ID D3PSB0_MEIRD Unreviewed; 813 AA.
AC D3PSB0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN OrderedLocusNames=Mrub_1581 {ECO:0000313|EMBL:ADD28343.1};
GN ORFNames=K649_14655 {ECO:0000313|EMBL:AGK06217.1};
OS Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS ruber).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK06217.1, ECO:0000313|Proteomes:UP000013026};
RN [1] {ECO:0000313|EMBL:ADD28343.1, ECO:0000313|Proteomes:UP000006655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000006655}, and DSM 1279
RC {ECO:0000313|EMBL:ADD28343.1};
RX PubMed=21304689; DOI=10.4056/sigs.1032748;
RA Tindall B.J., Sikorski J., Lucas S., Goltsman E., Copeland A.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Han C., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Ovchinnikova G., Pati A.,
RA Fahnrich R., Goodwin L., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Meiothermus ruber type strain (21).";
RL Stand. Genomic Sci. 3:26-36(2010).
RN [2] {ECO:0000313|EMBL:AGK06217.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK06217.1};
RA Klammer A., Drake J., Heiner C., Clum A., Copeland A., Huddleston J.,
RA Eichler E., Turner S.W.;
RT "Non-Hybrid, Finished Microbial Genome Assemblies from Long-Read SMRT
RT Sequencing Data.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AGK06217.1, ECO:0000313|Proteomes:UP000013026}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC {ECO:0000313|Proteomes:UP000013026}, and DSM 1279
RC {ECO:0000313|EMBL:AGK06217.1};
RA Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC monophosphates and is involved in maturation of structured RNAs.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.13.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001849, ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR EMBL; CP001743; ADD28343.1; -; Genomic_DNA.
DR EMBL; CP005385; AGK06217.1; -; Genomic_DNA.
DR RefSeq; WP_013013845.1; NC_021081.1.
DR AlphaFoldDB; D3PSB0; -.
DR STRING; 504728.K649_14655; -.
DR KEGG; mrb:Mrub_1581; -.
DR KEGG; mre:K649_14655; -.
DR PATRIC; fig|504728.9.peg.3009; -.
DR eggNOG; COG0557; Bacteria.
DR OrthoDB; 9764149at2; -.
DR Proteomes; UP000006655; Chromosome.
DR Proteomes; UP000013026; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016070; P:RNA metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04471; S1_RNase_R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 1.
DR NCBIfam; TIGR02063; RNase_R; 1.
DR PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR Pfam; PF17876; CSD2; 1.
DR Pfam; PF08206; OB_RNB; 1.
DR Pfam; PF00773; RNB; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839, ECO:0000256|HAMAP-
KW Rule:MF_01895};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_01895};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 626..706
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 709..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 91698 MW; 5ECD4F9E2043167F CRC64;
MLEQRIYEHL KQHPKKRFSL RELVRSLRLD KDEAKEALDL LVAEGKVVEP RRKLYQLPEG
PGKKGLEGRL QAHAAGFAFV IPTNPDLPDL YIPKGHLGGA WHGDLVRAEP RPPGRGRDGK
PWGVVVEVLE RAHHQVVGRL YFKQGFAWLK PDDPRLPALK LKPEGLEGLE SGARLVVRVT
FPSGRKPQEP YGEFAGYLGQ GDSPEVETEA IIAKYELRSV FPPEALAEAE KVAHLDPKEV
ARREDFRALR VFTIDGADAK DFDDAIHLEL LPNGNYRVGI HIADVSHYVK EFSPLDHEAY
ARATSVYLPG RVLPMLPEQL SNGICSLKPH QDRLVLSVLV ELTPKGRVKD YRFAEGVIRS
VARLTYTEVE AFAEALEAPE KALAPAPSDW SLELQNDLKL LLGLTRTLKE RRLEQGALDF
RFTEVKVEVD EEGNLHLIPQ KEPRARSLIE ELMLLANRVV AKHLAEREIP TLFRVHEDPS
EEAYNKLVAA LGRLGYSLPG GEPSPKALQS ILKQAEGRPE EAVVSTLLLR SLRLARYAAE
NLGHFGLAAE HYLHFTSPIR RYPDLVVHRV LRALLKRRVT QARKEDWAQR FPKIAEHASE
RERAAESAER ELTKYYQCLW AQKHQGETFR GTVSGVTGFG VFVSLDNGVE GMIRLGALED
DHYEYIEELL ALEGLRTKRR IRIGDEMEVK IEGANPSARQ IDLVPTEKFY QTETQPEPEQ
PKRKKRRRGK RGKAAEAPSK AARKVVATEP KSPAPHARAR SRRVVGPPEE RGGFQKPVKV
RAQKIYFGSW GGDQEQAPPS KAEKSGKKKR RRR
//
