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 13-SEP-2023, entry version 114. 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; Bacillota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; cd00315; Cyt_C5_DNA_methylase; 1. DR CDD; cd00093; HTH_XRE; 1. DR Gene3D; 3.90.120.30; -; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00675; dcm; 1. DR PANTHER; PTHR46098; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1. DR PANTHER; PTHR46098:SF1; TRNA (CYTOSINE(38)-C(5))-METHYLTRANSFERASE; 1. 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; lambda repressor-like DNA-binding domains; 1. 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; 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 //