ID R2QCD1_9ENTE Unreviewed; 1043 AA.
AC R2QCD1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=UAW_02929 {ECO:0000313|EMBL:EOH92888.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH92888.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH92888.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH92888.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) 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:EOH92888.1}.
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DR EMBL; AJAR01000027; EOH92888.1; -; Genomic_DNA.
DR RefSeq; WP_010763085.1; NZ_KE136479.1.
DR AlphaFoldDB; R2QCD1; -.
DR STRING; 155618.RV06_GL001907; -.
DR PATRIC; fig|1158608.3.peg.2863; -.
DR eggNOG; COG0610; Bacteria.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000013858; 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 Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 278..430
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1043 AA; 120293 MW; FF3E436BBD0962B1 CRC64;
MNENQFETEL IKHIKNIAGT KQWQYEENIK TTEALWFNFK NILEQHNQNL LEKPLSEAEF
SQVKKVICDI KSPYEAGQFL YGLNGVSQIE IDLDDGRHVF LTVFDQKQIG AGNTIYQVVN
QIKRPAVIVG KKDRRFDTTL MVNGLPIIQI EEKTDTRDVN EALNQMHQYA DEKQFRDIFS
TLQILVAITP NNVKYMANTP SNKFNKDFAF NWQRKEDNMI VRNWKEFANS MLSIPMAHQM
ATNFMILDGT KNKQMLKVMR PYQVYATQNV MESLKKVDFE LGVNKIGYIW HTTGSGKTIT
SFKTAWLASR MPKVDKVVFV VDRIALTKQT NENYQAYDPD GDIDDSKIGN VQGTNSTNDL
NQKLKSKDNQ IIVTSVQKLG TLVNRQNFES PDKNIVFIVD EAHRSTGSNN FAMIQKAFKK
ACWIGYTGTP MFDDTTKGLR TEDIFGELLH AYTIREAISD RNVLGFKVDF ETTIDEEQVK
SDYLPKFYKE RYPTWTDEKI QEKIENLSPE DMDDAVEPSF YDENAEHIKM VVEDIFKNWR
NRSNEGRYNA LFTTHVGGGK ASTPMAMMYF NEFQRVNVEN KQNGKQTLKV AVTFSLNTSN
NDSQLLTNQG LFEAIQAYND EFGTSFGMDD VSGYTQEVTS RLNRTITDKK YLDIVIVVDQ
LLTGFDAPEL NTLYVDRTLK GAGLIQAYSR TNRIADLQEK PWGRIVNYRW PAQNEKLMNQ
ALAIYANKDS AILSEEEQRE SNKKEGIVAK PFLEVFNEVK KIVAKLDTLT SEFQQLPPSE
KKKEKMFDLL KEYNAGMSKL KQYDPSEVDG DTVGFNYDEP DELVAKLGMT TDQEVMLSTV
LSNELKQHIA KKKDVPFYQI ELKMTHVKDI KVDYDYLTEL VERLLNQVHD KQYQEAKETK
EKLDQFADGL DDRKYAEMIK NAATAIYKGH FIVEKYPAKL KESDSIIQLA SNVSLDRRFQ
DFRIKWGIID IVTSAEMRKL FEKHRYGQQD LDDTGQIREI VSKASIDYQT LAHDEAIQSL
SRIKYRNGLR AEIYKLADEL TRD
//
