ID A0A3L6SXY5_PANMI Unreviewed; 878 AA.
AC A0A3L6SXY5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN ORFNames=C2845_PM05G09170 {ECO:0000313|EMBL:RLN28385.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN28385.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC DDX11/CHL1 sub-subfamily. {ECO:0000256|ARBA:ARBA00008435}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLN28385.1}.
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DR EMBL; PQIB02000003; RLN28385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6SXY5; -.
DR STRING; 4540.A0A3L6SXY5; -.
DR Proteomes; UP000275267; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0006974; P:DNA damage response; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472:SF41; ATP-DEPENDENT DNA HELICASE DDX11-RELATED; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:RLN28385.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267}.
FT DOMAIN 17..413
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 878 AA; 97202 MW; 4ECC7E1EF65B12B8 CRC64;
MPTPPMPPPP TPTPTPRKEF PAFPFAPYPI QAEFMSFLYA ALSSGPGALA LLESPTGTGK
TLSIICSALQ WLLDRRDAAA TAPAHPGGGA GPGEDDDEPD WMRDFTPLPP EKEVAKKKKK
AKPPAMRKTA GSGKPDGFGE QSAGDDDGEF LLEEFESDGE DGAMRGVGKR THCGSSSSSE
GESDEEEEEE VTPKVYFTSR THSQLSQFVG ELKRTEFAGR IRTVALGSRK NLCINKDVLK
LGSANRINER CLELQKNKKT SKTKVEEDKR KARQAKNSCG CPMLRNRSLQ KEFRSEVSDQ
GALDIEDLAH IGKKIGTCPY YGSRDMVRSA DLVVLPYQSL LLKSARESLG LNLKNSIVII
DEAHNLADSL TNMYNSKITS SQLKAVLSHL DAYLNRFHDV LGAGNRRYIQ TLTVLTRSFL
RVLINNQDGA STMSSMTINQ FLFSLDIDNI NIVKLCQYVK ESNVIHKVSG YANKITSIQA
GVNQFDLQQE HDEGSSISCF QALVDFLRSL MNSNDDGRII VAKQKLSGQP EEAYLKFVML
CAEKILSEVT RDAYAVILVG GTLQPIEETR LRLCPSLPPA DIKFFTCNHI VPPESILPIA
VTRGPSGMTF DFSYNSRSSP SMIEELGRFI CNIVTVVPEG VVMFFSSYDY ERHVYDAWTT
AGTISKICKK KHVFREPRNS ADVEAVLNKY KETIQSCSKN SQDTGINGAL LLAVVGGKIS
EGINFSDGMG RCVIMIGLPY PSPSDVELIE TIKHIETISS SFLVGDDKAS GRKYDDECEL
QPGYNILRKC TKGGREYYEN LCMKAVNQSI GRAIRHINDY AAMLLVDSRY AQTSSSKSYS
SPTDKLPQWI KARLSCAQNY GEVHRLLHQF FKFNKQKR
//