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Database: UniProt
Entry: A0A387BNF9_9MICO
LinkDB: A0A387BNF9_9MICO
Original site: A0A387BNF9_9MICO 
ID   A0A387BNF9_9MICO        Unreviewed;      1070 AA.
AC   A0A387BNF9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=D7I44_02630 {ECO:0000313|EMBL:AYG02527.1};
OS   Gryllotalpicola protaetiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Gryllotalpicola.
OX   NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG02527.1, ECO:0000313|Proteomes:UP000275069};
RN   [1] {ECO:0000313|EMBL:AYG02527.1, ECO:0000313|Proteomes:UP000275069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG02527.1,
RC   ECO:0000313|Proteomes:UP000275069};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of strain 2DFW10M-5.";
RL   Submitted (SEP-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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; CP032624; AYG02527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A387BNF9; -.
DR   KEGG; gry:D7I44_02630; -.
DR   OrthoDB; 5240387at2; -.
DR   Proteomes; UP000275069; 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; 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; 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:SF59; DNA HELICASE; 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   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:UP000275069}.
FT   DOMAIN          58..351
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          355..655
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         79..86
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1070 AA;  113401 MW;  EF0FFB4E350729F4 CRC64;
     MPMRISTVVP FVVDCVEPIE CVRTPVRVFA RGDAAPCRTM SGQVRTMSVE PYSFASVQLD
     ASQQAVLDLP LGQSAVVLGA PGTGKTSTVV ELIAARVASG AIGPDEVLAL CSSRTAATAL
     RDRLSLRLGV ATQGPRARTA NSLAFSVVGE HAAGVGAPEP RLLTGAEQDQ LLAEQLAGDV
     DDETIAWPEH LSADVRRLAG FRAELRELME RMVENRISAA RLVELGCERG LAEWVAAGEF
     IARYQDTLDT LRPGFVTAAE LLADAARLVA SGEVSPGVRL LVVDDLQEFT RAGLDFLAAL
     ARRGVPVVAF GDPDVATTTF RGADPAAVAG FGARVGGGAP TLTLSTAHRQ PAALREVTKR
     VTERVGTALA GAQRRAASVT DRVGLVQSIV APSDAEQYAT LARRLRELHL LDPRTPWSRM
     AVIVRSGRQV PELARALAVA EVPTRTTAAA GALRDDYAAK QLLTAVAVVL GITALDGAVA
     TELLLGPLGG LDVVQLRKLR LALRHEELAG DGSRPGDALL AEALADPGAL VTIEDMAPGR
     AARKLAQTLQ TARGQARRGA TIEELLWTLW DRSGLAATWS KQAARGGVVG GEANRDLDGV
     VALFAAAKRF VERSPGRPPG DFVTELLEAA VPEDTLAPRS LADAVLVCTP PAAVGLEFEV
     VAIAAVQEGT WPNVRLRGSL LHPQALGGAA DSDVLDERTA VLHDELRMFA LAVSRASSLV
     IVTASEGDDQ QASPFLRLAE GEQVPIAGHP FTLRGLVGQL RRRLASVPAD AAAAASLATL
     AEAGVAGADP AEWYGVLDPS VDGPLVDLDA DLEATVAVSP SRMASFEQSP LKWFVDVMSG
     SSGGLATGVG TIMHAIMEVV AAEPEGDISV DRIWGDVERR WGELNLEPGW VERREKRRVQ
     KMAQGLHDYL DEFEHSGATL LEAEGTFSLR LGQTVINGAI DRVERRPDGT VVIVDLKTGR
     QYPSGPEVPA HPQLGAYQLA YHDGALRDEG PLGGAKLVFI APETTTTKKT FREIPQRAKT
     EAEFDEFRVR VHEAGRGMAG AEFIGVRSDN GRDGYDYRIH LVPEVSEADE
//
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