ID A0A373NMT2_9FIRM Unreviewed; 1278 AA.
AC A0A373NMT2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ECO:0000313|EMBL:RGF76132.1};
GN ORFNames=DWZ38_04935 {ECO:0000313|EMBL:RGF76132.1};
OS Ruminococcus sp. AF31-8BH.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=2293174 {ECO:0000313|EMBL:RGF76132.1, ECO:0000313|Proteomes:UP000262205};
RN [1] {ECO:0000313|EMBL:RGF76132.1, ECO:0000313|Proteomes:UP000262205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF31-8BH {ECO:0000313|EMBL:RGF76132.1,
RC ECO:0000313|Proteomes:UP000262205};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:RGF76132.1}.
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DR EMBL; QTVN01000003; RGF76132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A373NMT2; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000262205; 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; 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:UP000262205}.
FT DOMAIN 3..514
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 543..841
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 1278 AA; 146472 MW; 79B3C6562ED4C8D4 CRC64;
MAVKWTKEQE QVIGLRNRNI LVSAAAGSGK TAVLVQRILG KVMDPEHPVD IDRLLIMTFT
RAAAGEMRER IANALEDALG ENPENEHLQR QTTLIHTAQI TTIDGFCAYV IRNYFHLIGL
DPGYRTGEEG ELKLLQEDVM KELLEAYYAK DQEKYKYFIE CYAAGKSDEG IRDLIYSLYH
AAMSNPYPDE WLEKCIDSYK NTDIESIKAS EWMKLLWKNV LADLEQAKGL AEEARKLCFS
PGGPYLYDDA ISSDLLLIRD AQEKALTGDF DGTRAVLGSP AFARLSTKKP KEPVDDLLKE
QVKALRENEK DILKDLGSRY FTVGEEELPL LLECCREPVE MLVELTREFI RLYGEKKREK
NILDFTDMEH FALEILMERV EDEGANEQAF EMTFGNQENS HITKSEKKTS GYEDKKREVV
YRIMSQAARE LSMKYDEVMV DEYQDSNLVQ EMITTCVSGW AKKSKNIFMV GDVKQSIYRF
RLARPELFME KYKKYTLTDS EEQRIDLHKN FRSRSQVLSC ANFIFRQIMG EDLGGIAYDE
AAALYPGAVF PEGARDEFLS TEVLLVEKDS EELEDLMEGQ DARELEALTI SHRIQEMVGK
EKILDKETGE YRPVRYGDIV ILLRTASGWS ETFTDVLSAH GIPVYAASKT GYFSALEVVT
VLNYLQVCDN PLQDIPLAGV LRSPLAGCTT QELAVIREED PEGMLYESVL HFLGEEEQCS
LISPKEREAL QEKLHGFITL LNEMRDLAVY TPVHELILEI LRRTGYGNYA KALPNGAQRS
ANLAMLVEKA MDYEKTSYRG LFNFVRYIEH LQKYEVDYGE VNLSGAGEGS VEIMTIHKSK
GLEFPVVILA GMGKQFNFQD LNAKLLIHPD YGLGADAILP DRRMVVSTLN KQVIRRQLLE
ESLGEEIRVL YVALTRAKEK MILTGAVSNL DKELISLSHF RENQTELLPA ETRLKGKNYL
DYVLPALARH RCMDSLYEEI GLFPTKENPL YEDPAQFQVK RITAQMLTEA EVVDQATGQM
EENLLEDWDS EKVMDPGIRE ELDKRFGFVY PYEYRRDIPV KVTVSDLKKK SYHEDEEIEE
AVYFEPDIVP LVPRFIEEKT EAEEEFAGAA RGTAYHRVME CLEYGKTDTS QNLKEQIEEL
VQNQKLSEVE AKCVRVSDIR GFVECDLGQR MKAAALKGRL FREQPFVISR SAAEIDESWD
ESERVLVQGI IDAYFLEDEE IVLVDYKTDY VRRGEEKKLI ERYHTQLEDY GQALERMTGR
RVKEKYIYSF ALKKAILL
//
