ID Q63M03_BURPS Unreviewed; 755 AA.
AC Q63M03;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0000259|PROSITE:PS51193};
GN OrderedLocusNames=BPSS0856 {ECO:0000313|EMBL:CAH38319.1};
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH38319.1, ECO:0000313|Proteomes:UP000000605};
RN [1] {ECO:0000313|EMBL:CAH38319.1, ECO:0000313|Proteomes:UP000000605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243 {ECO:0000313|EMBL:CAH38319.1,
RC ECO:0000313|Proteomes:UP000000605};
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC {ECO:0000256|ARBA:ARBA00038058}.
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DR EMBL; BX571966; CAH38319.1; -; Genomic_DNA.
DR RefSeq; WP_004523967.1; NZ_CP009537.1.
DR RefSeq; YP_110868.1; NC_006351.1.
DR AlphaFoldDB; Q63M03; -.
DR STRING; 272560.BPSS0856; -.
DR KEGG; bps:BPSS0856; -.
DR PATRIC; fig|272560.51.peg.7143; -.
DR eggNOG; COG1199; Bacteria.
DR Proteomes; UP000000605; Chromosome 2.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000000605}.
FT DOMAIN 173..425
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51193"
SQ SEQUENCE 755 AA; 82880 MW; DC646264990DA7C7 CRC64;
MSYVVAVRAM CEFTARAGDL DLRFTPAPSA LEGIAGHATV VSRRGTGYEK EIALSGEHRG
LTVRGRADGY DPALNRLEEI KTHRGDLDRM PANQRALHWA QARVYGHLLC ESRGLAELSV
ALVYFDVGTL RETVLTETHT AATLKAGFVE QCERFADWAA REDAHRAARD AALRALAFPH
ARFRSGQREL AVAAYRAARD GRVLLAQAPT GIGKTLGALF PLLKACGQAH LDRLFFLTAK
TPGRALALDA ADTLRAAAGG VLPLRVLELV ARDKACEHPD AACHGESCPL ARGFYDRLAA
ARAAALEHGR LDRAAVRAAA LAHDVCPYYL AQELARWCDV VVGDYNYYYD GSALLHALTL
QNQWRVGVLV DEAHNLLDRA RGMYSAALDQ RELAGVRKLA PAPLAKALER LNREWNALNR
EQAGAYVVHP DVPQRVLSAA QNLIGCFSEF AAQAPLALDD AVLRFCFDAI HFVALAEQFG
THSIFDATRV RAGAPRRGGH ASILCVRNVI PADFLAPRHG AARATVMFSG TLSPFDFYRD
TLGLPGDTGT LDVEGPFRAE QLTVKVASHV STRWRDRERS LEPIVELIAE QYAARPGNYL
GFLSSFEYLQ QVVARLRERH PALPVWEQAP GMDEAARDAF LARFEPNGRG IGFAVLGGAF
SEGVDLAGDR LIGAFVATLG LPQVNGVNEE MRRAMDARFG SGYDYIYLFP GLRKVVQAAG
RVIRTEHDEG VLHLIDDRFH RGEVRRLLPR WWRLS
//
