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Database: UniProt
Entry: H1PKQ2_9FIRM
LinkDB: H1PKQ2_9FIRM
Original site: H1PKQ2_9FIRM 
ID   H1PKQ2_9FIRM            Unreviewed;       646 AA.
AC   H1PKQ2;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
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=HMPREF0380_00760 {ECO:0000313|EMBL:EHO85908.1};
OS   Eubacterium infirmum F0142.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=883109 {ECO:0000313|EMBL:EHO85908.1, ECO:0000313|Proteomes:UP000004504};
RN   [1] {ECO:0000313|EMBL:EHO85908.1, ECO:0000313|Proteomes:UP000004504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0142 {ECO:0000313|EMBL:EHO85908.1,
RC   ECO:0000313|Proteomes:UP000004504};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA   Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Eubacterium infirmum F0142.";
RL   Submitted (DEC-2011) 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; AGWI01000010; EHO85908.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1PKQ2; -.
DR   STRING; 883109.HMPREF0380_00760; -.
DR   PATRIC; fig|883109.3.peg.754; -.
DR   eggNOG; COG0557; Bacteria.
DR   HOGENOM; CLU_002333_4_1_9; -.
DR   Proteomes; UP000004504; 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; 3.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
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; 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; SM00357; CSP; 2.
DR   SMART; SM00955; RNB; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
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:UP000004504};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          566..646
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   646 AA;  73898 MW;  A10D5AB8B0AECD1C CRC64;
     MSKKSKSKKK LITGEIYKAK GGFGFLKCDA FEKDVFIARK HMKDAMDGDI AEVALIPMPL
     WENGPEGFVV NIKERMVTEL VGTLDKSGKN GFLIPIEKRL KEDVFIPSKW LRGAKNGDKL
     LVKIRKYPQD DRLAEGEVLK IIARKDDSDR DIKALIYEHD VSVEFPKEIE AETRKVADLV
     LEYTDTGSRL DLRKEEIITI DGAYSKDLDD AVSLKKNEKG NFVLGVHIAD VSEFVREGMA
     LDAEALNRGN SIYLIDHVVP MLPVLLSNKL CSLNEGEDRF TLSCIMEIDR RGKVQEYKIC
     ESIIKSSARL VYDEVSDFLE HGKANAKLEA HGAMLKDMQE LAECLKKARE ELGSIDFDID
     EAEFEIDKDG VPVDISLTER RTANLLIEEF MLVANRTVAE HYFWMEYPFI YRVHEKPLPE
     KVMELKSFLK GIGISLPLNE GNIHPLALRN LLEEADKDGK LSLVSAVMVR SMQKAFYSPE
     CLGHYGLAFK QYCHFTSPIR RYADLWIHRM IKHQMHEELS DEQLSKYHEK AKKVSDIVSE
     TERKAISMER ELEKLKKAQY MERWVGYEEQ GVISGITSFG IFVQLPNTVE GLVRFDTLTD
     DYYEFDQENY RLVGCNHGRE FRLGDSVKVV CTRVDTLIGT IDFRLS
//
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