ID F2IJ92_FLUTR Unreviewed; 1035 AA.
AC F2IJ92;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 OrderedLocusNames=Fluta_2983 {ECO:0000313|EMBL:AEA44962.1};
OS Fluviicola taffensis (strain DSM 16823 / NCIMB 13979 / RW262).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Crocinitomicaceae; Fluviicola.
OX NCBI_TaxID=755732 {ECO:0000313|EMBL:AEA44962.1, ECO:0000313|Proteomes:UP000007463};
RN [1] {ECO:0000313|EMBL:AEA44962.1, ECO:0000313|Proteomes:UP000007463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463};
RX PubMed=22180807; DOI=10.4056/sigs.2124912;
RA Woyke T., Chertkov O., Lapidus A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Mwirichia R., Sikorski J., Tindall B.J., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of the gliding freshwater bacterium Fluviicola
RT taffensis type strain (RW262).";
RL Stand. Genomic Sci. 5:21-29(2011).
RN [2] {ECO:0000313|Proteomes:UP000007463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16823 / RW262 / RW262 {ECO:0000313|Proteomes:UP000007463};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Pomrenke H.G., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Fluviicola taffensis DSM 16823.";
RL Submitted (FEB-2011) 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; CP002542; AEA44962.1; -; Genomic_DNA.
DR RefSeq; WP_013687731.1; NC_015321.1.
DR AlphaFoldDB; F2IJ92; -.
DR STRING; 755732.Fluta_2983; -.
DR REBASE; 33800; FtaORF2980P.
DR KEGG; fte:Fluta_2983; -.
DR eggNOG; COG0610; Bacteria.
DR HOGENOM; CLU_004848_1_0_10; -.
DR OrthoDB; 9758243at2; -.
DR Proteomes; UP000007463; 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; 1.10.10.2110; -; 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; 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 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:UP000007463};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747,
KW ECO:0000256|RuleBase:RU364115}.
FT DOMAIN 297..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
SQ SEQUENCE 1035 AA; 119779 MW; D39B76353CC01452 CRC64;
MKQYKTIAES NNFIVLDQYI KFSAWNEAPA VYQTESALEK EFLQDLINQG YDNPTNLNTI
EAMLANARIQ LQTLNDMEFT DSEWIRYVEE YLDKPSDNLV EKTRKIHDNY IYDFVFDDGH
IQNIYLVDKK NVACNKVQVI SQFGQKGTHA NRYDVTILVN GLPLVQVELK KRGVAIREAF
NQVHRYTKES LNSTNSLFKY VQIFVISNGT DSRYFANTVE RNKNSFDFTM NWAKSDNALI
KDLKDFTATF FQKQTLLQVL LTYSVFDTSD TLLTMRPYQI AATERILWKI NSSFQSKNWS
KTEGGGYIWH TTGSGKTLTS FKAARLATQL DFIDKVFFVV DRKDLDFQTM KEYQRFSPDS
VNGSDSTAGL KSNIEKEDNK IIVTTIQKLN NLMKTESDLA IYQKQVVFIF DEAHRSQFGE
AQKNLNKKFK KFYQFGFTGT PIFPVNALGA ETTASVFGTE LHSYVITDAI RDEKVLKFKV
DYNDVRPHFK SIETEIDEKK LSAAENKKAF LHPARISEIS QYILQNFRIK THRNQGSNKG
FNAMFAVSSV DAAKCYYEEI NRLQKESDKP LKIATIFSFA ANEEQNAIGE IVDESFEPNA
LDSSSKEFLT EAINDYNKMF KTSFGVESKE FQNYYRDLAK RVKSKEVDLI IVVGMFLTGF
DAPTLNTLFV DKNLRYHGLM QAFSRTNRIY DATKTFGNII TFRDLENATV EAITLFGDKN
TKNVVLEKSF KEYLEGFTDS TTGDARRGYI EVVNELNEKF PNPDEIETEK SKKEFSKLFG
EYLRVENILQ NYDEFSNLKA FQAIDKNDPE AIETFKETHF LSDDDIVVLQ EIELLPERTV
QDYRSTYNDI RDWLRREKGG KEAEESKIDW DDVVFEIDLL KSQEINLDYI LELIFEQNKK
NKDKASLIEE IRRVVRASIG NRAKEGLVVD FINETDLETI QDKANVLDLF YAYAQEKLKI
EASELIEEEN LNEEEAIRYI SASLKRKYTS ENGTELNAIL PKMSPLNPQY LTKKQNVFKK
ISLFIEKYKE IDEKI
//
