ID A0A091C2F5_9ENTE Unreviewed; 1017 AA.
AC A0A091C2F5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=TMU3MR103_1621 {ECO:0000313|EMBL:KFN90242.1};
OS Tetragenococcus muriaticus 3MR10-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Tetragenococcus.
OX NCBI_TaxID=1302648 {ECO:0000313|EMBL:KFN90242.1, ECO:0000313|Proteomes:UP000029381};
RN [1] {ECO:0000313|EMBL:KFN90242.1, ECO:0000313|Proteomes:UP000029381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3MR10-3 {ECO:0000313|EMBL:KFN90242.1,
RC ECO:0000313|Proteomes:UP000029381};
RA Chuea-nongthon C., Rodtong S., Yongsawatdigul J., Steele J.L., Liu X.-y.,
RA Speers J., Glasner J.D., Neeno-Eckwall E.C.;
RT "Genome sequence of Tetragenococcus muriaticus.";
RL Submitted (AUG-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}.
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:KFN90242.1}.
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DR EMBL; JPVT01000171; KFN90242.1; -; Genomic_DNA.
DR RefSeq; WP_038023743.1; NZ_JPVT01000171.1.
DR AlphaFoldDB; A0A091C2F5; -.
DR REBASE; 195040; Tmu103ORF1621P.
DR PATRIC; fig|1302648.3.peg.1583; -.
DR Proteomes; UP000029381; 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; 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:UP000029381};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 272..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 962..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 118801 MW; EA3B7BBD06BABE78 CRC64;
MVQFTAEQEL ENNLIKQLIS GISQWTYRDD LHTEDELWEN FRKKLEANNK DVLNSVPLTE
QEFRQIQNQL QFPNFYEAAR WLSGENGIAK VQVQREDAAL GTIRLRVINR QDVAGGSSSY
EVINQFKSNK RSLDDNDRRF DVTLLINGLP MIHIELKNRA HPYMDAFRQI RKYLKEGKFT
GIYSTLQMFV VTNGTETRYI ASAVDTKLNE QFLTKWVDHE NEPVNDYLAF AQDVLSIPMA
HKMVTQYTVI DNSRKSLILL RPYQIHAVEA VKQASMQAKS GYVWHTTGSG KTLTSYKVAR
NLLQIPSIQK TIFIVDRRDL DQQTTASFLS YSENDVIDID ETNSVNDLIK KLLSDDRTVV
VTTIQKLNYV MKRFADKEGT KRYEKMTQLK LAFVVDECHR AVSPQKKREI EAFFRQSLWY
GFTGTPIFVE NKKSVLGDLP QTTEQQYGEC LHQYTVKEAI HDQAVLGFQV EYKATFAENT
LNKIIEESHP QKRFNLDEML LEEKEELLPK DVYEREDHML KVIDSIVNNS RTKLGFSKGA
GQTYDAILTT SSINKALNYY DLIKKVKSGE TDIRVEEKTK RVLPDFPKVA ITYSISENEE
SSSKEQEKMK EILRDYNEEF ETNFTLETMR AYNRNINDRL SRKKEKYLAR SEQLDLVIVV
DRLLTGFDAP CLSTLFIDRQ PMQPHDLIQA FSRTNRLFDK NKKYGQIVTF QKPEIFEKEV
KEALILYSNG GETEVLAPSW EEATDNFITA IEEMREIVSS PAEVENLNEA ELKKFIKAYQ
KLDRTYSSVQ VYTDFTEDKM GTVFPINEDE IEEFHGRYKN ALDEVKKEDK DEDETEPIDI
YYELESVKTE EINYEYILNL IQAFVPSGDD EYELISKVDQ KAMNEVDQYI DQLAKSNEKL
ARLMRHLWNN IQQEPENYRD QNVSNLLEDM VQGTSYEVQQ EFSDKWQVDE EELAYVMENY
NPKKKHQNGE QELQRTADYS TYKEKAEEPV SKLKYGKTMR KELDKVMKEE ILPLRRQ
//
