ID R6ULS5_9FIRM Unreviewed; 1008 AA.
AC R6ULS5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-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=BN746_00098 {ECO:0000313|EMBL:CDC82949.1};
OS Erysipelotrichaceae bacterium CAG:64.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=1262981 {ECO:0000313|EMBL:CDC82949.1, ECO:0000313|Proteomes:UP000018179};
RN [1] {ECO:0000313|EMBL:CDC82949.1, ECO:0000313|Proteomes:UP000018179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:64 {ECO:0000313|Proteomes:UP000018179};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDC82949.1}.
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DR EMBL; CBGA010000035; CDC82949.1; -; Genomic_DNA.
DR AlphaFoldDB; R6ULS5; -.
DR Proteomes; UP000018179; 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; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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; 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 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 310..472
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1008 AA; 117684 MW; 1E972477CC7E075B CRC64;
MNTLNIVAST NESTVVTEYI PETSRSDAYQ SEAQLEQEFI RLLTMQGYEY IALNSEQEMI
SNLRKQLEIL NHYDFSDTEW ERFFRECIAS SNEGIVEKTR KIQADHIQNL KKDDSSTKNM
MLIDKKNIYN NRLQVVNQYE EKNGSHETRY DVTILVNGLP MVHIELKRRG VAIREAFNQI
KRYQRNSFWA GSGLYEYIQI FVISNGTHTK YYSNTTRISH IKENSTSGRN ASRKTSNSFE
FTSYWADGKN KVIADLIDFT KTFFARYTIL NILTRYCVFT AEDLLMAMRP YQISATEKIL
KRIEISTNYK KTGTIEAGGY IWHTTGSGKT LTSFKTAQLA TALPYIDKVL FVVDRKDLDY
QTMKEYDRFE KGSANSNKST KILQRQLETD STKIIITTIQ KLDNFIRRNK THKIYKKHVV
IIFDECHRSQ FGDMHTAIIK AFQNYHIFGF TGTPIFSENA PSSSRTLLKT TPQTFGDKLH
TYTIVNAIND GNVLPFRIDY VDTVKKKEEI SDRQVKAIDI EKAMQAPERV EKIVSYILEH
FDQKTQRNSF YSLKGQRVAG FNSIFAVSSI PMAKKYYVEL KKQLEKNNRK LTIATIFSYS
ANEEDPEDVI QEEEFETDGL DKTSRDFLQS AIDDYNKEFK QSFDTSSEGF QNYYKDLSQR
MKRREIDLLI VVNMFLTGFD ATTLNTLWVD KNLRMHGLIQ AFSRTNRILN SVKTYGNIVC
FRDLQKETDE AIALFGDENA GSIVLLKNYE SYYYGYDEDG KHHAGYMELI EKLKMIYPVN
EQVIGEQNQR DFISLFGAIL RLKNILSSFD KFDGNEILTQ RQQQEYQSIY LDLYQEWKKK
DEVEKENIND DIVFEMELVR QVEINIDYIL MLVSKYHDSN CEDKEILVDI RKAVDSSMQL
RSKKELIENF IEKVNVNTKV EEDWQKFVKE QKETDLSELI KAERLKDEDT RRFIDNSFRD
GVLKTTGTDI DRILPPVSRF SGGNRVKKKQ TVIEKLMNFF EKYFGLIS
//
