ID A0A061E749_THECC Unreviewed; 925 AA.
AC A0A061E749;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=DEAD/DEAH box RNA helicase family protein isoform 2 {ECO:0000313|EMBL:EOY00835.1};
GN ORFNames=TCM_010767 {ECO:0000313|EMBL:EOY00835.1};
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:EOY00835.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY00835.1, 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 -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; CM001880; EOY00835.1; -; Genomic_DNA.
DR EMBL; CM001880; EOY00837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061E749; -.
DR EnsemblPlants; EOY00835; EOY00835; TCM_010767.
DR EnsemblPlants; EOY00837; EOY00837; TCM_010767.
DR Gramene; EOY00835; EOY00835; TCM_010767.
DR Gramene; EOY00837; EOY00837; TCM_010767.
DR HOGENOM; CLU_001103_10_2_1; -.
DR Proteomes; UP000026915; Chromosome 2.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd18018; DEXHc_RecQ4-like; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF108; ATP-DEPENDENT DNA HELICASE Q4; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EOY00835.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 293..463
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 484..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..38
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 102872 MW; 6131951FF23C44DB CRC64;
MDSDSDSDGS HISATPPRDP FPPPRRPPPP PPKPPTSSYK SKIKPSSHSE TISKLKKPSP
KHTKPEPPPK SIPQTEPPPL PSPIGTLPFQ IRRPPNQPHP VSTVRSLETL PAGFFSTHRA
SFSKIQKPSL SFEPEITPQK TTERKISISD FSDSSKTSNK KLPNLIRADA PLPPVNLQKR
SVEGNFVKLN INGYKRKFTT KGKKTNSYSS KSKYFKRSKR RVKSEVNTES ICDEEGLVAE
IKQQPKSEKN IKFESIKAAI SAVRKEASDE NLVRLLKAMY GYDSFRDGQV EAIKMVLAGK
STILVLPTGA GKSLCYQIPA VVLPGITLVV SPLVALMIDQ LKQLPPVIRG GLLSSSQGPE
EAAETQRLIQ EGSIKVLFVS PERFLNADFL SIFSATTFVS LVVVDEAHCV SEWSHNFRPS
YMRLRASLLR AELNVECILA MTATATTTTL HSVMSALEIP STNLIQKAQL RDNLRLSVSL
SGNRMKDMLK LMKSSPFSEA QSIIVYCKFQ SETDLISRHL CDNNISAKSY HSGMMARDRS
RIQELFCANK IRVVVATVAF GMGLDKRDVG AVIHYSLPES LEEYVQEIGR GGRDGRLSYC
HLFLDDVTYY KLRSLMHSDG VDEYAVNKFL CQVFADDTNS HGKVCSLIKE SASRKFDMKE
EVMLTLLTHL ELGETQYLHL LPQLNVTCTL NFHKTSPTLL ADKDTAVAAI LKKSEIKQGQ
YALDIPTVAN SIGVAPSDLL NHLQNLKVKG EITYELKDPA YCYKIVEVPS DFCSLSALLT
RWLLDIENCK VWKLDTVYSA VVFAVDACEK AHGCNVSQQT SCLQQRVLDY FKGDNNPDVL
DKMTHNSPFL RADIKVFLQS NSHIKFTPRA VARIMHGIGS PAYPSSTWSK SHFWGRYTQI
DFKAVMNAAK AELMSFVGKD APLFA
//
