ID   T2A1_ACICA              Reviewed;         366 AA.
AC   P24546;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-MAY-2023, entry version 64.
DE   RecName: Full=Type II restriction enzyme AccI {ECO:0000303|PubMed:12654995};
DE            Short=R.AccI;
DE            EC=3.1.21.4 {ECO:0000269|PubMed:1368703};
DE   AltName: Full=Endonuclease AccI;
DE   AltName: Full=Type-2 restriction enzyme AccI;
GN   Name=accIR;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP   CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 49823;
RX   PubMed=1368703; DOI=10.1271/bbb1961.55.1553;
RA   Kawakami B., Hilzheber C., Nagatomo M., Oka M.;
RT   "Cloning and nucleotide sequences of the AccI restriction-modification
RT   genes in Acinetobacter calcoaceticus.";
RL   Agric. Biol. Chem. 55:1553-1559(1991).
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'-GTMKAC-3' and cleaves after T-2.
CC       {ECO:0000269|PubMed:1368703, 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         Evidence={ECO:0000269|PubMed:1368703};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:1368703}.
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DR   EMBL; D10671; BAA01522.1; -; Genomic_DNA.
DR   PIR; JU0469; JU0469.
DR   AlphaFoldDB; P24546; -.
DR   REBASE; 18; AccI.
DR   PRO; PR:P24546; -.
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; IPR019054; Restrct_endonuc_II_AccI.
DR   Pfam; PF09545; RE_AccI; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endonuclease; Hydrolase; Nuclease;
KW   Restriction system.
FT   CHAIN           1..366
FT                   /note="Type II restriction enzyme AccI"
FT                   /id="PRO_0000077276"
SQ   SEQUENCE   366 AA;  42495 MW;  DB663B74351C415E CRC64;
     MDYYDRIREL TKNVPVELVD FEQPRDLART PTQASSNFIT NKEQGDWAED LVTRAINENS
     KNFVAVKYGK SDNLVAGENG FDTFYQDFQT ELDTIGKRPD LLIFKKTDFD TTLGFDVSQI
     PHHQITDYVK KAIAGIEVRS SAFLIDKYEE AMQVRTQRFT EIAFQTRDKI LAEFLDVLDH
     PSRSKYITLL NTLTLETISI FDFKVPGWRS NERLIEVNNL FKRLKVAIKE IQKRDYLSIT
     PKVEDIKVVY KWIETFNVPH FYFQVFFDKV YGISFEQILT IISNSDNDGV IFSVEKDVQN
     QNKTTIKINS KTGYPIASKV DEPTHESIRK EMDRGRLLFY VTFKGGTAYL DLDNLRTILG
     IEEAEF
//