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Database: UniProt
Entry: A0A0R1JN58_9LACO
LinkDB: A0A0R1JN58_9LACO
Original site: A0A0R1JN58_9LACO 
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
//
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