ID D6RXI4_BORVA Unreviewed; 698 AA.
AC D6RXI4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BVAVS116_0341 {ECO:0000313|EMBL:EEF82066.1};
OS Borreliella valaisiana VS116.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=445987 {ECO:0000313|EMBL:EEF82066.1, ECO:0000313|Proteomes:UP000006163};
RN [1] {ECO:0000313|EMBL:EEF82066.1, ECO:0000313|Proteomes:UP000006163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS116 {ECO:0000313|EMBL:EEF82066.1,
RC ECO:0000313|Proteomes:UP000006163};
RA Fraser-Liggett C.M., Mongodin E.F., Casjens B., Dunn J., Luft B., Qiu W.,
RA Schutzer S., Sebastian Y.;
RL Submitted (JAN-2009) 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:EEF82066.1}.
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DR EMBL; ABCY02000001; EEF82066.1; -; Genomic_DNA.
DR RefSeq; WP_006068868.1; NZ_ABCY02000001.1.
DR AlphaFoldDB; D6RXI4; -.
DR GeneID; 63641117; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_5_12; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000006163; 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; 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 10..280
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 281..545
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 698 AA; 81583 MW; 13C34C4CE419A189 CRC64;
MVKIKNFFSS LNTSQEKIVF SKSKNPILVL AGPGSGKTRV IIAKIVYLIK HMNIDPNEIL
ALTFTNKAAN EMNARINDLL KFDKKLHIQT FHSFGSWLLR FYYKDFDKNY DSNFTIWDTN
DVARFIKQID LAPSLEMAKH IAALILKDKE NFFLEKFIEF REKEHEYIKI YEEEKAKNNA
FDFSDLIIKP ILMLRQSKSL KEYIQSKFKV IFVDEYQDTN YSQFLFLKEL YLDGMYFMVV
GDEDQSIYSF RGARIENILE FEKTFGNVVK FYLMQNYRSN SNIVDIANEV ISKNKNRYEK
QITTRNSSDK RMKFLVFQST SDEAEYFSNL LVDNDIDTAI LYRFNSQSFH FETSFLKKNI
PYKVLGSIKF YDREEIKDII CLLRLFINKR DKIAFLRMIN KPSRGIGKNT LEKIISTLND
DDVNFNLFCA SKKVLSLLKN RVKESLLLFL NTYDELGKKL FEDNYINLSA FIEDVVIKFG
ILDYYKKFDK DEKLRNIDEL INSGIEYSGT FEGLAIFLEN SSLSPLISGD FKSNIFLSSI
HGVKGLEFDR VVISGLEKGL LPAEIEELTE DRLEEERRLF YVAITRAKSE LIVTLNLRRA
FRGSFKSTAP SVFFQDIDKN SYDIIFIPEY LKENFSNFFI DNKRDSKFNI GDYIIYNGEK
GIVVDSWYQG SLQFVKISLT NGKKAILSPE YVKKIIKV
//
