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 03-MAY-2023, entry version 71. 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; Pseudomonadota; 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 / RC NCTC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Restriction endonuclease-like; 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 //