ID   T2M1_MORSP              Reviewed;         262 AA.
AC   P11405;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-MAY-2023, entry version 96.
DE   RecName: Full=Type II restriction enzyme MspI {ECO:0000303|PubMed:12654995};
DE            Short=R.MspI;
DE            EC=3.1.21.4 {ECO:0000305|PubMed:2471145};
DE   AltName: Full=Endonuclease MspI;
DE   AltName: Full=Type-2 restriction enzyme MspI;
GN   Name=mspIR;
OS   Moraxella sp.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 49670;
RX   PubMed=2471145; DOI=10.1093/nar/17.8.3001;
RA   Lin P.M., Lee C.H., Roberts R.J.;
RT   "Cloning and characterization of the genes encoding the MspI restriction
RT   modification system.";
RL   Nucleic Acids Res. 17:3001-3011(1989).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPE.
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 P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CCGG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2471145}.
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         Evidence={ECO:0000305|PubMed:2471145};
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DR   EMBL; X14191; CAA32394.1; -; Genomic_DNA.
DR   PIR; S04187; NDKE2M.
DR   PDB; 1SA3; X-ray; 1.95 A; A/B=1-262.
DR   PDB; 1YFI; X-ray; 2.70 A; A/B=1-262.
DR   PDBsum; 1SA3; -.
DR   PDBsum; 1YFI; -.
DR   AlphaFoldDB; P11405; -.
DR   SMR; P11405; -.
DR   REBASE; 1277; MspI.
DR   EvolutionaryTrace; P11405; -.
DR   PRO; PR:P11405; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR015291; Restrct_endonuc_II_MspI.
DR   Pfam; PF09208; Endonuc-MspI; 1.
DR   SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..262
FT                   /note="Type II restriction enzyme MspI"
FT                   /id="PRO_0000077338"
FT   HELIX           4..12
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           15..17
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           23..41
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           57..69
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          111..124
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           133..140
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           146..157
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           176..178
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           179..188
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          202..210
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          213..221
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           222..234
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   HELIX           239..242
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          252..255
FT                   /evidence="ECO:0007829|PDB:1SA3"
FT   STRAND          258..262
FT                   /evidence="ECO:0007829|PDB:1SA3"
SQ   SEQUENCE   262 AA;  29829 MW;  E724275DCE50E6E8 CRC64;
     MRTELLSKLY DDFGIDQLPH TQHGVTSDRL GKLYEKYILD IFKDIESLKK YNTNAFPQEK
     DISSKLLKAL NLDLDNIIDV SSSDTDLGRT IAGGSPKTDA TIRFTFHNQS SRLVPLNIKH
     SSKKKVSIAE YDVETICTGV GISDGELKEL IRKHQNDQSA KLFTPVQKQR LTELLEPYRE
     RFIRWCVTLR AEKSEGNILH PDLLIRFQVI DREYVDVTIK NIDDYVSDRI AEGSKARKPG
     FGTGLNWTYA SGSKAKKMQF KG
//