ID   T2A1_ACEPA              Reviewed;         375 AA.
AC   O52703;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Type II restriction enzyme ApaLI {ECO:0000303|PubMed:12654995};
DE            Short=R.ApaLI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease ApaLI;
DE   AltName: Full=Type-2 restriction enzyme ApaLI;
GN   Name=apaLIR {ECO:0000303|PubMed:9862476};
OS   Acetobacter pasteurianus (Acetobacter turbidans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 12875;
RX   PubMed=9862476; DOI=10.1007/s004380050890;
RA   Xu S.-Y., Xiao J.-P., Ettwiller L., Holden M., Aliotta J., Poh C.L.,
RA   Dalton M., Robinson D.P., Petronzio T.R., Moran L., Ganatra M., Ware J.,
RA   Slatko B., Benner J. II;
RT   "Cloning and expression of the ApaLI, NspI, NspHI, SacI, ScaI, and SapI
RT   restriction-modification systems in Escherichia coli.";
RL   Mol. Gen. Genet. 260:226-231(1998).
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 subtype P restriction enzyme that recognizes the double-
CC       stranded sequence 5'-GTGCAC-3' and cleaves after G-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:9862476}.
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; AF044847; AAC97181.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52703; -.
DR   BRENDA; 3.1.21.4; 44.
DR   PRO; PR:O52703; -.
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.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..375
FT                   /note="Type II restriction enzyme ApaLI"
FT                   /id="PRO_0000077275"
SQ   SEQUENCE   375 AA;  41730 MW;  9E4FFBB05279A94C CRC64;
     MTTRQRLSAE RSQQLTRLLT ITKTANMRAL MEASELAKVI ALVAVDIGKS DEMARAFPVL
     WPKISPQQEY YATAVDWFTN PDETVTSFDV VDMLDAGTSL DQDFMTYLKC LTELHKRRRK
     YGLILQRQPL PTMVQVSPRA LMEYGPDFPP EALASWLTWR KFFYDLDNRS AQETGYLFEP
     ILAAAIGGEA KSARERVVRR TDDPTKGRQV DCWKVLPDGT PLAYELKLRV TIAASGQGRF
     GEELSFARDC SSSGAKPILV VLDPTENDKL TGLQAAYREV GGAAYVGDAA WAHLEDEAGA
     TMASFIERYV RVPVASVSSF ERVIEGDATK RSLILQDLQA RLDGNELTIS LGGHQRLVER
     HEDQSLAADG DDDSE