MTR1_CERSP
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 03-AUG-2022, entry version 105.
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; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; 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 + H(+) + S-adenosyl-L-
CC homocysteine; 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}.
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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 PDBsum; 1EG2; -.
DR PDBsum; 1NW5; -.
DR PDBsum; 1NW6; -.
DR PDBsum; 1NW7; -.
DR PDBsum; 1NW8; -.
DR AlphaFoldDB; 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:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 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; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
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 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 STRAND 156..165
FT /evidence="ECO:0007829|PDB:1EG2"
FT HELIX 173..175
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 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..308
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
