ID R5TL24_9FIRM Unreviewed; 992 AA.
AC R5TL24;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, 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 ORFNames=BN683_01084 {ECO:0000313|EMBL:CCZ64004.1};
OS Roseburia sp. CAG:50.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262949 {ECO:0000313|EMBL:CCZ64004.1, ECO:0000313|Proteomes:UP000018378};
RN [1] {ECO:0000313|EMBL:CCZ64004.1, ECO:0000313|Proteomes:UP000018378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:50 {ECO:0000313|Proteomes:UP000018378};
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:CCZ64004.1}.
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DR EMBL; CBAK010000037; CCZ64004.1; -; Genomic_DNA.
DR AlphaFoldDB; R5TL24; -.
DR Proteomes; UP000018378; 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; 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; 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:UP000018378};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 271..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 992 AA; 114307 MW; 9A661BF0E6FEA148 CRC64;
MPELEKMIEE KLIEQLVYGE SQWTYRDDLK TEADLWKNFK YILEQNNKDR LNGEPLSDTE
FEQVKNQLQF SSFYKAGEWL VGENGKVQVH VQRDTERLHL VVMNHEHIAG GSSVYEVINQ
YSALGDSESS STSSRDRRFD VTLMINGLPM IHIELKNKQH SYMDAFWQIK KYIGEGKFTG
IFSAVQMFVV SNGVDTKYFA AASDTELNPK FMSGWVDQEN NPVPDYIDFA KSVLRIPEAH
EMIARYTVLD EDAKRLILLR PYQIHAIESI REASKTGKSG YVWHTTGSGK TLTSYKATRN
LLMDIPAIDK AIFLIDRKDL DTQTTMAFQA YANNDLVDVD ETDNVNDLKK KLKSDDRQVI
VTTIQKMQIL ISKRLKEGTP EYSKIKNLKI AFVVDECHRA VTPKTKRELE RFFGRSLWYG
FTGTPRFGEN PYPQLGDLPR TTEELYGKCL HKYTIQNAIH DKAVLGFQVE HNGPKNIIDE
TDASAYDNET HMLRVLDIIL NKSYHKLGFQ NGKGKTYEGL LTTSSIQLAQ KYYELLSRVK
RGETDLVIDE KIKQVLPDFP KFAITYSVTE NEEGSHVNQQ KMQQSLDDYN GMFGTKFELS
QIQSYNGNLN KRLARKDAKF ASRNEQLDLV IVVDRLLTGF DAPCMSTIFI DRQPMGPHDL
IQAFSRTNRI FDTNKTYGQI VTFQAPKLFK EGVDNAIKLY SAGSTEVALV SEWDEVEPAF
RKSLAALRVS AATPEEVSTM SMKEKRVFAK MFQTFDRLFA QLKSFTRFED SMLEDYGITE
TEYEDYVGRY KNVMEEIKLE DGGKDNTDED PVEVDPDYEL MAYSNTKIDY EYIIHLIQNI
VTPADDSEDI TPEERQKQID EVKQYVEEMR KDNAKVADIM SNLISEIEVD ENKYKGQSIL
NIVENMKRDC IDRVISDFCY TWYASKEDVM YAALHYRNGE IPNESVIKGT IDYTSYKAAQ
EKALPKFKYY KKCMDELRKT LDEEIKPLLS IA
//
