ID MTR1_CERSP Reviewed; 319 AA. AC P14751; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 02-SEP-2026, entry version 114. DE RecName: Full=Type II methyltransferase M.RsrI {ECO:0000303|PubMed:2602165}; DE Short=M.RsrI {ECO:0000303|PubMed:2690017}; DE EC=2.1.1.72 {ECO:0000269|PubMed:2690017}; DE AltName: Full=Adenine-specific methyltransferase RsrI; DE AltName: Full=Modification methylase RsrI; GN Name=rsrIM {ECO:0000303|PubMed:2690017}; OS Cereibacter sphaeroides (Rhodobacter sphaeroides). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rhodobacterales; Paracoccaceae; Cereibacter. OX NCBI_TaxID=1063; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-18, FUNCTION, RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=630; RX PubMed=2690017; DOI=10.1093/nar/17.24.10403; RA Kaszubska W., Aiken C., O'Connor D., Gumport R.I., Stephenson F.H., RA Greene P.J.; RT "Purification, cloning and sequence analysis of RsrI DNA methyltransferase: RT lack of homology between two enzymes, RsrI and EcoRI, that methylate the RT same nucleotide in identical recognition sequences."; RL Nucleic Acids Res. 17:10403-10425(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=630; RX PubMed=2602165; DOI=10.1093/nar/17.24.10503; RA Stephenson F.H., Greene P.J.; RT "Nucleotide sequence of the gene encoding the RsrI methyltransferase."; RL Nucleic Acids Res. 17:10503-10503(1989). RN [3] RP NOMENCLATURE, AND SUBTYPE. 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). RN [4] {ECO:0007744|PDB:1EG2} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). RX PubMed=11024175; DOI=10.1093/nar/28.20.3950; RA Scavetta R.D., Thomas C.B., Walsh M.A., Szegedi S., Joachimiak A., RA Gumport R.I., Churchill M.E.; RT "Structure of RsrI methyltransferase, a member of the N6-adenine beta class RT of DNA methyltransferases."; RL Nucleic Acids Res. 28:3950-3961(2000). CC -!- FUNCTION: A beta subtype methylase, recognizes the double-stranded CC sequence 5'-GAATTC-3', methylates A-3 on both strands, and protects the CC DNA from cleavage by the RsrI endonuclease. CC {ECO:0000269|PubMed:2690017, ECO:0000303|PubMed:12654995}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an CC N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine + CC H(+); Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA- CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72; CC Evidence={ECO:0000269|PubMed:2690017}; CC -!- ACTIVITY REGULATION: Strongly inhibited by N-ethylmaleimide, CC inactivated by MgCl(2) or MgSO(4). {ECO:0000269|PubMed:2690017}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:2690017}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. It has about 60% activity CC at 30 degrees Celsius, the optimal growth temperature for this CC bacteria. {ECO:0000269|PubMed:2690017}; CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {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; X16456; CAA34475.1; -; Genomic_DNA. DR PIR; S07570; S07570. DR PDB; 1EG2; X-ray; 1.75 A; A=1-319. DR PDB; 1NW5; X-ray; 2.05 A; A=1-319. DR PDB; 1NW6; X-ray; 1.94 A; A=1-319. DR PDB; 1NW7; X-ray; 2.10 A; A=1-319. DR PDB; 1NW8; X-ray; 2.25 A; A=1-319. DR AlphaFoldDB; P14751; -. DR MDRepo; P14751; -. DR SMR; P14751; -. DR DrugBank; DB02282; 5'-S-methyl-5'-thioadenosine. DR DrugBank; DB01752; S-adenosyl-L-homocysteine. DR DrugBank; DB01910; Sinefungin. DR REBASE; 3487; M.RsrI. DR BRENDA; 2.1.1.72; 5383. DR EvolutionaryTrace; P14751; -. DR PRO; PR:P14751; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; EXP:UniProtKB. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00506; D21N6MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS00092; N6_MTASE; 1. DR PDBsum; 1EG2; -. DR PDBsum; 1NW5; -. DR PDBsum; 1NW6; -. DR PDBsum; 1NW7; -. DR PDBsum; 1NW8; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; DNA-binding; Methyltransferase; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:2690017" FT CHAIN 2..319 FT /note="Type II methyltransferase M.RsrI" FT /id="PRO_0000087970" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..10 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 47..52 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 59..64 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 72..76 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 96..106 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 119..129 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 156..165 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 181..188 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 195..200 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 229..239 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:1EG2" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1NW6" FT HELIX 255..263 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 275..286 FT /evidence="ECO:0007829|PDB:1EG2" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 305..307 FT /evidence="ECO:0007829|PDB:1EG2" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:1EG2" SQ SEQUENCE 319 AA; 35655 MW; 806E7BF702D4EC85 CRC64; MANRSHHNAG HRAMNALRKS GQKHSSESQL GSSEIGTTRH VYDVCDCLDT LAKLPDDSVQ LIICDPPYNI MLADWDDHMD YIGWAKRWLA EAERVLSPTG SIAIFGGLQY QGEAGSGDLI SIISHMRQNS KMLLANLIIW NYPNGMSAQR FFANRHEEIA WFAKTKKYFF DLDAVREPYD EETKAAYMKD KRLNPESVEK GRNPTNVWRM SRLNGNSLER VGHPTQKPAA VIERLVRALS HPGSTVLDFF AGSGVTARVA IQEGRNSICT DAAPVFKEYY QKQLTFLQDD GLIDKARSYE IVEGAANFGA ALQRGDVAS //