ID U5MMC3_CLOSA Unreviewed; 1003 AA.
AC U5MMC3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=type I site-specific deoxyribonuclease {ECO:0000256|ARBA:ARBA00012654};
DE EC=3.1.21.3 {ECO:0000256|ARBA:ARBA00012654};
GN ORFNames=CLSA_c09070 {ECO:0000313|EMBL:AGX41919.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX41919.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX41919.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX41919.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006721; AGX41919.1; -; Genomic_DNA.
DR RefSeq; WP_022744205.1; NZ_AYXL01000151.1.
DR AlphaFoldDB; U5MMC3; -.
DR REBASE; 71971; Csa13864ORF9040P.
DR GeneID; 55473439; -.
DR KEGG; csb:CLSA_c09070; -.
DR PATRIC; fig|1345695.10.peg.746; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_015458_1_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000017118; 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; cd22332; HsdR_N; 1.
DR Gene3D; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N.
DR InterPro; IPR040980; SWI2_SNF2.
DR PANTHER; PTHR30195:SF15; TYPE I RESTRICTION ENYME HINDI ENDONUCLEASE SUBUNIT; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF04313; HSDR_N; 1.
DR Pfam; PF18766; SWI2_SNF2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AGX41919.1};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 312..486
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 697..724
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 871..898
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1003 AA; 116531 MW; 0D99526B76EFEE00 CRC64;
MGRPEDSRVK IPALVHFTRL GYSYMSLKNK KRGIDYDEDT NIFFDLFRSA INKINNTELS
VDDVKKLISD IKIKLENDDL GRAFFTILHE GYNGLKLIDF NNYENKNNYT VVTELPYENG
DNNFRPDIVV LINGMPLSFV EVKRQNNREG ILVERERMTK RFSSPIYKRY VNITQFTVFS
NNHKYDDTTI EPIQGAFYAS SNYGKMFFSK FREQRAEEIN KNILPIDDAT EHLILKDNNL
IAIKGSPEYQ SSINSDSPTN RIVTSLYSKE RVLFILKYGI CYKKTTDKNG ITHIEKHIMR
YPQIFATYAI RDKLDEGIRK GVIWHTQGSG KTALAYSNVN YLKDYYQSQG KIAKFYFIVD
RLDLATQAKA EFEARGLHVD FVNSKEDFTS NISSVGESGK NGKVTITVVN IQKFSDESVT
KQTDYNVSVQ RVYFMDEAHR SYNPKGSFLA NLMASDRNAV LIALTGTPLI GKDYNTKDVF
GNYIHKYYYN QSIADGYTLK LIREEIETTY RAQIKATLEQ LEVEQGSIEK KDLYAHPKFV
SDMVDYIVLD FTKGRTALDS SIGAMIVCDS APQAREVSAQ LQRYSTYSHA LVLHDEGTKQ
DRKDIQEDFK KGKIDILVVY NMLLTGFDAP RLKKQYLARM IKAHNLLQTL TRVNRPYKDY
HYGFVVDFAN IKDEFDKTNK AYFDELQSEL GNEVENYSDI FKSKEEIEQD LNEVKNQLFL
YNTDNVVEFI NQINGIDDKK QLLDLKKALE NYKTLHNLIR LFGFDDLYMH FDIDNAIKML
NEINNRINIL NFKQNMDSSD DMASVLNIAL DQIVFQFRKI KEEELIIADA FRSSLEKTRQ
EIVERCLDPK DPEYIALLDE LKRVFKKKNI EELTSDEMKD LMAELDDLRK RAERKNHADQ
MLAAKYDGDV KFMRTHKRIM GSPPPIADTI TTFKILMEIK ELTDNKIAHN ENILDNEPYF
FKELRPYIKN ACRKQNVALT RPQLDFIDTC ISQEYITERN WAS
//
