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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//