ID A0A1I6L063_9EURY Unreviewed; 985 AA.
AC A0A1I6L063;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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=SAMN05216559_1721 {ECO:0000313|EMBL:SFR96845.1};
OS Halomicrobium zhouii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=767519 {ECO:0000313|EMBL:SFR96845.1, ECO:0000313|Proteomes:UP000199062};
RN [1] {ECO:0000313|EMBL:SFR96845.1, ECO:0000313|Proteomes:UP000199062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFR96845.1,
RC ECO:0000313|Proteomes:UP000199062};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOZK01000002; SFR96845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6L063; -.
DR STRING; 767519.SAMN05216559_1721; -.
DR OrthoDB; 203178at2157; -.
DR Proteomes; UP000199062; 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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_UvrD; 1.
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, ECO:0000313|EMBL:SFR96845.1};
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:UP000199062}.
FT DOMAIN 29..419
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 420..674
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 985 AA; 110582 MW; 80400C91B9D0E833 CRC64;
MSDPAVDEPA ESDSAASESA KGDLAESAPT PNAKQRQLIE NTAGIYVVDA GAGTGKTFAV
TRRYAAIVDQ PDVEPADVLL VTFTRSAATE MKERIVDHST YSLRELADAS IQTFHSHCLD
LLEEHGYRAP THLGIDDRIT GATRVVEDEL VEAELFREFL DGFQDDHPEY AEFFRALSDR
SDLLDVVTEF ASKGVFPTAD GWYRDGESFV DGDFETFQDL FDEVNEPRNG GSKQSVLRSK
LNGYGKRRTY LPDAPDKGVL RGDGTKQAPE ETARRAFDED REDLKAFVHD VYHEYLAFAL
SRSYLTFGFL QLFAFVLLCE NESLRDRVSF EYVMVDEFQD TSEIQFKLAL LLAGTDNLCA
VGDWKQSIYS FQYADVENIR SFEDRIDRFA SDLNDDQERV AFPVDDVETI ELEENYRSTQ
SILDFSEETL VTPASNNEDV DEDVLDDVVS LSSNASFDNT TIEGIHHPDQ HEAVLTKIQS
IVGNDDYAVE DEDGDPRPPQ FGDVAVLTRT RDFGRELLSV ADDYDFPMAY DGGVELFRTD
QAKLLLAWLR ILESDADRGW AVVMEEAGYT LDEIDHVLEN RNYPSNMVTF RERLDAMEAV
GAVARRVFDR YGFTGEYADV ILHTVQSLHD TSTLTRGDLV RIVERGIENG STHDVVTSAG
VDSVTVQTIH SAKGLEYPIV VLANMNAGKF PPNVGGSSVV QYEEPVGLRQ RKIYADVEEH
AHPHVYDNWT HDVLRHCLQD DNDEERRLLY VAVTRAENHV VFAGGEDPNT FYEELPFEGT
RLDPAVEPVD RRETVQTQLP FSVVTPEGPT GHTPHTLMDD AVFEDADVEL ETTESMAFRG
RDFGSRVHDF AEAYALGEDV SPTTDGHDDQ RHVKAFIDGL SGDLHVEERA VLPLEIDGEQ
VTVSGIVDLV HETADRIEII DYKTDQSRRA ESEYRKQLSV YYHVVSECFP EKVVTARLFY
TATNERRTIE PVSLAELEDV VRASS
//
