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Database: UniProt
Entry: E2ZBG2_9FIRM
LinkDB: E2ZBG2_9FIRM
Original site: E2ZBG2_9FIRM 
ID   E2ZBG2_9FIRM            Unreviewed;      1220 AA.
AC   E2ZBG2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   Name=addA {ECO:0000313|EMBL:EFQ04359.1};
GN   ORFNames=HMPREF9429_00789 {ECO:0000313|EMBL:EFQ04359.1};
OS   Megasphaera micronuciformis F0359.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=706434 {ECO:0000313|EMBL:EFQ04359.1, ECO:0000313|Proteomes:UP000003195};
RN   [1] {ECO:0000313|EMBL:EFQ04359.1, ECO:0000313|Proteomes:UP000003195}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0359 {ECO:0000313|EMBL:EFQ04359.1,
RC   ECO:0000313|Proteomes:UP000003195};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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};
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:EFQ04359.1}.
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DR   EMBL; AECS01000035; EFQ04359.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2ZBG2; -.
DR   STRING; 706434.HMPREF9429_00789; -.
DR   eggNOG; COG1074; Bacteria.
DR   HOGENOM; CLU_001114_3_1_9; -.
DR   Proteomes; UP000003195; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000003195}.
FT   DOMAIN          5..481
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          517..795
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1220 AA;  138858 MW;  1909BF3D98A130B2 CRC64;
     MVDKMAWTEA QEKAITSRNQ NLLLSAAAGS GKTAVLVERI IRRLIDVDNP TDITEIMVVT
     FTKAAAGEMR ERIGGALLKA AEDETLSAAV RESARRQAAL LPSARISTFH AFCQYVLRTR
     FYTIDLDPQF TIAGTEELEL LKQSVWDDVA LSYYEDEEKV RTMTALTDVF GNDRGDAGLT
     EIVMKAYEYI RSQPWPLQWL EEATAAYEKV DSSTDLGSLP WASPILANIR SALSRCADEY
     DESLKILEYV EELNGQYERF KEERNRFKAA SEIKSWSRME DFFSDFDFGR LKSMRNLVAD
     VADAWNDCKA HRDKAKDTVK KIRDTYFTKT SKQWVDDLIQ AGHTMSALSG LIRDFYKAYN
     AAKREKNWLD FGDLEHYCLQ ILTVHDEQTG EVLPSAAAKE MRSTFKEILI DEYQDTNGVQ
     ELITTLVSDG TNRFMVGDIK QSIYRFRLAD PTLFLEKYMT FERRAEAVNR CIVLSMTFRS
     APAVIEAVND IFSYAMTEAA TGMDYGDNEK LYVGRTDDEP GVAELHILDE VTTYESLETD
     GGEESDDDDD SAEESSFIRQ CRFVAARIGE LKAADPSLKY KDIVVLLRSV SRKAEDLLTV
     LQDAGIPAYA EQKGGYFNVT EVRLMTALLA CIDNPCRDIE LAAVLRSPIV GINEATLAEI
     RMYRDGYLVD ALEAYTAGLH DGVYKERLSE FLFRLDAWRT YSRRAGVAEL LRRIYEKTSY
     IDYVAAMKNG DLRRANLEAL YERAGQYERA GFRGLFRFLK FIERMKKKGL DLAPARVVGE
     EEDVVRIMTI HKSKGLEFPV VFLVNTEKTF NKQDEQEPVL YHKELGIGIR AFDAKWRMTW
     PTLAYNGIKE RTVWENRAEE ERLLYVAMTR AKNRLILVGT VKSRGSKNTD CLYDRLARFR
     NDVHAEAGTS YLDWILPPLL RKLPDVTDLT ASDENSEFVH AGVWQVTVHT EPVDAGKAMA
     DVLRPEEAHL EAVRADMPTG TAIPAWLDEA LSFTYPFEAA THTVAKLSVS EIKRRLAEAT
     EEEDLLQEGE HLFSTGVEDD ETDLTRPPWL CEKASQSPTF AGTVFHKAVQ LLDFADLTKE
     NIVEQVEGWK NSGRFTSEEL SRLRMNDLYH FAESHLAARI QASPDVRREY GFTFLADSDK
     VSRVEGERIL VQGVVDCLFV EGDEWIIVDY KTDRLNTADE FKKRYAVQLN LYKLAVEQIS
     QRKVKEMIIY SSRLGKEIFI
//
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