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Database: UniProt
Entry: A0A1D7XNS3_9CLOT
LinkDB: A0A1D7XNS3_9CLOT
Original site: A0A1D7XNS3_9CLOT 
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
//
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