ID   MTAP_ARTPN              Reviewed;         345 AA.
AC   D4ZX35;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Type II methyltransferase M.AplI {ECO:0000303|PubMed:12654995};
DE            Short=M.AplI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.37 {ECO:0000269|PubMed:23563565};
DE   AltName: Full=Cytosine-specific methyltransferase AplI;
DE   AltName: Full=Modification methylase AplI;
GN   Name=aplIM; ORFNames=NIES39_K04650;
OS   Arthrospira platensis (strain NIES-39 / UTEX 3086 / IAM M-135) (Spirulina
OS   platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=696747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-39 / UTEX 3086 / IAM M-135;
RX   PubMed=20203057; DOI=10.1093/dnares/dsq004;
RA   Fujisawa T., Narikawa R., Okamoto S., Ehira S., Yoshimura H., Suzuki I.,
RA   Masuda T., Mochimaru M., Takaichi S., Awai K., Sekine M., Horikawa H.,
RA   Yashiro I., Omata S., Takarada H., Katano Y., Kosugi H., Tanikawa S.,
RA   Ohmori K., Sato N., Ikeuchi M., Fujita N., Ohmori M.;
RT   "Genomic structure of an economically important cyanobacterium, Arthrospira
RT   (Spirulina) platensis NIES-39.";
RL   DNA Res. 17:85-103(2010).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=NIES-39 / UTEX 3086 / IAM M-135;
RX   PubMed=23563565; DOI=10.1271/bbb.120919;
RA   Shiraishi H., Tabuse Y.;
RT   "The AplI restriction-modification system in an edible cyanobacterium,
RT   Arthrospira (Spirulina) platensis NIES-39, recognizes the nucleotide
RT   sequence 5'-CTGCAG-3'.";
RL   Biosci. Biotechnol. Biochem. 77:782-788(2013).
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, recognizes the double-stranded sequence 5'-
CC       CTGCAG-3', methylates C-4 on both strands, and protects the DNA from
CC       cleavage by the AplI endonuclease. {ECO:0000269|PubMed:23563565,
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         ECO:0000269|PubMed:23563565};
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; AP011615; BAI92110.1; -; Genomic_DNA.
DR   RefSeq; WP_006618672.1; NC_016640.1.
DR   AlphaFoldDB; D4ZX35; -.
DR   SMR; D4ZX35; -.
DR   STRING; 696747.NIES39_K04650; -.
DR   REBASE; 25961; M.AplI.
DR   EnsemblBacteria; BAI92110; BAI92110; NIES39_K04650.
DR   KEGG; arp:NIES39_K04650; -.
DR   PATRIC; fig|696747.3.peg.2191; -.
DR   eggNOG; COG0270; Bacteria.
DR   HOGENOM; CLU_006958_2_0_3; -.
DR   OMA; CENVRGL; -.
DR   OrthoDB; 1178320at2; -.
DR   PRO; PR:D4ZX35; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0032776; P:DNA methylation on cytosine; IDA:UniProtKB.
DR   GO; GO:0009307; P:DNA restriction-modification system; IDA:UniProtKB.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF00145; DNA_methylase; 2.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..345
FT                   /note="Type II methyltransferase M.AplI"
FT                   /id="PRO_0000423855"
FT   DOMAIN          25..325
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   345 AA;  38880 MW;  5E069E36946D8BE5 CRC64;
     MSNRLSYWEY LHQELKLNAD IQSQLVVLDL FAGCGGFSLG FKAAGFQTIG YEMLADAAAT
     YTRNLQDPCY CQTLEIGQDL CNHPDVIIGG PPCQPFSVGG LQKGPRDSRD GLPIFIDAIA
     RYQPEIAIFE NVRGMLYKNR QYLEKIVAEL ERLNYRVDIK LINAVNYGVP QKRERLFVVA
     YQTAWNWPEA ETLAIPYTAG DAIYDTASTI PIGAKFLTPS MLEYIGRYEA KSKCVKPRDI
     YLDIPCRTLT CRNLSGATSD MLRLLLPDGR RRRLTVREAA RLQSFPDWFE LVGSENSQFN
     QIGNAVPPLL AKAIAKSVKM TLENKPSRPT DYFSPFPQQL KLPFA