ID A0A0S1SB00_9FLAO Unreviewed; 932 AA.
AC A0A0S1SB00;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=SB49_07960 {ECO:0000313|EMBL:ALM07745.1};
OS Sediminicola sp. YIK13.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Sediminicola.
OX NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM07745.1, ECO:0000313|Proteomes:UP000063759};
RN [1] {ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA Kwon Y.M., Kim S.-J.;
RT "Genome sequence of Sediminicola sp. YIK13.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM07745.1, ECO:0000313|Proteomes:UP000063759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIK13 {ECO:0000313|EMBL:ALM07745.1,
RC ECO:0000313|Proteomes:UP000063759};
RX PubMed=26823585;
RA Kwon Y.M., Kim S.J.;
RT "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT Bacterium Sediminicola sp. YIK13.";
RL Genome Announc. 4:e01635-15(2016).
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; CP010535; ALM07745.1; -; Genomic_DNA.
DR RefSeq; WP_062055489.1; NZ_CP010535.1.
DR AlphaFoldDB; A0A0S1SB00; -.
DR STRING; 1453352.SB49_07960; -.
DR REBASE; 131535; Ssp13IIP.
DR KEGG; syi:SB49_07960; -.
DR PATRIC; fig|1453352.4.peg.1657; -.
DR OrthoDB; 9759819at2; -.
DR Proteomes; UP000063759; 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; 2.
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:ALM07745.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000063759};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 171..327
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 932 AA; 107640 MW; 7CC4DDCBC5AC6B63 CRC64;
MNESTTRKEL IDIHLKEAGW DVNDHTQVVE EYVVDLIAGN QAKEPTGKNL NNQFSDYVLL
GKNGKPLAVV EAKKSIKDAN TGREQAKQYC YNIQKQTNDI LPFCFYTNGH DIFFWDLENA
PPRKVIGYPN REDLERYQYI REVKKPLTSE LINTKVAGRD YQIRAIRSVM DGLEQKRRTF
LIVMATGTGK TRTTIALVEA LMRAGWAEKA LFLVDRIALR DQALEAFKEH LPNEPRWPKQ
GEKSIAKDRR IYISTYPTML NIVREEKETL SPHFFDLIVV DESHRSIYNT YKEVLDYFNT
ITIGLTATPT DVIDHNTFKI FNCEDGLPSF AYTYEEAVNN IPPYLCNFQV MKIKTKFQTD
GISKRTVSLE DQKKLILEGK EIAEINFEGV ELEKKVINKG TNTLIVKEFM EESIKDINGV
LPGKTIFFCA NIAHARRIEE IFDQLYPQYN GELAKVMVSE DSRVHGKGGL LDQFKNKDFP
RVAISVDMLD TGIDIRELVN LVFAKPVYSY TKFWQMIGRG TRLLEPTQMK SWCTEKDVFL
ILDCWDNFEY FKLKPKGKEL KQAIPIPVKL FGLRLEKLEF VFEASIQETI IEECKRLQKL
IALLPKNSVV IKDNSKAVAE VNNPDFWEVI NSNKIDFLKA EILPLMRTIS GVDYKAMRFE
KDILEVSLAK MQNETEKYDM LKDALIERIS DLPLSLNIVA KQQELIRDSQ RNQFWNNIKE
NDFNNLIDKL SPLARYIDSR DTTSGPSKFN FEDELVAKEM VEFGPQNEAV SITRYKEMVE
EKIRELTESN PILQKIIDGN AITEEEVETL AHELQEENPH ITIGLLQRVY QNRKAKFLQF
IKHILGLEVL ETFTESVASA FGDFIREHNY LSSRQLQFLD ILKKYILEKG NLEKKNLIES
PFTMIHPEGI RGVFSPKEIN EILQLTNKIL AA
//
