ID   T2M2_MORBO              Reviewed;         416 AA.
AC   P23191;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Type II restriction enzyme MboII {ECO:0000303|PubMed:12654995};
DE            Short=R.MboII {ECO:0000303|PubMed:2020540};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease MboII;
DE   AltName: Full=Type IIS restriction enzyme MboII;
DE   AltName: Full=Type-2 restriction enzyme MboII;
GN   Name=mboIIR {ECO:0000303|PubMed:2020540};
OS   Moraxella bovis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-5; 7-12 AND
RP   15-19.
RC   STRAIN=ATCC 10900 / DSM 6328 / CIP 70.40 / JCM 17254 / LMG 986 / NCTC
RC   11013;
RX   PubMed=2020540; DOI=10.1093/nar/19.5.1007;
RA   Bocklage H., Heeger K., Mueller-Hill B.;
RT   "Cloning and characterization of the MboII restriction-modification
RT   system.";
RL   Nucleic Acids Res. 19:1007-1013(1991).
RN   [2]
RP   NOMENCLATURE, AND SUBTYPES.
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: An E and S subtype restriction enzyme that recognizes the
CC       double-stranded sequences 5'-GAAGA-3' and 5'-TCTTC-3' and cleaves
CC       respectively 13 bases after G-1 and 7 bases before T-1, leaving a
CC       single 3' protruding nucleotide. {ECO:0000303|PubMed:12654995}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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DR   EMBL; X56977; CAA40298.1; -; Genomic_DNA.
DR   PIR; S26836; S26836.
DR   AlphaFoldDB; P23191; -.
DR   REBASE; 1205; MboII.
DR   PRIDE; P23191; -.
DR   PRO; PR:P23191; -.
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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW   Restriction system.
FT   CHAIN           1..416
FT                   /note="Type II restriction enzyme MboII"
FT                   /id="PRO_0000077331"
SQ   SEQUENCE   416 AA;  48617 MW;  C5A0008775B635CF CRC64;
     MKNYVSNINL GNSSLKFIDE RLQSENYRGI HLSQHNRYDL PKLIDILTLL NKHAPNQSLM
     QIRTTDISKR PQNIPEEQSY AEFCNEAKSL TNIGTQDAMR KNLFVDFARM GLINRYNDKK
     VLTDPFKRGV TKYVALSDMG VKLIDPKLDI LSKNLIFSKS LNKLLTGFVE DVLSLLTNSD
     LKEISFDEFM LFVSAMNCNF NFSISTEQCE SLIKEYRLLS RVQKNAVIDT LKSELIPDNF
     NGDKKDKRDY HNWANENQQI WTLFENIPFF IMEKDSRKLI LITSDVDLSK YSKSKMKRSQ
     QAKNDYFKHH KVNKIKGYEL DHIIPLLEAE SVDEYRYLDN WLNLLYIDGK THAIKSQSGS
     KYYIFTFDDN DYNQIYFLDT QGDKLSINND DTALFDKNKV PKIYEYNQNF INAKTS