ID   MTC2_HERAU              Reviewed;         437 AA.
AC   P25264;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   13-SEP-2023, entry version 95.
DE   RecName: Full=Type II methyltransferase M.HgiCII {ECO:0000303|PubMed:12654995};
DE            Short=M.HgiCII {ECO:0000303|PubMed:1644308};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase HgiCII;
DE   AltName: Full=Modification methylase HgiCII;
GN   Name=hgiCIIM {ECO:0000303|PubMed:1644308};
OS   Herpetosiphon aurantiacus (Herpetosiphon giganteus).
OC   Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC   Herpetosiphonaceae; Herpetosiphon.
OX   NCBI_TaxID=65;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=HPG9;
RX   PubMed=1644308; DOI=10.1016/0378-1119(92)90484-7;
RA   Erdmann D., Horst G., Duesterhoeft A., Kroeger M.;
RT   "Stepwise cloning and genetic organization of the seemingly unclonable
RT   HgiCII restriction-modification system from Herpetosiphon giganteus strain
RT   Hpg9, using PCR technique.";
RL   Gene 117:15-22(1992).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=7607523; DOI=10.1016/0378-1119(94)00779-r;
RA   Kroeger M., Blum E., Deppe E., Duesterhoeft A., Erdmann D., Kilz S.,
RA   Meyer-Rogge S., Moestl D.;
RT   "Organization and gene expression within restriction-modification systems
RT   of Herpetosiphon giganteus.";
RL   Gene 157:43-47(1995).
RN   [3]
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 that recognizes the double-stranded sequence 5'-
CC       GGWCC-3', methylates C-? on both strands and protects the DNA from
CC       cleavage by the HgiCII endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:1644308}.
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; X55139; CAA38935.1; -; Genomic_DNA.
DR   PIR; JC1165; JC1165.
DR   AlphaFoldDB; P25264; -.
DR   SMR; P25264; -.
DR   REBASE; 3416; M.HgiCII.
DR   PRO; PR:P25264; -.
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   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..437
FT                   /note="Type II methyltransferase M.HgiCII"
FT                   /id="PRO_0000087887"
FT   DOMAIN          4..431
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   437 AA;  49622 MW;  721217050B382081 CRC64;
     MKQFRFIDLF AGIGGFRLGL EAVGGICVGS AEIDQQAIKV YRQNWPTDRS EHNLGDITTL
     QQLPAHDLVV GGVPCQPWSI AGKNQAFDDP RGQLWADVIR LVRINQPKAF IFENVKGLID
     PRNRLCLESI LDSFKAEGYN VYYKLLNSFD YGVAQNRDRV FIIGIQQKLG VPDFSFPEYS
     ESEQRLYDIL DNLQTPSIIP ESLPIQRNLF GERIEVGFNK LTPRGAFNDF FILNDIRNGP
     TSIHSWEIYA TTEREKQICT TIMRNRGNPR YGDCDGNPMS YQDIADLVVD LAESELQVLI
     QKRILRQYED GKYEFFNRRL SGGIDGTYRI FLPHARFFGR LTARGMHDEI AEISVSGATA
     EAYKQNFIQQ ILIPKRHRPI TVNEAARIQG FPATFKFHSN QSANFRLIGN SVAPPVIMAL
     GKALPNDHLF EPELCEV
//