ID Q2W9E6_MAGSA Unreviewed; 864 AA.
AC Q2W9E6;
DT 10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN OrderedLocusNames=amb0725 {ECO:0000313|EMBL:BAE49529.1};
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE49529.1, ECO:0000313|Proteomes:UP000007058};
RN [1] {ECO:0000313|EMBL:BAE49529.1, ECO:0000313|Proteomes:UP000007058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034617};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
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DR EMBL; AP007255; BAE49529.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2W9E6; -.
DR STRING; 342108.amb0725; -.
DR KEGG; mag:amb0725; -.
DR HOGENOM; CLU_004585_5_2_5; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000007058}.
FT DOMAIN 137..414
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 415..686
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 85..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 864 AA; 95744 MW; D75726B9174C3099 CRC64;
MAVRARVAAM RRRLRMADLP AYGWNALLCQ GVWASRGFAS MNRLTERHCR NSWDWDSCSP
LCLSACLRHA WPRPRWPLER SVSDSAQVAP PLHGGTGSAN IRSMSDPFAL DDEAPASPPP
SRASGPRPVP PDAPWLQGLN PEQFQAVTTT DGPVLVLSGA GTGKTKVLTS RLAHILASNL
AQPWQCLAVT FTNRAAREMK ERVGQLVGPV SDGIWLGTFH SLCLRILRSH AEAVGLGGDF
TVLDSDDQMR VLKQVMAEAH VDPKGTPPQG LMATIQRWKD RAVTPDKAAA DGGAEGQAKT
LYRAYQDRLR SLNACDFGDL LLHVLTVFLS DAEALARWQG RFRYLLVDEY QDTNVAQYLW
LRLLAQTHRN ICCVGDDDQS IYSWRGAEVG NILRFEKDFP GAKVVRLESN YRSTPHILAA
ASTLIANNEG RLGKTLRPGI IHEPEAIEKI RTKAVWDGEA EARMVAEEIE TLQRRGEKLS
SMAILVRAGF QTREFEERLI TTGIPYRVIG GPRFYERLEI RDAMAYLRLV VSAADGLAFE
RVVNTPKRGL GEAAVQTIHM VARAEQVPLL EAARRLVDTD ELKPKARQAL ARFIEDVDRW
RSLLESMPHP ELAATILDES GYVDMWKADK SADAPGRVEN LKELVAALEE YDSLASFLEH
VALVMENDSR ADLDSVVIMT LHGAKGLEFD SVFLPGWEEE VFPHSRALAE SGTKGLEEER
RLAYVGLTRA RKRVLVSFAA NRRIYNQWKS QLPSRFVEEL PESHVERSGE RGLHGGGLAE
SKAAWNDPAW SRARFGQPRR ETAAAPSWGQ AKPRESAGGF KPGARVFHDK FGNGTVLSLD
GNKLEIAFDK AGIKKVLDSF VSAV
//
