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Database: UniProt
Entry: D1VTU8_9FIRM
LinkDB: D1VTU8_9FIRM
Original site: D1VTU8_9FIRM 
ID   D1VTU8_9FIRM            Unreviewed;       977 AA.
AC   D1VTU8;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE            EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN   ORFNames=HMPREF0628_0832 {ECO:0000313|EMBL:EFA90061.1};
OS   Peptoniphilus lacrimalis 315-B.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC   Peptoniphilus.
OX   NCBI_TaxID=596330 {ECO:0000313|EMBL:EFA90061.1, ECO:0000313|Proteomes:UP000005711};
RN   [1] {ECO:0000313|EMBL:EFA90061.1, ECO:0000313|Proteomes:UP000005711}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=315-B {ECO:0000313|EMBL:EFA90061.1,
RC   ECO:0000313|Proteomes:UP000005711};
RA   Durkin A.S., Madupu R., Torralba M., Methe B., Sutton G., Strausberg R.L.,
RA   Nelson K.E.;
RT   "Genome Sequence of Peptoniphilus lacrimalis 315-B.";
RL   Submitted (DEC-2009) 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:EFA90061.1}.
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DR   EMBL; ADDO01000043; EFA90061.1; -; Genomic_DNA.
DR   RefSeq; WP_004824921.1; NZ_ADDO01000043.1.
DR   AlphaFoldDB; D1VTU8; -.
DR   eggNOG; COG1074; Bacteria.
DR   Proteomes; UP000005711; 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; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 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   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:UP000005711}.
FT   DOMAIN          1..393
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51198"
FT   DOMAIN          393..637
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51217"
FT   BINDING         22..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ   SEQUENCE   977 AA;  115272 MW;  3CC4704CE54BCE89 CRC64;
     MVLNEIQQKA STILDKNISL ISGAGTGKTG VLTQRFINII KAQNGKFDNI LALTFTDKAT
     EEMNNRIYHE LAKTSYDFNI DKLNIMTIHS FCKDLILSYN RYLHINSNFD LDNDFFCQIL
     LKESIKKILS TYNNEDYLSF LLDLNFSIVP RDVEDIFFDL YNRLRNKNIS LDDLKNASFV
     NFESCEDKNS LKNNLLTLGK NKSLKTLNKF INSSIFSEIF DKENLDSSDL YTIKENLGQS
     KNFEDELNSV KEQISNLLLA LDDSNYKYYE IIIEILEKIH KLYTKEKRQR GLLDFDDLLI
     YGNELVQNKD VSDKLNKKFT YILIDEFQDV NILQNNIICG LNAKNIFIVG DPQQAIYGFR
     GSFIGIFDNF YKLFRDKDKE ILTLNMNKNY RTDAFIISDI NTLFNNIFTD YQGLVANNKA
     SRKIEKYTVD DEDDYLKLIK YLLSENDSKD IGILARTNGE LEKLETYLKQ NNIDVNRGKI
     NLKQTQVIKF ILSFLRSIFN KNDFTSFMDY ISSPFCDLSF NSLVTVLLKG YRSIDEVCHG
     DISDSNLARA IDVYIKIKKI KNVSSLDYLI KKCIDEFRIF KLNRNDWDYI LILYEKSIEF
     KEKGLSSFRV FERYIESVEV NDKSQGVNLL TIHKSKGLEF KTVVLINMSK PLSNKTSQKI
     TFNKKFGLAI DSQRSNGKFD LINNEQKDIN FEEERRVLYV AMTRARDRLI ICSEKKQSPA
     SYMSILNAPD KFFKEVNIDE EEYQVKVNED TRKLINLNEA FKYRYRQNYS ITDFLNYDYD
     EDAYLMKFFF NRDTKKLQGN TYYIDPKVRG NMLHFFAEHY NEEKIDDYIE FLFKIFKEDI
     NGNKFNEIRE LIVNYLNLRD KEILYKELEF FYDFNGHIVR GFIDQVVYDE AIYIVDLKTS
     DLSEEELVKN YKWQLVFYSK VFKNIYKKEV KGAFIYSLKH CKKVPVEIND KIINELDEKF
     LKFIEQSRKI NFYKIFS
//
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