ID R6F179_9FIRM Unreviewed; 1021 AA.
AC R6F179;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=BN497_00049 {ECO:0000313|EMBL:CDB02781.1};
OS Firmicutes bacterium CAG:145.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263005 {ECO:0000313|EMBL:CDB02781.1, ECO:0000313|Proteomes:UP000018044};
RN [1] {ECO:0000313|EMBL:CDB02781.1, ECO:0000313|Proteomes:UP000018044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:145 {ECO:0000313|Proteomes:UP000018044};
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:CDB02781.1}.
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DR EMBL; CBCX010000071; CDB02781.1; -; Genomic_DNA.
DR AlphaFoldDB; R6F179; -.
DR STRING; 1263005.BN497_00049; -.
DR Proteomes; UP000018044; 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; 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:UP000018044};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 275..458
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1021 AA; 116780 MW; 32DD22E9F706A2AA CRC64;
MPGLYTEADY ENSVIELFRN ELGYEYAYGP DIERDFYSPL YEEVLLDSLY NLNRDLPDDA
IQDALFKLKN FENGELVQKN AVFMDYLQNG IPVRYFVGGE EHSSIVYLVD YKNPDNNSFI
VANQWTFIEN SNKRPDVILF LNGLPVVLVE LKSPSREETD ASEAYRQLRN YMQEIPSMFI
YNAICVMSDQ LTSKAGTITS GEDRFMEWKT KDGDYENTQY AQFDTFFEGM FQKERLLDII
KNFICFSNEG INSFKILAGY HQYFAVRKAI ESTKHATVTD GKGGVFWHTQ GSGKSLSMVF
YAHLLQEALN SPTIVVLTDR NDLDDQLYGQ FAKCKDFLRQ EPMHAESREN LKTLLAGRQA
NGIIFTTMQK FEESDEPLSE RNNIVVMADE AHRGQYGLAE KIKITKNEEG EDIAKRVVGT
ARIIRNSLPN ATYIGFTGTP ISSKDRSTRE VFGDYIDIYD MTQAVEDGAT RPVYYESRVI
KLNLDEATLK MIDTEYDIMA ANADEEVIEK SKRELGQMEA VLGNDNTINS LVCDILDHYE
NNRENLLTGK AMIVAYSRPI AMKIYKRILE LRPAWKEKVA VVMTSGNNDP EEWRQIIGNK
HHKDELARKF KDNNSPLKIA IVVDMWLTGF DVPSLATMYV YKPMSGHNLM QAIARVNRVF
RDKEGGLVVD YVGIASALKQ AMNDYTSRDK KNYGDTDVAK VAYPKFLEKL SICRDKFHEY
DYSKFVNGTD LERAKTISGA VNFIIGREKV DEKDSFVKEA LMLHQALSLC SSLVAEDDRF
EAAFFESVRV LVLRLTNTGV GKKISLPEMN ARINELLKQS IKSDGVINLF SDIKEEFSLF
DPKFLQEVAN MKEKNLAVEL LKKLIAEQVS VYRRTNVVKS EKFSEIMQRS LNAYLNGMLT
NEEVIEEMLK LAKQIAAAQK EGDQLGLTAD ELAFYDALTK PQAIKDFYKN EELIAITKEL
ADTLRKNKTI DWQKRESARA KMRMLIKKLL KKHKYPPEGM EDAVQTVMTQ CELWTDNVME
A
//
