T2A1_THAGE
ID T2A1_THAGE Reviewed; 278 AA.
AC Q9KHV6;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 3.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Type II restriction enzyme AgeI {ECO:0000303|PubMed:12654995};
DE Short=R.AgeI;
DE EC=3.1.21.4;
DE AltName: Full=Endonuclease AgeI;
DE AltName: Full=Type-2 restriction enzyme AgeI;
GN Name=ageIR;
OS Thalassobius gelatinovorus (Ruegeria gelatinovora).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassobius.
OX NCBI_TaxID=53501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25655 / DSM 5887 / IAM 12617 / JCM 20688 / NBRC 15761 / NCIMB
RC 2206 / B6;
RA Xu S.-Y., Maunus R.E., Lunnen K.D., Allen R.;
RT "Method for cloning and producing AgeI restriction endonuclease in
RT E.coli.";
RL Patent number EP0959131, 26-APR-1999.
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Xu S.-Y., Maunus R.E., Lunnen K.D., Allen R.;
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SEQUENCE REVISION TO 245 AND C-TERMINUS.
RA Xu S.-Y., Maunus R.E., Lunnen K.D., Allen R.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
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'-ACCGGT-3' and cleaves after A-1.
CC {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;
CC -!- SIMILARITY: Belongs to the BsaWI type II restriction endonuclease
CC family. {ECO:0000305}.
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DR EMBL; AF247972; AAF71526.3; -; Genomic_DNA.
DR RefSeq; WP_058263487.1; NZ_CP051181.1.
DR PDB; 5DWA; X-ray; 1.50 A; A/B=1-278.
DR PDB; 5DWB; X-ray; 2.40 A; A/B=1-278.
DR PDB; 5DWC; X-ray; 2.50 A; A=1-278.
DR PDBsum; 5DWA; -.
DR PDBsum; 5DWB; -.
DR PDBsum; 5DWC; -.
DR AlphaFoldDB; Q9KHV6; -.
DR SASBDB; Q9KHV6; -.
DR SMR; Q9KHV6; -.
DR REBASE; 42; AgeI.
DR OrthoDB; 1759899at2; -.
DR BRENDA; 3.1.21.4; 201.
DR PRO; PR:Q9KHV6; -.
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; IPR041551; RE_BsaWI.
DR Pfam; PF18643; RE_BsaWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Restriction system.
FT CHAIN 1..278
FT /note="Type II restriction enzyme AgeI"
FT /id="PRO_0000077278"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 84..109
FT /evidence="ECO:0007829|PDB:5DWA"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5DWA"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:5DWA"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5DWB"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5DWA"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:5DWB"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:5DWA"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5DWA"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:5DWA"
SQ SEQUENCE 278 AA; 30539 MW; A02D953D3A30DB32 CRC64;
MRLDLDFGRG LVAHVMLDNV SEEQYQQISD YFVPLVNKPK LKSRDAIGQA FVMATEVCPD
ANPSDLWHHV LYRIYIREKI GTDPSQSWVR TSGEAFEVAL VERYNPVLAR HGIRLTALFK
GQKGLALTRM GVADRVGSRK VDVMIEKQGG GRSPDAEGFG VVGGIHAKVS LAERVSDDIP
ASRIMMGEGL LSVLSTLDVK SFPPPHGDLV NRGELGTPDR PSDKRNYIEG HGDFSACFSY
NLRTSPSNAT TPSGRHIYVS GFSGQDDEFT DYLVAQLA
