ID R7M9R1_9CLOT Unreviewed; 1227 AA.
AC R7M9R1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=BN712_01026 {ECO:0000313|EMBL:CDE97111.1};
OS Clostridium sp. CAG:567.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262820 {ECO:0000313|EMBL:CDE97111.1, ECO:0000313|Proteomes:UP000018055};
RN [1] {ECO:0000313|EMBL:CDE97111.1, ECO:0000313|Proteomes:UP000018055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:567 {ECO:0000313|Proteomes:UP000018055};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE97111.1}.
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DR EMBL; CBJZ010000060; CDE97111.1; -; Genomic_DNA.
DR AlphaFoldDB; R7M9R1; -.
DR STRING; 1262820.BN712_01026; -.
DR Proteomes; UP000018055; 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}.
FT DOMAIN 4..465
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 508..793
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1227 AA; 143396 MW; 88DB9FD66ED61B9A CRC64;
MAEVKWTNEQ LQAIQEKNSN ILVAAAAGSG KTAVLVERII HKIIDEQMDI DKILVVTFTN
AAASEMRERI LEAIYKKLEE NPENVHLQRQ IILLNKASIC TIHSFCLDVI HNHFYEIDLP
SNFKIADTAE IDLLKQEVLD DLFEQKYTEN DKNFIELLEN YTNYRGDEAL QELVLKIYKF
IQSSPFPIKW LQEKLELLKI EDKDISQTIW GKLIIQTVDD DIQESIMQLE VTKSKMALYP
EMTKFYQTIS EDIINLQDLQ KYNSWDELYI KLLNFNFSKW PVDKKVINDL KEDSKEIRDK
VKKHIKEKTA KLLSCSQEQA VKDLKIITPI LEKLSNLVTE FTKNFAEKKK EKNCIDFNDI
EHFALKILLD ENNNPTEVAK KYKEKFEEIA IDEYQDSNLV QEAILTSISK GNNIFMVGDV
KQSIYKFRQA RPELFLQKYD EYKNKEEKAQ EDNLKIQLFR NFRSRQNILN ITNLVFESIM
SKELGDINYN ENEYLNYGAN YPEPEEIKNY AGIAELDIID LKEDESITAF EGEEDEEEQE
RVEDDVLEAK FVANKIQELL NSNYMVFDKK QGYRKIRPKD IVILLRATSN LSPIYEKELS
DLELPVFSDT SGTYLDTVEI QTILSVLKII DNPLQDIPLV VVLRSSICNF TDNDLITIRL
TDRNCNFYEA LIKTRLICDG DLKNKIESFL EKLEKWKSIS QYMPLDEFIW QIYLDTGYYQ
YVGLLPNGAM RQANLKTLFE KAKQYEKASF KGLFNFIQFI DKLKKQNGDL ASAKLIGENE
DVIRIMSIHK SKGLEFPVVF LCNSHKKFNM QDLNDNILLH QDIGFGPTIM DTTRKIKYSS
IAKDAIKLKM KQETLSEEQR ILYVALTRAK EKLYITGRSK DFTKYVQDKN KVLEMYESEN
IKLDAKLMKK ANSYLDWLMY VYLFNQGRTI TLKGESYKLS DIITLNVSNK KDLLKALAKE
EVVEQIDLKE KIEQILKNKS DEENKKSEQA LKELLEWKYD YIVDTTLPTK SSVTKIKQEK
IKLEEILKGI ESEEVEYKKS YTPKFMQEDK KISSAEKGTL VHLCIQRLDE RKDYELKDIQ
NMILNLVEKE IITQNEADAI DVNLIYQYTK SQLFEELRKA KEVHKEQPFY INIPAKDVVS
EAENSKKNIL VQGIIDLYYI DKNDNLVLID FKTDYISNEP NAKEKILDKY KVQLEIYKTA
LEQALNRKTS KTALCLVKSE YEEVVLE
//
