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Database: UniProt
Entry: A0A1H0UXL5_9CLOT
LinkDB: A0A1H0UXL5_9CLOT
Original site: A0A1H0UXL5_9CLOT 
ID   A0A1H0UXL5_9CLOT        Unreviewed;       739 AA.
AC   A0A1H0UXL5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=SAMN04488529_11332 {ECO:0000313|EMBL:SDP70920.1};
OS   Clostridium gasigenes.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP70920.1, ECO:0000313|Proteomes:UP000198597};
RN   [1] {ECO:0000313|EMBL:SDP70920.1, ECO:0000313|Proteomes:UP000198597}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP70920.1,
RC   ECO:0000313|Proteomes:UP000198597};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNJM01000013; SDP70920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0UXL5; -.
DR   STRING; 94869.SAMN04488529_11332; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000198597; 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; 4.
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:UP000198597};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
SQ   SEQUENCE   739 AA;  85302 MW;  ADF2B8D68C4276F5 CRC64;
     MGMKKTLLNF MREEAYRPMD IQELVTVFDI SQEEYKPFKK TLKTMEKEGT IIRTKKDKFG
     IPERMGLVRG KLQAHQKGFG FLIPETEGER DVFIPSSFMN GAMNGDKILV QVTKEDKNGT
     KKREGEVVDI LERGNSKIIG IYEGNKNFGF VVPEDTRLNQ DIFVSKKDKN GAEDGDVVVV
     EITRWPDQRR SPEGVVEQVL GKKGDKGLDI LTIIKKYGLP EEFSEKILSY AEGVSETIED
     KEYRRRKDLR NMKMVTIDGE DAKDLDDAVS IEKLENGTFK LGVHIADVTH YVREQSPLDK
     EAFDRATSVY LLDRVIPMLP RKLSNGICSL NPSVDRLTLS CFMTIDQSGK IIDHEIAETI
     INTTARMTYT DVTKILKDKD AELIKKYENL HQDFLDMEEL CAILRNKRMR RGAIDFDFPE
     SKIILNELGK PVDIKPYERG IANKIIEEFM LAANETVAEY MHWAHMPFVY RIHEEPDEEK
     LTKFKEFVYN LGYGIRWTQD VQPKLLQEVL EKVKGKPEEP VVSKLLLRSM MQAKYSPECV
     GHFGLAAKYY CHFTSPIRRY PDLQIHRIIK EHLNAKIDEK RAEKLAVIVD QTSKQSSERE
     RVAEQAEREV DDLKKAEYMQ NRIGEEFEGM ISSVTSFGIF VQLPNTIEGL VHITELDDDY
     YIYDEAHLCL IGERTKKVYR LGAVVKVKCT KVDIDNREVY FNLTEEEEAP KTEIKANKKL
     VDELLEVKEE MKTNYVDEE
//
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