ID A0A166V2U9_9CYAN Unreviewed; 827 AA. AC A0A166V2U9; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 31-JUL-2019, entry version 15. 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=AY599_03785 {ECO:0000313|EMBL:OAB62357.1}; OS Leptolyngbya valderiana BDU 20041. OC Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae; OC Leptolyngbya. OX NCBI_TaxID=322866 {ECO:0000313|EMBL:OAB62357.1}; RN [1] {ECO:0000313|EMBL:OAB62357.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB62357.1}; RA Wen L., He K., Yang H.; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:OAB62357.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BDU 20041 {ECO:0000313|EMBL:OAB62357.1}; RA Peter A.P., Garlapati D., Kaliaperumal E.M., Lakshmanan K., RA Tyagaraj B.; RT "De novo Whole Genome Sequencing of Leptolyngbya valderiana BDU RT 20041."; RL Submitted (MAY-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 CC yield nucleoside 5'-phosphates.; EC=3.1.13.1; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01895, CC ECO:0000256|SAAS:SAAS01124678}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895, CC ECO:0000256|SAAS:SAAS00089931}. CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:OAB62357.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LSYZ01000072; OAB62357.1; -; Genomic_DNA. DR RefSeq; WP_063715972.1; NZ_LSYZ01000072.1. DR EnsemblBacteria; OAB62357; OAB62357; AY599_03785. DR OrthoDB; 1602988at2; -. DR BioCyc; GCF_001637395:G1ET2-1795-MONOMER; -. 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 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; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. 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; SSF50249; 4. DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1. 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 ECO:0000256|SAAS:SAAS00462075}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00089915}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00089892}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462054}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895, KW ECO:0000256|SAAS:SAAS00462035}. FT DOMAIN 675 764 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT REGION 786 827 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. SQ SEQUENCE 827 AA; 90857 MW; FCBEDE25A466C0D7 CRC64; MSTSTEAVLK YREAILRHVG HDQYAPSTVE VLAQDLRAED PQQFQSAVDA LVDQGLLSMS NAGQVMLPSF GDADGEVEGT FNRNPKGFGF FKPLTRVREG DVFVPPDDTM GALSGDRVKA RIRRDRKRES SGRGGFGPQY VASIVEILER KRSSYAATMQ KRGATWLAMP DGDTSIGPVV IADADSKYVN EGDKVIIDLT EYPEGQALAE GVITRVLGEA GQPDVETQAV IAAYGLPADE FPDACLDQAR ESTRYFDDAV ARFLSEGPSA LPDRLDLTED YITTIDPPDA KDYDDAISVK RTENGWELGI HIADVAHFIA PGSPLDVEAR ERGNSVYLPR HVIPMLPEIL SNGICSLQPQ VPRFAKSIFI HYDLSGRVTR TGAAQTIINS AKRMTYLEAQ ALIDGDEEEA KKHARTAPEY TPKLKNTVKL MDELARTIRE RRRAAGMIHL DLPDAELIYD DNGHVVDAEP EDDAFTHTII EMFMVEANEA VARLFERMNV PVMRRVHPAP TPAGTEEAQK VAKVAGYSLP KNPTREQLQS ILDATRGKAS GRAVHMAVLR TLSKAEYSPA PIGHFALASD AYSHFTSPIR RYADLLTHRL LQDYLALTDN GQKPPKGEKE MKLLGRKLSD AESFIPQEEL VTIGRHISDT EANAADAERE LRSFLVLQLL SNKVGEVFDG VVTGLNTRGI FIQIDKYLAD GFIRVEDLPG DTTREGKTPK WITVKDTGAL VDKNSGRSFN FGDRVRVQIG AVDLPKRRLE LLVADAESRA VGKAVTKGVE GLTLGEGGGG LEHADGAGFK KMPGGTRRSR KSKARDKGKK DYRRDKK //