ID A0A3S0KB18_9BACI Unreviewed; 1027 AA.
AC A0A3S0KB18;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=EKG37_20635 {ECO:0000313|EMBL:RTR26716.1};
OS Bacillus yapensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2492960 {ECO:0000313|EMBL:RTR26716.1, ECO:0000313|Proteomes:UP000271374};
RN [1] {ECO:0000313|EMBL:RTR26716.1, ECO:0000313|Proteomes:UP000271374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XXST-01 {ECO:0000313|EMBL:RTR26716.1,
RC ECO:0000313|Proteomes:UP000271374};
RA Yu L., Xu X., Tang X.;
RT "Bacillus yapensis draft genome sequence.";
RL Submitted (DEC-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RTR26716.1}.
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DR EMBL; RXNT01000022; RTR26716.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0KB18; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000271374; Unassembled WGS sequence.
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; 1.20.58.910; -; 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 ENDONUCLEASE SUBUNIT; 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; 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:UP000271374};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 291..460
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1027 AA; 117696 MW; 09E7AD2D32A9EAFE CRC64;
MSNAPKSAAE KTFQQNFVKE LQKYKWEAPD FLDGNKLKVT VADLVSHWRS ELNRINADQL
EGVELTDNEF RQVMAKVNQI SNSYEAAKIL AIEESKGKID GIYRDDNPKI TRKQMTLTIF
KKAEVRGGDS SYRIAREVQT PNNNRFDIVL LINGLPLINI EMKRTDKTLD EAFGQFMRYY
RDGEYSNNFM AFSQMMVITS EIATRYFATP KTAGDFNPSF VFHWSDNNNK PINDWKKVID
SFLMIPMAHQ MVGDYLVIDE DKEEENRRHL LLRPYQVYAL QAIEGAAFGW DNDEKVPHGG
FVWHTTGSGK TITSFKTALF LSTRGGFDKV VFLVDRRELD KNTREKFKAY AVYESVSVDE
TKFTYQLKKK LKSAQNGIVV TTTFKLNSLV KEMEEAYDAS LADKKIVFII DEAHRTTMGQ
MMGTIKSYFK NNGLFFGFTG TPLFDENKIK GKFNEKSEVI NTTEKLFGPK LHQYTIDEAI
ADKNVLGFHV DYINTGEFKS YDDLREQLAE KIKEEHPELT DREIERQVQE MSEVEVEMQA
KKQGLLIYQD ETHIPRVVEE ILNNWESQSQ GREFNAILTV AYKNRVIAYY NEFKKQLADR
GEKLNVAMTF SFGNENDPTL LDPIIAKDMF KDYAKFTGIE FVAGDKKHGE DAYFEDVVER
ATRGGSRRNP KNIDLVIVAD QLLTGYDSKR LNTLYVDRSL ELQGLIQAYS RTNRVFGSNK
EFGTIINFQY PRITEEIVNK ALKLYGSGGK SSKAIVDTYE TAVQKLAIKV TEMIPNLPDP
TEWQTIEHIE DEKEAFTLAF KDAAEQLNLV EQYYQFKWDD VSFGIDEHSW LQYVGAYKNL
TWKPGTPPQP TPINPLVGKT KLAGTQVIDA HHILSLIGSK ITSPYGIQTV DIETLRIIYE
QIQELSNMGE HEQAQLLKEF VDTQLVPGNL SNDLDFDEAY EIWKGDKLKD TVISFSSEWG
LDSELLLKSV NSYSTSQPDI VPYINELISS IDFNKATNQS AVNLLRHNMA LTVKLPEWIA
ETKQKYS
//
