ID A0A0Q9N193_9MICC Unreviewed; 1058 AA.
AC A0A0Q9N193;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=ASG77_11710 {ECO:0000313|EMBL:KRE71676.1};
OS Arthrobacter sp. Soil762.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE71676.1, ECO:0000313|Proteomes:UP000051715};
RN [1] {ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE71676.1, ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE71676.1,
RC ECO:0000313|Proteomes:UP000051715};
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 -!- 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:KRE71676.1}.
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DR EMBL; LMSG01000019; KRE71676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q9N193; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000051715; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; 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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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 3: Inferred from homology;
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 1..426
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 427..699
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1058 AA; 115540 MW; D147AAE9AB74A61F CRC64;
MNMLENVTMV SASAGTGKTY TLTGKIVEQI AAGLPAGAIM ATTFTKKAAG ELRERIAARL
LEQAEVTDDA DAAAALRLAS QQLPVNLIGT VNSVCGQLLQ DHAIDAGLSP ALEVIGEEQL
AGIFNLATDE ILAEHAPAIL PIAHRMGTDD AGARDAKTWQ EMVRSVVDAA RTNLLDAEEL
ADCAERSWTG LRELLDTPGT DDRASWLRDL HLGGMEFREM VRSGTGTDGK KALTDTAKFR
EQCPKVLPKI DQAQTAEDTP WEIWRGFIAS APAAPIKDIF WDLRQRIHAG LLSNPAFHHD
LEQYIRRIFA CAADCLDAYS EFKRLHGLMD FVDQETLVLK LARDNEAFRR SFPGRVQFLV
VDEFQDTSPL QLELFLQLSG LVEEAVWVGD PKQAIYEFRG TDPELMEAVV AKVSQREQLS
ETWRSHQAVV DLSNAVFEPV FEPHGMPPET VHLELPNAHA EWSPGTLEAW TRPQSNDAER
LKATAAGVAS LLGRRPELRA GDVAILARSN KDVESLSTAL DALGIRASRN PRKLSAAREV
QLARAGMAFI ADGYDTVALT ELVALHPGHS AHATWQQQLL EAPDAAVVLE SWNADPLVTA
LDGLRERAAM ATPTEVFEAV TGVLGLPRLI ASWSSPATRF RNLDAARGAI HTYYERCLAL
RSPATLRGFL AFFDSEEQQS AENAGDDIVN VLTYHKAKGL EWPVVVMEGL DKDLRLAAFG
AAVEQDGTFD LAQPLAGRWI RFWPTPFPYG GSPLDTKGKN SEVAERAQER DRRNMSRLMY
VGMTRAVETT VLTAKNGKPE LLNNLGVAGL VSWSKEDENS TEGIIQVDDG EGFPAFVEEL
EPFDAVQTAA VWTPRFADAL STRSGAAALP ARFAASSVDS TGHDAAVAAV AELGSRLADH
GSDDWGAVGS AVHAYLGTQF SALSAPERRD LAERIVARWQ VAGTVDPSLL ITSGDRFEAY
LDIEFPEWVR HKEAAIGWRP DHQVMEGWID LLLESSDGFV LVDHKTYPGN DPAGHVREKY
LGQMAAYRNA VLAATGKPVL RTLIHFPALG RVYEISEF
//
