ID A0A1Q4GRP7_9PROT Unreviewed; 703 AA.
AC A0A1Q4GRP7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BGP21_01100 {ECO:0000313|EMBL:OJZ18065.1};
OS Thiobacillus sp. 65-29.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1895862 {ECO:0000313|EMBL:OJZ18065.1, ECO:0000313|Proteomes:UP000186483};
RN [1] {ECO:0000313|EMBL:OJZ18065.1, ECO:0000313|Proteomes:UP000186483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=65-29 {ECO:0000313|EMBL:OJZ18065.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJZ18065.1}.
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DR EMBL; MKWN01000033; OJZ18065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4GRP7; -.
DR STRING; 1895862.BGP21_01100; -.
DR Proteomes; UP000186483; 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}.
FT DOMAIN 7..284
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 285..547
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 28..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 703 AA; 77742 MW; C2DA93998F83240D CRC64;
MSDPLLDGLN PEQRAAVTLP HESALILAGA GSGKTRVLTT RIAWLIQTGQ VSPHGILAVT
FTNKAAKEML VRIAAMLPIN TRGMWVGTFH GLANRLLRTH WREAGLPQSF QILDAQDQLS
AIKRLLKSLN IDTEKYEPKK VQGYINGHKE AGRRARDADA HDEFSMQLAE LYEAYDAQCQ
REGVADFAEL LLRAYELLYR NEPLRQHYQT RFRHILIDEF QDTNALQYRW LKLFAGPDTA
LFAVGDDDQS IYAFRGANTG NMLEFEREFA QGRVIKLEQN YRSHGNILTA ANALIERNQR
RLGKNLWTAD GDGEPIRVFE AFNDQEEAAF VVDEVKALNR EGVALSDMAL LYRSNAQSRV
LEHALFTAGV AYRVYGGLRF FERQEIRHAL AYLRLLTHPE DDGAFLRVVN FPTRGIGARS
VEQLADAAAR TGASLWQAAC TASGKVAAFA RLIEGIKQAT AGLTLAETID HVIEASGLAD
HYRADKDGAD RLENLAELVN AAALFSEEAE DDTLDAFLAH AALEAGEHQA EPGRDALQLM
TVHAAKGLEF HAVFITGLEE GLFPHEQSAH DEFGLEEERR LMYVAITRAR RRLYLSHAQS
RMLHGQVRYG FASRFLAELP DAVLLPLNRR GASRDAPAAA PARATPAGHG TGYRVGQSVA
HAKFGTGIII DFEGRGADAR VQVKFGDAGT KWLALAYAKL SPA
//
