ADDA_DESHY
ID ADDA_DESHY Reviewed; 1392 AA.
AC Q24WW8;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01451};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000255|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000255|HAMAP-Rule:MF_01451}; OrderedLocusNames=DSY1685;
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Firmicutes; 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 AddA nuclease domain is
CC required for chi fragment generation; this subunit has the helicase and
CC 3' -> 5' nuclease activities. {ECO:0000255|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=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000255|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01451}.
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DR EMBL; AP008230; BAE83474.1; -; Genomic_DNA.
DR RefSeq; WP_011459831.1; NC_007907.1.
DR AlphaFoldDB; Q24WW8; -.
DR SMR; Q24WW8; -.
DR STRING; 138119.DSY1685; -.
DR PRIDE; Q24WW8; -.
DR EnsemblBacteria; BAE83474; BAE83474; DSY1685.
DR KEGG; dsy:DSY1685; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000001946; 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:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 4.
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; 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 PANTHER; PTHR11070; PTHR11070; 1.
DR PANTHER; PTHR11070:SF48; PTHR11070:SF48; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1392
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379267"
FT DOMAIN 3..489
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 556..886
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT REGION 291..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1067..1086
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1392 AA; 157155 MW; 5384AE0487735C0E CRC64;
MNNPKWTPAQ QAAIDLKGQL LVAAAAGSGK TAVLVQRLFK QITDVDEQVD VDRFLVVTFT
KAAAAEMRER IGKALDEALF GAAEPAQVEH LLQQRALLYR ASITTLHSFC MELIRQYFYL
IELDPAFRVA DEAEADLLRQ DTLEDLFEAY YGEETPAFQS LVDAFGTDRD DQPLMASILR
LHEFAMSQVH PGEWLEHLPA AYDWHSLDDL MESPWGQVVR QGVRDKVEEG LILLERAYRL
AELPGGPVHY LPVLEDDQSR LGFLREMAEK GTWSDIETAF KSAAAFPGLP RGSKKNLPDS
LIDEENSKRL REESKKARDE AKKKLEEIKN TVFSVPLTDQ LPFLNKMGEL VGTLAQVTQH
FAREYQKAKR QRNCVDFSDL EHYALQLLAK DKQPTEIALK LQAYYAEVLV DEYQDINPVQ
ERILQLVSRQ EEGKANLFMV GDVKQSIYRF RMADPGLFLR KYGEFPHYQE GGGAAPNLVI
DLNQNFRSRP EVIQGINYLF YQIMTEGAGE IIYDEQAALR PGAKFVSDGE LRTAEGPIEV
HLFDPKAIDL SLGQKRGAED AATGADSPAK GEGEEFEQNR EPESGDDESS LEEAETARIE
ARLVAARIQK MVLEREFQIH DKELGDYRPV QYADIVILMR SLASVASVYA EEFQKAGIPV
YAETNSGYFG TNEVDTVLSL LKIIDNPRLD IPFAAVLRSP LVGMNGTELG KLRSLLPQGD
FYETLVLTFW AGDAHRQEEG HEFYSEIREI LGKHWESLPQ LEVKVRHILE TSPEIKEKVD
AFFPKLQEWR HRSRRTSLAD LLWHLYEDTG YLAYVGTLPA GAQRQANLRV LYDRACRYEA
TNYRGLFRFL RFLEKFQSQG KDLGNASIVG EKENVVRFIT VHSSKGLEFP VVFIAGLGKK
FNTRSLSSQL LLHSHLGVGI PLIDIENQVR YPSVIQYAVK ERLWQEALAE ELRILYVALT
RGKERLFLFG HQHKLAEAIN KWRSLALSCP DTAFPDGQLR GAKTYLDWLG PALVRHPEDL
FKLGSFPTAS ELPDSSSQWK VILHDQIAGK GPVQEATSSQ DEIILPDQET LGEREASEET
EIPGETEASG KTEIPGETKN SEETKTSEDK KNLEAQTPET ADLDTKNLQE EVFRQLNWQY
PYPEGVNQSA KTSVSELKRQ SLWYMDNEYS SPSSSSSSSP SALSAPSFLR PQFIVSRKEL
TPAERGTAVH AAIQHLPLAL WRDTWEELAQ EVRESMLQEH IDSLIRREIL SAEQGGAVSV
SQLKNLLDST SGKRLWEAEE VRREVPFTLS LRLRAQKEPV LVQGIIDAVL LSHQEHEAQV
MDFKTDNLAG VPDPELVLTQ RYGLQLGLYA LAVERLLKVP VRECIIYATS LNREFVMQRE
AVQAALESVV IV
