ID A0A1D7XNS3_9CLOT Unreviewed; 917 AA.
AC A0A1D7XNS3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Type I restriction enzyme endonuclease subunit {ECO:0000256|RuleBase:RU364115};
DE Short=R protein {ECO:0000256|RuleBase:RU364115};
DE EC=3.1.21.3 {ECO:0000256|RuleBase:RU364115};
DE AltName: Full=Type-1 restriction enzyme R protein {ECO:0000256|RuleBase:RU364115};
GN ORFNames=BGI42_14690 {ECO:0000313|EMBL:AOR24991.1};
OS Clostridium taeniosporum.
OG Plasmid pct2 {ECO:0000313|Proteomes:UP000094652}.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR24991.1, ECO:0000313|Proteomes:UP000094652};
RN [1] {ECO:0000313|Proteomes:UP000094652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RC PLASMID=Plasmid pct2 {ECO:0000313|Proteomes:UP000094652};
RA Walker J.R.;
RT "Genomics of Clostridium taeniosporum, an organism which forms endospores
RT with ribbon-like appendages.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase
CC activities, but not for modification. {ECO:0000256|RuleBase:RU364115}.
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 ECO:0000256|RuleBase:RU364115};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S. {ECO:0000256|ARBA:ARBA00011296,
CC ECO:0000256|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; CP017255; AOR24991.1; -; Genomic_DNA.
DR RefSeq; WP_069681110.1; NZ_CP017255.2.
DR AlphaFoldDB; A0A1D7XNS3; -.
DR REBASE; 161957; Cta1kORF15000P.
DR KEGG; ctae:BGI42_14690; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000094652; Plasmid pct2.
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; cd18030; DEXHc_RE_I_HsdR; 1.
DR CDD; cd22332; HsdR_N; 1.
DR CDD; cd18800; SF2_C_EcoR124I-like; 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; IPR004473; Restrct_endonuc_typeI_HsdR.
DR InterPro; IPR040980; SWI2_SNF2.
DR InterPro; IPR022625; TypeI_RM_Rsu_C.
DR NCBIfam; TIGR00348; hsdR; 1.
DR PANTHER; PTHR30195:SF16; TYPE I RESTRICTION ENZYME R PROTEIN; 1.
DR PANTHER; PTHR30195; TYPE I SITE-SPECIFIC DEOXYRIBONUCLEASE PROTEIN SUBUNIT M AND R; 1.
DR Pfam; PF12008; EcoR124_C; 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; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364115};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000313|EMBL:AOR24991.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364115};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364115}; Plasmid {ECO:0000313|EMBL:AOR24991.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094652};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 254..402
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 792..819
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 917 AA; 107409 MW; 0E89632682D068F4 CRC64;
MSYQSEAELE RLLVKQLVSQ GYEKVKIDDE DGLIENFRHQ LYLHNKNKLD DVRFTDKEFQ
RILRHVEGKS VFQSAKILRD KFILEREDGK KVYIEFFDSK HWCKNRFQVT TQTTVIGKYT
NRYDVTLLIN GLPLIQIELK RRGLDLKEAF NQIERYRKHS YQGLYRYIQV FVVSNGVDTK
YFANTDKELL FSQTFFWTDV KNERISNLND FTESFLEKCH IAKVVARYMV INESDKALMV
MRPYQIFAVE ALINRALETN NNGYIWHTTG SGKTLTSFKV SQILSNEPSI KKVFFLVDRK
DLDSQTLAEF NKFEPDSVDT TDKTFTLVNQ IKDINKPLIV TTIQKMANAI KTPKYANIMD
KYKDEKVVFI IDECHRSQFG DMHKAINKHF SKAQYFGFTG TPRFEENKSQ DGRVTADLFE
KCLHTYLIKD AINDGNVLGF SVEYIKTFDG YYDENDDTKV NAIDTDEVFM NDKRISLVAE
HIIKNHPAKT RNMEYTAIFT VQSIEMVVKY YDMFKKLNHN LKIAGIFTYG ANEDFQGKDE
HSRDSLERMI SDYNGIFDTN YSTDTFSNYF SDVSKRVKKA QIDILLVVNM FLTGFDSKTL
NTLYVDKNLK YHDLIQAFSR TNRVQKATKP YGNIVCYRNL KKNTDAAIGL FSQTHNTDIV
LMESYKYYLD RFKNELKGLF TLTKSPEDVD LLESEEDKKK FIISFRELSK ALVKLQTFTD
FEFKEDILGI SEQTYQDFKS KYFLIYDSVK KGEGNKVSIL ADIDFGIELM HTDKINVSYI
MNLIRDIDLS DKEKRDKDVK NILKELDRAD NEELRLKVEL LKTFLNKVVP TLLPEDSIDE
AYSKYHEEKR EEEVEDFASK VGLEKENIKS YLSEYEYSGL VNQKEISDDI TAPFLKKRNL
VKKIKSFIFE HVEKFSL
//