ID A0A1Y4L6E5_9FIRM Unreviewed; 1198 AA.
AC A0A1Y4L6E5;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=B5F18_07160 {ECO:0000313|EMBL:OUP49572.1};
OS Lachnoclostridium sp. An181.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965575 {ECO:0000313|EMBL:OUP49572.1, ECO:0000313|Proteomes:UP000242090};
RN [1] {ECO:0000313|Proteomes:UP000242090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An181 {ECO:0000313|Proteomes:UP000242090};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUP49572.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NFKJ01000009; OUP49572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4L6E5; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000242090; 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};
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:UP000242090}.
FT DOMAIN 3..472
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 503..789
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 1198 AA; 138913 MW; 23AB94EB3D9F9D53 CRC64;
MSVAFTKEQQ KVIDMRGCNI LVSAAAGSGK TAVLVERIIK RLTKDVPPLN VDELLVVTYT
EAAAAEMKER LRDALEKALE ENPGNVHLLK QATLVHNAKI TTIHSFCLSV IREHFHEIDL
DPGFRIAEEG ELKLLKQDVL DNVLENAYEE ADEGFLDFTE SYASGRDDKK LEELILKVYE
FSRSFPSPAQ WMSECREQYH AENLAGLEEK EFIKTIVKNT HSYMESLKQV LENAKDICRM
ELGPKNYEEN VHLAWENVDS LCREKTFCGM YEKMKSLNWG RLKPNKGIEV EKELEDTVKD
LKKQAKDTVD DIVKQYFYEE PEEMRKDLCH TEKMARVLFE LVSRFSEEFQ QEKASKNLID
FGDMEHMAMQ ILTVSKDGKR YPSRTAKEYQ KQFKEIMIDE YQDSNFIQET ILQSVSGVEN
GIYNIFMVGD VKQSIYRFRL SRPELFIEKF ETYSQTGGEK VRIDLHKNFR SREEVLASVN
YFFEKIMDKD LGDVAYDEKA ALYPGADFGG DEQGPAKEDR KTEMYLIDTK EENGKGLDAK
EWEARVIAAK IKKLLCSHTV LDKTSKRQRP VRFGDIVILV RSPKSCGETF AKTFADEGIP
VYTGSREGYF QTQEISVLLD YLKILDNRRQ DIPLAGVMLS VIGGFTSEEL AKMRAEFPGM
KFHEAMIGYP KEGEDECLRE KIQSFWAGVE KFRERIPYTA IHELLFQIMD ETGYEDYMDA
FPDGAKRSAN IRMLVEKARA FEKTSYKGVF HFVRYIEKLN KYEVDYGEAS VTDEVSDVVR
IMSIHKSKGL EFPIVFVAGM SGKFNTQDYK NSICVHPKFG IGMDCVDLER RTKAPTILKR
MMQRELKLEN AGEELRLLYV AMTRAKEKLI LVGSAADAEQ KVEKYAVWKG NGKIKMPFHL
RASADSYYGF LIPALEGERE LPDVKVKIVD PLELYEEKQL EIRETGWKKD NYENLPVEKP
FDREMEKNIN EQFAFSYPYE NEQKRKQKFS VSELKRPEFE DEYSENMYGK KEDETYVPSF
MREEKSGGAF RGTAFHKMLE LWDFTKEGTK TSIQRQMKQW RESGYMDGDM LKLLDVEKLE
KFLYTSLAKR MTDAQKNGSL YREQPFVMGV EPEEIYEGEK DGDLILVQGI IDAWFEEPDG
VVLVDYKTDR VSSTEELKRR YEKQLYYYAE ALERMTGKRV KENLIYSFAL GQLIEVKE
//
