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 27-MAR-2024, entry version 81. 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; Bacillota; 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}. 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; 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 KEGG; spr:spr1665; -. DR PATRIC; fig|171101.6.peg.1799; -. DR eggNOG; ENOG502Z8N2; Bacteria. DR HOGENOM; CLU_095681_0_0_9; -. 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 CDD; cd22319; DpnI-like; 1. DR Gene3D; 3.40.210.30; Dam replacing family, catalytic PD-(D/E)XK domain; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 //