T2MU_MYCSP
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 25-MAY-2022, entry version 75.
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; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma;
OC unclassified 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 Gene3D; 3.40.580.10; -; 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; SSF52980; 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
