ID A0A061GY85_THECC Unreviewed; 2585 AA.
AC A0A061GY85;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Chromatin remodeling complex subunit, putative isoform 2 {ECO:0000313|EMBL:EOY34408.1};
GN ORFNames=TCM_042089 {ECO:0000313|EMBL:EOY34408.1};
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:EOY34408.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY34408.1, 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; EOY34408.1; -; Genomic_DNA.
DR STRING; 3641.A0A061GY85; -.
DR EnsemblPlants; EOY34408; EOY34408; TCM_042089.
DR Gramene; EOY34408; EOY34408; TCM_042089.
DR eggNOG; KOG0383; Eukaryota.
DR eggNOG; KOG0384; Eukaryota.
DR HOGENOM; CLU_228174_0_0_1; -.
DR InParanoid; A0A061GY85; -.
DR OMA; LTMPAME; -.
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:UniProtKB-KW.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0031507; P:heterochromatin formation; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.250.1310; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR039322; MOM1.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR35116:SF2; ATP-DEPENDENT HELICASE FAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR35116; HELICASE PROTEIN MOM1; 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; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
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.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 422..471
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 482..549
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 567..633
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 668..832
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 957..1119
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1764..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1945..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2105..2135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2363..2394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2444..2518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2564..2585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1524..1570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2285..2316
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1947..1970
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1979..2016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2105..2128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2449..2471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2564..2578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2585 AA; 285253 MW; EDAADF69DF8ABE2F CRC64;
MVNGTRSSRK AKDDEDNNSK GGQSSGKKSV NSGASTAEVS GFRRSLRETL SKKSMNPLSS
SGTRKSERLE KQTSNSNTMT RPSKRKSERI EKQKHRCPLR RSERGKMPSL SGSSGSKKSD
KSLDSLDAKR KKEKKEKSVK QLTMETVEVN KIENKDGQVD EAQKKRMDAR AYRAMFRKQL
KSANGTDHGD DLNRTDSERR DEDPLKVHAE RTCEITMARG TSQSVEEAPE NDNEHTLFPT
SQKDSCKDMS SNGDGLRVSK SGLVAIEMND DAEKAVQDPE LVNSMLHERI LDCNISLEMV
QEVVFSERKR HDIDIDSVAS PITSSKDICT SMAGAETLLT SGCKRKDCSE TCGTCSKRQR
VDCDSTKQEI CFSNKKLNQL FQSSDIKDRW KLDAGVSTGH VEKCCNDMQK HMSTDLRTDP
DQNTCIVCKL VGKLLCCEGK GCRRSYHLSC LEHPLEEVPV GVWHCPVCMS KKIESGVHSV
SEGIEAILDS REVEASEDGL QRQKQYFVKY KGLAHVHNRW VPENQALLEA PSLVAKYNRR
NQGAVWKQQW AVPHRVLQKR FLVTPEECDE SHLKGHDGEK LNSHVEWLVK WRGLGYEHAS
WELENASFFS CPEGQSLIRD YETRHKKAKS ASKFDKERGE VACLKLSQLS AGASPGLDAN
LDAFNKMCNY WRKGQNAIIF DDQERILNVI SFILSFSSNI SQPFLIISTS SSQYSWDEEF
LHLAPSVDVV VYSGSKEIRK SIRTLEFYEE GGCIMFQVLI TSPEVISEDL DVLASIGWEA
IIVDECQRPR IASCFEQIKM LTASKRLLIV SGQLKDNVAE YLNLLSLLDS QSNLNGSDSL
LMNSSDNIGT LKERLAKYIA YECKLESSRF VEYWVPVLLS NVQLEQYCFA LLSNSFSLCS
PSKTDPVGAL RNILISSRKC CDHPYVVDQS LQMLLTKSLK EIEFLDVGIK ASGKLQLLDA
MLSEIKKREL KVLILFQSIG GSGRDLLGDI LDDFLRQRFG ADSYERIDGG VFLSKKQSAL
NKFNNERERF VFLLETRACL PSIKLSAVGT VIIFGSDWSP MNDLRALQRI TLDSQFEQIK
IFRLYSSFTV EEKVLMLSKQ DKTLDSNTHS VSPSSCHMLL KWGASHLFNQ LDKFHGIPTS
DAGTLSEQSH LIDVIKECFI ILDQTGIDND ASKLSLILLA KQKQGTYRTE MPLFGEQKIQ
VMNEDPPYIF WTKLLEGKNP QWKYSSCSSQ RNRKRVQNFD GLLKKPEAES SEVVKRRKKV
VSDCNDHLSP KAGLREGKMA AGDREGSLGI SANGLSHSLS RSTASESDEI HATSNSLHLA
NNISKIPAFN MVEWERRRKQ RDSQKNLHVL LMPQIAQLCE VFHLSEVVKA MVERFLEYVM
NNHLVYREPE TLLQAFQISL CWSAASLLKQ KIDHKESLAL AKQHLGFTCK KDEADYVYSL
LRCLKTMFRY RTGYLKVPNS PKASELSSKA LGRDYSNARS YHQSAKAKIE DLLGFQEGSA
VQVCAESGVA PEFHLAQRDL LKSIKEIQKK CDKHMTKLRE KQREEMKQFN QKYEEEKAQL
ENKKRTEAAV IRLLSNVSMR TDKLKKLDIE YAGKFDELKL QMDVHLKNLE AVQVRARSSV
LESKTRWVEA VKNWAQAEFV RPPVSEVNLS EGRSSTGIIH SVSGNEVRVS KSIHIVSDDI
MACSDPICRV TCLARPFKEN SEGASVEECN VTVCSGGGEE QAVYKASYAR EGVSGGEIPY
GGVALDVPVT VSSGYVTESF PSMRCSDEDK ISDGSKLNMS NGDPETVPPT DGPENLICVE
APSCEEIPDG ATLSKPIPFR AADGVSFCED QEKLASLQAP SSEKISNRDS LRKIDEDVPL
RESVTVISGE GQEDLISLEA PSSVEVPDGT NLRKVDGQVP LGEPLIAISG EGQENLGSAE
APSSEEIPDG AALSMADVVL PSSAAEAVGS SEGQENIISG NSSSEKQIPG GATFIVSDGE
VPKSTSEIET SSHGMVCQNP SSKEQITDTA EEGSLAESET APSEVLEGGS IHRENVQTSA
TGIDQQDVEV CTMNQEPEFE EPSLADLPPV QRVPIVDQGG PFPPDEVSPN AGFLPSAIQA
RDVVNSETQN ASQVAETSSP NATIDVRYNE PNPDTPVLEL SERTQLLRSG ESTSYLSPPN
LPSVSAIEHH SNNEGQTANQ ISQALRQSVA NHIELSNQDV LQPLHSPIDG TIGGLVRQAS
ETRTASLPPV SSGLPVQTAP AVSSRMPLPL YNDPLQNEME RIRKETDQTI KIHEDMKLQL
KSECEKQIEE AVAQIRRNYK AKLKEKEAEF LLQKKELDVN YNKVLLNKIL AEAFRSKCMD
IRASGLAGAH QETSSSFMQQ LVQLSSQQTV QQPSTASGLP PTGSPSTQPV SPAVVNAQTM
GPPLQAVNPS AFFSGTPTRP PHISSISPSA GNLQMSSEIR APAPHLQPFR PSTSISPSSL
PSQSRGMLNQ QAHGNHPVAP PLRGQSYGNP LAHRPISTAC QSGRIPPETA GGLAPPPSSS
LPSLDVLMGI NNLSGANTNP LSNLLPGVSS SLATLVCQES SLPRIQSNPA QQSGATDIVC
LSDDD
//
