GenomeNet

Database: UniProt
Entry: ADDB_DESHY
LinkDB: ADDB_DESHY
Original site: ADDB_DESHY 
ID   ADDB_DESHY              Reviewed;        1220 AA.
AC   Q24WW7;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=ATP-dependent helicase/deoxyribonuclease subunit B {ECO:0000255|HAMAP-Rule:MF_01452};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01452};
DE   AltName: Full=ATP-dependent helicase/nuclease subunit AddB {ECO:0000255|HAMAP-Rule:MF_01452};
GN   Name=addB {ECO:0000255|HAMAP-Rule:MF_01452}; OrderedLocusNames=DSY1686;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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 AddB subunit has 5' -> 3'
CC       nuclease activity but not helicase activity. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01452};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01452};
CC   -!- SUBUNIT: Heterodimer of AddA and AddB. {ECO:0000255|HAMAP-
CC       Rule:MF_01452}.
CC   -!- MISCELLANEOUS: Despite having conserved helicase domains, this subunit
CC       does not have helicase activity. {ECO:0000255|HAMAP-Rule:MF_01452}.
CC   -!- SIMILARITY: Belongs to the helicase family. AddB/RexB type 1 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01452}.
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; AP008230; BAE83475.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24WW7; -.
DR   SMR; Q24WW7; -.
DR   STRING; 138119.DSY1686; -.
DR   KEGG; dsy:DSY1686; -.
DR   eggNOG; COG3857; Bacteria.
DR   HOGENOM; CLU_007838_0_0_9; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008409; F:5'-3' 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   HAMAP; MF_01452; AddB_type1; 1.
DR   InterPro; IPR049035; ADDB_N.
DR   InterPro; IPR014140; DNA_helicase_suAddB.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   NCBIfam; TIGR02773; addB_Gpos; 1.
DR   PANTHER; PTHR30591; RECBCD ENZYME SUBUNIT RECC; 1.
DR   PANTHER; PTHR30591:SF1; RECBCD ENZYME SUBUNIT RECC; 1.
DR   Pfam; PF21445; ADDB_N; 1.
DR   Pfam; PF12705; PDDEXK_1; 1.
DR   Pfam; PF13361; UvrD_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; DNA damage; DNA repair; DNA-binding; Exonuclease;
KW   Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nuclease;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1220
FT                   /note="ATP-dependent helicase/deoxyribonuclease subunit B"
FT                   /id="PRO_0000379187"
FT   DOMAIN          1..281
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   DOMAIN          283..590
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   REGION          989..1008
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         788
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1128
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1131
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
FT   BINDING         1137
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01452"
SQ   SEQUENCE   1220 AA;  137379 MW;  DB7917CE372FD21D CRC64;
     MSMRFIVGRA GTGKSTLCRQ EIHKESQEHP EGLPLILLVP EQATHQMEMS LAHDPQSGGI
     LRAQVLSFRR LGWRVFSEVG GGGKAVIGEV GKRMLLRRLL LNHRSDLRVF ARSATRPGMA
     DLLAQAIAEF KIYRITPDQL RGIEDADELL LQKTHELAFL YEELNKSLGT AARDPDDELN
     LVAGKISQAP FLQGAKIWVD GFKGFTPQEL YVIQAMLGTA AEITVSLPLD PELLKAGTPR
     FKPGEELFYE PRQTYQGLVD LAREAKASIS HVFLTETHRF EKAGLKHLER FYNAYPTQTF
     PGGDDSTAPD PLGIALFPAA NKRAEVEGVA RELRRLAREE GRTWRDCSVV TRDLPGYQGI
     IEQVFNAHEI PYFLDHKRPV IHHPLLELLL SAIETVQKDW AYEPLFRCLK TDFFPCSKDR
     IDRLENYCLA YGIHGSAWKG NRSWSYYPDP NHKEETAGLN ETRQIIYDLF SPFDQAIRPH
     PEAGGPSVTV AQITEAIYEL LIRLKVPEHL QEWAEAAHSR GDLAEAQLQN QIWDAVIQVL
     DELVAGLGEE VMDLSDFAMI LTSGLENLQL GLIPPGYDQV LVGSLDRSRN PETAVLFLLG
     ANDGILPGKP SDEGVFDELE RLRLESKGIM LAPKGKVQVY EEQYFIYTAL TRAREQLYIS
     YPLTDEEGRG LTVSPVIHRL KMIFPGLPEK YLSLDEEEPG ALPHPYALLP AYALHLQKLR
     QGSSLSPLWQ AIRLWFLSQT AAFPQVQLLE KGLRDQNEEG KLPQPLARQL YGKRLVTSVS
     RLELFARCPF AHFAQYGLKL KERSNYRLSP PDMGQFFHAV LHDYAIALRE RGLDWGELSK
     EQSWQLVNET AEPIALQLQN KILLSNARYR YLTHKLKRTV HHAVRVLGEH ARQGVFLPME
     LEVKFGPQEA LPPLEVPLSG GNSLLLRGQI DRIDGAVLGH EIYLRIFDYK SREAHVSLNQ
     IYHGLDLQLL AYLDAALQGA QILVSSSGLA EGSKGSEGSE GSEDSEDSTI HPAGFLYFPV
     LEPQLKSKTL LYPEQLEKDR IKAVKVKGYL LADRQVLLAM DRDLENSSLL GIKLTKSGEF
     KKGSPILTEE QFALLRKHLQ HFLRCSGEAL LEGDISITPY RQGKHTACQF CSYKPLCHFD
     PYLPENNYRN LPVIQDEEFW QRVQSQDSEQ YPEQHPPTSV PGETSRRALQ KDGGNSPRGQ
     ELIWLGEDEA GAGKEDDGHE
//
DBGET integrated database retrieval system