ID ADDA_CLOK1 Reviewed; 1238 AA.
AC B9DZK4;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 33.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A;
DE EC=3.1.-.-;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase/nuclease AddA;
GN Name=addA; OrderedLocusNames=CKR_0628;
OS Clostridium kluyveri (strain NBRC 12016).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=583346;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 12016;
RA Inui M., Nonaka H., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Vertes A.A., Yukawa H.;
RT "Complete genome sequence of Clostridium kluyveri and comparative
RT genomics of Clostridia species.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The heterodimer acts as both an ATP-dependent DNA
CC helicase and an ATP-dependent, dual-direction single-stranded
CC exonuclease. Recognizes the chi site generating a DNA molecule
CC suitable for the initiation of homologous recombination. The AddA
CC nuclease domain is required for chi fragment generation; this
CC subunit has the helicase and 3' -> 5' nuclease activities (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Magnesium (By similarity).
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB (By similarity).
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain.
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DR EMBL; AP009049; BAH05679.1; -; Genomic_DNA.
DR RefSeq; YP_002471093.1; NC_011837.1.
DR STRING; 583346.CKR_0628; -.
DR EnsemblBacteria; BAH05679; BAH05679; CKR_0628.
DR GeneID; 7274105; -.
DR KEGG; ckr:CKR_0628; -.
DR PATRIC; 19471012; VBICloKlu118830_0764.
DR eggNOG; COG1074; -.
DR HOGENOM; HOG000015621; -.
DR ProtClustDB; CLSK971605; -.
DR BioCyc; CKLU583346:GJNQ-662-MONOMER; -.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:HAMAP.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:HAMAP.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR Gene3D; 3.90.320.10; -; 1.
DR HAMAP; MF_01451; AddA; 1; -.
DR InterPro; IPR014152; DNA_helicase_suAddA.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR011604; Exonuc_phg/RecB_C.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52980; Restrict_endonuc_II-like_core; 1.
DR TIGRFAMs; TIGR02785; addA_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW Exonuclease; Helicase; Hydrolase; Nuclease; Nucleotide-binding.
FT CHAIN 1 1238 ATP-dependent helicase/nuclease subunit
FT A.
FT /FTId=PRO_0000379259.
FT DOMAIN 6 474 UvrD-like helicase ATP-binding.
FT DOMAIN 512 811 UvrD-like helicase C-terminal.
FT NP_BIND 27 34 ATP (By similarity).
SQ SEQUENCE 1238 AA; 144811 MW; A7C797B4897E5CCD CRC64;
MINVNTKWTE TQKSAIFTPN CNLLVAAGAG TGKTAVLVER ILQKVINDSE EVDIDKLLVV
TFTNAAASEM KERVGEALSK LLELNCTSKN LQRQLALLNQ SNIMTIHSFC LKVIKNNFHR
IDLDPNFRIC DDTESKLLKQ DALLELFEEK YEEENLGFLN LADGYGGKND SKLQDIVLSL
YEFSQGSPWP KRWLQDVLKD FNLGSDFDFG DTKWAKVLMH NVTVELKGCK NKMKNILNTI
ENIEGLEHYL EPFKSDIESI DKLINITTWD EIRDEFIKLS FNKLPSKRTD PLVKSYKDKA
RNTRDEVKKK LISIREDIIL CTDDIYENFK EVYPLMKSLT FLVMDFYEKY HNKKSERNMI
DFNDIEHFCL EILTSKDKNG DIIPSEAALE YREYFEEIFI DEYQDSNEVQ EVIMNMISRK
NIYANLFMVG DVKQSIYRFR QARPELFLEK YNSYDEKEGS KNRKIKLSEN FRSRKEIIDA
INYIFKQIMC REVGELDYGE EECLKSSARY EPFEGNCGGD VELHVVDKKE NENKLEDENE
EELLDAISVE ARLVASKINE LVNPSLDQYS FKVYDKEIDN YRSIMYKDIV ILMRATQNWA
PAFVEELNNS GIPVFADTSV GYFQAIEIKT IISLLQIIDN PLQDIPFIAL LRSPIGGFSP
EDLIDLRVVN REISFYEILK AIKEHSLELK YSLEHIDERL EYKVEQFFNK LCLWRRKVIH
MPIDEFIWHI YIETGYYGFV GAMPGGIQRQ ANLRMLFERA KQYKNISYKG LFNFINFINK
LKSSSTDMGN AKILGENENV VRIMSIHKSK GLEFPVIILS GAGKRFNLTD INKSVLFHKE
LGLGPEYVNS ERHISYPTIV KQVLKRKLKM ETLSEEMRIL YVAFTRAKEK LIITGTVDNI
ENTFQRWCEA AYCEEDKLPE YSLINSRNFL DWIGPAVARH PCGEIIRKVC PFEYNLNLIT
GDDSKWKVFV YSKDNFKSTL DENIDEDIIG KIKSLELDNN KEIYKNEVYR RLNWTYKYEQ
SSKIAAKFSV SELKRRFKLI DTENGIEFME PIYLKKPAFL RESKGLTPSE RGIVMHLVMQ
HIDIDKVGSY EQIKEQVDKL VFREFITEAE AKSISVYKII KFFNSEIGIR MKKSNNVYRE
VPFYMEIEST ELYKQLPQHI YRDEKVLIQG IIDCYFEENN ELILVDYKTD HVGDIDSIKE
KYQVQIYYYG RALEKLTGKK VKKKYLYLFS KDYILDLS
//
