ID   MTC1_RHOHA              Reviewed;         517 AA.
AC   P42828;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Type II methyltransferase M.CeqI {ECO:0000303|PubMed:12654995};
DE            Short=M.CeqI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase CeqI;
DE   AltName: Full=Modification methylase CeqI;
GN   Name=ceqIM; Synonyms=mceQI;
OS   Rhodococcus hoagii (Corynebacterium equii).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=43767;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9304804; DOI=10.1016/s1357-2725(97)00029-0;
RA   Izsvak Z., Jobbagy Z., Takacs I., Duda E.;
RT   "Cloning and characterization of the genes of the CeqI restriction-
RT   modification system.";
RL   Int. J. Biochem. Cell Biol. 29:895-900(1997).
RN   [2]
RP   NOMENCLATURE.
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 methylase, recognizes the double-stranded sequence 5'-
CC       GATATC-3', methylates A-? on both strands, and protects the DNA from
CC       cleavage by the CeqI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:9304804}.
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;
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DR   EMBL; Z34099; CAA84006.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42828; -.
DR   SMR; P42828; -.
DR   PRIDE; P42828; -.
DR   PRO; PR:P42828; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   DNA-binding; Methyltransferase; Repeat; Restriction system;
KW   S-adenosyl-L-methionine; TPR repeat; Transferase.
FT   CHAIN           1..517
FT                   /note="Type II methyltransferase M.CeqI"
FT                   /id="PRO_0000087951"
FT   REPEAT          283..316
FT                   /note="TPR 1"
FT   REPEAT          361..394
FT                   /note="TPR 2"
FT   REPEAT          476..509
FT                   /note="TPR 3"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          33..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   517 AA;  59936 MW;  8F0A259D871EAE39 CRC64;
     MVVTSSAGCA SRPRGRGRWP RLSRRSGCLE VPGRPRRPFL RPTVPGPTSA RPRRGRAPHG
     RSTRCTGWRV QLSFSCPPFI KNRQFQFYLI RSPFSRVGYG LSDVNSSSLL GLWGIKFFAC
     WENSNMIYIF KMLGYNQDKL PITSERLVPM ASSISPEKLG AKIVEWYSCI VSREVEQAEE
     YKQEIGQLVN QLERSDEKVL SYYSLVLFRH QLLTEDVQQK RVEPTSLQAV NVEDTIYDGL
     LAFLYYFMSG QYEFYEGRYQ SALRLYKIAE QKIDHVHDQS EKAEFYFRLG ESYFAHHQYT
     FAVSYLEQAI DLFENNNFIW TILNCRLLLA AIKTELNLFD EAEKEYQSAL ADATPYPTTH
     ALLLRALGLN RVRQRKLYEA EMYFAEALTI GDHSKSVEGL KTKANLANVR LRQNANNAEA
     IRLLQEAKAG ATAIHLEECM VRCAITEALY INEGRDERLT SELQRLLERE FYTEYSELAE
     EIAEYYKQQS LLEKAFYYMK EALHYRTNMK MIGVEQQ