T2M4_NEIGO
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-AUG-2022, entry version 117.
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; Proteobacteria; 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}.
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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 Gene3D; 3.40.50.10010; -; 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; SSF52980; 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
