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MTS1_STRCS
ID   MTS1_STRCS              Reviewed;         304 AA.
AC   O52692;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Type II methyltransferase M.ScaI {ECO:0000303|PubMed:12654995};
DE            Short=M.ScaI {ECO:0000303|PubMed:9862476};
DE            EC=2.1.1.113 {ECO:0000250|UniProtKB:Q04845};
DE   AltName: Full=Modification methylase ScaI;
DE   AltName: Full=N-4 cytosine-specific methyltransferase ScaI;
GN   Name=scaIM {ECO:0000303|PubMed:9862476};
OS   Streptomyces caespitosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=53502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RX   PubMed=9862476; DOI=10.1007/s004380050890;
RA   Xu S.-Y., Xiao J.-P., Ettwiller L., Holden M., Aliotta J., Poh C.L.,
RA   Dalton M., Robinson D.P., Petronzio T.R., Moran L., Ganatra M., Ware J.,
RA   Slatko B., Benner J. II;
RT   "Cloning and expression of the ApaLI, NspI, NspHI, SacI, ScaI, and SapI
RT   restriction-modification systems in Escherichia coli.";
RL   Mol. Gen. Genet. 260:226-231(1998).
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: A methylase that recognizes the double-stranded sequence 5'-
CC       AGTACT-3', methylates C-5 on both strands, and protects the DNA from
CC       cleavage by the ScaI endonuclease. {ECO:0000303|PubMed:12654995,
CC       ECO:0000305|PubMed:9862476}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC         Evidence={ECO:0000250|UniProtKB:Q04845};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF044681; AAC97178.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52692; -.
DR   SMR; O52692; -.
DR   REBASE; 3498; M.ScaI.
DR   BRENDA; 2.1.1.113; 5987.
DR   PRO; PR:O52692; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-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; IPR002941; DNA_methylase_N4/N6.
DR   InterPro; IPR017985; MeTrfase_CN4_CS.
DR   InterPro; IPR001091; RM_Methyltransferase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01555; N6_N4_Mtase; 1.
DR   PRINTS; PR00508; S21N4MTFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00093; N4_MTASE; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..304
FT                   /note="Type II methyltransferase M.ScaI"
FT                   /id="PRO_0000087933"
SQ   SEQUENCE   304 AA;  34187 MW;  F589CF18B62C3634 CRC64;
     MSGRDFGYVI QSSAALWNRL STFSQRGKAL DTRLADIKKA LGKPYYETSD VLLYHGDSLE
     LLKSMPQQIF DLTVTSPPYN IGKEYEGVLS IEEYISWCET WMSRVHRATS AGGAFWLNVG
     YVPVPNQGKA VPIPYLLWDK SPFYMIQEVV WNYGAGVASR KSFSPRNEKF LWYVRDPLNY
     YFDLDSVRDP NVKYPNQKKN GKLKCNPLGK NPTDVWQFPK VTSGAKRSSV ERTAHPAQFP
     SAVIERVIKA CSPSDGVILD PFLGSGTTSL TARKQGRCSV GIEIREDYLD IAVGRLEAEA
     QSLF
 
 
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