ID A0A346PKA8_9EURY Unreviewed; 959 AA.
AC A0A346PKA8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=AArcMg_4128 {ECO:0000313|EMBL:AXR79953.1};
OS Natrarchaeobaculum sulfurireducens.
OG Plasmid paarc-mg-01 {ECO:0000313|Proteomes:UP000258613}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobaculum.
OX NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR79953.1, ECO:0000313|Proteomes:UP000258613};
RN [1] {ECO:0000313|EMBL:AXR79953.1, ECO:0000313|Proteomes:UP000258613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc-Mg {ECO:0000313|EMBL:AXR79953.1,
RC ECO:0000313|Proteomes:UP000258613};
RC PLASMID=paarc-mg-01 {ECO:0000313|Proteomes:UP000258613};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena M.D.C., Ferrer M., Messina E.,
RA Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT reducing natronoarchaea from hypersaline soda lakes.";
RL Submitted (FEB-2018) 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}.
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DR EMBL; CP027032; AXR79953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346PKA8; -.
DR KEGG; nag:AArcMg_4128; -.
DR OrthoDB; 203178at2157; -.
DR Proteomes; UP000258613; Plasmid pAArc-Mg-01.
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; 2.
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}; Plasmid {ECO:0000313|EMBL:AXR79953.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000258613}.
FT DOMAIN 13..404
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 414..661
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 959 AA; 107888 MW; 95C703C182217EB7 CRC64;
MTQSPNGAST ATPTPNAGQR ELIDSIDGLY LVDAGAGTGK TFTVTRRYAN IVAQDDVEPD
DILLITFTRN AATEMKDRIV ASCDYEMRAL NDAPIQTFHS LCNDILDQHR FHAPSYLGID
DAITGSTQIL ENETIERRYF REFVTRFSDD HDEYADLLRC LSSPTELLDL ITNLASKGVF
PTGTGWYRDS RDALEGDFET FEALFDEVNQ PRNDGSKQSK LRSSLGSYGR TKCFLPDAPD
RSELRGERGS KAVPDEVAKQ VFAEDRDHLI AFVHDVYFEY LEFALGRNYL NFSFLQLFAF
VLCCEDDDLR ESLQFEYVMI DEFQDSSEIQ FKLALLLSGT DNFCVVGDWK QSIYSFQYAA
IENITKFESR LERFASELND TAERVSFSTD EVTRIELEQN YRSTQSILDF SENALVAPGS
NRESIERESI LERVVSLFSN TGHDHSRIEA FQHADEQEAI LTKIQGIVGN EEYAVEEDGE
LRPPTYGDVA VLTRTRNFGR ELLATAEEYD FPIAYEGGIE LFRTDQTKLL LAWLRILEDD
SAAERGWAVV LERAGYTLNE IDAILEREAY PDAMAQFRSK LSALETHTAV ARRVFDRYGY
DGPTADVILT TTEALHSSTT MTRGDLIQTI EDGIESGYTQ DVQAVAGTDS VTVQTVHSVK
GLEHPIVILG NMNRGAFPPS GGSGGTITYS KQTGLRQRKC YDDTHSDPYV YDNWRADVLR
RCQPTEYDEE RRLLYVAMTR AKDHLFFAAG DEPNTFLEEL PVAIEPLEPA VSPVDVDETS
WSPLSVDVPS DVGPVGYSPH TLMDDSVYED VSDGRGTDFG TRVHEFAEAY ALGQDVTPEA
DDERNVKAFL DSLHGELLVE EQAFLPLEVD GEQVTLSGVI DLVHITDETA DIVDFKTDLG
RHAESEYRIQ LSVYYHVLEQ WFDDRTVTAS IYYTADDARV EIDPLSKREL ETLASVEFD
//
