ID A0A0V8QEL9_9FIRM Unreviewed; 1191 AA.
AC A0A0V8QEL9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=ATP-dependent helicase/nuclease subunit A {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=3.1.-.- {ECO:0000256|HAMAP-Rule:MF_01451};
DE EC=5.6.2.4 {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=ATP-dependent helicase/nuclease AddA {ECO:0000256|HAMAP-Rule:MF_01451};
DE AltName: Full=DNA 3'-5' helicase AddA {ECO:0000256|HAMAP-Rule:MF_01451};
GN Name=addA {ECO:0000256|HAMAP-Rule:MF_01451};
GN ORFNames=ASU35_10645 {ECO:0000313|EMBL:KSV59008.1};
OS Acetivibrio ethanolgignens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetivibrio.
OX NCBI_TaxID=290052 {ECO:0000313|EMBL:KSV59008.1, ECO:0000313|Proteomes:UP000054874};
RN [1] {ECO:0000313|EMBL:KSV59008.1, ECO:0000313|Proteomes:UP000054874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACET-33324 {ECO:0000313|EMBL:KSV59008.1,
RC ECO:0000313|Proteomes:UP000054874};
RA Zou Y., Xue W., Luo G., Lv M.;
RT "Butyribacter intestini gen. nov., sp. nov., a butyric acid-producing
RT bacterium of the family Lachnospiraceae isolated from the human faeces.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618, ECO:0000256|HAMAP-
CC Rule:MF_01451};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01451};
CC -!- SUBUNIT: Heterodimer of AddA and AddB/RexB. {ECO:0000256|HAMAP-
CC Rule:MF_01451}.
CC -!- SIMILARITY: Belongs to the helicase family. AddA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01451}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KSV59008.1}.
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DR EMBL; LNAM01000154; KSV59008.1; -; Genomic_DNA.
DR RefSeq; WP_058352792.1; NZ_LNAM01000154.1.
DR AlphaFoldDB; A0A0V8QEL9; -.
DR STRING; 290052.ASU35_10645; -.
DR Proteomes; UP000054874; Unassembled WGS sequence.
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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.274.50; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR HAMAP; MF_01451; AddA; 1.
DR InterPro; IPR014152; AddA.
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 NCBIfam; TIGR02785; addA_Gpos; 1.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01451};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01451};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01451};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_01451};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01451};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01451}; Reference proteome {ECO:0000313|Proteomes:UP000054874}.
FT DOMAIN 4..481
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 501..776
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 981..1051
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1191 AA; 136654 MW; 13C709DDCA3436C6 CRC64;
MGKVKFTEDQ QKVIDLRNCN VLVSAAAGSG KTAVLVERIL EKISSREHPV DIDHLLIVTF
TDAAAGEMRE RISRAIEERL LLEPDNVHLE RQAALVHNAR ITTIHSFCLG VIRDYFNEID
LDPGFRLGDE TELLLLKGEA MEAVVEAFYA EKSPGYLSFV ESYAAGKRDE SIEKLVYRLY
DFAMSYPWPK LWIEGQRKNF SVEKEEDFFE ADWQKELVGF LKTEIRDCLE VNKTALELAG
MSDGPYMYEA ALLSDAEQLE RLCKAEDYPS IGHFLERISW AKLSAKKDDC VDTEKREAVK
LLRDSVKKAI NGLKEKYYFQ PMEEMIADIK KAAPAMNAFL DLTLAFMEAY QEKKEEKNLL
DFNDMEHYAL KILTKEPEKL ENKATGGALI LPTQTAVELS HYYEEILIDE YQDSNLVQET
LLNSISQEKF GRPNVFMVGD VKQSIYKFRL ARPELFMEKF NTYQEKGDYV RVDLKKNFRS
RESVLEAINY IFFGIMKRDL GNIDYDAAAA LYPGRPALEE TEEEAGLWKD CEILIAQSSE
EVTDKELEGK ILARQMKKLH EEQNIPYKDM VVLLRSMKGW SEELVNVLKE EGIPARAATQ
TGYFSAVEVM TMLNLLLIID NPRQDIPLAA VLRSNIGGFS DEELAALRCI DKEGELYDCL
SAAEGQKKVQ DFLTLLNRLR KLVPIVGIYE LLTIIYEETG YYNYVKALPG GKARCANLDM
LLQKGADFEK TSYGGLFQFN RYIERLHQYE VDFGEAFVLG ENQDTVSIMS IHKSKGLEFP
VVFLAAMGKG FNKQDTRERI LMHPDLGLGP DYIDSELRTK SPTLLKQVMK RKTDLENMGE
ELRVLYVAMT RAREKLILTG CVKDVEKAQL KWQQAEPLLF SQRAGAGNYL DLIMPRVFTW
QEEPVDKLSY RVEYITEEEL SFEAVAARIS GEQRRAELLS LEQRELWSEE EQIEAERYIS
FQYPYTVEEK IKSKLTVSEL KQQAMQRQEE EGQLLEELVE KEAYIPSFIQ AREEKSGSLR
GTVYHRVMEN LSFLQAEKNG LETELAALVE AGRISREELS LISTKKLSWF LSSKLGQRMK
KAEAEGKLYR EQPFVIGLPA SKLQPELKSE ETVLVQGVID SFFEEKGQLI LMDYKTDRVA
SGDELIKRYK SQLEYYKAAL EQLTGKKVAE CYIYSFYLGE TIAPHDKRMN E
//
