ID A0A1T4NUU1_9FIRM Unreviewed; 1033 AA.
AC A0A1T4NUU1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN02745973_01806 {ECO:0000313|EMBL:SJZ83011.1};
OS Garciella nitratireducens DSM 15102.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae; Garciella.
OX NCBI_TaxID=1121911 {ECO:0000313|EMBL:SJZ83011.1, ECO:0000313|Proteomes:UP000196365};
RN [1] {ECO:0000313|EMBL:SJZ83011.1, ECO:0000313|Proteomes:UP000196365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15102 {ECO:0000313|EMBL:SJZ83011.1,
RC ECO:0000313|Proteomes:UP000196365};
RA Peterson S.W.;
RL Submitted (FEB-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|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; FUWV01000013; SJZ83011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4NUU1; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000196365; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000196365};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 311..480
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1033 AA; 119886 MW; 1B116F24EB321041 CRC64;
MSIYNIVAST DEATVVAEYS AEYNVRSEKY QSEAELERDF IRQLTSQGYE YISVHNEAAL
IENLRKQLEL LNDFTFTDSE WDRFFTECIA NTNEGIVEKT RKIQDDHIQI LKREDGTTKN
IYLLDKKNIH NNCLQVINQY EEAGGKHETR YDVTILVNGL PLVHVELKRR GVAIREAFNQ
IKRYQRDSFW ASSGLFEYVQ VFVISNGTHT KYYSNTTRNA HIKEQSSSER RRSKKTSNSF
EFTSFWADAN NKIIPDLVDF TKTFFAKHTL LNILTKYCIF TSEDLLLVMR PYQIAAAERI
LSRIVVSTNY KKMGTTAAGG YIWHTTGSGK TLTSFKTAQL ASVLPYIDKV LFVVDRKDLD
YQTMKEYDRF EKGSANGNTS TRVLQRQLED KDEKGNPHEY KIIVTTIQKL DIFIRKNKQH
DIYKKHVVLI FDECHRSQFG EMHQAITKSF KNYHIFGFTG TPIFAANASS GGNPLLRTTE
QAFGEKLHTY TIVDAINDGN VLPFRIDFIN TIKMPDYVND KKVYNIDREK ALADPQRISE
IVSYVLEHFD QKTKRNSYYT FSAKWEEADK HNPKKMIEKR ETRRVAGFNS IFAAASIPMA
IRYYNEFKKQ IAEKKRNLTI ATIFSFSANE EEPDGLLPEE DFNMENLDQS SRDFLEAAIR
DYNTTFNTNY DTSSEKFQNY YKDLSLRVKN REIDILIVVN MFLTGFDATT LNTLWVDKNL
RQHGLIQAFS RTNRILNSVK TYGNIVCFRD LKEETDKAIA LFGNKDAGGI VLLKTFQEYY
NGYDDKGEHK PGYAELIATL TTQYPLGQPI LGEKAEKDFI RLYGAILRLR NILTSFDDFE
GNEILSERDF QDYQSIYIDL YQEYRKSTDG DKETINDDIV FEIELVKQIE VNIDYILMLV
AKYQKSNCKD KTILTTIDKA INSSIELRSK KELIERFIEQ VNVSTKVDED WRKFLHERKE
ADITAIIEEE RLKPKETRRF IDNAFRDGML KTTGTDIDKI MPPVSRFGGG RAAKKQGIIE
KLMIFFEKYL GLV
//
