ID A0A231RV98_9BACL Unreviewed; 729 AA.
AC A0A231RV98;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=B1A99_01740 {ECO:0000313|EMBL:OXS62605.1};
OS Cohnella sp. CIP 111063.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=1955714 {ECO:0000313|EMBL:OXS62605.1, ECO:0000313|Proteomes:UP000215193};
RN [1] {ECO:0000313|EMBL:OXS62605.1, ECO:0000313|Proteomes:UP000215193}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 111063 {ECO:0000313|EMBL:OXS62605.1,
RC ECO:0000313|Proteomes:UP000215193};
RA Dastager S.G., Neurgaonkar P.S., Dharne M.S.;
RT "Cohnella sp SGD-V74 (T) CIP 111063, whole genome shotgun sequencing
RT project.";
RL Submitted (MAR-2017) 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:OXS62605.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MWSG01000001; OXS62605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A231RV98; -.
DR Proteomes; UP000215193; 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 GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 2.
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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000215193}.
FT DOMAIN 13..302
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 303..567
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 648..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 729 AA; 82921 MW; 58F2AF01B11424DB CRC64;
MNFFERMARE AGVALNEQQR RAASHAEGPL LLLASPGSGK TTTMLMRIAY LIEEKKVSAE
RIKAVTFSKA SAEDMKTRFV KLFPALAANA PDFSTIHSLA FEIVRDHFRR RGITYRIIEG
RGGDEDDGRP NKPKIIRELY RRANGDYPPD DRMEELTRYI GFAKNKLIPP DRLSSVKCDV
PRAETIYREY EHYKRMAEDR LLIDFDDMLT EADAALGTDA SLLAKYQGRF DYVMTDESQD
TSLVQHEIVE KLIRKHGNLW VVADDDQSIY GWRAAEPKYL LDFKEKHPKA AVLLLEQNYR
STSNIVDVAN RFIKRNRDRY DKNMFTGNPA GEDIVVTALP DYRYQAKYVT EKIVDEGELG
DTAVLYRNNS SSIMLMNALD RAGIPFYMKD GDARFFSHWI VEDVLNFMRL TFNDRRADIL
GKIHLKFGGY ISKKQMERLL ELQADPDDSV FDRLVKHIPL RDYQGKALAA CKQAFHGMQG
AKPLAAIRTI RGKLGYDKAI DKSCERMGYR KEALLGILNA LEEIAEPLET MEQFAARLKF
LEERMKRSKG GKKEEAVTLS TLHSAKGLEF SRVYIVDLIE GVLPSTDDVR KWEKGDGHDM
EEAARLFYVG MTRAKRRLEL ISYARKEDEP VTLSRFVEDV RRLQLRTPEP TVAGAKGRPR
PSAPANPNAI RDPSLLVVGA KVRHTVFGNG EIVLTLGDSL DIRFREQTKR LSANICVQMG
LLEPMASPG
//
