UniProt: F9D320

Database: UniProt
Entry: F9D320_PREDD

LinkDB:  F9D320_PREDD 
Original site:  F9D320_PREDD

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (14)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
All databases (23)   

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ID   F9D320_PREDD            Unreviewed;       732 AA.
AC   F9D320;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 70.
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   ECO:0000313|EMBL:EGQ15202.1};
GN   OrderedLocusNames=Prede_1376 {ECO:0000313|EMBL:AGB28692.1};
GN   ORFNames=HMPREF9136_1248 {ECO:0000313|EMBL:EGQ15202.1};
OS   Prevotella dentalis (strain ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043
OS   / ES 2772) (Mitsuokella dentalis).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=908937 {ECO:0000313|EMBL:EGQ15202.1, ECO:0000313|Proteomes:UP000007820};
RN   [1] {ECO:0000313|EMBL:EGQ15202.1, ECO:0000313|Proteomes:UP000007820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3688 {ECO:0000313|EMBL:EGQ15202.1,
RC   ECO:0000313|Proteomes:UP000007820};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGB28692.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3688 {ECO:0000313|EMBL:AGB28692.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome 1 of Prevotella dentalis DSM 3688.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000010862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49559 / DSM 3688 / JCM 13448 / NCTC 12043 / ES 2772
RC   {ECO:0000313|Proteomes:UP000010862};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Chertkov O.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete sequence of chromosome 1 of Prevotella dentalis DSM 3688.";
RL   Submitted (FEB-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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001849, 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}.
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DR   EMBL; CP003368; AGB28692.1; -; Genomic_DNA.
DR   EMBL; AFPW01000016; EGQ15202.1; -; Genomic_DNA.
DR   RefSeq; WP_005845308.1; NZ_GL982488.1.
DR   AlphaFoldDB; F9D320; -.
DR   STRING; 908937.Prede_1376; -.
DR   KEGG; pdt:Prede_1376; -.
DR   PATRIC; fig|908937.9.peg.1443; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_7_0_10; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000007820; Unassembled WGS sequence.
DR   Proteomes; UP000010862; Chromosome 1.
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; 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; 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|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   Reference proteome {ECO:0000313|Proteomes:UP000010862};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          649..730
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   732 AA;  83964 MW;  8F69E8DD31D3E68F CRC64;
     MAKGKKGGKR MTKKQLTEKL VQFFSSQPGK TLSFKEIFRM LHLDTHPLKM LAIDVMEEMA
     WDDFITKVTE TSYALNTKGQ VQDGTFIRKT NGKNSFVPDG GDKPIFVAER NSMSALTGDR
     VRVSFMARRQ RHIKEAQVIE ILKRAKDVFV GRLRVDRDIA FLVPQNDTFV HDVLIPKKKL
     KGGKTGDKAL VRIVQWPDQD HRNLMGEVVD VLGPSGENDV EMNTILAQYG LPYKYPKHVE
     EAANRISGEI TPEDEAERED FRSVWTCTID PADAKDFDDA LSIRQLDKGL YQVGVHIADV
     SHYVTEGSII DKEAVKRATS VYLVDRTIPM LPERLCNFIC SLRPDEDKLA YSVVFNLDEE
     ANIKNHRIVH TIIRSKRRYA YEEAQQVLEA NGVVDGTGNP APDPGKKGYK GDNGWELCTL
     DRLAKKLRAQ RFRNGSVKFD SEELHFDIDE KGHPTRAFFK RSKDANKLIE EFMLLANRTV
     AESIGRRPKG KTAKTLPYRI HDNPDPQKME NLREFIVKFG YKVKTDGTRS AMARSINKLM
     DDCEGKREQK LIQAVALRAM MKAKYSVHNI GHFGLAFDYY THFTSPIRRY PDMMVHRLLT
     KYAQGGRSAN EKHCEELCEH CSEMEQIAQN AERDSIKYKM VEYMADKLGN EYDAHISGIT
     SYGIYAEIDE NHCEGMVPMR DLDDDYYDFD ERNFLLRGRR HHHKYQLGDA VRIKVAKANL
     EKRQLDFTLA EK
//

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