ID   T2S1_STRCS              Reviewed;         227 AA.
AC   O52691;
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 ScaI {ECO:0000303|PubMed:12654995};
DE            Short=R.ScaI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease ScaI;
DE   AltName: Full=Type-2 restriction enzyme ScaI;
GN   Name=scaIR {ECO:0000303|PubMed:9862476};
OS   Streptomyces caespitosus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=53502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-AGTACT-3' and cleaves after T-3.
CC       {ECO:0000269|PubMed:9862476, 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; AF044681; AAC97177.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52691; -.
DR   BindingDB; O52691; -.
DR   ChEMBL; CHEMBL5782; -.
DR   DrugCentral; O52691; -.
DR   REBASE; 1628; ScaI.
DR   BRENDA; 3.1.21.4; 5987.
DR   PRO; PR:O52691; -.
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; IPR019069; Restrct_endonuc_II_ScaI.
DR   Pfam; PF09569; RE_ScaI; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..227
FT                   /note="Type II restriction enzyme ScaI"
FT                   /id="PRO_0000077367"
FT   REGION          12..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   227 AA;  25464 MW;  A4E48072756B6009 CRC64;
     MINDQLPRWV REARVGTRTG GPAMRPKTSD SPYFGWDSED WPEVTRQLLS EQPLSGDTLV
     DAVLASWESI FESRLGSGFH IGTQIRPTPQ VMGFLLHALI PLELANGDPS WRADLNSSEK
     DLVYQPDHKY SIEMKTSSHK DQIFGNRSFG VENPGKGKKA KDGYYVAVNF EKWSDAPGRL
     PRIRTIRYGW LDHTDWVAQK SQTGQQSSLP AVVSNTQLLA IHTGGQR