ID A0A147ENM8_9MICO Unreviewed; 855 AA.
AC A0A147ENM8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=NS354_06570 {ECO:0000313|EMBL:KTR86064.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR86064.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR86064.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR86064.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
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:KTR86064.1}.
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DR EMBL; LDRK01000030; KTR86064.1; -; Genomic_DNA.
DR RefSeq; WP_058593775.1; NZ_LDRK01000030.1.
DR AlphaFoldDB; A0A147ENM8; -.
DR PATRIC; fig|1079994.3.peg.1430; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000070810; 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; 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:UP000070810}.
FT DOMAIN 29..335
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 336..623
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 703..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 855 AA; 93200 MW; 1D0DA3AC950D4593 CRC64;
MSDFELLDPS GLPIGGSAAH DAGGDPLVDG LNPAQARAVT TRGPALLIVA GAGSGKTRVL
THRIAHLIRE REAWPSQILA ITFTNKAAAE MRERIEGLLG DASQGMWIST FHSACVRILR
REAERFGYVS GFTIYDSADS RALLKRIIKE LDADTYGFTP ANSGAKISKL KNELVDAATH
AATMNENDPR ERLFVEIFRM YEQELKRANA FDFDDLIGQT VHLFRAHPDV AAVYQRRFRH
ILVDEYQDTN HAQYSLIREL TRPVEPEEVE RLVPPARAKE LDASGRIPPA SLTVVGDSDQ
SIYAFRGADI RNIVEFERDF AGAEVVKLEQ NYRSTQNILS AANAVIGNNF DRQEKHLWTS
EGDGERIVGF TGYSQHDEAR FVAEEIEDLH RAGLAYSDIA VFYRTNSQTR ALEELFIRSA
IPYRVLGGTK FYERAEVKDA MAYLTSIANP YDPIAWSRLL GAPKRGVGAM AEAHLANFQE
AQGVSFHEAM LRAEEVTAIG PKIRATVRAL GEMLVRASRM AVGGGATDVA GEDAKPAPVA
DVMKLVLDET DMIEKLRAKR DPQDDARAEN LEELLAVARE FDVKQPGAGL LAFLTEVSLV
AAADDLDDSS GTVSLMTMHT AKGLEFKAVF ITGVEEGLLP HQMSVDEIGG ISEERRLMYV
GITRARERLY LTLASTRATF GDVSVAMPSR FLQEIPEGLI DWRQSPGEVT GRGGTASRAL
NAPRSSGGGS WSRTRTDSAV TFSGGGSGSG AVSEPASGNM QSALDKWRER KRLAKEAQAS
GGGFPNLVGG SVRDNGDLEL ATGDRIRHDE YGEGRVTGVS GVGTKRIAHV VFDTVGERKL
LVKLAPIEKV EAGEE
//
