ID A0A385BU41_9FLAO Unreviewed; 1000 AA.
AC A0A385BU41;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=CJ739_3623 {ECO:0000313|EMBL:AXP82685.1};
OS Mariniflexile sp. TRM1-10.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Mariniflexile.
OX NCBI_TaxID=2027857 {ECO:0000313|EMBL:AXP82685.1, ECO:0000313|Proteomes:UP000259852};
RN [1] {ECO:0000313|Proteomes:UP000259852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM1-10 {ECO:0000313|Proteomes:UP000259852};
RA Kim J.F., Kwak M.-J.;
RL Submitted (AUG-2017) 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|RuleBase:RU364115}.
CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000256|ARBA:ARBA00008598,
CC ECO:0000256|RuleBase:RU364115}.
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DR EMBL; CP022985; AXP82685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A385BU41; -.
DR REBASE; 266827; Msp110ORF3626P.
DR KEGG; marf:CJ739_3623; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000259852; 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; 3.90.1570.50; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000259852};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 275..451
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT COILED 860..908
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1000 AA; 113456 MW; 902379C74C78A0AB CRC64;
MTKEATIEQA TIDWLTDLKY IHKSGTTLPQ NNHEVVLKDQ LLGFIQKQYS ELPKDMQALV
VAEFTNNEGA DLEHRNRTFH LKLTKGLEFT YEDNDGKEKA IHIYPIDFNT PKNNTFWAVN
QFSITGKNKR RPDIIIYING LPLIVFELKN WYDENTNIKE AHNQIEHYKK DIPLLFEYNA
LTIISDGNEA QHGMFSSSME WFSAWKSMNG KDTVQEDDFQ MHTLLFGLFP KDRLLNYIKN
FVFHEDHNGT LIKKGAKYHQ FFGVNFAVEA AKKSVRPFGD GRIGVIWHTQ GSGKSISMAI
YTGILRSLPE LKNPTIVVQV DRSDLDMQLY ENFVLAKDLV GDVQHADTTD DLRQLLSAGA
GGVIFTTIEK FRLKQTTDEQ LGELEHPTLS ERENIIVMAD EAHRTQYGLL DGFASNMRKA
LPNASFIGFT GTPVDSKDAD TQEVFGNVIH TYDIKQSVDD NATVNIFYEP RLAKLHLWNE
NIDDDADEIT EANEESGNLK WAAIEDAAGS EDRVNKIAND ILNHFTNRTN TLKGKAMVVC
MSRRNCVKMY NALTALEGCP EVAVVMTGNI SKDPITWNDH IRTKDATEGL KKRFRKEEDP
LKIVIVRDMW LTGFDAPCVH TMYVDKIMKG HNLMQAITRT NRVFKDKKNG VIVDYIGIGD
NLKTATTKYT GSGGEGQPTI DIEQALELFL NQIDICKTFI PETIDYSQWR ALRDAEKVLL
VKQAVNAIIK YDEDSNNFMK AEKTLSGLLS IVKSQSAIQE FAVDVLFIQH ISKAVRNAKS
VKSSRSEQQE RIKELISQSI DSEDIVDVFA MAGIEKPDIS ILDETFLLGT KKEKDGLALK
IELIKNILKD EIKLRLHKNI KKYTSLKEEL EKVIDRYHSN ALDSYATIAE LVERAKALQN
DDDRVKELGL SEEELAFYDI LAAKQDIIKE EGPIQNIVHA IVKAVKSNLQ LDWTKKENAK
AAIRLAVKKE LRGKMSLAIL NDILQEIMQQ AEGQFSDWSA
//
