ID   MTP1_PSYTA              Reviewed;         416 AA.
AC   O33481;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Type II methyltransferase M.PspPI {ECO:0000303|PubMed:12654995};
DE            Short=M.PspPI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase PspPI;
DE   AltName: Full=Modification methylase PspPI;
GN   Name=pspPIM {ECO:0000303|PubMed:9332385};
OS   Psychrobacter sp. (strain TA137).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=203703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=TA137;
RX   PubMed=9332385; DOI=10.1016/s0378-1119(97)00283-7;
RA   Rina M., Caufrier F., Markaki M., Mavromatis K., Kokkinidis M.,
RA   Bouriotis V.;
RT   "Cloning and characterization of the gene encoding PspPI methyltransferase
RT   from the Antarctic psychrotroph Psychrobacter sp. strain TA137. Predicted
RT   interactions with DNA and organization of the variable region.";
RL   Gene 197:353-360(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       GGNCC-3', methylates C-4 on both strands, and protects the DNA from
CC       cleavage by the PspPI endonuclease. {ECO:0000269|PubMed:9332385,
CC       ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; Y07554; CAA68841.1; -; Genomic_DNA.
DR   AlphaFoldDB; O33481; -.
DR   SMR; O33481; -.
DR   REBASE; 203181; M.Bam1267ORF3198P.
DR   REBASE; 2771; PspPI.
DR   REBASE; 3564; M.PspPI.
DR   PRIDE; O33481; -.
DR   PRO; PR:O33481; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..416
FT                   /note="Type II methyltransferase M.PspPI"
FT                   /id="PRO_0000087904"
FT   DOMAIN          77..410
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   416 AA;  46858 MW;  B4CFD816AD147A9A CRC64;
     MKFPDNHFSA AIVADTLSVS KRNVETWTQN GKLVPALDPN IHEKPYTKDQ LETFEQFSAM
     FNSSWCEEMA VEPSRSYSLV ELFAGAGGLA LGLEQAGFKS VLLNEKDKYA CATLRANRPN
     WNVIEDDIEN VDFTHLNGKV DLLTGGFPCQ PFSYAGKQLG FEDLRGTLVF EMARAIKEIK
     PKVFLAENVK GLAENDGGRT LSIIIKVLED LGYKILEKEV YKAIFYKVPQ KRERLIIIGV
     RTDLYDKLAY EKPSPYYKVL TVADALKAGE LYDVDVPEST GQLYPERKAE IMSYVPEGGY
     WRDLPIRIAK EYMMKSFYLG GGKTGMARRL SWDEPSLTLV CTPAQKQTER CHPSESRPLT
     TREYARIQTF PDDWEFKGSV GQIYKQIGNA VPVNLALAIG KAIIRMLNAA PKDVFE