MTM1_MICAM
ID MTM1_MICAM Reviewed; 362 AA.
AC P50190;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Type II methyltransferase M.MamI {ECO:0000303|PubMed:12654995};
DE Short=M.MamI {ECO:0000303|PubMed:8654988};
DE EC=2.1.1.72;
DE AltName: Full=Adenine-specific methyltransferase MamI;
DE AltName: Full=Modification methylase MamI;
GN Name=mamIM {ECO:0000303|PubMed:8654988};
OS Microbacterium ammoniaphilum.
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Microbacterium.
OX NCBI_TaxID=42460;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 15354 / DSM 20156 / BCRC 11670 / NCIMB 10335 / NRRL B-4247;
RX PubMed=8654988; DOI=10.1016/0378-1119(96)00189-8;
RA Striebel H.-M., Seeber S., Jarsch M., Kessler C.;
RT "Cloning and characterization of the MamI restriction-modification system
RT from Microbacterium ammoniaphilum in Escherichia coli.";
RL Gene 172:41-46(1996).
RN [2]
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).
CC -!- FUNCTION: A gamma subtype methylase that recognizes the double-stranded
CC sequence 5'-GATNNNNATC-3', methylates A-? on both strands, and protects
CC the DNA from cleavage by the MamI endonuclease.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8654988}.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X79027; CAA55646.1; -; Genomic_DNA.
DR PIR; T45131; T45131.
DR AlphaFoldDB; P50190; -.
DR SMR; P50190; -.
DR REBASE; 3439; M.MamI.
DR PRO; PR:P50190; -.
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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..362
FT /note="Type II methyltransferase M.MamI"
FT /id="PRO_0000087975"
SQ SEQUENCE 362 AA; 38501 MW; 85CE1ADFB54ADC84 CRC64;
MRPLRHAVGS STVTLETDLT LFPEDLHAPL LGSAGNATVD ELALAARFDG LHQLLYTRGG
VRPTNAAIEE VGKLLLLRLW LSRDDEASVD GVGLRALFDG AVPDESVVEV TKKAFTQVLT
VDRMSLRAVD GSSRPLWPYD EPFRLAEPTV LQSALALVNE ILGGGTRVAD PLGTAFDAFL
SGRYDHSGGL GTYLTPSSVA RMMAEVVLDL LSSDALADVR APIIADPFCG TGRFLVAAFD
AAEERHENVD LAGLLDGGLV GADQSTTAIA KSGLNLLLYG AQQPEVYAVA DSMTDPGLDR
LRGTLAAVLT NPPFGGGKYD DALGIDRTRE LFPSVRPNRP MDPRLLDSRC LSNFCDPGES
LG