ID G5SR89_9BACT Unreviewed; 635 AA.
AC G5SR89;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=ATP-dependent DNA helicase, RecQ family {ECO:0000313|EMBL:EHH00642.1};
GN ORFNames=HMPREF9441_01879 {ECO:0000313|EMBL:EHH00642.1};
OS Paraprevotella clara YIT 11840.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Paraprevotella.
OX NCBI_TaxID=762968 {ECO:0000313|EMBL:EHH00642.1, ECO:0000313|Proteomes:UP000003598};
RN [1] {ECO:0000313|EMBL:EHH00642.1, ECO:0000313|Proteomes:UP000003598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11840 {ECO:0000313|EMBL:EHH00642.1,
RC ECO:0000313|Proteomes:UP000003598};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:EHH00642.1}.
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DR EMBL; AFFY01000022; EHH00642.1; -; Genomic_DNA.
DR RefSeq; WP_008620056.1; NZ_JH376597.1.
DR AlphaFoldDB; G5SR89; -.
DR STRING; 762968.HMPREF9441_01879; -.
DR GeneID; 78582880; -.
DR PATRIC; fig|762968.3.peg.1679; -.
DR eggNOG; COG0514; Bacteria.
DR HOGENOM; CLU_001103_9_7_10; -.
DR OrthoDB; 9763310at2; -.
DR Proteomes; UP000003598; Unassembled WGS sequence.
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; cd17920; DEXHc_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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 InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF105; BLOOM SYNDROME PROTEIN; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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 Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EHH00642.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 26..194
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 218..369
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 635 AA; 73546 MW; D19ABC557B3EEC05 CRC64;
MEDVYLSILK KYWGYDGFRG IQREIIESIG NGRDTLGLMP TGGGKSITFQ VPALSRDGIC
IVVTPLIALM KDQVRNLRGR GIKAAAVYSG LSREEILVTL ENCIFGNYKF LYVSPERLAS
DIFLAKVRHM PVSFLTVDEA HCISQWGYDF RPSYTRIAEI RKILPDIPVL ALTATATPEV
VKDIQRQLAF REENAFRMSF ERKNLAYIVR HTEDKFGELI HILNSTKGSA IVYTRSRRNT
RETTEKLQAA GMSATFYHAG LNDAEKDLRQ HQWQEDKIRI MVATNAFGMG IDKPDVRLVI
HLDLPDSIEA YFQEAGRAGR DGAQAYAVLL YQRHDRTRLM KRIPDTFPDK DAIREVYEHI
CYYYQMAMGD GYNVTREFDL DEFCRNFKHF PVQTDSALHL LERAGYIEYT EEQDNASRIH
FLLRRDELYR IHELEAEQEQ LIQWVLRSYG GVFSDYVFID ERRIATLSGL TTDQVYHGLL
ALGRARILHY IPRKKTPYIT FSCKRIEKER IVFPSSVYDE RKKNFKERIE AMLYYAEEAD
FCRSKVLLHY FGEKDAQPCE QCDVCRIRKS HPHADATDEQ IIALILETLK DGQKHNLSEM
TFPGISREKT AQLLHQMIEE ETVRIQNGVL FLPHP
//
