MTC2_HERAU
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 03-AUG-2022, entry version 91.
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; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC 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 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..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
