ID F7X1G4_SINMM Unreviewed; 636 AA.
AC F7X1G4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN Name=recQ {ECO:0000313|EMBL:AEH78140.1};
GN OrderedLocusNames=SM11_chr0862 {ECO:0000313|EMBL:AEH78140.1};
OS Sinorhizobium meliloti (strain SM11).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=707241 {ECO:0000313|EMBL:AEH78140.1, ECO:0000313|Proteomes:UP000009045};
RN [1] {ECO:0000313|EMBL:AEH78140.1, ECO:0000313|Proteomes:UP000009045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM11 {ECO:0000313|EMBL:AEH78140.1,
RC ECO:0000313|Proteomes:UP000009045};
RX PubMed=21396969; DOI=10.1016/j.jbiotec.2010.12.018;
RA Schneiker-Bekel S., Wibberg D., Bekel T., Blom J., Linke B., Neuweger H.,
RA Stiens M., Vorholter F.J., Weidner S., Goesmann A., Puhler A., Schluter A.;
RT "The complete genome sequence of the dominant Sinorhizobium meliloti field
RT isolate SM11 extends the S. meliloti pan-genome.";
RL J. Biotechnol. 155:20-33(2011).
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 -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446}.
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DR EMBL; CP001830; AEH78140.1; -; Genomic_DNA.
DR RefSeq; WP_010969854.1; NZ_JAJJBH010000001.1.
DR AlphaFoldDB; F7X1G4; -.
DR GeneID; 61603783; -.
DR KEGG; smx:SM11_chr0862; -.
DR PATRIC; fig|707241.3.peg.902; -.
DR HOGENOM; CLU_001103_14_3_5; -.
DR Proteomes; UP000009045; Chromosome.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 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; IPR006293; DNA_helicase_ATP-dep_RecQ_bac.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR002121; HRDC_dom.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR018982; RQC_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR01389; recQ; 1.
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; PF00570; HRDC; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR Pfam; PF09382; RQC; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00341; HRDC; 1.
DR SMART; SM00956; RQC; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50967; HRDC; 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:AEH78140.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 58..226
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 250..396
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 561..636
FT /note="HRDC"
FT /evidence="ECO:0000259|PROSITE:PS50967"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 70065 MW; DB495493467930F8 CRC64;
MPSISLDSIL RAPDESDSMP ESHNTGRLFE TEGVSNPLDL LKRIYGYSTF RGQQQAVVDH
VVAGGDAVVL FPTGAGKSLC FQIPALCRRG VGIVVSPLIA LMRDQVEALK QLGIRAAALN
SSLTRDEAIA VRRALSRDEL DLLYVTPERA VTDGFAEMIA DADIALFAID EAHCVSQWGH
DFRPEYRGLG CLAERFPGVP RIALTATADP HTRDDMIERL GLGGARVFAS SFDRPNIAYE
IVERDQPRQQ LLRFLSRFKD ASGIVYCLSR AKVEDTAEWL DAQGIRALPY HAGMERAARD
AHQDAFLKEE NLCLVATVAF GMGIDKPDVR YVAHLDLPGS VEAYYQETGR AGRDGLPSEV
WMAYGMADVI QRRRMIDEGG APEEIKRIER AKLNSLLAIC ETAGCRRQAI LAHFGEAHPG
GCGHCDTCLK PVETWDGTEA AIKALAAVYR TGERFGTGHL IDVLTGSVNE KTERFGHVDM
PVFGAGKDLP ARTWQSIFRQ LLAAGLISVD HAAFGALKLE PEARSVFRRE RQVLFRKDRP
SSGKAKTARG SKPASERSDL AGSDLELFER LRSERLSLAR EMDVPPYVVF PDTTLIALAK
RRPRDFEELL DVPGIGESKR ERYGEAFLAV IEAFEG
//
