ID A0A1U7NPU1_9FIRM Unreviewed; 1046 AA.
AC A0A1U7NPU1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=BO225_02090 {ECO:0000313|EMBL:OLU47655.1};
OS Dubosiella newyorkensis.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Dubosiella.
OX NCBI_TaxID=1862672 {ECO:0000313|EMBL:OLU47655.1, ECO:0000313|Proteomes:UP000186705};
RN [1] {ECO:0000313|EMBL:OLU47655.1, ECO:0000313|Proteomes:UP000186705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NYU-BL-A4 {ECO:0000313|EMBL:OLU47655.1,
RC ECO:0000313|Proteomes:UP000186705};
RA Cox L.M., Sohn J., Tyrrell K.L., Citron D.M., Lawson P.A., Patel N.B.,
RA Iizumi T., Perez-Perez G.I., Goldstein E.J., Blaser M.J.;
RT "Description of two novel members of the family Erysipelotrichaceae:
RT Ileibacterium lipovorans gen. nov., sp. nov. and Dubosiella newyorkensis,
RT gen. nov., sp. nov.";
RL Submitted (NOV-2016) 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:OLU47655.1}.
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DR EMBL; MPKA01000044; OLU47655.1; -; Genomic_DNA.
DR RefSeq; WP_076340628.1; NZ_MPKA01000044.1.
DR AlphaFoldDB; A0A1U7NPU1; -.
DR STRING; 1862672.BO225_02090; -.
DR GeneID; 78274736; -.
DR OrthoDB; 9810135at2; -.
DR Proteomes; UP000186705; 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 Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF48; ATP-DEPENDENT HELICASE_NUCLEASE SUBUNIT A; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 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|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:UP000186705}.
FT DOMAIN 2..441
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 453..727
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 23..30
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1046 AA; 122218 MW; B3AB292CB6A94FC9 CRC64;
MIHYSSQQQK TIDSRNKNVV VSASAGSGKT SVLVERLCRL VIDDQIPINE ILAMTFTDDA
ANEMKARLKH RLSSLEPTPY ILDQLALLET ADISTIDSFC YKIVQRYYYQ IPIPYAMALH
VDNGSLRSQA FELAYERALI SLEGERIAAM NRYFAAFNVS SETLFKAINR FLEMANAKAD
PKGWIESCKQ EHADVKKWFL TFFQERVETM ISIVQEMLDE LDEMEFSKIK TYESNKELFE
QKALYLKRCQ DDLAQEEYDR FARDFIAYID TTKRFPSTVN KKSFANIKKE FQSMESAITE
NLFDLRQFQA DQERTQPILE TWCDLSILLM DYFQEEKERL QILDFSDMEH FAYRLLCIPT
IQEQVKNQFK TILIDEFQDT NELQESIIQQ IASKNNVFRV GDIKQSIYGF RQADPSIMIH
HMEKEDENNE TLVMSENYRS TKTLIDFNNT FYEKIMNLSF LDSRFLPSDR AMPGTSKQES
SPQYPVRFLF SQYEPWAIEH ENQKREAKKL HRAHRVDLIA NDILKHHQAG VPYRSMCILT
RTHGTHQALK DGLEAYGIPV LAEIDHGFYT NQAVQIILSC LQIIQDPNQD IPLMAALCSP
IGQVDQATLS KIMIENDAPV SLFSKVRNES FMKELNAIFQ WKKEPVATIV RKLYNFHNYY
YLFTNGQDKT NLDLLLERAS QYANPYDLNG FIELILQEAD LDKTAEAFPY GKEEDVVKIK
TMHHSKGLQF PIVYLLSDHE RRDMEASSPI LLDDHLGVSL RSLNDKGNVY RPSLSSIAFK
TKKFHKEIEE EMRILYVATT RAEEELVIVD AIKSLDDYRY PLNTRALLQN QNYTGWLLHT
FLTEPSSLFE LEEVEELYER KIVQRKFMKN IPFQIFDQKV RSVESMTASG SKKQPQWSPV
RMRINDRLKR GTMLHELVAT LPFPYQKDVL ETKLTNQEDI QQILALNANP EYVGWMERKH
IFECPYTVKK GNELIHGFMD LVVFEDKRTI ILDFKSDYVN DEKELVSMYQ KQLMIYKEAM
ELIEPNRTIV TYIYSFYLKK LIQIAC
//
