ID A0A078LY96_9STAP Unreviewed; 927 AA.
AC A0A078LY96;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=hsdR {ECO:0000313|EMBL:CDZ98985.1};
GN ORFNames=BN1048_00104 {ECO:0000313|EMBL:CDZ98985.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ98985.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CDZ98985.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ98985.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) 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; CCSE01000001; CDZ98985.1; -; Genomic_DNA.
DR RefSeq; WP_035807409.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078LY96; -.
DR STRING; 1461582.BN1048_00104; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000044136; 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:UP000044136};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 254..400
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 927 AA; 108345 MW; 4448273DB2B732C1 CRC64;
MGYQSEAALE NQVMEQLGRQ GFENVKLYSI EAIIDNFRKI LNERHQDKLN GKPLTDSEFD
RLMTQINGKN VFTSAQILRD KFVLRRDDET DIYLEFFSKD SWRKNIYQVT NQVAVSDKYK
GRYDVTILVN GLPVTQIELK RSGVAIEEAF NQIERYRRDN YKGLFKYVQL FIVSNSQNTR
YFANSDKEIY KSSMFYWSDD QNNTINRLSD FLGDFCTPCR LSKMISRYMI INETDHNLMV
MRPYQVYATE ALIERATETN NNGYIWHTTG SGKTLTSFKA SQLLSERPEI QKVIFLVDRK
DLDAQTMSEF NKFQKDSVDF TTNTAKLERQ LADKSQPMIV TTIQKLNNAV KRNNSVMDQY
KTDKVIFIID ECHRSQFGDM HTQIAKHFTN AQFFGFTGTP RFEENRSADG RATADIFDKC
LHYYLIKDAI RDGNVLGFSV EYINTFKGEN PFLDDEYVSG IEANKIWLAD DRINLVTDHI
YNIHSKKTAQ KEYSAILATQ SIEMAMKYYD TFKAREAEHK KKKLKVATIF SYEANQSLRE
GEIKEAGKDQ LARVIADYNE MYNTNFSLET YDGYFNDISK RVKKGLKGGK IDVLIVVGMF
LTGFDSKKLN TLYVDKNLRH HDLIQAYSRT NRVEKKTKPY GNIVCFRNLK QETDDAIKLF
SRTDDTDTVL QRPYEEYLEE FKQALVVLKG IAPSPIDVPR IEKEEEIKFF VETFRRLSRA
LVKLKTFMDF EFKEEVTGID SQEHQDYRSH YIDLYNEHIK KPDPEKASIL DDIDFEIEII
RNEMINVSYI INLINNIDLE DKDNQRREIA SIRNILDGAD DEQLRLKSEL IKEFLDTVVP
TLGKDANVAA EYLDFEEEQR IREIQEFAKE NDYSQEQLNT LLSEFQFSGQ VYRKDIEEGI
SGSFLVRRKK VDKIQSYIRE VTEKYGV
//
