ID K2LDG6_HELPX Unreviewed; 276 AA.
AC K2LDG6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Type-2 restriction enzyme {ECO:0000256|PIRNR:PIRNR016080};
DE EC=3.1.21.4 {ECO:0000256|PIRNR:PIRNR016080};
GN Name=mboIR {ECO:0000313|EMBL:EKE92654.1};
GN ORFNames=OUO_0017 {ECO:0000313|EMBL:EKE92654.1};
OS Helicobacter pylori R046Wa.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145116 {ECO:0000313|EMBL:EKE92654.1, ECO:0000313|Proteomes:UP000006763};
RN [1] {ECO:0000313|EMBL:EKE92654.1, ECO:0000313|Proteomes:UP000006763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R046Wa {ECO:0000313|EMBL:EKE92654.1,
RC ECO:0000313|Proteomes:UP000006763};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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}.
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:EKE92654.1}.
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DR EMBL; AMOW01000001; EKE92654.1; -; Genomic_DNA.
DR RefSeq; WP_000788570.1; NZ_AMOW01000001.1.
DR AlphaFoldDB; K2LDG6; -.
DR PATRIC; fig|1145116.3.peg.16; -.
DR Proteomes; UP000006763; 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 Gene3D; 3.40.91.80; -; 1.
DR InterPro; IPR038365; EcoRII_C_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
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.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR016080, ECO:0000313|EMBL:EKE92654.1};
KW Nuclease {ECO:0000256|PIRNR:PIRNR016080};
KW Restriction system {ECO:0000256|PIRNR:PIRNR016080}.
FT DOMAIN 7..271
FT /note="Restriction endonuclease type II DpnII-like"
FT /evidence="ECO:0000259|Pfam:PF04556"
SQ SEQUENCE 276 AA; 32205 MW; C02071ADF68CEEE6 CRC64;
MKNHLPFDTF LKSLKTSNRT LDFFTDWQKC LKNKNKISIA LNHLNFLLGK DTKELKNCIK
SLFKEYPKAF NVLNILIAVR DKNDIVLDAN GNFYPLCSYF EDDEKVYEFI RQTGLERIFC
NRNIKDLNDF VFGIEVGLDS NARKNRSGKA MENHLSGLFI QAQLNFKEQV DIREFEDLCQ
AFGNDIKKFD FVVCGKDKTY FIEANFYTIS GSKLNEVARS YQDLALKFEA FPNYEFIWIT
DGTGWLDAKS KLQEAYKSVE IYNLSYVNDF ISKVQK
//
