ID A0A0R2CYV7_9LACO Unreviewed; 972 AA.
AC A0A0R2CYV7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=FC56_GL000957 {ECO:0000313|EMBL:KRM93291.1};
OS Lentilactobacillus senioris DSM 24302 = JCM 17472.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lentilactobacillus.
OX NCBI_TaxID=1423802 {ECO:0000313|EMBL:KRM93291.1, ECO:0000313|Proteomes:UP000051256};
RN [1] {ECO:0000313|EMBL:KRM93291.1, ECO:0000313|Proteomes:UP000051256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24302 {ECO:0000313|EMBL:KRM93291.1,
RC ECO:0000313|Proteomes:UP000051256};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRM93291.1}.
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DR EMBL; AYZR01000009; KRM93291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2CYV7; -.
DR STRING; 1423802.FC56_GL000957; -.
DR PATRIC; fig|1423802.4.peg.970; -.
DR Proteomes; UP000051256; 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; 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; 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:UP000051256};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 259..456
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
SQ SEQUENCE 972 AA; 111552 MW; EAEDACA8758C9BB4 CRC64;
MTDMKDSKEV SQVAKEVESE AQLEDRFMQQ LAKQGYQTIQ IDKEADLINH FRRILNQRNQ
VNLKDEELTD TEFSRVMNEL VGSKTLFEIA QLLRGSDIQP AGKISIQRDD GSNVYLEFFD
GRVVENNIFE VTHQVTVNAR YTNRYDVTIL VNGLPLVQVE LKRRGGDFEE AFHQIIRYRN
DSFRNLYRFV QIFVVSDGVD TRYFANGDGN LNANFMFYWT DEENNWLNDI TDFTASFLSK
SRLHSMISKY TVFDHSNDSI MIMRPYQVYA VEAIVNQAQN HPDKNGYVWH TTGSGKTITA
FKASQILTRE TDAEKVIFLI DRSDLDIQTA KNFNAYSAQS TTNEPAIDQT NSTASLVRQL
QASDTPLIIS TIQKMNTAVK EDSSYRKLLT EFHDKHVIFI EDEAHRSQFG DMRKNINQWF
ANSQHFGFTG TPIFAENVGQ DGRTTESLYD EELHHYLIKD AIRDHNVLGF SVQYINTLKG
KADFSAEEIN EKVAKINTAE VFEADERIQL VTKHILMNHG QLTKNGHYNA IFTVPSTEIA
LKYYQAFKQL DPNHELKVTT IFTWVANEEN AVEKQDQAIK SSRLGLDQVI ADYNEQYGTE
FSTDTFSEYF ADVSKRMKEH NDQSPDSNID ILIVVNMFLT GFDSKRLATL YVDKNLQYQG
LIQAFSRTNR VETDSKPSGN IVSYRNLKAA TDQAVTLYSA GSKEDFYVKS YDELAAELRP
AIATLVTITP DAKAVDELFN QGDSAIKTFV LAFREVLRIH NKIRVYEDFK WDNFAADGLN
AQLMADFQSK YVDAYRYLQR NREQPEAASI LEDINFEIEL LETDRIDVDY IINLVKAIDL
DSQANRQSDS KRIKQMLNDT NDLKLRSKAD LIAAFLDSVV PNLPDNANVG DELNQFLAQR
RKLEVNDFAE ENKLPAQLIN SEIDDYDFYG HTNPRRVTEE LNKAGYGFKE KVSLSKKIKS
FVLQTVERFT MS
//
