T2N1_LENAE
ID T2N1_LENAE Reviewed; 317 AA.
AC P50187;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Type II restriction enzyme NaeI;
DE Short=R.NaeI;
DE EC=3.1.21.4 {ECO:0000269|PubMed:7892605};
DE AltName: Full=Endonuclease NaeI;
DE AltName: Full=Type-2 restriction enzyme NaeI;
GN Name=naeIR {ECO:0000303|PubMed:7698663};
OS Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix
OS aerocolonigenes).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=68170;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 23870 / DSM 40034 / BCRC 13661 / CBS 609.68 / CIP 107109 / JCM
RC 4614 / KCTC 9379 / NBRC 13195 / NCIMB 12944 / NRRL B-3298 / 701;
RX PubMed=7698663; DOI=10.1016/0378-1119(94)00806-4;
RA Taron C.H., van Cott E.M., Wilson G.G., Moran L.S., Slatko B.E.,
RA Hornstra L.J., Benner J.S., Kucera R.B., Guthrie E.P.;
RT "Cloning and expression of the NaeI restriction endonuclease-encoding gene
RT and sequence analysis of the NaeI restriction-modification system.";
RL Gene 155:19-25(1995).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF LEU-43.
RX PubMed=7892605; DOI=10.1126/science.7892605;
RA Jo K., Topal M.D.;
RT "DNA topoisomerase and recombinase activities in Nae I restriction
RT endonuclease.";
RL Science 267:1817-1820(1995).
RN [3]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-43.
RX PubMed=8932368; DOI=10.1093/nar/24.21.4171;
RA Jo K., Topal M.D.;
RT "Effects on NaeI-DNA recognition of the leucine to lysine substitution that
RT transforms restriction endonuclease NaeI to a topoisomerase: a model for
RT restriction endonuclease evolution.";
RL Nucleic Acids Res. 24:4171-4175(1996).
RN [4]
RP NOMENCLATURE, AND SUBTYPES.
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
RX PubMed=10856254; DOI=10.1093/emboj/19.12.3110;
RA Huai Q., Colandene J.D., Chen Y., Luo F., Zhao Y., Topal M.D., Ke H.;
RT "Crystal structure of NaeI-an evolutionary bridge between DNA endonuclease
RT and topoisomerase.";
RL EMBO J. 19:3110-3118(2000).
CC -!- FUNCTION: An E and P subtype restriction enzyme that recognizes the
CC double-stranded unmethylated sequence 5'-GCCGGC-3' and cleaves after C-
CC 3. {ECO:0000269|PubMed:7892605, ECO:0000269|PubMed:8932368,
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;
CC Evidence={ECO:0000269|PubMed:7892605, ECO:0000269|PubMed:8932368};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8932368}.
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DR EMBL; U09581; AAC43324.1; -; Genomic_DNA.
DR RefSeq; WP_030468110.1; NZ_JOFI01000013.1.
DR PDB; 1EV7; X-ray; 2.38 A; A/B=1-317.
DR PDB; 1IAW; X-ray; 2.40 A; A/B=1-317.
DR PDBsum; 1EV7; -.
DR PDBsum; 1IAW; -.
DR AlphaFoldDB; P50187; -.
DR SMR; P50187; -.
DR REBASE; 1294; NaeI.
DR REBASE; 165907; Nse506ORF6588P.
DR EvolutionaryTrace; P50187; -.
DR PRO; PR:P50187; -.
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 Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.600.10; -; 1.
DR InterPro; IPR037057; DNA_rep_MutH/T2_RE_sf.
DR InterPro; IPR015210; NaeI.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF09126; NaeI; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Restriction system.
FT CHAIN 1..317
FT /note="Type II restriction enzyme NaeI"
FT /id="PRO_0000077343"
FT MUTAGEN 43
FT /note="L->K: Change of function; becomes a topoisomerase
FT that recognizes single-stranded mismatched DNA."
FT /evidence="ECO:0000269|PubMed:7892605,
FT ECO:0000269|PubMed:8932368"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 30..44
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 65..77
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:1EV7"
FT TURN 123..126
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1IAW"
FT HELIX 196..207
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:1EV7"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1IAW"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:1EV7"
FT STRAND 288..298
FT /evidence="ECO:0007829|PDB:1EV7"
SQ SEQUENCE 317 AA; 35335 MW; 2D646D6814935B97 CRC64;
MTELPLQFAE PDDDLERVRA TLYSLDPDGD RTAGVLRDTL DQLYDGQRTG RWNFDQLHKT
EKTHMGTLVE INLHREFQFG DGFETDYEIA GVQVDCKFSM SQGAWMLPPE SIGHICLVIW
ASDQQCAWTA GLVKVIPQFL GTANRDLKRR LTPEGRAQVV KLWPDHGKLQ ENLLLHIPGD
VRDQIFSAKS SRGNQHGQAR VNELFRRVHG RLIGRAVIAT VAQQDDFMKR VRGSGGARSI
LRPEGIIILG HQDNDPKVAN DLGLPVPRKG QVVAARVVPA DEGDQRQTAE IQGRRWAVAV
PGDPIVEAPV VPRKSAE
