ADDA_DESHD
ID ADDA_DESHD Reviewed; 1392 AA.
AC B8FXD7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Dhaf_2832;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL20856.1; -; Genomic_DNA.
DR RefSeq; WP_015944254.1; NC_011830.1.
DR AlphaFoldDB; B8FXD7; -.
DR SMR; B8FXD7; -.
DR EnsemblBacteria; ACL20856; ACL20856; Dhaf_2832.
DR KEGG; dhd:Dhaf_2832; -.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR Proteomes; UP000007726; 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.
FT CHAIN 1..1392
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379266"
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 555..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 559..578
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; 157241 MW; 3E36F482FA63233F 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 IVYDEQAALR PGAKFVSDGE LRTAEGPIEV
HLFDPKAIDL SLGQKRGAED AATEVDSPAK 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
