ID A0A261QI87_9BACI Unreviewed; 711 AA.
AC A0A261QI87;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=CEW92_06730 {ECO:0000313|EMBL:OZI12411.1};
OS Bacillaceae bacterium SAS-127.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae.
OX NCBI_TaxID=2015203 {ECO:0000313|EMBL:OZI12411.1, ECO:0000313|Proteomes:UP000217062};
RN [1] {ECO:0000313|EMBL:OZI12411.1, ECO:0000313|Proteomes:UP000217062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAS-127 {ECO:0000313|EMBL:OZI12411.1,
RC ECO:0000313|Proteomes:UP000217062};
RA Verma A., Pal Y., Krishnamurthi S.;
RT "Indiibacillus sp. (SAS-127) genome sequencing.";
RL Submitted (JUN-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:OZI12411.1}.
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; NKXN01000029; OZI12411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261QI87; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000217062; 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; 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}; Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000217062}.
FT DOMAIN 17..299
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 300..562
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 711 AA; 82798 MW; EBCEC63778394312 CRC64;
MTVKEDFFVR KKSELGVSLN QMQRQAALQT EGPLLLLASP GSGKTTTMIM RIGYLIEEKG
IAPARVKAIT FSRAAAHDMK LRFERFFPDL PAIDFSTIHG LAFEVVREYF RETRTPYQMI
EGDKSPLHKK IILRNLFKSI VGEHITEDQM DELTTYISFM KNKMIPEDKW STVKVDVPEA
ERIFREYEAY KKTGTHQLLL DYDDMLTIAN EVFEENRELL DRYQRRYDYV LTDESQDTSM
VQHAMIEKLV QQHKNLCVVA DDDQAIYSWR GAEPSYLLNF KQVYPNATVL FMEQNYRSSQ
EIVDAANQFI KRNKQRYDKN MFTDNPSVEP IKVKDLADYK YQAKYLVKEM KKMEQLAEVA
VLYRNHSSSI MLMNEFDRAG IPFYMKDVDN RFFSHWVVDD ILNFMRMTFT DKRPDILEKI
HLKFNGYISK QQMAALKQIR NNESVFDNLL NHVQLKDYQV KQLKTCKETF LHMSGMPPLQ
AIRVIRDRLG YEKALEKTCE QLGFRKEYLF GILNTLEEIA DTLETMEEFA GRLKHLESVL
KTAQTRKGQN AVTFSTFHSA KGLEFERVYM IDLVEGVIPS SDDDKKGAEE KMEEATRLFY
VGMTRAKRHL ELIHYKVRDG KRTTESRFVT DVKKIISPKE EKPHEEAPMQ NPNAIRSRSG
LAVGNLVKHR VFGSGEIIQL TKEVVEIQFQ EVVKKLAVAT CLEMGLLEKV K
//
