVDHQ
RKKGKASLRK LDEQPEWLRG GKLRDYQLEG LNFLVNSWRN DTNVILADEM GLGKTVQSVS
MLGFLQNAQQ IPGPFLVVVP LSTLSNWAKE FRKWLPDMNV IVYVGTRASR EVCQQYEFYN
DKKIGRPIKF NTLLTTYEVV LKDKAVLSKI RWNYLMVDEA HRLKNSEAQL YTTLSEFSTK
NKLLITGTPL QNSVEELWAL LHFLDPDKFK SKDDFVQNYK NLSSFNEIEL ANLHMELRPH
ILRRVIKDVE KSLPPKIERI LRVEMSPLQK QYYKWILERN FHDLNKGVRG NQVSLLNIVV
ELKKCCNHPF LFESADHGYG GDISMNDISK LERIILSSGK LVILDKLLVR LHETKHRVLI
FSQVCIRIFY ILLSHLFTGS FYAMLRNLEG KGRKFKGEES RDDERMVRML DILAEYMSLR
GFQFQRLDGS TKAELRQQAM DHFNAPGSDD FCFLLSTRAG GLGINLATAD TVIIFDSDWN
PQNDLQAMSR AHRIGQQEVV NIYRFVTSKS VEEDILERAK KKMVLDHLVI QKLNAEGRLE
RKETKKGSYF DKNELSAILR FGAEELFKEE RSDEESKKRL LSMDIDEILE RAEKVEEKQG
EEQENELLSA FKVANFCNAE DDGTFWSRWI KPDAIAQAEE ALAPRAARNT KSYAETSQPE
RSNKRKKKGS DPQEFQERVQ KRRKAEYSAP LAPMIEGATA QVRGWSYGNL PKRDALRFSR
AVMKFGNESQ VTLIAEEVGG AVAAAPADAQ IELFKALVEG CREAVEVGNA EPKGPLLDFF
GVPVKANDLI NRVQELQLLA KRINRYEDPI KQFRVLMYLK PSNWSKGCGW NQIDDARLLL
GIHYHGFGNW EKIRLDERLG LTKKIAPVEL QHHETFLPRA PNLKERANAL LEMEVVAVGG
KNTGIKAGRK AAKKEKENSL NVSTSRGRDK KGKPGSPKVS FKMGRDRPQR PQKVEPLVKE
EGEMSDNEEV YEQFKEVKWM EWCEDVMIDE IKTLRRLQRL QTTSADLPKD KVLSKIRNYL
QLLGRRIDQI VLDHEDELYR QDRMTMRLWN YVSTFSNLSG ERLHQIYSKL KQEQEEDGGV
GPSHVDGSVT GHVDRDGDSN YFPPFSRSVE KQRGYKNVMA YQTSQPIHKG IDTAKFEAWK
RRRRAEADIH PQLQPPTQRP MSNGSRVIDP NSLGILGAGP PDKRLVNNER PYRMRQTGFP
QRQGFPSGIK
//
