ID   A0A1I0FVV4_9GAMM        Unreviewed;       765 AA.
AC   A0A1I0FVV4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
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};
GN   ORFNames=SAMN02583745_02913 {ECO:0000313|EMBL:SET62544.1};
OS   Thorsellia anophelis DSM 18579.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Thorselliaceae; Thorsellia.
OX   NCBI_TaxID=1123402 {ECO:0000313|EMBL:SET62544.1, ECO:0000313|Proteomes:UP000242642};
RN   [1] {ECO:0000313|Proteomes:UP000242642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18579 {ECO:0000313|Proteomes:UP000242642};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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|RuleBase:RU364115};
CC   -!- SUBUNIT: The type I restriction/modification system is composed of
CC       three polypeptides R, M and S. {ECO:0000256|RuleBase:RU364115}.
CC   -!- SIMILARITY: Belongs to the HsdR family.
CC       {ECO:0000256|RuleBase:RU364115}.
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DR   EMBL; FOHV01000050; SET62544.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0FVV4; -.
DR   STRING; 1123402.SAMN02583745_02913; -.
DR   Proteomes; UP000242642; 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; cd18800; SF2_C_EcoR124I-like; 1.
DR   Gene3D; 1.10.10.2110; -; 1.
DR   Gene3D; 1.20.58.2040; -; 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; 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; 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|RuleBase:RU364115};
KW   DNA-binding {ECO:0000256|RuleBase:RU364115};
KW   Hydrolase {ECO:0000256|RuleBase:RU364115};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU364115};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242642};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW   ECO:0000256|RuleBase:RU364115}.
FT   DOMAIN          23..168
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
SQ   SEQUENCE   765 AA;  87985 MW;  EE88008C78611808 CRC64;
     MRPYQIAATE RILWKIKSSY LAKTWSDTQS GGYIWHTTGS GKTLTSFKAA RLATELDFID
     KVFFVVDRKD LDYQTMKEYQ RFSPDSVNGS NSTQGLRQNI EKDDNRIIVT TIQKLNNLIR
     AENDLAIYQK QVVFIFDEAH RSQFGEAQKN IQKKFKKYYQ FGFTGTPIFT QNALGSETTQ
     SVFGTELHAY VITDAIRDEK VLKFKVDYND LRPHFKQIEM EQDEEKLSSA ALKQAFLHPE
     RIKEVTQYIL KHFRHKTHRL KPGSKGFNAM FAVSSVDAAK AYYESFKRLQ QEQMAISPNT
     KPLNVATIFS YAANEEQDAI GDITDESLET SAMNSTAREF LDGVIKDYNA HFNANFSTEG
     EGFQQYYRDL AKRVKSQEVD LLIVVGMFLT GFDAPTLNTL FVDKNLKYHG LIQAFSRTNR
     IYDATKSFGN IVTFRNLEQE TIDAIKLFGD KNTKNVILEK SFDEYMNGFT DILSGKARRG
     FIEIVAELNA RFPNPQEIET EADKKAFVKL FGEYLRVENL LQNFDEFTAL SELQAIDINN
     AEALEAFKIE HHLTDEMLTE LKGIKLPTER ELQDYRSVYN DTRDWLRAPE EGKESPTLDW
     NDVVFEVEIL NSLEINLDYI LTLIFKEKQS QKTKADLIEE VRRVIRSSLD NRAKESLLID
     FINQTHLESI SDSASIIDAF FTFAKAELRR EVEQLIQTEN LNDTAARRYI NSSLKREHAS
     ESGTELNDAL PKMSLLNPEY KTKKQTVYQK VSELVEKYKG IGSGV
//