T1S1_METJA
ID T1S1_METJA Reviewed; 425 AA.
AC Q57594;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 3.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Type I restriction enzyme MjaVII specificity subunit {ECO:0000305};
DE Short=S protein;
DE AltName: Full=Type I specificity subunit S.MjaVII {ECO:0000303|PubMed:12654995};
DE Short=S.MjaVII {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type-1 restriction enzyme MjaXIP specificity subunit;
DE Short=S.MjaXIP;
GN OrderedLocusNames=MJ0130;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
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 SEQUENCE REVISION.
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.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
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).
RN [4] {ECO:0007744|PDB:1YF2}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=15728358; DOI=10.1073/pnas.0409851102;
RA Kim J.-S., DeGiovanni A., Jancarik J., Adams P.D., Yokota H., Kim R.,
RA Kim S.-H.;
RT "Crystal structure of DNA sequence specificity subunit of a type I
RT restriction-modification enzyme and its functional implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3248-3253(2005).
CC -!- FUNCTION: The specificity (S) subunit of a type I restriction enzyme;
CC this subunit dictates DNA sequence specificity. The M and S subunits
CC together form a methyltransferase (MTase) that methylates A-3 on the
CC top and bottom strands of the sequence 5'-CAAN(7)TGG-3'. In the
CC presence of the R subunit the complex can also act as an endonuclease,
CC binding to the same target sequence but cutting the DNA some distance
CC from this site. Whether the DNA is cut or modified depends on the
CC methylation state of the target sequence. When the target site is
CC unmodified, the DNA is cut. When the target site is hemimethylated, the
CC complex acts as a maintenance MTase modifying the DNA so that both
CC strands become methylated (PubMed:12654995) (Probable). After locating
CC a non-methylated recognition site, the enzyme complex serves as a
CC molecular motor that translocates DNA in an ATP-dependent manner until
CC a collision occurs that triggers cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P05719, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:15728358}.
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000305|PubMed:15728358}.
CC -!- DOMAIN: Contains two target DNA recognition domains (TDR), each
CC specifying recognition of one of the two defined components of the
CC target sequence (Probable). The TDRs show high structural similarity
CC and each forms a globular structure. The two TDRs are separated by 2
CC long, conserved antiparallel helices that form a coiled coil structure.
CC These conserved regions may act as a molecular ruler for the separation
CC between the two recognized DNA sequences (PubMed:15728358).
CC {ECO:0000269|PubMed:15728358, ECO:0000305|PubMed:15728358}.
CC -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC multifunctional systems which require ATP, S-adenosyl methionine and
CC Mg(2+) as cofactors and, in addition to their endonucleolytic and
CC methylase activities, are potent DNA-dependent ATPases.
CC {ECO:0000250|UniProtKB:P05719}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB98112.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L77117; AAB98112.1; ALT_FRAME; Genomic_DNA.
DR PDB; 1YF2; X-ray; 2.40 A; A/B=1-425.
DR PDBsum; 1YF2; -.
DR AlphaFoldDB; Q57594; -.
DR SMR; Q57594; -.
DR STRING; 243232.MJ_0130; -.
DR REBASE; 154997; S.VscVS12ORF1031P.
DR REBASE; 182833; S.Bli37I.
DR REBASE; 191882; S2.Apa1468ORF2954P.
DR REBASE; 203440; S3.Lpl434ORF2272P.
DR REBASE; 203797; S.Ppe892ORF47P.
DR REBASE; 203829; S.Bli141ORF4598P.
DR REBASE; 203832; S.Bli27ORF807P.
DR REBASE; 290906; S.Msa27082ORF3559P.
DR REBASE; 3901; S.MjaVII.
DR EnsemblBacteria; AAB98112; AAB98112; MJ_0130.
DR KEGG; mja:MJ_0130; -.
DR eggNOG; arCOG02626; Archaea.
DR HOGENOM; CLU_021095_10_3_2; -.
DR InParanoid; Q57594; -.
DR OMA; RMSITND; -.
DR PhylomeDB; Q57594; -.
DR EvolutionaryTrace; Q57594; -.
DR PRO; PR:Q57594; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.220.20; -; 2.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR Pfam; PF01420; Methylase_S; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA-binding; Reference proteome;
KW Restriction system.
FT CHAIN 1..425
FT /note="Type I restriction enzyme MjaVII specificity
FT subunit"
FT /id="PRO_0000106708"
FT REGION 9..168
FT /note="Target recognition domain 1"
FT /evidence="ECO:0000305|PubMed:15728358"
FT REGION 169..208
FT /note="Central conserved region (CCR)"
FT /evidence="ECO:0000305|PubMed:15728358"
FT REGION 209..368
FT /note="Target recognition domain 2"
FT /evidence="ECO:0000305|PubMed:15728358"
FT REGION 369..418
FT /note="Distal conserved region (DCR)"
FT /evidence="ECO:0000305|PubMed:15728358"
FT COILED 169..208
FT /evidence="ECO:0000269|PubMed:15728358,
FT ECO:0007744|PDB:1YF2"
FT COILED 369..418
FT /evidence="ECO:0000269|PubMed:15728358,
FT ECO:0007744|PDB:1YF2"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 25..28
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1YF2"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:1YF2"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 168..209
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:1YF2"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:1YF2"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 284..289
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 337..346
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 348..355
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1YF2"
FT HELIX 378..416
FT /evidence="ECO:0007829|PDB:1YF2"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1YF2"
SQ SEQUENCE 425 AA; 48568 MW; E196A947574FE91D CRC64;
MFYKEENFKK TEIGEIPEDW EIVELKDVCK KIKAGGTPKT SVEEYYKNGT IPFVKIEDIT
NSNKYLTNTK IKITEEGLNN SNAWIVPKNS VLFAMYGSIG ETAINKIEVA TNQAILGIIP
KDNILESEFL YYILAKNKNY YSKLGMQTTQ KNLNAQIVKS FKIPLPPLEE QKQIAKILTK
IDEGIEIIEK SINKLERIKK GLMHKLLTKG IGHSRFKKSE IGEIPEDWEV FEIKDIFEVK
TGTTPSTKKS EYWENGEINW ITPLDLSRLN EKIYIGSSER KVTKIALEKC NLNLIPKGSI
IISTRAPVGY VAVLTVESTF NQGCKGLFQK NNDSVNTEFY AYYLKFKKNL LENLSGGSTF
KELSKSMLEN FKIPLPPLEE QKQIAKILSS VDKSIELKKQ KKEKLQRMKK KIMELLLTGK
VRVKT
