MT872_AERPE
ID MT872_AERPE Reviewed; 469 AA.
AC Q9YDP3;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA (cytosine-5-)-methyltransferase M.ApeKI {ECO:0000303|PubMed:34585946};
DE Short=M.ApeKI {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:34585946};
DE EC=2.1.1.37 {ECO:0000255|PROSITE-ProRule:PRU10018, ECO:0000269|PubMed:34585946};
DE AltName: Full=Cytosine-specific methyltransferase ApeKI {ECO:0000305};
DE AltName: Full=Modification methylase ApeKI {ECO:0000305};
DE AltName: Full=Type II methyltransferase M.ApeKI {ECO:0000303|PubMed:12654995};
GN OrderedLocusNames=APE_0872.1 {ECO:0000312|EMBL:BAA79854.2};
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557 {ECO:0000312|EMBL:BAA79854.2};
RN [1] {ECO:0000312|EMBL:BAA79854.2, ECO:0000312|Proteomes:UP000002518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1
RC {ECO:0000312|Proteomes:UP000002518};
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP BIOTECHNOLOGY.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1
RC {ECO:0000303|PubMed:34585946};
RX PubMed=34585946; DOI=10.1128/spectrum.00186-21;
RA Hayashi M., Sugahara K., Yamamura A., Iida Y.;
RT "Evaluation of the Properties of the DNA Methyltransferase from Aeropyrum
RT pernix K1.";
RL Microbiol. Spectr. 9:e0018621-e0018621(2021).
CC -!- FUNCTION: Cytosine methylase that recognizes the double-stranded
CC sequence 5'-GC(A/T)GC-3', methylates C-5 position of the second
CC cytosine on both strands, and protects the DNA from cleavage by the
CC ApeKI endonuclease. {ECO:0000269|PubMed:34585946}.
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:34585946};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13682;
CC Evidence={ECO:0000269|PubMed:34585946};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is between 70-90 degrees Celsius. Highly
CC thermostable. 34% of the activity of the unheated sample after
CC incubation at 90 degrees Celsius for 10 hours. Lowest activity
CC detected at 10 degrees Celsius. {ECO:0000269|PubMed:34585946};
CC -!- BIOTECHNOLOGY: This protein may be useful as an epigenetic editing tool
CC due to its high thermostability. {ECO:0000305|PubMed:34585946}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016, ECO:0000255|RuleBase:RU000416}.
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DR EMBL; BA000002; BAA79854.2; -; Genomic_DNA.
DR PIR; F72681; F72681.
DR STRING; 272557.APE_0872.1; -.
DR REBASE; 4179; M.ApeKI.
DR EnsemblBacteria; BAA79854; BAA79854; APE_0872.1.
DR KEGG; ape:APE_0872.1; -.
DR PATRIC; fig|272557.25.peg.626; -.
DR eggNOG; arCOG04157; Archaea.
DR OMA; GTHGYHY; -.
DR Proteomes; UP000002518; Chromosome.
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:0090116; P:C-5 methylation of cytosine; IDA:UniProtKB.
DR GO; GO:0032776; P:DNA methylation on cytosine; IDA:UniProtKB.
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; 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; PS51679; SAM_MT_C5; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..469
FT /note="DNA (cytosine-5-)-methyltransferase M.ApeKI"
FT /id="PRO_0000454724"
FT DOMAIN 4..469
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 469 AA; 52923 MW; CBB72588139C3AFC CRC64;
MSRYSTISLF SGAGGLDLGF VQSGRFRIVF ANEILLPAAV TYSRNLGLRL EVCGDEPRVE
AQPGTIMACD VAKLDFTGLS GVDADVIIGG PPCQDFSIVR GPDWDRRGIN VKRGRLYAHF
VRALASLQPK AFVFENVPGL VSANRGLAYK VILEDFARLS IRWDEIKRIV SSNGNGGKVE
GYEIVFTGIV DFSKLGVPQK RERLVIIGLR KDLAGGGFET ISRLRARIDH VLSGKRWLLH
RYPLTPIEVF EGQPLDRLGD KYKEVMLKWE GVWDEVGTER AFEWKRRVWD RLTFDIISDY
LSFNGIKHAD KQELEEALMQ HEVLLKELGY YGRPVYSLKL PDSTTEPPYE GKAVVERMKR
IPPDENHEFV RGTRWEVEGR GISLVYRRIH PLKPSYTVVA YGGGGTHGYH YDRDRATLTL
RERARLQTFP DSFLFYGKKP EIRAQIGEAV PPLAAKRIAE ALAEVLDAV
