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T2M1_MORBO
ID   T2M1_MORBO              Reviewed;         280 AA.
AC   P34719;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Type II restriction enzyme MboI {ECO:0000303|PubMed:12654995};
DE            Short=R.MboI {ECO:0000303|PubMed:8506128};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease MboI;
DE   AltName: Full=Type-2 restriction enzyme MboI;
GN   Name=mboIR; Synonyms=mboB {ECO:0000303|PubMed:8506128};
OS   Moraxella bovis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Moraxella.
OX   NCBI_TaxID=476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, AND FUNCTION.
RC   STRAIN=ATCC 10900 / DSM 6328 / CIP 70.40 / JCM 17254 / LMG 986 / NCTC
RC   11013;
RX   PubMed=8506128; DOI=10.1093/nar/21.10.2309;
RA   Ueno T., Ito H., Kimizuka F., Kotani H., Nakajima K.;
RT   "Gene structure and expression of the MboI restriction-modification
RT   system.";
RL   Nucleic Acids Res. 21:2309-2313(1993).
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 unmethylated sequence 5'-GATC-3' and cleaves before G-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8506128}.
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   -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; D13968; BAA03072.1; -; Genomic_DNA.
DR   PIR; S35648; S35648.
DR   AlphaFoldDB; P34719; -.
DR   STRING; 476.B0182_10405; -.
DR   PRO; PR:P34719; -.
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; IPR021191; Restrct_endonuc_II_DpnII.
DR   InterPro; IPR007637; Restrct_endonuc_II_DpnII-like.
DR   Pfam; PF04556; DpnII; 1.
DR   PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Restriction system.
FT   CHAIN           1..280
FT                   /note="Type II restriction enzyme MboI"
FT                   /id="PRO_0000077330"
SQ   SEQUENCE   280 AA;  32248 MW;  D208B25B5C078C72 CRC64;
     MKLAFDDFLN SMSETNTTLD YFTDFDKVKK NVAQIEIHLN QLNYLLGKDD LKQAVYDLYA
     ECPNAFSILE ILIAVRKKEQ KKSLDEKGQV VTLNSYFQSA DKIIDFLNNT GLADVFRDKN
     IKNLVDYVFG IEVGLDTNAR KNRGGDNMSK AVQLLFDNAD IYYKKEVRNT IFTDIESLGA
     DVKQFDFVIK TKRKTYVIET NYYNSGGSKL NEVARAYTDV APKINQYSQY EFVWITDGQG
     WKTAKNKLQE AYTHIPSVYN LYTLHGFIEQ LNSEGVIKDW
 
 
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