ID A0A2S0N3A9_9BURK Unreviewed; 932 AA.
AC A0A2S0N3A9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=C6571_14900 {ECO:0000313|EMBL:AVO42403.1};
OS Simplicispira suum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2109915 {ECO:0000313|EMBL:AVO42403.1, ECO:0000313|Proteomes:UP000239326};
RN [1] {ECO:0000313|EMBL:AVO42403.1, ECO:0000313|Proteomes:UP000239326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC1-8 {ECO:0000313|EMBL:AVO42403.1,
RC ECO:0000313|Proteomes:UP000239326};
RA Kim S.-J., Heo J., Kwon S.-W.;
RT "Genome sequencing of Simplicispira sp.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give random double-stranded
CC fragments with terminal 5'-phosphates, ATP is simultaneously
CC hydrolyzed.; EC=3.1.21.3; Evidence={ECO:0000256|ARBA:ARBA00000851};
CC -!- SIMILARITY: Belongs to the HsdR family.
CC {ECO:0000256|ARBA:ARBA00008598}.
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DR EMBL; CP027669; AVO42403.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0N3A9; -.
DR REBASE; 244289; SspSC18IP.
DR KEGG; simp:C6571_14900; -.
DR OrthoDB; 9804086at2; -.
DR Proteomes; UP000239326; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009035; F:type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd18032; DEXHc_RE_I_III_res; 1.
DR CDD; cd18799; SF2_C_EcoAI-like; 1.
DR Gene3D; 3.90.1570.30; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013670; EcoEI_R_C_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR PANTHER; PTHR47396:SF1; ATP-DEPENDENT HELICASE IRC3-RELATED; 1.
DR PANTHER; PTHR47396; TYPE I RESTRICTION ENZYME ECOKI R PROTEIN; 1.
DR Pfam; PF08463; EcoEI_R_C; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:AVO42403.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 173..329
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 932 AA; 106911 MW; D056893B05FC424F CRC64;
MTYSEAATRS ALIDNALGQS GWNVKDPTQV VEEFDIKVGL APGVKEPRTP YEGHHFSDYV
LLGKDGKPLA VVEAKRTSKD AALGREQAKQ YCYNIQKQLG GELPFCFYTN GHDTYFWDLE
NTPPRKVVGF PTRDDLERFS YIRRNRKPLT HEFINTSIAG RDYQIRAIRS VLEGIEQKKR
DFLLVMATGT GKTRTCIALV DALMRAGHAE KVLFLVDRIA LREQALAAFK EHMPNEPRWP
NPGEKLVAKD RRVYVATYPT MLNVIRDEAQ HLSPHFFDFI VVDESHRSIY NTFGEVLDYF
KTITVGLTAT PTALIDHNTF QLFHCEDGIP TFAYTYEEAV NNFPPYLSNF QVMKIQTKFQ
MEGISKRTIS LEDQKRLILQ GKDVEEINFE GSQLEKQVIN KGTNTLIVRE FMEESIKDAN
GVLPGKTIFF CATKAHARRM EEIFDKLYPQ YHGELAKVLV SDDPRVYGKG GLLDQFTNND
MPRIAISVDM LDTGIDVREI VNLVFAKPVY SYTKFWQMVG RGTRLLETNK PKPWCLEKDV
FLILDCWDNF EYFKLNPKGR ELKPQLSLPV RLVGLRLDKI ERANDSEHAE TAAREVTKLR
SQIAALPNES VVIKEAAAVL ARLQDENFWI SLNHDRLEFL RAEVKPLFRT VSEADFKAMR
FERDVLEYSL AVLSEAKEQA ETLKDGIVEQ IVELPLSVSF VKKEEALIRA AQTNHYWAKA
DEDAFDELVA KLGPLMKFRE HNTGQEQTHL DLADELHKKE RVEFGPQHES VSITRYREMV
EALVTELTDY NPVLQKIKNG EPISAEEASQ LADLLHEEHP HITEDLLRQV YKNRKARFIQ
FIRHILGIEV LRSFPDEVSA AFDQFIRAHT TLSSRQMEFL NLLKGFIIER EKVEKKDLIN
APFTVIHPQG IRGVFSPLEI NEILQLTERL AA
//