ID T2M4_NEIGO Reviewed; 286 AA. AC P31032; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 03-MAY-2023, entry version 120. DE RecName: Full=Type II restriction enzyme NgoMIV {ECO:0000303|PubMed:12654995}; DE Short=R.NgoMIV {ECO:0000303|PubMed:12654995}; DE EC=3.1.21.4; DE AltName: Full=Endonuclease NgoMIV; DE AltName: Full=Restriction enzyme NgoMI {ECO:0000303|PubMed:1321116}; DE Short=NgoMI {ECO:0000303|PubMed:1321116}; DE AltName: Full=Type-2 restriction enzyme NgoMIV; GN Name=ngoMIVR; OS Neisseria gonorrhoeae. OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=485; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RC STRAIN=MS11; RX PubMed=1321116; DOI=10.1128/jb.174.15.4899-4906.1992; RA Stein D.C., Chien R., Seifert H.S.; RT "Construction of a Neisseria gonorrhoeae MS11 derivative deficient in NgoMI RT restriction and modification."; RL J. Bacteriol. 174:4899-4906(1992). 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 (1.6 ANGSTROMS), AND SUBUNIT. RX PubMed=10966652; DOI=10.1038/79032; RA Deibert M., Grazulis S., Sasnauskas G., Siksnys V., Huber R.; RT "Structure of the tetrameric restriction endonuclease NgoMIV in complex RT with cleaved DNA."; RL Nat. Struct. Biol. 7:792-799(2000). CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double- CC stranded sequence 5'-GCCGGC-3' and cleaves after G-1. CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1321116}. 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; CC Note=Binds 2 magnesium ions per subunit.; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10966652}. CC -!- CAUTION: Was originally known as R.NgoMI. {ECO:0000305|PubMed:1321116}. 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; M86915; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B42709; B42709. DR RefSeq; WP_003688519.1; NZ_WHPL01000002.1. DR PDB; 1FIU; X-ray; 1.60 A; A/B/C/D=1-286. DR PDB; 4ABT; X-ray; 2.22 A; A/B=3-286. DR PDBsum; 1FIU; -. DR PDBsum; 4ABT; -. DR AlphaFoldDB; P31032; -. DR SMR; P31032; -. DR GeneID; 66753208; -. DR EvolutionaryTrace; P31032; -. DR PRO; PR:P31032; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; cd22340; NgoMIV-like; 1. DR Gene3D; 3.40.50.10010; Type-2 restriction enzyme NgoMIV; 1. DR InterPro; IPR015105; NgoMIV. DR InterPro; IPR037083; NgoMIV_sf. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR Pfam; PF09015; NgoMIV_restric; 1. DR SUPFAM; SSF52980; Restriction endonuclease-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Restriction system. FT CHAIN 1..286 FT /note="Type II restriction enzyme NgoMIV" FT /id="PRO_0000077347" FT BINDING 140 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 140 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT HELIX 4..18 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 38..50 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 62..81 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:1FIU" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 92..96 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:4ABT" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 109..112 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 113..121 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 125..131 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 179..189 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 194..196 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 197..208 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 225..232 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 233..237 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 239..243 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 246..256 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 259..270 FT /evidence="ECO:0007829|PDB:1FIU" FT STRAND 273..276 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 277..279 FT /evidence="ECO:0007829|PDB:1FIU" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:1FIU" SQ SEQUENCE 286 AA; 31760 MW; 6609772EF21083F6 CRC64; MNPLFTQERR IFHKKLLDGN ILATNNRGVV SNADGSNTRS FNIAKGIADL LHSETVSERL PGQTSGNAFE AICSEFVQSA FEKLQHIRPG DWNVKQVGSR NRLEIARYQQ YAHLTALAKA AEENPELAAA LGSDYTITPD IIVTRNLIAD AEINRNEFLV DENIATYASL RAGNGNMPLL HASISCKWTI RSDRAQNARS EGLNLVRNRK GRLPHIVVVT AEPTPSRISS IALGTGEIDC VYHFALYELE QILQSLNYED ALDLFYIMVN GKRLKDISDL PLDLAV //