ID D2NS46_ROTMD Unreviewed; 1279 AA.
AC D2NS46;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN OrderedLocusNames=RMDY18_06400 {ECO:0000313|EMBL:BAI64472.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64472.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64472.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64472.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64472.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64472.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP011540; BAI64472.1; -; Genomic_DNA.
DR RefSeq; WP_012903183.1; NC_013715.1.
DR AlphaFoldDB; D2NS46; -.
DR STRING; 680646.RMDY18_06400; -.
DR KEGG; rmu:RMDY18_06400; -.
DR eggNOG; COG0210; Bacteria.
DR eggNOG; COG2887; Bacteria.
DR HOGENOM; CLU_004900_0_0_11; -.
DR Proteomes; UP000001883; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
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; 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; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF59; 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}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
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:UP000001883}.
FT DOMAIN 1..307
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 364..718
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 941..961
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1279 AA; 139849 MW; C579AE8A20D0E3ED CRC64;
MTTQLLTGIP GTGKTHHLTE RALRYLADGN DPARLLILAP TRTAATRMRD TIAASSDRSL
SVAPTRAWAA YAFDLLKRAQ TRGLLSGVEG NLKLLSGPEQ DVIIGELLAN HAEGIAPGPA
WPDVLRDALA TRGFRHEIRD FFDRMAEYDL TAEDVHALAT EHNQPAWHAL AQLHTEYRAV
RALRAKNAYD PAVLINDACR LLLRAPEFLA EERRRYDLIL IDDVQELSPS IYRLLRLIAA
EVAPADAAHL TETHPDLFAE GPRVVMTYSD EAVVQGFRGA RPDLVTTLQA SFPSMRTRTL
TTSYRLPALM MPLVADIRRR LPRYTRFVPL TAEQEGTKNG AQEGSKNGAP ATFGRINTTP
ADEALTWGAA DEPLLHLGAD GKILDPAHYR TAPAGVYKYA LSSSQDEANL IAQMLLEERI
YGNHPYRESA IIVRSSADVA RIRRVLSSNG IPSRTSAALV PVRDEPAVRP FLDALSLLVY
ARKRGEKALN PAVHMPAAEG AEAAERGGYE ALSASEAEEL MRRSLDDVIA EESRANPLGG
AQSAITLLTS RLGGASSMDV RRLRQQLRSI ELQSGGHRPS DDLLLGALLH PETLPEEGVG
RAVHRIAAVL SAGRKALARP ESTSTEVLWA LWEASGLEKT WVTQSRGAGP DADAAHRNLD
AMIGLFEAAD RFDEQMRGAG AEQFLDFIDA QDLPMDTLAA RGVRQDAVEI LTPALAAGQS
WRTVYVCGLQ EGTWPNTTVR GSLLSTGDLT DLCDARLRQR AQQAEQQAGE SEQPVPPARI
RSYPERVRDT RHDELRMFAV AATRASTRLV LTAVRNDDQA PGEFFDFVLP TDAENESPEV
PITRVRRPAT LRSLVAELRR TLVEESLNAM RAEDAQDGAP AGSMPEEEAL TPEASTYRLD
AASRTLARLA NAQAPGAAPD DWWGLLPLSS TELLFAHRPA DHAEDENHSE EPAEEQAEKP
SRRTIALSPS RLETIHSSPL DWLVSAARAE AQTDLSRSLG TLIHAIAEEY PTGTLEELQT
ALDERISSLG VPARKEDETD EEYRERVPWE SYALYERAKR MILRLSYYYR QHMGDAGWQN
LGVEGSFAVR VPVPFDPAGE VGELDALLTG RVDRLEGTAP AEDGTRRYAI VDLKTGKSKP
TGSEMETHPQ LAAYQIAVEA GAGEQLEERY RAEAAALEAG EPLPDARPQE LEYTGYTGHS
AGAALVQLGA SGVNDESKTR LQVQPALTEH DSWAAELVQH AAELIAGSQV QARHREGGYG
CRLPEICPIC TRGRQVTQP
//
