ID A0A095APM3_9SPHN Unreviewed; 768 AA.
AC A0A095APM3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=FG95_03930 {ECO:0000313|EMBL:KGB51444.1};
OS Sphingopyxis sp. LC363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB51444.1, ECO:0000313|Proteomes:UP000029625};
RN [1] {ECO:0000313|EMBL:KGB51444.1, ECO:0000313|Proteomes:UP000029625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC363 {ECO:0000313|EMBL:KGB51444.1,
RC ECO:0000313|Proteomes:UP000029625};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-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:KGB51444.1}.
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DR EMBL; JNFC01000073; KGB51444.1; -; Genomic_DNA.
DR RefSeq; WP_037558204.1; NZ_JNFC01000073.1.
DR AlphaFoldDB; A0A095APM3; -.
DR STRING; 1120705.FG95_03930; -.
DR PATRIC; fig|1120705.3.peg.3931; -.
DR eggNOG; COG0210; Bacteria.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000029625; 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; 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:UP000029625}.
FT DOMAIN 21..302
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 303..570
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 768 AA; 86138 MW; 5E8642A8B63147E3 CRC64;
MSPTSTPDLT RPDPSDPPYL QGLNGPQRQA VLTTEGPVLM LAGAGTGKTA ALTARLAHII
ATRRAWPSEI LAVTFTNKAA REMRERIGRM IGDAVEGMPW LGTFHSICAK MLRRHAELVG
LQSNFTILDT DDQLRVLKQL IQAEGLDEKR WPARQLAGLI DKWKNRGLTP ADLDAADKEA
YADGKGQHFY ALYQARLKTL NACDFGDLLL HMLVILKTHR DVLEQYQQRF KYILVDEYQD
TNASQYLWLR LLAQARKNIC VVGDDDQSVY SWRGAEVANI LRFDKDFPDA TVIRLEQNYR
STPQILAAAS ALIAQNSGRL GKTLWTELDP GDKLRVVGVW DGPEEARRIG EELESLQRQR
VSLDRAAILV RAQFQTREFE DRFIAIGMPY RIVGGFRFYE RAEIRDALAY LRLVQSSADD
LAFERIVNVP KRGLGDKALA RIHQFARAEQ APLFHAASRI TETDELTPQA RRQLVNFVAQ
MRGWQAKANE LSHPELTQLI LDESGYTAML QADRSAEAAG RLENLSELVR AMEEYETLEE
FLEHVSLVMD RDNDDQTETV TIMTIHAAKG LEFDHVFLAG WEDGVFPSQR SMDEGGTASL
EEERRLAYVA ITRARQRASI YHAANRRIYG QWMSSIPSRF IGEIPPEHVD SENSFGGGQS
LWRANWSAQG DPFAHVAERQ PARTMTRGPA WQRALASSST VTRAPAPSEK GPAASVGAKP
RADLAIGIRV FHEKFGYGEI IDIDGNKLEV EFDQAGSKRV LDSFVKLA
//
