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Database: UniProt
Entry: D9SL36_CLOC7
LinkDB: D9SL36_CLOC7
Original site: D9SL36_CLOC7 
ID   D9SL36_CLOC7            Unreviewed;      1287 AA.
AC   D9SL36;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE            EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE            EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE   AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE   AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN   Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN   OrderedLocusNames=Clocel_1808 {ECO:0000313|EMBL:ADL51552.1};
OS   Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=573061 {ECO:0000313|EMBL:ADL51552.1, ECO:0000313|Proteomes:UP000002730};
RN   [1] {ECO:0000313|EMBL:ADL51552.1, ECO:0000313|Proteomes:UP000002730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35296 / DSM 3052 / OCM 3 / 743B
RC   {ECO:0000313|Proteomes:UP000002730};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium cellulovorans 743B.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA helicase
CC       and an ATP-dependent, dual-direction single-stranded exonuclease.
CC       Recognizes the chi site generating a DNA molecule suitable for the
CC       initiation of homologous recombination. The AddA nuclease domain is
CC       required for chi fragment generation; this subunit has the helicase and
CC       3' -> 5' nuclease activities. {ECO:0000256|HAMAP-Rule:MF_01451}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_01451};
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|HAMAP-Rule:MF_01451};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC       Rule:MF_01451}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01451}.
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DR   EMBL; CP002160; ADL51552.1; -; Genomic_DNA.
DR   STRING; 573061.Clocel_1808; -.
DR   KEGG; ccb:Clocel_1808; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   OMA; KQSIYRW; -.
DR   OrthoDB; 9810135at2; -.
DR   Proteomes; UP000002730; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   HAMAP; MF_01451; AddA; 1.
DR   InterPro; IPR014152; AddA.
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   NCBIfam; TIGR02785; addA_Gpos; 1.
DR   PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE/NUCLEASE SUBUNIT A; 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|HAMAP-
KW   Rule:MF_01451}; DNA damage {ECO:0000256|HAMAP-Rule:MF_01451};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01451};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01451};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW   Rule:MF_01451};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01451, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01451, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Isomerase {ECO:0000256|HAMAP-Rule:MF_01451};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000002730}.
FT   DOMAIN          7..486
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          527..822
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         28..35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1287 AA;  149943 MW;  0F1ED3712ACAD6A4 CRC64;
     MKNIGTRKWT EEQKAAIDTH GVNLLVAAAA GSGKTAVLVE RIIELVSNKE AKTDIDKLLV
     VTFTKAAAAE MRERIGNALA EKISENPDDT HLHRQLVLLN KANITTMHSF CQSLIKNYFH
     KLDIDPAFRI GDATEIELLL LETIEEVLEE CYKEENITIG FQRLVEGYGK NEDDKSVQDV
     IIRLYRFVMA MPWPESYLEK VVEAYRAFEE TSPFKTSFEN SEFSKEICKI VYDKVEPDLK
     TLRILIREVE AQESINPNLP LLIKEEAYLS NIVKNSKEGY EALRNILMSV EFGRLSTKKT
     SILIETKEQM KNVRDQYKET ISSIIEDFFY DDIEAINEEF RFIAPIISIL KEILISVIHT
     FKEKKRSKGI IDFNDMEHYV LELLCTKNDK DETVPTEVAL EIRRKFEEIM IDEYQDSSFI
     QEEIMTTISR KDEAVPNMFM VGDVKQSIYK FRQAKPELFL EKYETYEELD GARNRKILLY
     KNFRSRKEIL DGTNFIFKSI MSKELGELEY TDKEALNLGA DYVTFEDESL TFAEPIDVII
     FEKPSGNIEI QKDTDEDAED LEEINEFQME AKIIGAEIKK IMGREAGYRR KKVFDKGSYR
     DVEYKDIVIL LRSTVNRTDV FLEELKNLEI PVYADSTSGF FDNIEVKTIL ALLQVIDNPK
     QDIPLLAVLR SPIGGFSDDE LIDIKISMDK EYCYFFDKLS NYCVVGSDND LREKTKAFLR
     RLNDYRSKSL HLSLVELIWF LFTDTGYLAF VGTLPNGMQR QGNLRILFHR AKQYEATSYR
     GLFNFINFME KMKNTSSDLG DAKLLGENDN VVRIMTIHKS KGLEFPVVFL ASTSKRFNNR
     ELNNEFLFHH NFGIGIKYTD FEKRISYSSI LRNLIQEKMK IENYSEEMRV LYVALTRAKE
     KLIITGGVKE IEKSIRKWAL SCETQQHQEN FFINSLEQCE EDDKVNSNSL IESSLEEKIS
     KDIIIKANSY LDWIVFALMR HKSTNEIREL YNIHCSPLVL TNSPSKWNIK LLNSEDILAF
     KKNGALDDQM DSREQLFQKI IEEISEKDTD QYKAEIQRRL SFKYKYSVAT EIPSLLSVTE
     IKRRFNDINQ GGEDIYIPKL LKTPRFLEEE KALTSAERGT IVHLVMQHLD LNRALTMESI
     NEQISEMIKR EFINEKEAKV VDIRKILRFF SSTIGLRMLR ADKIYREYPF KIRVKSNEIL
     KLSKSDDENE DIIVQGVIDT IFVENDEIVI IDYKNDYVND NIVDTIKTQY KTQLNYYKIA
     AEKILNKRVK NIYLYLFYSG EVLEYDF
//
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