T2P7_PSEAI
ID T2P7_PSEAI Reviewed; 246 AA.
AC P05104;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Type II restriction enzyme PaeR7I {ECO:0000303|PubMed:12654995};
DE Short=R.PaeR7I;
DE EC=3.1.21.4 {ECO:0000305|PubMed:3001639};
DE AltName: Full=Endonuclease PaeR7I;
DE AltName: Full=Type-2 restriction enzyme PaeR7I;
GN Name=paeR7IR;
OS Pseudomonas aeruginosa.
OG Plasmid pMG7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=3001639; DOI=10.1093/nar/13.23.8441;
RA Theriault G., Roy P.H., Howard K.A., Benner J.S., Brooks J.E., Waters A.F.,
RA Gingeras T.R.;
RT "Nucleotide sequence of the PaeR7 restriction/modification system and
RT partial characterization of its protein products.";
RL Nucleic Acids Res. 13:8441-8461(1985).
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 sequence 5'-CTCGAG-3' and cleaves after C-1.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:3001639}.
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:0000305|PubMed:3001639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the XhoI type II restriction endonuclease
CC family. {ECO:0000305}.
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DR EMBL; X03274; CAA27026.1; -; Genomic_DNA.
DR PIR; S07935; NDPS7A.
DR RefSeq; WP_004356305.1; NZ_WOAW01000029.1.
DR AlphaFoldDB; P05104; -.
DR REBASE; 1451; PaeR7I.
DR PRO; PR:P05104; -.
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; IPR007636; Restrct_endonuc_II_XhoI.
DR Pfam; PF04555; XhoI; 1.
DR PIRSF; PIRSF000994; Restrict_endonuc_II_XhoI; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW Plasmid; Restriction system.
FT CHAIN 1..246
FT /note="Type II restriction enzyme PaeR7I"
FT /id="PRO_0000077353"
SQ SEQUENCE 246 AA; 27279 MW; 3BC63AC987BDF3BA CRC64;
MALDLVDYEQ KARDAVKAFW GNREAARQKQ IESGKADQGE RAGVTGGKNM DGFLALVLDV
IKANGLAHAE IHQNRAMLTL PGYFRPTKLW DLLVIYKGEL IAAIELKSHV GPSFSNNFNN
RTEEAIGTAH DLWTAYREEA FGKQPRPFVG WLMMVEDAPE SRRPVRDSSP HFPVFEEFKG
ASYLTRYDLL CQRLVQEQLY TTAAVIAAER SAVDTGNFTE LSSMTSLKTF VSALAGHIAA
EAARLG