ID   T2MU_MYCSP              Reviewed;         202 AA.
AC   P43642;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   28-JUN-2023, entry version 79.
DE   RecName: Full=Type II restriction enzyme MunI {ECO:0000303|PubMed:12654995};
DE            Short=R.MunI {ECO:0000303|PubMed:8181741};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease MunI;
DE   AltName: Full=Type-2 restriction enzyme MunI;
GN   Name=munIR {ECO:0000303|PubMed:8181741};
OS   Mycoplasma sp.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=2108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8181741; DOI=10.1016/0378-1119(94)90347-6;
RA   Siksnys V., Zareckaja N., Vaisvila R., Timinskas A., Stakenas P.,
RA   Butkus V., Janulaitis A.;
RT   "CAATTG-specific restriction-modification munI genes from Mycoplasma:
RT   sequence similarities between R.MunI and R.EcoRI.";
RL   Gene 142:1-8(1994).
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX   PubMed=10545092; DOI=10.1093/emboj/18.21.5805;
RA   Deibert M., Grazulis S., Janulaitis A., Siksnys V., Huber R.;
RT   "Crystal structure of MunI restriction endonuclease in complex with cognate
RT   DNA at 1.7 A resolution.";
RL   EMBO J. 18:5805-5816(1999).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CAATTG-3' and cleaves after C-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:10545092}.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10545092}.
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DR   EMBL; X76192; CAA53788.1; -; Genomic_DNA.
DR   PIR; S38901; S38901.
DR   PDB; 1D02; X-ray; 1.70 A; A/B=1-202.
DR   PDBsum; 1D02; -.
DR   AlphaFoldDB; P43642; -.
DR   SMR; P43642; -.
DR   REBASE; 1285; MunI.
DR   EvolutionaryTrace; P43642; -.
DR   PRO; PR:P43642; -.
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   CDD; cd22336; MunI-like; 1.
DR   Gene3D; 3.40.580.10; Eco RI Endonuclease, subunit A; 1.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   InterPro; IPR011336; Restrct_endonuc_II_EcoRI/MunI.
DR   InterPro; IPR022725; Restrct_endonuc_II_MunI.
DR   Pfam; PF11407; RestrictionMunI; 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..202
FT                   /note="Type II restriction enzyme MunI"
FT                   /id="PRO_0000077341"
FT   HELIX           12..20
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           27..34
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          38..45
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          50..53
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           60..65
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          94..101
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           111..114
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           118..126
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           128..138
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          147..154
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           155..158
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           160..170
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   STRAND          176..180
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           186..196
FT                   /evidence="ECO:0007829|PDB:1D02"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:1D02"
SQ   SEQUENCE   202 AA;  23389 MW;  7964F7C8EBFEC469 CRC64;
     MGKSELSGRL NWQALAGLKA SGAEQNLYNV FNAVFEGTKY VLYEKPKHLK NLYAQVVLPD
     DVIKEIFNPL IDLSTTQWGV SPDFAIENTE THKILFGEIK RQDGWVEGKD PSAGRGNAHE
     RSCKLFTPGL LKAYRTIGGI NDEEILPFWV VFEGDITRDP KRVREITFWY DHYQDNYFMW
     RPNESGEKLV QHFNEKLKKY LD
//