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Database: UniProt
Entry: A0A1H7FZH4_STRJI
LinkDB: A0A1H7FZH4_STRJI
Original site: A0A1H7FZH4_STRJI 
ID   A0A1H7FZH4_STRJI        Unreviewed;      1149 AA.
AC   A0A1H7FZH4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=SAMN05414137_101419 {ECO:0000313|EMBL:SEK29912.1};
OS   Streptacidiphilus jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=235985 {ECO:0000313|EMBL:SEK29912.1, ECO:0000313|Proteomes:UP000183015};
RN   [1] {ECO:0000313|Proteomes:UP000183015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC   / KCTC 19219 / NBRC 100920 / 33214
RC   {ECO:0000313|Proteomes:UP000183015};
RA   Varghese 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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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DR   EMBL; FOAZ01000001; SEK29912.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7FZH4; -.
DR   STRING; 235985.SAMN05414137_101419; -.
DR   eggNOG; COG0210; Bacteria.
DR   eggNOG; COG2887; Bacteria.
DR   Proteomes; UP000183015; 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:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 3.
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:SF55; 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   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:UP000183015}.
FT   DOMAIN          17..415
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          416..730
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          331..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..914
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1149 AA;  124262 MW;  04D9329F48CFA2EB CRC64;
     MPGRLTSPEE LRELLGIPFT AEQLRAITAP LAPAVIVAGA GSGKTTVMAA RVVWLVGTGQ
     VRPEQVLGLT FTNKAAAELA ERVRKALLHA GVVETERVEP SAQAGGDEFG EPEISTYHAF
     AGRLLTDHGL RIGLEPDVRL LADATRFQLA ARVLRQAPGP YPGLKDGVSS LIAKLVKLDG
     ELAEHLVPPE RLITHDTELL ASLAGVKLGN ESLRAVPVAA EARRELAELV VRYRARKREA
     QLMDFGDQIA ACARLALTRP EVGGLLREQF AVVLLDEYQD TSVAQRLMLA SLFGDGTGHP
     VTAVGDPCQA IYGWRGASVA NLDEFPHHFR EADSDRSREA DRDRSREADR DRSREADPTY
     RREADAARSL GAEPPVAAHD VGVADADARA DDAAPRGVQG APAARYSLSE NRRSGGRLLA
     FANDLAAPLR AMHEGVAALR PAPGEEQAGG LRCALLETHE AEVAWVADSI AHLVRTGTAP
     GRIAVLCRAG RELFPDVHAA LVARDVPVEV VGLSGLLHLP EIADLVATCE VLQDPTANAA
     LVRLLSGPRW RIGPRDLALL GRRARDLVRV AGDDGRQDKL EQAVAEADPT EIVSLADALE
     SFLYPGQAGE PELPFSADAA ARFQRLAVEI RELRRALAEP LMDVLHRVLT VTGLEVELAA
     SPHALAARRR ETLSAFLDVA AGFADLDGDP SLGAFLAFLR TAQEYDRGLD NNLPSGEDTV
     KVLTAHKSKG LEWDVVFVPG LVKGAFPSGT GRERWTSRPE VLPHTLRGDA ASLPADPAWT
     SAGLKEFEAE MKTHAATEEL RLGYVAFTRP RALLYASGHW WGPSQKRPRG PSPFLDALRI
     FGEEQPGSGV EIEHWAEPPA EDAQNPALDQ TVEHAWPLPL DAAAQAARRA AGTRVLAGSR
     GEASPEPEPE AAEERRLVAS WDRDLELLSA ELRRSRSRVR EVALPASLSA SQLLRVAADP
     DGFARELARP VPRPPQPAAR RGTRFHAWVE SRLAVEPLLL LGEEELPGLD DSGIEDERDL
     ARLKEAFLRT EYAARTPYRI EEPFQLVLGG RVVRGRIDAV YRTPQGFEVV DWKTNHRETA
     DPLQLAVYRL AWAEREGLDP ALVSAAFLYV RSGTVVRPQA LPGREGLEAL LDAVAPNGER
     IGEAATEAL
//
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