ID C8WH92_EGGLE Unreviewed; 1142 AA.
AC C8WH92;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN OrderedLocusNames=Elen_1515 {ECO:0000313|EMBL:ACV55483.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV55483.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV55483.1, ECO:0000313|Proteomes:UP000001377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; CP001726; ACV55483.1; -; Genomic_DNA.
DR RefSeq; WP_015760611.1; NC_013204.1.
DR AlphaFoldDB; C8WH92; -.
DR STRING; 479437.Elen_1515; -.
DR REBASE; 21955; EleORF1517P.
DR PaxDb; 479437-Elen_1515; -.
DR GeneID; 69510352; -.
DR KEGG; ele:Elen_1515; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_010804_0_0_11; -.
DR OrthoDB; 9758243at2; -.
DR BioCyc; ELEN479437:G1GFY-1523-MONOMER; -.
DR Proteomes; UP000001377; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR42927; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42927:SF1; HELICASE SUPERFAMILY 1 AND 2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001377};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 328..550
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1142 AA; 127052 MW; C94D4BF1D94C30C5 CRC64;
MTKVDMHIPG KSDLDVSFDG SRKIHQEAPF ERYISRKVAG LEHSGWALSP DDTGFDPNDA
LVFDDFVAWL EATAPEKLDK MRREKGARWA DQLKRALVKS LERNGTVLTL RKGFQMAGYQ
TIECMAGYPD DERVPGARER YDANILRFMH QVHYQTAGSK SLDFVLFVNG IPVATGEVKT
ELTQTVRDAI DEYADERKPV EPDGGRKNPL LMYKRGAVVH FAVSEDEVWM CTNLGPFPSK
SARPRFLPFN LGRDGGAGNP DAPEGEYRTH YLWDTILQRD NWLSIFDRFV FEEVEDRQDA
SGRWRRQATQ IFPRYHQFDA ERKVLADARE HGAGRRYLIE HSAGSGKTET ISWAAHDLAR
LRRADGEKMF SSVVVVTDRL SLDQNIKKTI SQLSKVTGQV VMIGRDERGN AVSDGSKSSQ
LVEALRQKRE IVVVTIQTFL YAWPDIAVLP ELDGAGFAVI VDEAHSSQEG SSAASLKTAF
NAAADKLKFE RMLDFDDDSG DDGSVMDAYF AQMQASNLMP PNVSFLAFTA TPKAETKTLF
GTPTGEEDED GNPVMGSFHL YPMRQAIEEG YIIDPLSGYV PLKTLTRIED ESEDADGRLV
DERRARRKIA KWRSLHPTNV MEKAKWIIDH FVDNVAPLLN GEAKAMIVTS GRPEVVRYKY
AIEAYLRARP DLDPAKVEPR LRFKVPGEPL VAFSQKVLGD RCVLPEDEYL EDNPFALIER
GYEYTEANMN PTGQGPVERA FDRPESRLLI VANKFQTGFD QKKLVALYVD KPLGNAIEIV
QTYSRVNRTC SGKDRVFVVD FVNDPETVLA AFKTYDKGAT MSAAQDPNVV YDLKDALDAA
DVFATRDVEG FKEALYRSKG LAAGGESDAY RTALYSAVSG PAEIFRERFA AARDSYETWL
ECANRAEAAG EAEEAERAKR SADEAAGRVA ELMTFRKKLS KYCSAYTFLS QALDFGDPDL
EVFYSFAKLL GHRIAGTSLD DVDVRGLVLR DFRISAQKVP EGVEGGELMP MGAGGSGAAP
KRDTMARIVE RLNRTWGDEG DPLVKARAVN AVSDAVAADP VTNTQITNTS NTKEAVLADG
RLRNIVIRAL MSMMSNELGD LAEQALDDPQ AIEPLADQVY DLISQGKRYD IAELASYLSK
GE
//
