ADDA_ANOFW
ID ADDA_ANOFW Reviewed; 1209 AA.
AC B7GM51;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Aflv_2230;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34589.1; -; Genomic_DNA.
DR RefSeq; WP_012575765.1; NC_011567.1.
DR AlphaFoldDB; B7GM51; -.
DR SMR; B7GM51; -.
DR STRING; 491915.Aflv_2230; -.
DR EnsemblBacteria; ACJ34589; ACJ34589; Aflv_2230.
DR KEGG; afl:Aflv_2230; -.
DR PATRIC; fig|491915.6.peg.2290; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR OMA; KQSIYRW; -.
DR OrthoDB; 137860at2; -.
DR Proteomes; UP000000742; 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 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; DNA damage; DNA repair; DNA-binding; Exonuclease; Helicase;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1209
FT /note="ATP-dependent helicase/nuclease subunit A"
FT /id="PRO_0000379229"
FT DOMAIN 9..482
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT DOMAIN 510..798
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01451"
SQ SEQUENCE 1209 AA; 140150 MW; 14A89E1C7F002011 CRC64;
MIPPKPRESQ WTDEQWQAIY ATGQHTLVAA AAGSGKTAVL VERIIQKILH KERPIDVDRL
LVVTFTNAAA AEMRQRIGEA LERALEKEPH SLHLRRQLSL LQKASISTIH SFCLDVIRKY
YYVIGIDPVF RIADEGEMAL LKEEVLETLF EQYYAENDEP FLTVVDRYTS DRTDADLQTL
ILRLYEFSRS HPNPSGWLQQ IVHMYDVEEG ARIDDLPYAH YLFQAVDLAL EAAEYRLAQA
LQKTKEPGGP DYLYDTLASD EQVIAKLKEA RHESWQQLHE AMKNVSFATA KRKPKDGAYD
EQLVEDVKKL RDQVKKEISS ITEELFSFQP VTYVRHLHEM KPIVTTIVQM VQRFAHLLQA
KKDEKGIVDF SDLEHYCLRI LRAPSLEHEL KPSEAALYYR AQFAEVLVDE YQDTNMVQES
ILRLVSNDDE ATGNMFMVGD VKQSIYGFRL AEPSLFLQKY NRFTKDGDGG LRIDLAKNFR
SRKEILDGTN FIFRQLMTET VGDMRYDDDA ALRFGAQDYP DKQIPVECVW INEAKEESDE
EEQEDVTAVQ LEARWIAKKI KQLLAEPFFV YDRRLKGERR LMYRDIVILC RSMSSASAML
EEFRKQNVPV YAELSSGYFS ATEVSIMLSL LKVIDNPYQD IPLAAVLRSP IVGLDEEALA
RIRLAKKDGA FYEALCAFVQ EPHDDELHEK MKRWLASLSE WRTAARQKPL ADLIWQLYRE
TNFYDYVGGM PGGKQRQANL RALYDRAKQY EQTSFRGIFR FLRFIERLKE REDDFGAARS
LTEQEDVVRM MTIHKSKGLE FPVVFLAGAA KSFNMQDLRS DYVLDKDFGL GMRFVHPTWR
ASYPTVAQLA IKKKMKWQLL AEEMRILYVA LTRAKEKLYI VCTAKDMEAK KKKWQEVAYT
STWELPAYVI EKAKSYADWI GYALARHQQG ICSSATVLHD PSLWDIHIVP AHELEQEDAQ
ANEHRDIVEA IQQLQPVAIK SEYEEEVNRR LFWTYTHAPA TVLRAKQSVS ELKRQRDIYG
GHAEQPFRKE LVERPRFLQA KMMTPAERGT MMHLVMQHVD VTKEVTVDAV REQIARMVNG
EWLTEEQATV IDVESIVAFF NTPIGKRMQR ATRLEREVPF YLAHEMEGET VVVQGVIDCV
FEDEHGLVLI DYKTDRVSWM NDPKQQLKRR YKGQLALYRE AIEAIWKREV TETYVYAFDG
ALLVPMEVD
