ID A0A346PPT8_9EURY Unreviewed; 1246 AA.
AC A0A346PPT8;
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_1520 {ECO:0000313|EMBL:AXR81533.1};
OS Natrarchaeobaculum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobaculum.
OX NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR81533.1, ECO:0000313|Proteomes:UP000258613};
RN [1] {ECO:0000313|Proteomes:UP000258613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc-Mg {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; CP027033; AXR81533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346PPT8; -.
DR KEGG; nag:AArcMg_1520; -.
DR OrthoDB; 203178at2157; -.
DR Proteomes; UP000258613; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000258613}.
FT DOMAIN 10..448
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 463..735
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 1246 AA; 139740 MW; 0D9FC8EDE1D80A43 CRC64;
MGDRSDGAAL EPKGDQQAVI DERASCLSVD AGAGTGKTTT MLLRIERAID RGEVDPDDVL
VLTFANEAAG SIREAVSRRL EPEAAAAIDV YTYHSFCHRL VREYAYHLGY SPDFEVVTDR
KRRRIIGRLL AETDYGFAAP FVESEASTAD LVDRVDTFVA TMSREDVSPA DLRAGLPDVR
TLELCTEFVL WLERRADDRL SFDEEAFRYF NREEHLETAR ESLVEYGKLV EYCREKIAES
PAPFRDDDVV RDIDRYFRAL QTCVTKTIET LSLDDPTTKH LPRALFGNQI HGTATTRIEQ
TPLGRLKHHV EFLRLARHYA DVYADYHAHL EGERALDFDE LVRTATALVA GEPDPAGVDR
PTAERIADGL TAEWDQVYCD EFQDTDETQF SLITALTDGP DRPELLAIGD KDQAIYGWRG
TDREGLDRLA DVYDDHEALA LELNFRSRQE ILDLTNHCYY DGQSTKTLRE DGRTPGEYWC
VDEPDDPDGP PDRVVVVESD DLESDPADQV AATVSRLLNG EATNVPRRDL ADVAVIVRTN
RHAQAVAGAL RDRQIPYEIS GSPRGTVAPG IQTLLSYLRA LVDPDADVHL RRVLTYRYRL
PAADLRTLQR RDGSLFEAVF DVNPETLERP NRLETARTHL EMLSEQRDVY PLSGFLRRFR
ELTRLEWFLT GEERAELDRL DRFVDAYGGD EIIRRLTDEF VDALERLFAG SGSDRTRGTR
SEDCVDVMTV HQAKGLEFDT VLVPYLSDEE WCVDRDYAER ARYRLLAATL AEDVQSPLCT
DLEAESVAEE WRVLHVALTR AENHLFVFGS AYDYDGEEGD LAASSADACL APEVEWSVTG
RRMDLWETLR SSFERVRETY PRSVADRTDE IGRSAGTSPG TITYYAGYDD RPIEPLETRE
AIETVHRLGR LLRTETLLPA ADAADVRERV ADVDGDVPTI RVPNGRSLSA LSADTVRFPL
TALTSRTDLE AAIYHSYSAL ETHETCPRKH YLEHVVRAID DPEPTGAGRR RRADRRPSAR
VVGTVFHDVA EEAFYREYRT REEWREAAVR QLTARGLLES RDELLACVDR YFEAHAPTVD
SPIAEWPQLA AELPFSLADV PGLAGDVVGY VDSVRRLPTS DAAAGEAGDG LVVLDYKTTA
ERIDPEDAVQ LALYVRACND RFDEPIVAAG YVYVGDVDGP GVELFDPAEL PAWDDVRDAL
EAVDDPSYQE TRPGAHCRFC PHRSLGCAPA EYGLSEIDAL EGTGDD
//