MTSA_LACLC
ID MTSA_LACLC Reviewed; 389 AA.
AC P34877;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Type II methyltransferase M1.ScrFI {ECO:0000303|PubMed:12654995};
DE Short=M1.ScrFI {ECO:0000303|PubMed:12654995};
DE EC=2.1.1.37;
DE AltName: Full=Cytosine-specific methyltransferase ScrFIA;
DE AltName: Full=Modification methylase ScrFIA;
DE Short=M.ScrFI-A;
DE Short=M.ScrFIA;
GN Name=scrFIAM;
OS Lactococcus lactis subsp. cremoris (Streptococcus cremoris).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=UC503;
RX PubMed=8481004; DOI=10.1128/aem.59.3.777-785.1993;
RA Davis R., van der Lelie D., Mercenier A., Daly C., Fitzgerald G.F.;
RT "ScrFI restriction-modification system of Lactococcus lactis subsp.
RT cremoris UC503: cloning and characterization of two ScrFI methylase
RT genes.";
RL Appl. Environ. Microbiol. 59:777-785(1993).
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 CCNGG-3', methylates C-2 on both strands, and protects the DNA from
CC cleavage by the ScrFI endonuclease. {ECO:0000269|PubMed:8481004,
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 -!- MISCELLANEOUS: The ScrFI restriction system has two different
CC methylases. {ECO:0000269|PubMed:8481004}.
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; M87289; AAA25220.1; -; Genomic_DNA.
DR EMBL; U89998; AAB66696.1; -; Genomic_DNA.
DR PIR; A48966; A48966.
DR RefSeq; WP_041931724.1; NZ_WJUW01000117.1.
DR AlphaFoldDB; P34877; -.
DR SMR; P34877; -.
DR REBASE; 3681; M1.ScrFI.
DR PRO; PR:P34877; -.
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; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
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; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF01381; HTH_3; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
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; PS50943; HTH_CROC1; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..389
FT /note="Type II methyltransferase M1.ScrFI"
FT /id="PRO_0000087892"
FT DOMAIN 16..71
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DOMAIN 79..387
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 389 AA; 44542 MW; 6F5FAFFD9973CC02 CRC64;
MTTISRNTGT EISIMIKEKR LRLNMTQKEL ADAVGMSKNG DRTIRRWENG ETCPSQLEIS
AILRFPEIAP FENRKTAKYK MIDLFAGIGG TRLGFHQTEK VKSVFSSEID KFAIKTYKAN
FGDEPHGDIT KIDEKDIPDH DILVGGFPCQ AFSQAGKKLG FDDTRGTLFF EIARIIKEKR
PKAFLLENVK NLKTHDKGRT FKTILNTLEE LDYEVHTALF KARDFGLPQN RERIYIVGFD
RKSISNYSDF QMPTPLQEKT RVGNILESVV DDKYTISDKL WDGHQRRKTE NKKNGKGFGY
TLFNQDSEYT NTLSARYYKD GSEILIEQKN KNPRKITPRE AARLQGFPEN FIIPVSDTQA
YKEFGNSVAV PTIHAIAEKM LEVLEKSKK
