ID A0A0F0CWC3_9BACT Unreviewed; 1119 AA.
AC A0A0F0CWC3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=OMAG_000397 {ECO:0000313|EMBL:KJJ85730.1};
OS Candidatus Omnitrophus magneticus.
OC Bacteria; Candidatus Omnitrophota; Omnitrophus.
OX NCBI_TaxID=1609969 {ECO:0000313|EMBL:KJJ85730.1, ECO:0000313|Proteomes:UP000033428};
RN [1] {ECO:0000313|EMBL:KJJ85730.1, ECO:0000313|Proteomes:UP000033428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKK-01 {ECO:0000313|EMBL:KJJ85730.1};
RA Kolinko S., Richter M., Glockner F.O., Brachmann A., Schuler D.;
RT "Single-cell genomics of uncultivated deep-branching MTB reveals a
RT conserved set of magnetosome genes.";
RL Submitted (FEB-2015) 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=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}.
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:KJJ85730.1}.
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DR EMBL; JYNY01000084; KJJ85730.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0CWC3; -.
DR PATRIC; fig|1609969.3.peg.438; -.
DR Proteomes; UP000033428; Unassembled WGS sequence.
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; cd19067; PfuEndoQ-like; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR016195; Pol/histidinol_Pase-like.
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; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF89550; PHP domain-like; 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:UP000033428}.
FT DOMAIN 514..790
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 791..1065
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 535..542
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1119 AA; 126727 MW; E605913996B36E90 CRC64;
MKFICDFHIH SRYSRATSSA VTPVNLAIWA AIKGVKVIGT GDFTHPAWLK ELKESLIPAE
EGLFKLNKEK ISPPFENKFS LNPYDVRFLL TAEISNIYKK NGKTRKIHSV ILAPSFEIAE
KINASLLKRK ANLVSDGRPI IGMDTKDLLD VSLNASPEIL FVPAHIWTPW FSILGKESGF
DSVEECFEDL AGHIYALETG LSADPPMIWM CSSLDKYTLL SNSDAHSLEK IGRNANIFDT
VFSYSAIAGA IKIGTRAENP KFLGTIDLFP QEGKYHYAGH RKCGVSWDPV ETLRHVGVCD
ICGNKITMGV MNRVLELADR EDIEKIADRK SLHYIIPLAE ILSEITGIGQ TSKKVTELYN
SAIQTIGSEF DILLNKSFDE IKKFGGEMLA EAVRRVRQGE VYIKEGFDGE YGIIKVFGEK
ESKSLIGNKT LFGGAGDMGK SGECPRHKLI NFDLKEYRKL DENKKLAENN SLFEDVKPDN
KYSGSSSKNI SRENFLSPKN IDLIEKEKFD SLLYRLNDEQ KIITGDFLGP SLILAGPGTG
KTRVLTFKIA RLIKEYGINP SNILALTFTN KAAKEIEERL IYILSEGSLA GYPRLNIHTF
HSFGLKIIEE NIGRMERAGR AGFSKDFFII NENEKIKILE TLGVAKQKTD EFLKYVTRVK
NLSVKEDAAS EDLKIIFKRY QETLIKINAL DFDDLLYEPL NIFSLYPEIL EHYRLKYKWL
LIDEYQDVNT AQYNFVRQLM PDVSSNISVI GDPNQAIYGF RGADVKFIKK FKEDFPSAKT
YHLSISYRCT DNILRAGENI IRSKKNEESI TLKALSKGLK INVASYGTYK EEAEYIARTI
ENMIGGLRFF SMDSGISKGI RADGIKSLSD FAVLVRFKEE MNVIEKAFKD HAIPYEIIGD
KALASEKIIK DIAGIIKSAR KGNYELFKRA LAPEKILNYF SIMNENNISL KDKIIKIADD
YFSRAEELKD NMYFAKMLDI AGDYENDIEG FLRFLATGMA VDAYEYGVEK VSIMTMHSAK
GLEFECVFIP ALEDGLIPYS IFENKKTDID EEKRLFYVAV TRAKKSLFLS RAGIRYVFGK
EYRFDESPFL KKIEKDIIEF TTGKNFLPGG NKETQLEFF
//
