T1SH_METJA
ID T1SH_METJA Reviewed; 432 AA.
AC Q60296;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Type I restriction enzyme MjaIX specificity subunit {ECO:0000305};
DE Short=S protein;
DE AltName: Full=Type I specificity subunit S.MjaIX {ECO:0000303|PubMed:12654995};
DE Short=S.MjaIX {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type-1 restriction enzyme MjaXP specificity subunit;
DE Short=S.MjaXP;
GN Name=hsdS; OrderedLocusNames=MJECL41;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OG Plasmid large 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.
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: 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 A-2 on the bottom strand of the sequence 5'-CCAN(5)GTR-3'. In
CC the presence of the R subunit the complex can also act as an
CC endonuclease, binding to the same target sequence but cutting the DNA
CC some distance from this site. Whether the DNA is cut or modified
CC depends on the methylation state of the target sequence. When the
CC target site is unmodified, the DNA is cut. When the target site is
CC hemimethylated, the complex acts as a maintenance MTase modifying the
CC DNA so that both strands become methylated. After locating a non-
CC methylated recognition site, the enzyme complex serves as a molecular
CC motor that translocates DNA in an ATP-dependent manner until a
CC collision occurs that triggers cleavage. {ECO:0000250|UniProtKB:P05719,
CC ECO:0000303|PubMed:12654995}.
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000250|UniProtKB:P05719}.
CC -!- DOMAIN: Contains two DNA recognition domains, each specifying
CC recognition of one of the two defined components of the target
CC sequence. {ECO:0000250|UniProtKB:P05719}.
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}.
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DR EMBL; L77118; AAC37110.1; -; Genomic_DNA.
DR PIR; H64514; H64514.
DR AlphaFoldDB; Q60296; -.
DR SMR; Q60296; -.
DR STRING; 243232.MJ_ECL41; -.
DR REBASE; 191890; S2.Apa1468ORF3072P.
DR REBASE; 3909; S.MjaIX.
DR EnsemblBacteria; AAC37110; AAC37110; MJ_ECL41.
DR KEGG; mja:MJ_ECL41; -.
DR eggNOG; arCOG02628; Archaea.
DR HOGENOM; CLU_021095_2_3_2; -.
DR InParanoid; Q60296; -.
DR OMA; KRWFVDF; -.
DR PhylomeDB; Q60296; -.
DR PRO; PR:Q60296; -.
DR Proteomes; UP000000805; Plasmid large ECE.
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 3: Inferred from homology;
KW DNA-binding; Plasmid; Reference proteome; Restriction system.
FT CHAIN 1..432
FT /note="Type I restriction enzyme MjaIX specificity subunit"
FT /id="PRO_0000198053"
SQ SEQUENCE 432 AA; 50160 MW; 84CD44CF20EBC42C CRC64;
MLFMVKFRWE TEFKETDIGK IPKDWDVKKI KDIGEVAGGS TPSTKIKEYW GGDIPWITPK
DLANYEYIYI SRGERNITEK AVKECSLRIF PKGTILLTSR APIGYVAIAK NPLTTNQGFR
NIIPKDGVVS EYLYYLFKTK TMSEYLKDIS GGSTFPELKG STLKEVEIPY PSPEEQQKIA
TVLSYFDDLI ENKKKQNEIL EKIALELFKN WFIDFEPFKN EEFVYNDELD KEIPKGWEVK
RLGDILKVES GSNAPQREIY FENAKIPFVR VKHLVKGVCI ESSDFINELA LKDYKMKLYN
EKSIIFQKSG ESLKEARVNI VPFKFTAVNH LAVIDSSMLN EKHYFIYCLL RFLLKEIVYS
VKGTTLPYLK ISDIENKYII IPPQPILQKF HSLVQPLFEK IINNQKQIMV LKKIRDALLP
KLVFGELRVE EL
