ID ADDB_DESHD Reviewed; 1218 AA.
AC B8FXD8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B;
DE EC=3.1.-.-;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase/nuclease AddB;
GN Name=addB; OrderedLocusNames=Dhaf_2833;
OS Desulfitobacterium hafniense (strain DCB-2 / DSM 10664).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCB-2 / DSM 10664;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ovchinnikova G., Madsen T., Christiansen N., Ahring B.,
RA Marsh T., Harzman C., Davis J.K., Kim S.-H., Tiedje J.M.;
RT "Complete sequence of Desulfitobacterium hafniense DCB-2.";
RL Submitted (DEC-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 AddB
CC nuclease domain is not required for chi fragment generation; this
CC subunit has 5' -> 3' nuclease activity (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- COFACTOR: Binds 1 4Fe-4S cluster. Magnesium (By similarity).
CC -!- SUBUNIT: Heterodimer of AddA and AddB (By similarity).
CC -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1
CC 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; CP001336; ACL20857.1; -; Genomic_DNA.
DR RefSeq; YP_002459293.1; NC_011830.1.
DR STRING; 272564.Dhaf_2833; -.
DR EnsemblBacteria; ACL20857; ACL20857; Dhaf_2833.
DR GeneID; 7259841; -.
DR KEGG; dhd:Dhaf_2833; -.
DR PATRIC; 21663565; VBIDesHaf15223_2949.
DR eggNOG; COG3857; -.
DR HOGENOM; HOG000285805; -.
DR OMA; DIGNYKA; -.
DR ProtClustDB; CLSK2465933; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:HAMAP.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:HAMAP.
DR GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 HAMAP; MF_01452; AddB_type1; 1; -.
DR InterPro; IPR014140; DNA_helicase_suAddB.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR Pfam; PF13361; UvrD_C; 1.
DR TIGRFAMs; TIGR02773; addB_Gpos; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; Complete proteome; DNA damage; DNA repair;
KW Exonuclease; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW Nucleotide-binding.
FT CHAIN 1 1218 ATP-dependent helicase/deoxyribonuclease
FT subunit B.
FT /FTId=PRO_0000379186.
FT DOMAIN 1 279 UvrD-like helicase ATP-binding.
FT DOMAIN 281 588 UvrD-like helicase C-terminal.
FT NP_BIND 6 13 ATP (By similarity).
FT METAL 786 786 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 1126 1126 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 1129 1129 Iron-sulfur (4Fe-4S) (By similarity).
FT METAL 1135 1135 Iron-sulfur (4Fe-4S) (By similarity).
SQ SEQUENCE 1218 AA; 137160 MW; 98538C90CD2CF436 CRC64;
MRFIVGRAGT GKSTLCRQEI HKESQEHPEG LPLILLVPEQ ATHQMEMSLA HDPQSGGILR
AQVLSFRRLG WRVFSEVGGG GKAVIGEVGK RMLLRRLLLN HRSDLRVFAR SATRPGMADL
LAQAIAEFKI YRITPDQLRG IEDADELLLQ KTHELAFLYE ELNKSLGTAA RDPDDELNLV
AGKISQAPFL QGAKIWVDGF KGFTPQELYV IQAMLGTAAE ITVSLPLDPE LLKAGTPRFK
PGEELFYEPR QTYQGLVDLA REAKASISHV FLTETHRFEK AGLKHLERFY NAYPTQTFPG
GDDSTAPDPL GIALFPAANK RAEVEGVARE LRRLAREEGR TWRDCSVVTR DLPGYQGIIE
QVFNAHEIPY FLDHKRPVIH HPLLELLLSA IETVQKDWAY EPLFRCLKTD FFPCSKDRID
RLENYCLAYG IHGSAWKGNR SWSYYPDPNH KEETAGLNET RQIIYDLFSP FDQAIRPHPE
AGGPSVTVAQ ITEAIYELLI RLKVPEHLQE WAEAAHSRGD LAEAQLQNQI WDAVIQVLDE
LVAGLGEEVM DLSDFAMILT SGLENLQLGL IPPGYDQVLV GSLDRSRNPE TAVLFLLGAN
DGILPGKPSD EGVFDELERL RLESKGIMLA PKGKVQVYEE QYFIYTALTR AREQLYISYP
LTDEEGRGLT VSPVIHRLKM IFPGLPEKYL SLDEEEPGAL PHPYALLPAY ALHLQKLRQG
SSLSPLWQAI RLWFLSQTAA FPQVQLLEKG LRDQNEEGKL PQPLARQLYG KRLVTSVSRL
ELFARCPFAH FAQYGLKLKE RSNYRLSPPD MGQFFHAVLH DYAIALRERG LDWGELSKEQ
SWQLVNETAE PIALQLQNKI LLSNARYRYL THKLKRTVHH AVRVLGEHAR QGVFLPMELE
VKFGPQEALP PLEVPLSGGN SLLLRGQIDR IDGAVLGHEI YLRIFDYKSR EAHVSLNQIY
HGLDLQLLAY LDAALQGAQI LVSSSGLAEG SKGSEGSEGS EDSEDSTIHP AGFLYFPVLE
PQLKSKTLLY PEQLEKDRIK AVKVKGYLLA DRQVLLAMDR DLENSSLLGI KLTKSGEFKK
GSPILTEEQF ALLRKHLQHF LRCSGEALLE GDISITPYRQ GKHTACQFCS YKPLCHFDPY
LPENNYRNLP VIQDEEFWQR VQSQDSEQYP EQHPPTSVPG ETSRRALQKD GGNSPRGQEL
IWLGEDEAGA GKEDDGHE
//
