ID R7PAQ1_9BACT Unreviewed; 774 AA.
AC R7PAQ1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=BN736_01198 {ECO:0000313|EMBL:CDF21407.1};
OS Prevotella sp. CAG:617.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262933 {ECO:0000313|EMBL:CDF21407.1, ECO:0000313|Proteomes:UP000018057};
RN [1] {ECO:0000313|EMBL:CDF21407.1, ECO:0000313|Proteomes:UP000018057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:617 {ECO:0000313|Proteomes:UP000018057};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01895}.
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:CDF21407.1}.
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DR EMBL; CBKM010000039; CDF21407.1; -; Genomic_DNA.
DR AlphaFoldDB; R7PAQ1; -.
DR STRING; 1262933.BN736_01198; -.
DR Proteomes; UP000018057; Unassembled WGS sequence.
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; 1.
DR HAMAP; MF_01895; RNase_R; 1.
DR InterPro; IPR040476; CSD2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR003029; S1_domain.
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; 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; 3.
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|HAMAP-Rule:MF_01895};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895};
KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01895};
KW Reference proteome {ECO:0000313|Proteomes:UP000018057};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 657..738
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 746..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..774
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 774 AA; 88198 MW; 038DEEDF97D6E0EF CRC64;
MGQKSKKGGR RLTKKEITEL LLKFFEQHAQ EEYNIQDLFH EIRATTHPAK MLTMDVLNEL
VLDDYLATDK QGHYRLAVRS QVMEGTFVRK RNGRNSFLPD DGGQPILVCE RNAHRALNGD
RVRVTMLARR RGHTREAEVI EIVKRSHDTF VGKLHVDKHY AFLITEDRAL ANDIFIPKDK
LKGGKTGDKA VVKIIEWPQD AKNPIGKVID ILGKTGDNDT EMNAILAEYN LPYEYPKAVE
EAADKISDVI SDEEIARRED VRQVTTFTID PHDAKDFDDA LSIRRIDAGT WEVGVHIADV
SYYVHEGDII DKEAQKRATS IYLVDRTIPM LPERLCNYIC SLRPDEDKLA YSTLFRMNEE
GDVLSWHLAK TVIRSNRRFT YEEVQTILEQ NGEASAEDLA LPGEHPEKVG PGPDGKPVGE
YAEELVTLNR LAKKLRKRRF SHGAIGFDRA EIRFEIDEKG HPISTYVKIA KDANKLVEEF
MLLANRSVAE SVGKVPKGKK AKVLPYRIHD VPDPEKLEKL SGFISRFGYR LRTEGTKTEV
SRSLNKLLSD VKGKKEQELV ETVALRAMMK ARYSTENIGH YGLMFDYYTH FTSPIRRYPD
TMVHRLLARY AAGGRSVSKD KYEELCEHAS AMEQLAASAE RASIKYKQVE FMADRLGQEF
AGTVSGVTEF GLYVAIDENQ CEGMVPLRDL QGDYYEFDEK NYCLRGRKNH HTYSLGDKVR
IKVARANLEK RQLDFELVSR PDEQPVALLP PTVKEKKGGK KGKRGGKAKR HKEK
//
