ID A0A1I7IB66_9FIRM Unreviewed; 1228 AA.
AC A0A1I7IB66;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05216540_106100 {ECO:0000313|EMBL:SFU70179.1};
OS Butyrivibrio sp. M55.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1855323 {ECO:0000313|EMBL:SFU70179.1, ECO:0000313|Proteomes:UP000199511};
RN [1] {ECO:0000313|EMBL:SFU70179.1, ECO:0000313|Proteomes:UP000199511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M55 {ECO:0000313|EMBL:SFU70179.1,
RC ECO:0000313|Proteomes:UP000199511};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FPCD01000006; SFU70179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7IB66; -.
DR Proteomes; UP000199511; 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; 3.90.320.10; -; 1.
DR Gene3D; 6.10.250.2380; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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};
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:UP000199511}.
FT DOMAIN 3..471
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 472..781
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1228 AA; 138692 MW; A36D11D080ECCB4D CRC64;
MKVEFTDEQK AVINARKCNV LVSAAAGSGK TAVLVERIIQ MINEGVDIDH LLVVTFTKAA
ASQMKEKITL AIQDKLLEDP ENTHLQKQET LIHNAQITTI DSFCQYIIKN NFNFVGLDPS
YSVGDEGELR LLQEDVMKNM LEEEYTKAKE GSNEDFIYCM EYFGTGSNDK AVEEYIERLY
RFSMSMPWPE AYIKERALDY DIEGKNFDEL EWVKECVTSV KRMLLEAQDK LSAAHELTLL
PDGPYMYGEL LEKEAEMMGR AAAYESYDEL YDAVRGISFD RLPAKKDESV SPEKKERAKE
LRDSVKKDIK KITENYLVLT SDMVAEQMKL CDRAVKELCR LTLRYIQLFD EKKREERLID
FSDMEHFALN ILIDYETGEP THVALEYREF FKEVLIDEYQ DSNSVQELIL QAISGVKAGS
SERFMVGDVK QSIYKFRLAR PEIFMEKLAT YSKDASASDR RIDLHKNFRS REEVLEGTNY
IFRKIMGKDL GSVEYDKDAE LVTGAGYDEP SFDMTPELIL IDDPEGKKEN EAHAIGNKIL
ELMREDPELK FKDIVILLRT NSGWDDVFKK ALEEQGIPSY IESKSGYFDA WEVSVMLNIL
SVIDNPTVDI PLVAVMHSPI GGFTDEELAL VKITLNKNEE TLGASSLYGG ILKLVRGDGT
NKALIQNQAL SDKLEKFVSL IEDLRDISTY TPVHELLQYI IDVTGFELIV SAMPAGNQRR
ANIELLLSKA ESFEKTSFKG LFHFVRYIEH IKVVQVDYGE AGIIDENADV VRIMSIHKSK
GLEFPVVFVA GMSKQFNKTD TKGNLIADMD LGIGVKCIDS KLRLRSETLK RVIIADKMNT
DSLGEELRVL YVALTRAKEK LIMTASVKKL PDVLAKELKR QPELAHGVSQ GKELMPFSIR
LSASCYLDLV LPSLVRHPAI RSLAEKYELS ELITDKFMDS EESVPKFAIS SVSVDEINAR
NEKESVKGLI RMDGIGAYYD KELAKKLEDK MDARYGFEHL KGLYTKTTVT ELKKHILEET
GEHFTKEEDY GAEYDDGRGA VNESGGRSDG LAGAERGTAY HRVMELLDYS VGSGMDALGV
WLDGLVQNDR ITKAYADSVE LKDISAFLGT GLGQRMATAF KAGVLMREKP FMMGVSASEL
DKKFPSDEIV LIQGIIDAWF IEDDEIVLVD YKTDHTRDSA ELVKRYKIQL DLYKRALEAS
TGKKVKSTFI YSFALGKEVD LGDGVSGP
//
