ID   T2BA_ANEAE              Reviewed;         354 AA.
AC   P19887;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-MAY-2023, entry version 68.
DE   RecName: Full=Type II restriction enzyme BanI {ECO:0000303|PubMed:12654995};
DE            Short=R.BanI;
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease BanI;
DE   AltName: Full=Type-2 restriction enzyme BanI;
GN   Name=banIR;
OS   Aneurinibacillus aneurinilyticus (Bacillus aneurinolyticus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, FUNCTION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 12856 / DSM 5562 / JCM 9024 / NBRC 15521 / IAM 1077 / NRS
RC   1589;
RX   PubMed=2358438; DOI=10.1093/oxfordjournals.jbchem.a123101;
RA   Maekawa Y., Yasukawa H., Kawakami B.;
RT   "Cloning and nucleotide sequences of the BanI restriction-modification
RT   genes in Bacillus aneurinolyticus.";
RL   J. Biochem. 107:645-649(1990).
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'-GGYRCC-3' and cleaves after G-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:2358438}.
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   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:2358438}.
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DR   EMBL; D00704; BAA00612.1; -; Genomic_DNA.
DR   PIR; JX0116; JX0116.
DR   AlphaFoldDB; P19887; -.
DR   PRO; PR:P19887; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Restriction system.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2358438"
FT   CHAIN           2..354
FT                   /note="Type II restriction enzyme BanI"
FT                   /id="PRO_0000077282"
SQ   SEQUENCE   354 AA;  39861 MW;  8AC3DD73BDAB4B2F CRC64;
     MAQLKYNKDI DELERNAAKW WPDFLAKKES STSIIPKLVE SQDAFISLLN LSKNNPFDIF
     QLIDASKFPP NLFLKHLVVL TDFGGEPLNR LNQNFDSLFP MIPYGIHYIT KVLGKFEFFW
     NEKKYEYVFQ ELPVTSLTNS KLKIDGASIS KTVPLSDLYK DVIVLLMFGA NAVNSEVSEV
     LMKCEVGNLI GKTDELKKFI KERYIFVSRI TGGAEANTLG QVAQTHVIDF LRTRFGSKGH
     DIKSNGHIEG VTHNDGQTLT TFDVVIKKGS KSVAIEISFQ VTTNSTIERK AGQAKARYDM
     VSDTGNYIAY IIDGAGNFQR KNAITTICNN SHCTVAYTEE ELNVLLKFIL EKLE
//