ID S2LJX0_9FIRM Unreviewed; 1210 AA.
AC S2LJX0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=HMPREF0994_07087 {ECO:0000313|EMBL:EPC05238.1};
OS Lachnospiraceae bacterium 3_1_57FAA_CT1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658086 {ECO:0000313|EMBL:EPC05238.1, ECO:0000313|Proteomes:UP000003336};
RN [1] {ECO:0000313|Proteomes:UP000003336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|Proteomes:UP000003336};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 2_1_58FAA.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EPC05238.1, ECO:0000313|Proteomes:UP000003336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_57FAA_CT1 {ECO:0000313|EMBL:EPC05238.1,
RC ECO:0000313|Proteomes:UP000003336};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M.,
RA Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-1-57FAA CT1.";
RL Submitted (APR-2013) 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:EPC05238.1}.
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DR EMBL; ACTP02000004; EPC05238.1; -; Genomic_DNA.
DR AlphaFoldDB; S2LJX0; -.
DR STRING; 658086.HMPREF0994_07087; -.
DR eggNOG; COG1074; Bacteria.
DR HOGENOM; CLU_001114_3_1_9; -.
DR Proteomes; UP000003336; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000003336}.
FT DOMAIN 3..471
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 485..786
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT COILED 940..975
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 24..31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1210 AA; 137896 MW; 4A9E0A265D362B84 CRC64;
MAVTFTPDQQ ATIDARGSSI LVSAAAGSGK TAVLVERIIQ MVSDGEHPVD IDRLLVVTFT
NAAAAQMRER ITQALSARVD DNPGNAHLLK QLTLIHNAQI TTIDSFCLYI IRNHFDEIDL
DPDFRVADDG EIKLLMQDVL AQMLEDYFTE GREDFLACVE YFAPTGKEKR LEEQILGLYE
FAMSYPWPGE WLELHKEDYA VSLEKLEECR WVGLLEDYIR TMLAEAGDSL DQARMLCEET
DGPYMYQDTL EADKNTIDRL AAADSLQDLY ERFSVLSFGR ISSKKDDSVS PEKREKAREI
RNSVKDLLNG LAKKYFYASP QAQAERMAAC APYVSCLLSL TDDFRMRLDA KKREKNLMDF
HDMEHMALQI LTEKREDGVY PTAAAREMRE YYAEIMIDEY QDSNLVQEYL LKSISGEEDG
KFNRFMVGDV KQSIYKFRLA RPELFMEKFD SYGKGEGKER RIDLKQNFRS RRQVTDSVNA
CFSVLMGRDL GGVEYDEDAA LYPGAVFPEP EGEEEDVYRT EVLLTMSEED GLEDREREAL
AIAGKIRRIV GTLPVVDKES GELRPAGYGD IVILLRTTAG WDEVFKKVLE KSGIPVYITS
KTGYFAATEV QTILNFLKVL SNPLQDIPLF GVLKSDAAGF TDEDIACMKA EMEGEGRTLF
TCLTSYTEKG SREALCEKAR HFCSMLERFR RYVAYMPIHQ LIEQFLKETG YLYTISALPG
GEQRRANVEM LLSRAENFEK TSYFGLFHFI RYMEQVEKYN IDYGEANIQD ENADTVRIMS
IHKSKGLEFP VCFVAGLSKK FNMQDTSKPV IMDMDYGIAL DFVDIESRVK GNTLKKSVLS
GKLRRDSLGE ELRVLYVAMT RPQEKLILTG SCKEEEKVRR ILENGEDYER AGGRLGFIPR
SEAASYLDWL LPAWAVCGQE VTLLSGSDLL QENMEEEQGR EYLRQRLRIF EREASEEKQE
EIEKLRLLRE RMESIYPHEN LKNLYTKTTV SELKKAGMEE AAEEAYHLFE EKEIVPYLPR
FVREEEAVSG TARGSAYHKA LEIFPFERLA QEKGASPAAR EKVEELLNQM TETGALSREF
RAAVNTDKIA RFLESDLAAR MAGAAVKKKL HKEQPFVLGL PASMLNPGFP QEETVLIQGI
IDVYLEEEDG LVVADYKTDS VTHAQELVNR YQVQLDYYAL ALEQLTGRRV KEKIIYSFAL
AEEVVLGDKS
//
