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Database: UniProt
Entry: A0A1G9X490_9GAMM
LinkDB: A0A1G9X490_9GAMM
Original site: A0A1G9X490_9GAMM 
ID   A0A1G9X490_9GAMM        Unreviewed;       732 AA.
AC   A0A1G9X490;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
DE   AltName: Full=DNA 3'-5' helicase II {ECO:0000256|ARBA:ARBA00034923};
GN   ORFNames=SAMN04487951_101127 {ECO:0000313|EMBL:SDM91594.1};
OS   Halomonas arcis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=416873 {ECO:0000313|EMBL:SDM91594.1, ECO:0000313|Proteomes:UP000199677};
RN   [1] {ECO:0000313|Proteomes:UP000199677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.6494 {ECO:0000313|Proteomes:UP000199677};
RA   Varghese N., Submissions S.;
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; FNII01000001; SDM91594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9X490; -.
DR   STRING; 416873.SAMN04487951_101127; -.
DR   OrthoDB; 9806690at2; -.
DR   Proteomes; UP000199677; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   CDD; cd18807; SF1_C_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; 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; PF21196; PcrA_UvrD_tudor; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000199677}.
FT   DOMAIN          9..287
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          288..571
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   732 AA;  82626 MW;  16B00BC6082D658F CRC64;
     MDDVTAILDQ LNADQREAVS ASQGNLLVLA GAGSGKTRVL VHRIAWLMQA EGLSPYALLA
     VTFTNKAARE MRTRLEALLG LSLRHVWVGT FHSISHRLLR THWQDARLPQ HFQIIDADDQ
     LRLVKRLLKD YSIDDERFPP RQVQGFISGC KEEGLRPHQV NVDGDAYLGQ MVELYERYQL
     TCERGGLVDF GELLLRSLEL LRDNPALLAH YRERFGHLLV DEFQDTNTLQ YAWLKLITGM
     QTPMTVVGDD DQSIYGWRGA KVENIRRFEQ EFPQTHTVRL EQNYRSTSAI LDAANALISH
     NSERMGKQLW TEGSEGEPIS IYAGFNDIEE ARFIVDTIKE KVDEGLNRRD MAILYRSNAQ
     SRLLEETLIR QGMPYRIYGG HRFYERLEIK NALAYLRLLL NRDDDASLER VINVPTRGIG
     TRTVEIVRLR AREQNIPLWQ ALHDAMQDGT LKGRAGNAVQ AFANLIEQLD NDAAGLPLHE
     IIDHVTDHTG LIEHHKSERG EKGQARVENL EELVNAARAF THGDAFETPE AGEGMAALEA
     FLSEAALNAG DHEAEEFEDS VQLMTLHSAK GLEFPVVFIA GVEEGLFPHK MSLEEPGRLE
     EERRLCYVGV TRAMQKLYLT HAETRRLHGK EVFPRPSRFI RELPPHLLEE VRLRGHISRP
     VTASRTSFAQ QSVESDGDLP SLHVGQGVEH PVFGEGIILN AEGEGARARV QVSFEGEGVK
     WLVLGFAKLT PL
//
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