T2N4_NEILA
ID T2N4_NEILA Reviewed; 243 AA.
AC P50183;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Type II restriction enzyme NlaIV {ECO:0000303|PubMed:12654995};
DE Short=R.NlaIV {ECO:0000303|PubMed:8190068};
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease NlaIV;
DE AltName: Full=Type-2 restriction enzyme NlaIV;
GN Name=nlaIVR;
OS Neisseria lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC A7515;
RX PubMed=8190068; DOI=10.1007/bf00283872;
RA Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RT "The NlaIV restriction and modification genes of Neisseria lactamica are
RT flanked by leucine biosynthesis genes.";
RL Mol. Gen. Genet. 243:24-31(1994).
RN [2]
RP ERRATUM OF PUBMED:8190068.
RA Lau P.C.K., Forghani F., Labbe D., Bergeron H., Brousseau R., Holtke H.J.;
RL Mol. Gen. Genet. 244:167-167(1994).
RN [3]
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 sequence 5'-GGNNCC-3' and cleaves after N-3.
CC {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;
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DR EMBL; U06074; AAA53238.1; -; Genomic_DNA.
DR PIR; S43887; S43887.
DR RefSeq; WP_003708504.1; NZ_QQML01000002.1.
DR PDB; 6QM2; X-ray; 2.80 A; A=1-243.
DR PDBsum; 6QM2; -.
DR AlphaFoldDB; P50183; -.
DR SMR; P50183; -.
DR REBASE; 1342; NlaIV.
DR PRO; PR:P50183; -.
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; IPR019064; Restrct_endonuc_II_NlaIV.
DR Pfam; PF09564; RE_NgoBV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Restriction system.
FT CHAIN 1..243
FT /note="Type II restriction enzyme NlaIV"
FT /id="PRO_0000077350"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:6QM2"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 188..201
FT /evidence="ECO:0007829|PDB:6QM2"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6QM2"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 212..224
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6QM2"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6QM2"
SQ SEQUENCE 243 AA; 28826 MW; 3068E972D6736A49 CRC64;
MIKLTAQQIF DKLLDEEKIL SANGQIRFFL GDVDIIVKQK DVVGNIIQEW LGGWLRKREI
EFDVSTNTQM PPDFFLNKKD RSRELLEVKA FNRNASPGFD IADFKMYSDE IIHKPYMLDV
DYLIFGYDMD DNGNVTIKDL WLKKVWQITR SMDGWAINLQ VKKGVVHKIR PGVWYSINKK
NMPMFECLED FVSAIEETVY QNPATRHNAS LWKRKFEEAY KKHYNRSISI PRWHEIAHKY
KKK
