ID A0A0Q9QN05_9MICC Unreviewed; 1164 AA.
AC A0A0Q9QN05;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ASH00_14020 {ECO:0000313|EMBL:KRF04231.1};
OS Arthrobacter sp. Soil782.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF04231.1, ECO:0000313|Proteomes:UP000053496};
RN [1] {ECO:0000313|EMBL:KRF04231.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04231.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF04231.1, ECO:0000313|Proteomes:UP000053496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil782 {ECO:0000313|EMBL:KRF04231.1,
RC ECO:0000313|Proteomes:UP000053496};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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 -!- 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:KRF04231.1}.
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DR EMBL; LMSO01000011; KRF04231.1; -; Genomic_DNA.
DR RefSeq; WP_056549667.1; NZ_LMSO01000011.1.
DR AlphaFoldDB; A0A0Q9QN05; -.
DR STRING; 1736410.ASH00_14020; -.
DR OrthoDB; 4812256at2; -.
DR Proteomes; UP000053496; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF55; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 40..376
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 400..746
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 570..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 61..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1164 AA; 126633 MW; 7461C0234B24629B CRC64;
MSPEAAHLRA TDTVSADTAS MYSAEALAQL LAGGTSADIL YPTGEQTRII EAPLQPLLVI
AGAGSGKTKT MADRVVWLVA NGLVRPDQIL GVTFTRKAAG ELAARIRQQL QALYRAQGES
TLESGEDRLE PTISTYHSYA NGIVQDYGLR LGVERDAVML GTAQSWQLAG RIVESYRGPW
EHLSAARTTL TGAVLTMASE CAEHLVDPAA VRISLLEQID SVAARPYLLG KPKPSTQGAR
DLLNRLRTRV TVTELVEQYA AAKSQGGQLD YGDLVSLAAR IVSEVPQAVD AERQKYAVIL
LDEFQDTSHA QMVLFARLFG DGRSVTAVGD PHQSIYGFRG ASAGQLGTFR SRFPVHTGAR
LEPAPMVNLS VAWRNSTSIL AAANAVAEPL NVPPPWLGPQ HQLKVPALLA RPKAPLGEVY
LARYRSESAA APQDPSAPDN PQANEAAALS RIIQEQRRRY FDLDDDGRPL RPTIAVLCRG
RRQFEPLRQE LQSLGIPVQV IGLGGLLRTP EIIEILSVLR VLGDPERSDA MLRLLAGARW
RLGSADLMAL GDWARQLAYD RELRISQLRV GTGKPDAQEG TAHQGNTRDS AVSEPEQLPT
PTEDAEPASL VDAVDHLPPV GWVSGSGRTF SETGRERLVR LRDELRGLRQ SVGDDLHSLI
GEIEQTLLLD IELAAKPGVS VHEARRNLDA FADAVSGFVS TSDRIDVQAF LAWLEAADSE
EDGLPVTALE TSREAVQLLT VHAAKGLEWD VVLVPGMNEG SFPSGTGSRW SSGDASVPWP
LRGDAAELPQ WDWDQPDQKS WLDSEKLFAE DALTHTEREE RRLAYVALTR ARHVLVCSSS
AWGGGRSKPT TPSRYLERLR ELAAAGEPGY RELAWIEDGA VGADNPARAH SDRAIWPIDP
LRRRRGGMEQ AAAAVRAAAD DLRHGSGPEP GTEDIDLPGR WSDEVRKSLA RQQSRLTSVP
VELPTHISAS LMVELTEDSD GVARRLRRPV PRRPGTAARR GTAFHAWIEE FYGTTGMLDL
GEFPGAADSF VDDGLQLEQL AETFRKSAWA QRVPYGIEVP VETRVGSVVV RGRIDAVFQD
DDGTWDLLDW KTGRPPAPAD REAKAIQLAI YRLAWSRLKN VPLAGVRAAF YYAAEDQLVR
PHDLASSETL EAIVRKATSA GSGG
//
