ID A0A0R1JN58_9LACO Unreviewed; 1023 AA.
AC A0A0R1JN58;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=FD02_GL001315 {ECO:0000313|EMBL:KRK72896.1};
OS Lacticaseibacillus nasuensis JCM 17158.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291734 {ECO:0000313|EMBL:KRK72896.1, ECO:0000313|Proteomes:UP000051804};
RN [1] {ECO:0000313|EMBL:KRK72896.1, ECO:0000313|Proteomes:UP000051804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 17158 {ECO:0000313|EMBL:KRK72896.1,
RC ECO:0000313|Proteomes:UP000051804};
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:KRK72896.1}.
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DR EMBL; AZDJ01000016; KRK72896.1; -; Genomic_DNA.
DR RefSeq; WP_056950834.1; NZ_AZDJ01000016.1.
DR AlphaFoldDB; A0A0R1JN58; -.
DR STRING; 1291734.FD02_GL001315; -.
DR PATRIC; fig|1291734.4.peg.1351; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000051804; 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; 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 R PROTEIN; 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:UP000051804};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 278..446
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1023 AA; 116320 MW; 13CF5D99E5377338 CRC64;
MTSELAFESE LIEHLCHIGG TKQWQYEPGI KNTDQLWANF KHILEQNNPH LSQPLSALEF
AQVKAEITKL KTPYEAGRFI YGLNGVTQVE VNLDNGEHVY LTVFDQDEVG AGNTRYQIVN
QIERPAVLAG RHDRRFDTTL LINGLPIIQI EEKKAAHDAR EALNQMQQYI DEQQYTGIFA
TLQILIGMTP NNIRYMANTP ADKFNTAFAF QWQREADSTN VRDWREFANL MLSIPMAHQM
ATNYIILDGT RNKQAIKVMR PYQVYATRNI IRKLRGFQFG LDPQEAGYIW HTTGSGKTIS
SFKAAWLASR LPNVDKVVFM VDRVALTNQT AANYAAYDPG TNDMNKDGVV SDTANISVLR
KKLREPGGII VTSIQKLDRL TQRASFKAPD KHIVFIVDEA HRSTAGEMLQ RIKKAFPKSA
WFGYTGTPSF DGITTEQLFG KPLHIYTIRE AIADRNVLGF KVDFDTTLSD KALKDQYLPE
FYRASHPDWT AADIRNKING MTAEDMDDAV LPSVYDMNAQ HVELVVKNIF EKWRNRSDDY
RYAALLTTHV GGGKASTPMA MMYYREFKKQ NVSQKHPLKV AITFSQSTNN QDEQLAANRS
LREAIEDYNQ LFNEHFDDTT VKEYTENVVS RLNRTIDDGN YLDLVIVIDQ LLTGFDAPQL
NTLYVDRTLQ GANLIQAYSR TNRIENMTHK PYGRIVNYRW PVHSKQLMND ALQVYANRGS
ANLQLDLVGD GDEPGVLAPD FEDLIKNARG VVNDLRNTTR NFTDLPASES KQEDMYNLLK
RYNGLINQLK QDQHYDYDHP ETLLNQIGLT SDQEQVLTGS LANDLKERIA QRRGVDFSDL
TLEMQHVEEV QVNYDYLDEL IAQLANQVHT GDHDAADATV AEVNKAADQL EDRKYAKQVK
QTASDIRSGE TTAGSYPMQA NQSRALVAGN AQRTRRRAIS QFRTKWGLLD INVEAMDAML
SRHAKNADDL DIDNTLTNLI NKGQAHYRDD AADEQVQALT KIKYRAEVRE AIKRFADSLI
DNY
//