ID D5V7L2_ARCNC Unreviewed; 292 AA.
AC D5V7L2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN OrderedLocusNames=Arnit_2984 {ECO:0000313|EMBL:ADG94632.1};
OS Arcobacter nitrofigilis (strain ATCC 33309 / DSM 7299 / CCUG 15893 / LMG
OS 7604 / NCTC 12251 / CI) (Campylobacter nitrofigilis).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Arcobacter.
OX NCBI_TaxID=572480 {ECO:0000313|EMBL:ADG94632.1, ECO:0000313|Proteomes:UP000000939};
RN [1] {ECO:0000313|EMBL:ADG94632.1, ECO:0000313|Proteomes:UP000000939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33309 / DSM 7299 / CCUG 15893 / LMG 7604 / NCTC 12251 / CI
RC {ECO:0000313|Proteomes:UP000000939};
RX PubMed=21304714; DOI=10.4056/sigs.912121;
RA Pati A., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T., Nolan M.,
RA Lucas S., Tice H., Cheng J.F., Han C., Chertkov O., Bruce D., Tapia R.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Arcobacter nitrofigilis type strain (CI).";
RL Stand. Genomic Sci. 2:300-308(2010).
CC -!- FUNCTION: A P subtype restriction enzyme that recognizes the double-
CC stranded unmethylated sequence 5'-GATC-3'.
CC {ECO:0000256|PIRNR:PIRNR016080}.
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:PIRNR016080};
CC -!- SIMILARITY: Belongs to the DpnII type II restriction endonuclease
CC family. {ECO:0000256|PIRNR:PIRNR016080}.
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DR EMBL; CP001999; ADG94632.1; -; Genomic_DNA.
DR RefSeq; WP_013136777.1; NC_014166.1.
DR AlphaFoldDB; D5V7L2; -.
DR STRING; 572480.Arnit_2984; -.
DR REBASE; 26107; Ani7299ORF2986P.
DR KEGG; ant:Arnit_2984; -.
DR eggNOG; ENOG502Z7V5; Bacteria.
DR HOGENOM; CLU_089327_0_0_7; -.
DR OrthoDB; 9771872at2; -.
DR Proteomes; UP000000939; Chromosome.
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; IPR021191; Restrct_endonuc_II_DpnII.
DR InterPro; IPR007637; Restrct_endonuc_II_DpnII-like.
DR Pfam; PF04556; DpnII; 1.
DR PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:ADG94632.1};
KW Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Reference proteome {ECO:0000313|Proteomes:UP000000939};
KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT DOMAIN 2..288
FT /note="Restriction endonuclease type II DpnII-like"
FT /evidence="ECO:0000259|Pfam:PF04556"
SQ SEQUENCE 292 AA; 34623 MW; A92095119FA97371 CRC64;
MDFRNFKNTL KDSIFTWDYF TNFNKVRLNV KKVEKELNIL NYLIGKENLE REFISLIEEY
PNVRKALPLL IAVRTNKLIV TPVLTNIETL IPENKHYIFY DELNDEIKRE LIIFFNQTGL
KEVFENKCIK NLVDYSFGVE VGFDTNARKN RTGTLMENIV AKFLDEFCEE NPEFTYIEQA
TQKRILNTFN YNIDIDKNSR RFDFALFNRK KKKLYLIEVN YYSGGGSKLK ATAGEYQYLH
NFLKMQNLDF IWITDGKGWL TALNPLEETF NHNDYVVNLE MLKNGILDEI IK
//
