ID   T2AP_ARTPN              Reviewed;         324 AA.
AC   D4ZX34;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Type II restriction enzyme AplI {ECO:0000303|PubMed:12654995};
DE            Short=R.AplI;
DE            EC=3.1.21.4 {ECO:0000269|PubMed:23563565};
DE   AltName: Full=Endonuclease AplI;
DE   AltName: Full=Type-2 restriction enzyme AplI;
GN   Name=aplIR; ORFNames=NIES39_K04640;
OS   Arthrospira platensis (strain NIES-39 / UTEX 3086 / IAM M-135) (Spirulina
OS   platensis).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Arthrospira.
OX   NCBI_TaxID=696747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-39 / UTEX 3086 / IAM M-135;
RX   PubMed=20203057; DOI=10.1093/dnares/dsq004;
RA   Fujisawa T., Narikawa R., Okamoto S., Ehira S., Yoshimura H., Suzuki I.,
RA   Masuda T., Mochimaru M., Takaichi S., Awai K., Sekine M., Horikawa H.,
RA   Yashiro I., Omata S., Takarada H., Katano Y., Kosugi H., Tanikawa S.,
RA   Ohmori K., Sato N., Ikeuchi M., Fujita N., Ohmori M.;
RT   "Genomic structure of an economically important cyanobacterium, Arthrospira
RT   (Spirulina) platensis NIES-39.";
RL   DNA Res. 17:85-103(2010).
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   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND PH DEPENDENCE.
RC   STRAIN=NIES-39 / UTEX 3086 / IAM M-135;
RX   PubMed=23563565; DOI=10.1271/bbb.120919;
RA   Shiraishi H., Tabuse Y.;
RT   "The AplI restriction-modification system in an edible cyanobacterium,
RT   Arthrospira (Spirulina) platensis NIES-39, recognizes the nucleotide
RT   sequence 5'-CTGCAG-3'.";
RL   Biosci. Biotechnol. Biochem. 77:782-788(2013).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CTGCAG-3' and cleaves after A-5.
CC       {ECO:0000269|PubMed:23563565}.
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:23563565};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by K(+) and Na(+) ions, whereas NH(4)(+)
CC       ions appear to inhibit endonuclease activity.
CC       {ECO:0000269|PubMed:23563565}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 9.5. {ECO:0000269|PubMed:23563565};
CC   -!- SIMILARITY: Belongs to the BsuBI/PstI type II restriction endonuclease
CC       family. {ECO:0000305}.
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DR   EMBL; AP011615; BAI92109.1; -; Genomic_DNA.
DR   RefSeq; WP_014276337.1; NC_016640.1.
DR   AlphaFoldDB; D4ZX34; -.
DR   SMR; D4ZX34; -.
DR   STRING; 696747.NIES39_K04640; -.
DR   REBASE; 25962; AplI.
DR   EnsemblBacteria; BAI92109; BAI92109; NIES39_K04640.
DR   KEGG; arp:NIES39_K04640; -.
DR   PATRIC; fig|696747.3.peg.2190; -.
DR   eggNOG; COG0827; Bacteria.
DR   HOGENOM; CLU_074525_0_0_3; -.
DR   OMA; RETHAWI; -.
DR   OrthoDB; 159044at2; -.
DR   PRO; PR:D4ZX34; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:UniProtKB.
DR   GO; GO:0009307; P:DNA restriction-modification system; IDA:UniProtKB.
DR   Gene3D; 1.10.10.1820; -; 1.
DR   Gene3D; 3.40.1350.80; -; 1.
DR   InterPro; IPR041963; BsuBI/PstI_C_sf.
DR   InterPro; IPR041454; BsuBI/PstI_N.
DR   InterPro; IPR041962; BsuBI/PstI_N_sf.
DR   InterPro; IPR009528; Restrct_endonuc_II_BsuBI_C.
DR   Pfam; PF06616; BsuBI_PstI_RE; 1.
DR   Pfam; PF17728; BsuBI_PstI_RE_N; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW   Restriction system.
FT   CHAIN           1..324
FT                   /note="Type II restriction enzyme AplI"
FT                   /id="PRO_0000423856"
SQ   SEQUENCE   324 AA;  37395 MW;  F54C3C8ADC2BB33C CRC64;
     MSSNNPTPNL EQLMLEARQL MKDLGLPDKM QGDTPIFVLL VMLDMKPAKS WSEANNQKWG
     ITPLMNKMRE LGFKNLAPNT RENIRDDCVG QLVDAELATE NPDKPRPKNS PKYCYQINQE
     VLYLVKKIGS ADYPIALNNF LSNYQTIKHK YQAKRQSQRL NVKIAHNFSV SIAPGGQGVL
     IKSVLQDFCK YFNIDKVLYI DNTVDTARGY SPFIDENLIN YLGIDIDKFK NSYDKPDIVL
     YKSDNKYLII IEAVKTGGAI NVERRDRLLS LFENVDVKLS FVNAFESFKE LKRLTKEITR
     ETHAWIMEFP DHMIHFNGDQ YLFH