ID   K5Z1E7_9PROT            Unreviewed;       246 AA.
AC   K5Z1E7;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR000994};
DE            EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR000994};
GN   ORFNames=MXAZACID_03856 {ECO:0000313|EMBL:EKN00768.1};
OS   Acidocella sp. MX-AZ02.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acidocella.
OX   NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKN00768.1, ECO:0000313|Proteomes:UP000006217};
RN   [1] {ECO:0000313|EMBL:EKN00768.1, ECO:0000313|Proteomes:UP000006217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKN00768.1,
RC   ECO:0000313|Proteomes:UP000006217};
RX   PubMed=23405365;
RA   Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT   "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT   AZ02.";
RL   Genome Announc. 1:E00041-12(2013).
CC   -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-CTCGAG-3' and cleaves after C-1.
CC       {ECO:0000256|PIRNR:PIRNR000994}.
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:0000256|PIRNR:PIRNR000994};
CC   -!- SIMILARITY: Belongs to the XhoI type II restriction endonuclease
CC       family. {ECO:0000256|PIRNR:PIRNR000994}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKN00768.1}.
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DR   EMBL; AMPS01000042; EKN00768.1; -; Genomic_DNA.
DR   RefSeq; WP_008492787.1; NZ_JH976207.1.
DR   AlphaFoldDB; K5Z1E7; -.
DR   STRING; 1214225.MXAZACID_03856; -.
DR   REBASE; 61828; AspAZ02ORF3861P.
DR   HOGENOM; CLU_097055_0_0_5; -.
DR   Proteomes; UP000006217; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-UniRule.
DR   InterPro; IPR007636; Restrct_endonuc_II_XhoI.
DR   Pfam; PF04555; XhoI; 1.
DR   PIRSF; PIRSF000994; Restrict_endonuc_II_XhoI; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR000994};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000994};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR000994};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006217};
KW   Restriction system {ECO:0000256|PIRNR:PIRNR000994}.
SQ   SEQUENCE   246 AA;  27335 MW;  460592539C61FB4E CRC64;
     MALDLVNYER KSSEAVKAFW GNREAARQKQ IESGKADQGE RAGVTAGKNM DGFLALVLDI
     IKANGLAHAE FYQNRAMLTL PGYFRPTKLW DLLVIYKNEL IAAVELKSHV GPSFGNNFNN
     RTEEAIGTAH DLWTAFREEA FGKQPRPFVG WLMMVEDAPE SRRAVKDSSP HFPVFEEFKG
     ASYLKRYDLL CQRLVQEQLY TTAAVIAAER SAVNTGHFTE MSSMTSLKTF VAALAGHVAA
     EAARLG
//