ID A0A1I1AXA4_9CLOT Unreviewed; 1251 AA.
AC A0A1I1AXA4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN04488528_10525 {ECO:0000313|EMBL:SFB42729.1};
OS Clostridium frigidicarnis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84698 {ECO:0000313|EMBL:SFB42729.1, ECO:0000313|Proteomes:UP000198619};
RN [1] {ECO:0000313|EMBL:SFB42729.1, ECO:0000313|Proteomes:UP000198619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12271 {ECO:0000313|EMBL:SFB42729.1,
RC ECO:0000313|Proteomes:UP000198619};
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; FOKI01000052; SFB42729.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1AXA4; -.
DR STRING; 84698.SAMN04488528_10525; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000198619; 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; 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};
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:UP000198619}.
FT DOMAIN 3..470
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 506..813
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 1251 AA; 145776 MW; 61F0D8737D48F5D6 CRC64;
MKTKWTEEQE SAIITRGCNL LVAAAAGSGK TAVLVERIIR MIIDEKDPVD IDKLLVVTFT
NAAASEMRER VGNAISKKLD ENPGSMKLQR QLTLLNRSNI TTMHSFCLDV VKNNFHYIDL
DPNFRIADQT EIILMKQDIL QDMFDEMYEE NSEDFIRLVD TLGGKRDDRN VQELVENIYN
FSMSGPSPKT WLRAKVEQLN LDNDVDLGSS MWVKILLNGT EEKLKSFIDD MENLKEICKE
GNLNKAEENI AETLSDLYML KDYYNKSLDD FIKTLKDVRF SRLTIKGVHE DTKKEITDTR
KSVKDSLAKF QKSINFTMEE SKDAIKYMYP IMKTLSELII NFMDRFENKK REKGILDFND
LEHLCLRILN EGYSTGELIP SEVAIQLREK FDEVLVDEYQ DSNNVQETII NLVSRKLTDK
PNVFMVGDVK QSIYRFRQAK PELFLEKYNT YLKDQGKDRK ILLYKNFRSR EEVINSVNYI
FKKVMSKAVG ELEYTDEEAL NLGAVYPKNE EENTIIGGPT EFHIIDMSSD KEDESSSEDE
IKLDEELDKV QIEARLVAKR IKELLNGKQK FKVFDKNLND YRDIKYKDIV VLLRATQNWA
DVFTEELASV DIPAYADASK GYFETIEVKT MISLLQIADN PLQDIPMISI LRSPIFSFTP
EELIDIRLFN KDKYFYEILE YIANEDMSKC KYESEYLLEE TTKNKAVLVV NSIKTWRSKA
LHMPIDEFVW YLYMDTHYYG YVGAMPNGIQ RQANLRVLFQ RAKQYEKTSF KGLFNFITFI
NKLKKSSGDM GSAKILGENE NVVRIMSIHK SKGLEFPVVF LSGCGKQFND LDLKGQILYH
EELGFGPDYI NSEENYKFPT IAKEAIKKKI KIENLSEEMR VLYVAFTRAR EKLIITGTTK
DLEKDCEKWS KTIGNNKVIP SSEVLSSNRY LDWIGLALIN HNDGNILREL TSKDNYNIDE
NLSTFHIVKY DKSYVFVDKN NNNVEKILKE DKFISLDESM ERLAYKNEIN RRLNWEYEFK
ESSKIPSNIS VSELKRTMFD DDEYNRTKSI NDNNLDIIIK KPVFLQEKKG LSSAERGTAV
HGVMQHIDIL KCNTIKEIQS QLAFMVAKEF LTSEEISSVS PFKIQKFFEC SIGKKIVEEY
KKNPKNVNRE TPFYIEISSK ILNKNLPSQY EKEKTRVQGV IDCFIEENDG IILIDYKTDY
IDIKDKDWEK AIEKRYKVQI DYYTEAIERI TGKKVKERYL YLFYLEKQLK I
//
