ID A9WD66_CHLAA Unreviewed; 1044 AA.
AC A9WD66;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
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};
GN OrderedLocusNames=Caur_1816 {ECO:0000313|EMBL:ABY35033.1};
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY35033.1, ECO:0000313|Proteomes:UP000002008};
RN [1] {ECO:0000313|Proteomes:UP000002008}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC {ECO:0000313|Proteomes:UP000002008};
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
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|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; CP000909; ABY35033.1; -; Genomic_DNA.
DR RefSeq; WP_012257687.1; NC_010175.1.
DR RefSeq; YP_001635422.1; NC_010175.1.
DR AlphaFoldDB; A9WD66; -.
DR STRING; 324602.Caur_1816; -.
DR REBASE; 16876; CauJORF1810P.
DR EnsemblBacteria; ABY35033; ABY35033; Caur_1816.
DR KEGG; cau:Caur_1816; -.
DR PATRIC; fig|324602.8.peg.2069; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_0; -.
DR InParanoid; A9WD66; -.
DR Proteomes; UP000002008; 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; 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; IPR021810; T1RH-like_C.
DR NCBIfam; TIGR00348; hsdR; 1.
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 Pfam; PF11867; T1RH-like_C; 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, ECO:0000256|RuleBase:RU364115};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU364115};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 309..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1044 AA; 117564 MW; 51EEFA6F29E14CE2 CRC64;
MAHLTESNIE TVALDWLKSL GWQVAHGPGI APGMSAAERQ NYGEVVLEQR LRDALARLNP
DLPTEALDDA FRKLTQPEGA DLLQRNRVVH LMLANGVTVE YRHPDGGIRG TQVRVIDFDD
PANNNWLAVN QFSIEENKHN RRADVVLFVN GLPLAIIELK NAADEHATIW SAFQQLQTYQ
VEIPSLFVFN ETLVISDGLE ARIGTLGAGR EWFKPWRTIS GMQVEDVGVP QLEVVLKGVF
EKNRFLTLIR DFIVFEDDGS GRLVKKMAGY HQFHAVLVAV KETLRASAVV SSNRMAESGG
VYEAGREPGG KPGDRRIGVV WHTQGSGKSL TMVFYAGCII RKPAMENPTI VVLTDRNDLD
DQLFNTFSRC QDLLRQPPVQ AESRVHLRQL LSVQSGGIVF TTIQKFLPEE KGDRHPVLSN
RRNIVVITDE AHRSQYDFID GFARHMRDAL PQASFIGFTG TPIEKADADT RAVFGDYISI
YDIQRAVEDG ATVSIYYEAR LAKLDLPDEL KPKIDDEFEE ITEGEEVERK EKLKTKWAQL
ESIVGTEQRL RLIANDIIEH FERRLEAIEG KGMVVCMSRR ICVELYNIIC TLRPNWHHED
DDKGVIKVVM TGSASDPVDW QPHIRNKQRR ELLAKRFRDP NDPLKLVIVR DMWLTGFDCP
SLHTMYLDKP MRGHGLMQAI ARVNRVFRDK PGGLVVDYLG LAHELKAALA VYTESGGTGK
TTIDQEETVA LMQEKYEICC GILHGFDWSD WASGDAHARI GLLPAAQEHV LARVKGKERF
VQAVRDLTKA FALAVPHEKA LEIRDDVAFF QALSAALTKR APGDVRTEEQ LDHAIRRIIA
QVIAPEGVED IFAAAGLKKP DISILSDEFL AEVRGMPHKN LAVEVLQKLL NGEIKRRSHK
NIVQARSFAE LLQQALHRYQ NRAIEAAQVI EELITLAKEM READRRGEVL GLSEEELAFY
DALETNDSAV AVLGDQTLRT IARELVETVR NSISIDWAQR EDVRANLRRL VKRILRKHGY
PPDKQEKATQ TVLEQAEVLS AEWA
//
