ID F9VKB2_ARTSS Unreviewed; 1040 AA.
AC F9VKB2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 OrderedLocusNames=SFBM_0800 {ECO:0000313|EMBL:BAK56570.1};
OS Arthromitus sp. (strain SFB-mouse-Japan).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Candidatus Arthromitus.
OX NCBI_TaxID=1029718 {ECO:0000313|EMBL:BAK56570.1, ECO:0000313|Proteomes:UP000001636};
RN [1] {ECO:0000313|EMBL:BAK56570.1, ECO:0000313|Proteomes:UP000001636}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SFB-mouse-Japan {ECO:0000313|Proteomes:UP000001636};
RX PubMed=21791478; DOI=10.1093/dnares/dsr022;
RA Kuwahara T., Ogura Y., Oshima K., Kurokawa K., Ooka T., Hirakawa H.,
RA Itoh T., Nakayama-Imaohji H., Ichimura M., Itoh K., Ishifune C.,
RA Maekawa Y., Yasutomo K., Hattori M., Hayashi T.;
RT "The lifestyle of the segmented filamentous bacterium: a non-culturable
RT gut-associated immunostimulating microbe inferred by whole-genome
RT sequencing.";
RL DNA Res. 18:291-303(2011).
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}.
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DR EMBL; AP012202; BAK56570.1; -; Genomic_DNA.
DR RefSeq; WP_005806216.1; NC_015913.1.
DR AlphaFoldDB; F9VKB2; -.
DR STRING; 1029718.SFBM_0800; -.
DR REBASE; 39160; AspSFBORF802P.
DR KEGG; asf:SFBM_0800; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_9; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000001636; Chromosome.
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; 1.20.58.2040; -; 1.
DR Gene3D; 3.90.1570.50; -; 2.
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; 1.
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 309..478
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1040 AA; 122047 MW; C23DE189739624C6 CRC64;
MSNYNIIVST DESTLVTEYT SQKKRSGAYQ SEASLEKEFI EILSSQGYQY AKDINSSEEM
ISNLRFQLEK LNNIKFSNNE WKNFYKDCIA NKNEGIVQKS RKIQEDFVQI LKRDDGSSKN
ILLIDKKDIH NNFLQVINQY STDDGKYKNR YDVTILINGI PIVHVELKRR GVALKEAFNQ
IERYQRDSFW AGDGLYEYIQ IFVISNGTNT KYYSNTTRES AIKDREKANK KNKTSNSFEF
TSFWADSKNK IIPDLVDFAR TFFAKHTLLN ILTKYCVFTS ENKLVVMRPY QIMATEEILK
RIQISKNYKK MGTIKAGGYI WHTTGSGKTL TSFKTSQLSS RLEYIDKVLF VVDRKDLDYQ
TIEAYERYEK GSANGSKNTK TLQRQLENKD ENGNFHEYKI IITTIQKLDR FISKNENHPI
YNKNIVMIFD ECHRNQFGNM HRAITKKFKN YFIFGFTGTP IFEENSVNGK FKDLQTTQDV
FGDRLHTYTI VNAINDGNVL PFKIDYINTM KIKENISDKK VSAIDYEKAL LAPQRISSVT
EYILEHFNQK TKRSYGFNGF NSIFAVSSIE AAKKYYLEFK KQMEEDPSKK LKISLIYSYG
VNEESNAEFM DDENSDDTDG LSDSSRDFLE MAIKDYNKEF GTSYDTSSEK FPNFYKDVSR
KMKNRKLDLL IVVNMFLTGF DATTLNTLWV DKNLRAHGLI QAFSRTNRIL DSVKKFGNIV
CFRDLIKETD DALIIFGNDS ERNSIRETVI LKTYEDYYYG YEDENGNYHR GYGEMIEELV
NNFSDQIIGE NAEKEFIYLF GEILKLRNIL SSFDDFEGNE ILTEIEFQDF TGKYNDLYEK
VRNVENNDKE NINDDIIFEM ELVKQIEVNI DYILNLLIKY HESNNKDEEI FVAIDKAVKS
SPDLRNKKDL IDKFMLKSKK KLITDFINKV NVEDEVINDW KEFVSEEMEK DIKRLINEQR
LNEDLFRKYI KNMFRDAEVK SIGTEINEIM KPVSRFGDKN ESRYYKKQQL VEEIREFFNK
YSGIIHKEDI EKNIKEVILT
//
