ID A0A0C2BIZ0_9BURK Unreviewed; 762 AA.
AC A0A0C2BIZ0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 ORFNames=TSA66_10830 {ECO:0000313|EMBL:KIF81195.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF81195.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF81195.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF81195.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-2014) 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:KIF81195.1}.
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DR EMBL; JWJG01000028; KIF81195.1; -; Genomic_DNA.
DR RefSeq; WP_040040019.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C2BIZ0; -.
DR STRING; 709839.TSA66_10830; -.
DR OrthoDB; 5905204at2; -.
DR Proteomes; UP000031572; 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 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:UP000031572}.
FT DOMAIN 6..283
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 284..589
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 27..34
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 762 AA; 85120 MW; A30511780C76A417 CRC64;
MQNLLHNLNP EQLAAVTLPA QSALILAGAG SGKTRVLTTR IAWLIQTGQV SPAGILAVTF
TNKAAKEMTA RLGAMLPINT RGMWLGTFHG LCNRLLRAHY RDAGLPQTFQ ILDSQDQLSA
IKRLLKSLNV DDEKYPPRNL MYFINNAKEQ GLRAHDVEAN DDYNRKFVEL YAAYDHQCQR
EGVVDFAELL LRTYELLTRN QPLREHYQAR FKHILVDEFQ DTNNLQYNWL KLMAGEHNAV
FAVGDDDQSI YAFRGANVGN MVAFEREFRV QNLIKLEQNY RSHGHILDAA NTLIANNSKR
LGKNLRTDAG HGEQLRVYEA SSDIQEANWI IEEAKSLIAE GAARSEIAIL YRSNAQSRVI
EHALFTAGIP YRVYGGQRFF ERAEIKHAIA YLQLMDNPHN DSAFLRVVNF PTRGIGARSI
EQLQDAARQY GISLYAAVPY VTGKAGSSLG SFVKLVEGMR FETQNLPLQE MVKVMLDMSG
LIPHYQNEKE GADRIENLEQ LVSAAMLFVS EEGFGIDAPA FLGPKGQQVA GEALTTADGV
EVLDADAPLP TVMSPLSAFL SHASLEAGDN QAQAGQDALQ LMTVHSAKGL EFDAVFITGL
EEGLFPHENS AQEEGGLEEE RRLMYVAITR AKKRLYLSFS QTRMLHGQTR YNMKSRFFDE
LPEEALKWLS PRVQPQWFGH RKSAWDEAPE AGANKIAQSF SRKDAGWRIG ETVMHQKFGE
GVIVNIEGGG TNMRAHINFG KHGMKLLDLG IAKLEKVAPR LH
//
