ID   T2RM_METJA              Reviewed;        1181 AA.
AC   Q60301;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative type II restriction enzyme and methyltransferase RM.MjaORFECS2P {ECO:0000303|PubMed:12654995};
DE            Short=RM.MjaORFECS2P {ECO:0000303|PubMed:12654995};
DE            EC=3.1.21.4;
DE   Includes:
DE     RecName: Full=Adenine-specific methyltransferase activity;
DE              EC=2.1.1.72;
GN   OrderedLocusNames=MJECS02;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OG   Plasmid small ECE.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPES.
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: Probably a G subtype restriction enzyme that recognizes an
CC       undetermined sequence and cleaves at an undetermined site. Probably
CC       also acts as an alpha subtype methylase, presumably on the same
CC       sequence. {ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC   -!- SIMILARITY: In the C-terminal section; belongs to the N(4)/N(6)-
CC       methyltransferase family. {ECO:0000305}.
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DR   EMBL; L77119; AAC37060.1; -; Genomic_DNA.
DR   PIR; B64516; B64516.
DR   RefSeq; WP_010890095.1; NC_001733.1.
DR   AlphaFoldDB; Q60301; -.
DR   STRING; 243232.MJ_ECS02; -.
DR   REBASE; 6813; MjaORFECS2P.
DR   PRIDE; Q60301; -.
DR   DNASU; 1450829; -.
DR   EnsemblBacteria; AAC37060; AAC37060; MJ_ECS02.
DR   GeneID; 1450829; -.
DR   KEGG; mja:MJ_ECS02; -.
DR   eggNOG; arCOG02635; Archaea.
DR   HOGENOM; CLU_270917_0_0_2; -.
DR   InParanoid; Q60301; -.
DR   OMA; HEENIGD; -.
DR   OrthoDB; 1425at2157; -.
DR   Proteomes; UP000000805; Plasmid small ECE.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF12950; TaqI_C; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Endonuclease; Hydrolase; Methyltransferase;
KW   Multifunctional enzyme; Nuclease; Plasmid; Reference proteome;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..1181
FT                   /note="Putative type II restriction enzyme and
FT                   methyltransferase RM.MjaORFECS2P"
FT                   /id="PRO_0000088002"
SQ   SEQUENCE   1181 AA;  138439 MW;  9F961D8F8C6A4BDD CRC64;
     MVVMAQTKLC SDIEIPKEVY NKWKDFIKLV GNIILSIKQI PELEGKFKEL LKKGRYNFKS
     DDFGGQLPEP FTRQKVIEPI LEFLGYEFTS EISKKSPLGD RKIPDYRVSV FNKEILIEAE
     PLGSDLNKKD SGIHQVKEWL IIKSYGVDTG IATNGLEWVL LHYDDTIKEI RTLKELNLKS
     IFEYVLENKK DKDLENELKQ VFSEFYYCFS KEYIEEYIEV ATKNIKHKKE EITNEFYKEF
     VKLVFGFEDV KDVKKKDKSS SEKDKGTKKC LYNCIEAPPN TSELDKKKFA VLLMNRLIFI
     KFLEDKGIVP RDLLRRTYED YKKSNVLINY YDAYLKPLFY EVLNTPEDER KENIRTNPYY
     KDIPYLNGGL FRSNNVPNEL SFTIKDNEII GEVINFLERY KFTLSTSEGS EEVELNPDIL
     GYVYEKLINI LAEKGQKGLG AYYTPDEITS YIAKNTIEPI VVERFKEIIK NWKINDINFS
     TLDEILNEDS KIAENKHILR AFLDELDKIR ILDPAVGSGH FLISALKELL QIKKRIYYLL
     REEMDIYKEK LGIILNNLYG VDIDDIAVEI AKLRLWLALI ENLDVEALKR GEVLLPNIEY
     NVRCGNSLVG WIDENLKQLS ISYLCDNVRI MCVLEGLIIN AHNSEERKKL KKAKELLEKR
     DGYVLDNYVE AYHLLYEVYR TSHGLKANLL KELLDEIRDS IYESVTPAYF AEIYQNGNNK
     KNNGKKSKKN RPRVEEFEKL KPFHWKIDFG WIIKEEGFDV IIGNPPYGNL LSPTEKEIMK
     RRDTPEFDIF VTFIVHSSKL LKNEGYLGFI IPSSFGTGVR YSNLRKELFT KMCLKKLIYL
     PFDVFSGAYV DNCIIILHKK PPKSEDLVLI YAFPKKTKKI SFEFKNDLFI EYSKILNDPK
     CRIFPKSPEI YIILDKIKQN CRESLTYLED LTESTIGILA SKYKFSDKKE NEYYLPYLEG
     NVYRYETKLK LKNYVDFSKH KNNEKLINLF MSPEKIFIRR IVNRQDRIMA SYGNIEGVVK
     KDLYVFVLKP DTPINYFYLL GILNSELISY IYIGKSAIAL KDDFRQTTLE ELRELPIVIP
     KNKNIINALT QLSKLRFELN DKLNENDRIF LENIIDSLVY GIYFQDLIPK EELNEICNEI
     NGIIKKYDEK SIDCLKYCQN IIKLLNTINT NELVRKIRNK N