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Database: UniProt
Entry: A0A1E8F1E5_9CLOT
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ID   A0A1E8F1E5_9CLOT        Unreviewed;       721 AA.
AC   A0A1E8F1E5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-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};
GN   Name=pcrA_2 {ECO:0000313|EMBL:OFI07004.1};
GN   ORFNames=CLOACE_05900 {ECO:0000313|EMBL:OFI07004.1};
OS   Clostridium acetireducens DSM 10703.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI07004.1, ECO:0000313|Proteomes:UP000175744};
RN   [1] {ECO:0000313|EMBL:OFI07004.1, ECO:0000313|Proteomes:UP000175744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI07004.1,
RC   ECO:0000313|Proteomes:UP000175744};
RA   Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT   "Genome sequence of Clostridium acetireducens DSM 10703.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OFI07004.1}.
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DR   EMBL; LZFO01000006; OFI07004.1; -; Genomic_DNA.
DR   RefSeq; WP_070109553.1; NZ_LZFO01000006.1.
DR   AlphaFoldDB; A0A1E8F1E5; -.
DR   STRING; 1121290.CLAOCE_05900; -.
DR   PATRIC; fig|1121290.3.peg.601; -.
DR   Proteomes; UP000175744; 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   Gene3D; 1.10.10.160; -; 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; 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; 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.
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:UP000175744}.
FT   DOMAIN          1..312
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   721 AA;  84464 MW;  37E4CA14DA137D59 CRC64;
     MGFRVDQKPV MEYSEGIMAV PAVPGAGKTF IVANLAAKII KEKLKKREKV LIVTYMNSAV
     NNFKNRIKCV LEEQDIKDIN SYEVMTIHSL ALRILKDRPD VVNVNENFKI LDEAQKSVYL
     NECIKSWRKF KGERIFKNVL NENGLKSYNN KQERYWNNFL TIVTALISEL KLNDIQAENL
     DNKLKIFNNK FSVIRDISDI YKNYTKRLKL DGYLDYDDIL ILAYKALKRD KKLREKFQKK
     YTYIFEDECQ DSNIVQYKIL TMLSEKSGNL VRVGDINQSI MATFTPSDPK FFKEFCSKAD
     KKYTMYMAGR SSKKIIDLAN YLVEFIINNH YQKQCREALQ NQKIQEVKGI EGLKNPSNDE
     SNLYAFLLPS WDKEIEKVIE SIKIFKKKHP NETIGVLITS NYKINKFVEK LDKENIDYDN
     LSSISKDKVK IVNIIGYLLK FLAEPDSSIK FKIFLDVFID DKYDKKDLIL QFIDNYKNPY
     DIIYRDFEKI KSNNNIVLLI KIIENIRKIF EYYYISIDNL IIFIGSIFDF NIQDKALIQA
     VALYVKNILR EEKNVVLNDI ADRLIDKNNP IFVHIGEIIY EMEGYEPSPE KVTIATYHKA
     KGLEWDCVFL MDNTEYNFPY TLKDKIQSDY WYIKEEIKNP VALGKAEIEK LKGNIVSVNP
     LIKSRIDVIN EKVRLLYVGI TRAKKYLILT ANFNKNSNSF KTQSCSRYFQ VLKNFINSKE
     V
//
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