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Database: UniProt
Entry: A0A1H6VIH2_9DEIO
LinkDB: A0A1H6VIH2_9DEIO
Original site: A0A1H6VIH2_9DEIO 
ID   A0A1H6VIH2_9DEIO        Unreviewed;       740 AA.
AC   A0A1H6VIH2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=SAMN04488058_103155 {ECO:0000313|EMBL:SEJ03466.1};
OS   Deinococcus reticulitermitis.
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=856736 {ECO:0000313|EMBL:SEJ03466.1, ECO:0000313|Proteomes:UP000199223};
RN   [1] {ECO:0000313|Proteomes:UP000199223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.10218 {ECO:0000313|Proteomes:UP000199223};
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; FNZA01000003; SEJ03466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6VIH2; -.
DR   STRING; 856736.SAMN04488058_103155; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000199223; 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}.
FT   DOMAIN          9..291
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          292..570
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   740 AA;  82335 MW;  2C2D076F6A7CE9FA CRC64;
     MTSGPDIWTQ LNEPQAQAAD HFTGPALVIA GAGSGKTRTL IYRIAHLIGH YGVHPGEILA
     VTFTNKAAAE MRERAGHLVP GADALWMSTF HSAGVRILRA YGEHIGLRRG FVIYDDDDQL
     DILKEVMGSV PGIGPETHPR VLRGIIDRAK SNLLTPDDLD RARDPFISGL PRESAAEAYR
     RYEARKRGQN AIDFGDLITE TVRLFKEVPE VLDRVQNRAK FIHVDEYQDT NKAQYELTKL
     LASRDRNLLV VGDPDQSIYK FRGADIQNIL DFQKDYPDAK IYRLEHNYRS SARVLSAANK
     LIENNTERLE KTLKAVKEEG HPVTFHRATD HRSEGDYVAE WLTRLHGEGR AWKDMAILYR
     TNAQSRVLEE SLRRVQIPAK IVGGVGFYDR REIRDILAYA RLALNPDDDV ALRRIIGRPR
     RGIGDTALQK LMEWARQNGT SVLTACAQAA EAGILERGAN RATEFAELMA SLSEAADNYE
     PAPFLRFVME ASGYLDLLRQ EGQEGQVRLE NLDELVNAAE EWSRENEGSI ADFLDDAALL
     SSVDDMRTKA ENKGAPEDAV TLMTLHNAKG LEFPVVFIVG VEQGLLPSKG AIAEGPGGIE
     EERRLFYVGI TRAMERLLMT AAQNRMQFGK TNAAEDSDFL EDIEGLFDTV DPYGQVVEYR
     ARTWKDFRAA PPAATPAVKN TSPLTAELAY RGGEAVRHPK FGEGQVLAVA GVGERQEVTV
     HFPSAGIKKL LVKFANLQKL
//
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