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T2D1_STRR6
ID   T2D1_STRR6              Reviewed;         254 AA.
AC   P0A460; P09356;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Type II Methyl-directed restriction enzyme DpnI {ECO:0000303|PubMed:12654995};
DE            Short=R.DpnI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease DpnI;
DE   AltName: Full=Type-2 restriction enzyme DpnI;
GN   Name=dpnC; OrderedLocusNames=spr1665;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPES.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
CC   -!- FUNCTION: An M and P subtype restriction enzyme that recognizes the
CC       double-stranded and methylated sequence 5'-G(Me)ATC-3' and cleaves
CC       after A-2. {ECO:0000250|UniProtKB:P0A459, ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC         Evidence={ECO:0000250|UniProtKB:P0A459};
CC   -!- SIMILARITY: Belongs to the DpnI type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; AE007317; AAL00468.1; -; Genomic_DNA.
DR   PIR; G98079; G98079.
DR   RefSeq; NP_359257.1; NC_003098.1.
DR   RefSeq; WP_000418960.1; NC_003098.1.
DR   PDB; 4ESJ; X-ray; 2.05 A; A/B=1-254.
DR   PDBsum; 4ESJ; -.
DR   AlphaFoldDB; P0A460; -.
DR   SMR; P0A460; -.
DR   STRING; 171101.spr1665; -.
DR   REBASE; 5630; SpnRORF1665P.
DR   EnsemblBacteria; AAL00468; AAL00468; spr1665.
DR   GeneID; 60234182; -.
DR   KEGG; spr:spr1665; -.
DR   PATRIC; fig|171101.6.peg.1799; -.
DR   eggNOG; ENOG502Z8N2; Bacteria.
DR   HOGENOM; CLU_095681_0_0_9; -.
DR   OMA; HHIMCSI; -.
DR   PRO; PR:P0A460; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.210.30; -; 1.
DR   InterPro; IPR010324; DRP.
DR   InterPro; IPR041368; DRP_C.
DR   InterPro; IPR043025; DRP_PD-(D/E)XK_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF06044; DpnI; 1.
DR   Pfam; PF17726; DpnI_C; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW   Restriction system.
FT   CHAIN           1..254
FT                   /note="Type II Methyl-directed restriction enzyme DpnI"
FT                   /id="PRO_0000077301"
FT   HELIX           7..12
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           19..31
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          53..55
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   TURN            57..59
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          62..71
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          105..113
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          123..129
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          154..158
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           165..174
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           175..180
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           183..198
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          201..205
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           213..219
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   HELIX           226..239
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          242..245
FT                   /evidence="ECO:0007829|PDB:4ESJ"
FT   STRAND          250..253
FT                   /evidence="ECO:0007829|PDB:4ESJ"
SQ   SEQUENCE   254 AA;  29785 MW;  7FFFFE14BB3EFEDB CRC64;
     MELHFNLELV ETYKSNSQKA RILTEDWVYR QSYCPNCGNN PLNHFENNRP VADFYCNHCS
     EEFELKSKKG NFSSTINDGA YATMMKRVQA DNNPNFFFLT YTKNFEVNNF LVLPKQFVTP
     KSIIQRKPLA PTARRAGWIG CNIDLSQVPS KGRIFLVQDG QVRDPEKVTK EFKQGLFLRK
     SSLSSRGWTI EILNCIDKIE GSEFTLEDMY RFESDLKNIF VKNNHIKEKI RQQLQILRDK
     EIIEFKGRGK YRKL
 
 
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