ID B7GLJ0_ANOFW Unreviewed; 1020 AA.
AC B7GLJ0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Aflv_2057 {ECO:0000313|EMBL:ACJ34416.1};
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ34416.1, ECO:0000313|Proteomes:UP000000742};
RN [1] {ECO:0000313|EMBL:ACJ34416.1, ECO:0000313|Proteomes:UP000000742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34416.1; -; Genomic_DNA.
DR RefSeq; WP_012575602.1; NC_011567.1.
DR AlphaFoldDB; B7GLJ0; -.
DR STRING; 491915.Aflv_2057; -.
DR REBASE; 19230; AflWKORF2059P.
DR GeneID; 7038309; -.
DR KEGG; afl:Aflv_2057; -.
DR PATRIC; fig|491915.6.peg.2110; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_005762_1_0_9; -.
DR Proteomes; UP000000742; 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:UP000000742};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 282..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1020 AA; 117347 MW; 8F0748EC1DD361E3 CRC64;
MTRPLGETEF EETTIERLKR LGYDYLHAQE LFQRGDRDSL HEVVLYGRLE AFLKKAYPAI
PEHEIKRLAQ ILTAPNGVKL INRNMHFHQM LTKGLEFSYE VNAETYTPHI FPIDWEHPEN
NDFLVVNQLP IEGRMSRRPD IVIYINGLPL IVFELKNPNS EQATVYDAYT QIQNYTYDIS
QLFNYNAFVV ISDNVETKHG MPFADYDFFA SWKSIDGRNV DNNCANTMRT LIEGLFPKDR
LLNYIRNFIV FLEEGSKITK VGAKYHQFFG VNFAVNEAIR ATRPDGDRKI GVMYHTTGSG
KSLSMLFFAG ILSRHPKMEN PSIVIQVDRN DLDKQLHDTF VQGKSYIDHV EHAEDTEQLR
TLLRGEAGQI IFSTIEKFRK KEGETQHPVL SKRRNIVVIA DEAHRTQAGF AGGFAAQLRY
ALPNASHIGF TGTPVDFVGN HTEEIFGHII HRYDMAQAVA DKATLPIYYE SRLIPLDLSA
EDIDEKYKEI IVDAGGDDEE SENYKRKWAA LEKVVGTPKR LRRLANDIVS HFNQVANPFQ
KAMIVCMSRR IAVDLYNYLR EIPECPPVEV IMTGDVSKDP KEWREVQPGS KYAHIKTKKE
QEEVKAKLRD PEDPLKFVIV VDMWLTGMDA KPLSYLYVDK PMKGHNLIQA IARVNRVFPG
KEGGVVVDYI GIATSLKEAT HKYTQSGGTG SPSYDISEAV KIFMGHLEAV REFIPSEIDV
QNWRTKPKIE REDFIADLVN VLLNSDPEEY IQEATKLEKS YQLVKNQPEV LELADEAMLY
LMIKAQLRKH LRPPIEKPSE NKTLEERLSE LIDNSLLAKE TVDIFKVAGI ERPDISILDD
AFLADLTKKE HEDLRLKLLK KLLEDQIKVT FSKGSPQSKA LSELLEKTLK DYHNRVIQAA
DVVRVMIKMR KEMEEEMRKR HDLGLSEEEI EFYKAITAME QESFSNEFLA DLIHKVVKAL
KKQLAVDWTS PHRRDVYAKV KLAVKHVLMK EKITGQQLQF LTNKFMEQAE QQYKDWPMHA
//
