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Database: UniProt
Entry: A0A161I1A3_9MICO
LinkDB: A0A161I1A3_9MICO
Original site: A0A161I1A3_9MICO 
ID   A0A161I1A3_9MICO        Unreviewed;      1181 AA.
AC   A0A161I1A3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=pcrA {ECO:0000313|EMBL:ANC30985.1};
GN   ORFNames=I598_1429 {ECO:0000313|EMBL:ANC30985.1};
OS   Isoptericola dokdonensis DS-3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=1300344 {ECO:0000313|EMBL:ANC30985.1, ECO:0000313|Proteomes:UP000076794};
RN   [1] {ECO:0000313|EMBL:ANC30985.1, ECO:0000313|Proteomes:UP000076794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS-3 {ECO:0000313|EMBL:ANC30985.1,
RC   ECO:0000313|Proteomes:UP000076794};
RA   Kwon S.-K., Kim J.F.;
RT   "Complete genome sequence of a soil Actinobacterium, Isoptericola
RT   dokdonensis DS-3.";
RL   Submitted (JAN-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; CP014209; ANC30985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A161I1A3; -.
DR   STRING; 1300344.I598_1429; -.
DR   KEGG; ido:I598_1429; -.
DR   PATRIC; fig|1300344.3.peg.1433; -.
DR   OrthoDB; 4812256at2; -.
DR   Proteomes; UP000076794; Chromosome.
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   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; 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; 2.
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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000076794}.
FT   DOMAIN          65..395
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          400..744
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   REGION          552..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..921
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1181 AA;  125438 MW;  7033861BC3788D67 CRC64;
     MTSHPTGDQL PEDDGHATLG DETWWAALDA DHRDTDLGFP ELESPVDVSR PRYSARDIAE
     KLGRPAPTDE QVAVIEAPLE PVLVVAGAGS GKTETMAARV VWLIANGLVE PEEVLGLTFT
     RKAAGELSTR VQSRLAQLAR AEGRTTADLD LLARPTVATY NAYAASLVAD HGLRLGVEPG
     SRLLGEANQW QLAAEVVESW DGDLGTDKAV STVVGAVLSL SGALGEHLRG VDEARDVLDG
     IVERLDSLPL GPRQRARTQD VEKLIRSVAE RARLLDLVAE YRRRKRVADS LDFGDQVAFA
     AELARTVPAV GAAERTRFRA VLLDEYQDTS FAQVELLAGL FGGGHAVTAV GDPHQSIYGW
     RGASAAGLSR FPDRFRHADG GAAPVRFLST SWRNDAAVLA AANVASGPLR DAGTAVPVPP
     LHLRDGAGQG VVRAHVAATL EEEAEVVAEL VAARWRRGTR PDGADRVTAA VLCRARSQFA
     VLETALRRRG LPVEVVGLGG LLTTPEVVDV VALLEAVHDP SRGDSLLRLL TGPRVNLGAA
     DLHALGSSAA DLARRDDPRR RHAAAGAPDD APGDVPDGDE VTVVEGDVVD HRSLVDALDD
     LPEPGRAARD GRVLTPEGRT RLAALARLLR DLRSLTYLSL PELVVAAERA LGLDVEVATA
     ELLADGLAGA GPYAADGVSR RGREHLDAFR DVAASFAQSA DVATLGAFLA WLGVADDQER
     GLDMPVREPD PDAVQIITAH AAKGLEWDVV AVPGLVDGVF PTVAESSRGR TSPGWLSGLG
     ELPYPLRGDA EDLPGLDLAS VADTKELMAR RDEFVLDCGA HQLAEERRLA YVAFTRARRE
     LFCTAHWWGT AAKPRALSPF LQELAEAGLV STEGWEPAPD GTDNPRDGEV PTGVWPAPEA
     GGTAPEPAVP GSAPTAPGDV PTARDLLRRT AARVRAAADA EPADGGLVDE TGHDLVGLAR
     LLLAERADRV EPSVEMPAHV SASGLVRLAR DRDEFARQLR RPVPVEPTVH ARRGTLFHAW
     VEQYFGAASL LDVEDMPGAE DAGDHSGDLA LDELKELFLG TPWAALTPVA VEQDVETPVG
     GVMVRSRIDA VFPDPDAPEP APGEAPAVVV VDWKTGRAPR DPVDRAQREV QLAAYRLAWS
     RWKGIPVEKV SAAFVHVADG TTVRPTELLD EAGLEALVRG A
//
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