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Database: UniProt
Entry: E1MBX8_9ACTO
LinkDB: E1MBX8_9ACTO
Original site: E1MBX8_9ACTO 
ID   E1MBX8_9ACTO            Unreviewed;      1213 AA.
AC   E1MBX8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=HMPREF9278_0019 {ECO:0000313|EMBL:EFN94019.1};
OS   Mobiluncus mulieris FB024-16.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=866770 {ECO:0000313|EMBL:EFN94019.1, ECO:0000313|Proteomes:UP000004387};
RN   [1] {ECO:0000313|EMBL:EFN94019.1, ECO:0000313|Proteomes:UP000004387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB024-16 {ECO:0000313|EMBL:EFN94019.1,
RC   ECO:0000313|Proteomes:UP000004387};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
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   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000256|ARBA:ARBA00009922}.
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:EFN94019.1}.
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DR   EMBL; AEGV01000008; EFN94019.1; -; Genomic_DNA.
DR   RefSeq; WP_004017456.1; NZ_AEGV01000008.1.
DR   AlphaFoldDB; E1MBX8; -.
DR   Proteomes; UP000004387; 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:InterPro.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR   CDD; cd17932; DEXQc_UvrD; 1.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038726; PDDEXK_AddAB-type.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070:SF55; DNA HELICASE; 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   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|PROSITE-
KW   ProRule:PRU00560};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00560};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00560}.
FT   DOMAIN          21..437
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          438..743
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   1213 AA;  136191 MW;  0C3617F15F035703 CRC64;
     MRKTSIEILN PEHLALLTKA FPPTEEQEQV IKAPLEPLLV VAGAGSGKTE TIANRLVYWV
     VNGAISPQSV LGLTFTKKAT AEMGQRFALR LDNLAQNLEK FVASPSRFEV EMCRQLKGDW
     QWRDDSKIHG FIRSLTAGLH ALRESGMTSR ILRSGVEVST YDALASKVLT EFGVLAGRDS
     GYQTITDGTR FQIMSQILET WVSNLSYREE EGASVGNFIE GLLHLAGDVN AHVVDLNTMK
     KLYADFLATA QRELLASQKL DEALEPLKAA KKAAKAANDK QREKALGAEI TNLDLPLTSQ
     AKKDLERTVE VMRFGVDAVE VIRAFNTRKA QLRFADFSDQ TREVVELLKK VANISQSYQQ
     RYQLVLLDEF QDTSVAQLKY LSALFRNHAV TAVGDPNQAI YAWRGASAAS IEEFPKYFSD
     NPSKVASLTL RTSWRNDAAI LNVANCIASE IAEQNRTEGK NENFIMPDLS LRPGASPDLG
     RVYGAPFLTD TDEAQAVANF LENWRKDLEQ AVEKTAAWQA AGRVGQPPSL PTAAVLCRKK
     SIMLPILREL SRRGIPFQLQ ARESALLDPG VVLVRAALNV VVNPQNSGSL LLLLNRFRLS
     REDLEAISKA AGRTVLPFQE VMKSQIGASV SQPGRERLAI LREIIAKLEK HVSYATPLQM
     AKLAAKLLGL DIEQRIPGTP YQEEAFTIFL SIIEDFERSG QATLRAFLEW LDVAESEEKE
     VGQFQEAVDT KKVQVITVHA AKGLEWDYVA VPGLSEGNFP DNRTEIWLKN YFVLPYPLRG
     DRDSLPQYEI NLRQLGEKDR SRKFLEQYDG VRTLHHLKEE ANLAYVAFTR AKSHLFLSMS
     WFKGCNVNTA KPGAFFRVLL GEDAKLFCME KPNKGMTLVN SQEFMHLPDW LGDINPCFTE
     PEEANPNVQE FEAGLWQAPS WLDLPPESIR PETFPWDVAG LQRSYQMVTV AAENPPDSQA
     LESAIPGSLS WRVWKLYNAP RPRLDSSMLL RQIAATSVVK LDESSDDFML QKLRPLPLPP
     SPAARLGIIM HAWIAQQLGQ PTLDIPDGSE ATLDADSRLK LDCYRQTWEN LQFLKGKAVM
     DIEHSGSLVV GEGTEGFEVP LRIDAVFQER SCGTTWIVDW KTASHPNPPQ YERYLHQLGI
     YRLYWLQTHP ELDSQDIQCA YVYLKEGETE HQVLTLESIL EHLKMPDYTP EYLYKLLKRG
     ETEATEFLSQ KNL
//
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