ID ADDA_EXIS2 Reviewed; 1183 AA.
AC B1YKM8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
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=Exig_0730;
OS Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15).
OC Bacteria; Firmicutes; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / JCM 13490 / 255-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O.,
RA Monk C., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Vishnivetskaya T., Rodrigues D.F., Gilichinsky D., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-
RT 15.";
RL Submitted (APR-2008) 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; CP001022; ACB60211.1; -; Genomic_DNA.
DR RefSeq; YP_001813228.1; NC_010556.1.
DR ProteinModelPortal; B1YKM8; -.
DR STRING; 262543.Exig_0730; -.
DR EnsemblBacteria; ACB60211; ACB60211; Exig_0730.
DR GeneID; 6173573; -.
DR KEGG; esi:Exig_0730; -.
DR PATRIC; 32135033; VBIExiSib53410_0744.
DR eggNOG; COG1074; -.
DR HOGENOM; HOG000015621; -.
DR OMA; MERINYI; -.
DR ProtClustDB; CLSK2489102; -.
DR BioCyc; ESIB262543:GHBP-804-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 1183 ATP-dependent helicase/nuclease subunit
FT A.
FT /FTId=PRO_0000379271.
FT DOMAIN 3 461 UvrD-like helicase ATP-binding.
FT DOMAIN 473 769 UvrD-like helicase C-terminal.
FT NP_BIND 24 31 ATP (By similarity).
SQ SEQUENCE 1183 AA; 136605 MW; 4CF4C1AA49C8F841 CRC64;
MSVQWTDEQQ RAIDARGGHI LVSAAAGSGK TAVLVERLTQ RVINQEDPLT ADRILVATFT
NAAAKEMKTR VIEAIEAKIK VAPDDLYLKK QRQMMNRAQI TTIHSFCLSI LRENYYRIGL
DPAFRIAEEA ELLLLQDDVL EEVFESFYAS ADPAFYELID SYTSDRDDQA MLTLISNLYR
FSRSLPDPEA FYDHLIAQYD QPIDPDESSL LTRLFELEWE RVGPVINRYM ELSYRLRQSG
YDEMADLLVQ DVTPVRRINP EQDRWTTVAL AFQAVEFGRW KGIRGDEEMK KFQTERTRLV
SDLKKMRDLF VEKDGVDYLE DLRSQLGHVE MIVTLVRSFS AAYLEAKQQR GIVDFSDLEH
FALAILEENG EPTDVARLLQ ERFIEVLVDE YQDTNEVQER ILRLVSKSDE ATGNLFMVGD
VKQSIYKFRH AEPGLFLNKF KRFQQTEVGT RIDLTKNFRS RLEVLDGTNH IFRQVMDEAV
GEIDYDEAAY LRLGNLGYVD STQVDPELLL VDQTDTNKEE LEAQVIATRI IEMVNDENPY
LVFDAKQKRF RKCEYRDIVI LVRSRGKRVQ ALVDVFEQYE LPVYADTTGG YFQATEIQIM
MSLLKTIDNP LQDIPFASVL RSPIFGLTDR DLGRIRAKSK DGSFYEAAIL VAKEQTPLGL
RVDEALNQLH HWRTEARGKS LASLIRSLFD QTGYFEYVGC LNGGRSRQAN LNALYERAHQ
YEASGYRGLY RFLRLIHRLV ERGEDFSEAR SLGEDEDVVR IMTIHQSKGL EFPVTIVSQL
GKQFNKQDQI QAIQLHKTYG IALDAIDPVK RLRSGTLLKE VIRREMDREM KAEEMRVLYV
AMTRAKEKLI LVGAIKGLED QLIKWQDQPL DELLLPEMDR RNAKTYADWV VPAVLRNFLL
SEDGPRWSFR IIALDEIAPY QELTKMVEQL EHVRVLEKID HAGDETLNIQ IEAAFAYQYP
YQVATDTAAK QTVTELKRTE QLERAAFEST HRQSTYYRTP QFLGPTLTGA ERGTVLHLAM
QLYESGRSFE EQILDWEQAE RISSLEAQTM REAIPELTTF LASDTGQLFE QRLLAGEVYR
ELPFTYKIDS ARFRSDWHGP SDQAVMQGIV DCLIRDGDTY ILLDYKSDQV FETTDNQNQA
EVLRTRYATQ LNLYQEALEA ILHIRISRKL IYAFALHEVI EIY
//
