ID A0A6M8BJ75_9CYAN Unreviewed; 797 AA.
AC A0A6M8BJ75;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 02-APR-2025, entry version 20.
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=HPC62_17385 {ECO:0000313|EMBL:QKD83731.1};
OS Thermoleptolyngbya sichuanensis A183.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oculatellales;
OC Oculatellaceae; Thermoleptolyngbya; Thermoleptolyngbya sichuanensis.
OX NCBI_TaxID=2737172 {ECO:0000313|EMBL:QKD83731.1, ECO:0000313|Proteomes:UP000505210};
RN [1] {ECO:0000313|EMBL:QKD83731.1, ECO:0000313|Proteomes:UP000505210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKUAC-SCTA183 {ECO:0000313|EMBL:QKD83731.1,
RC ECO:0000313|Proteomes:UP000505210};
RA Tang J., Daroch M., Li L., Waleron K., Waleron M., Waleron M.;
RT "Complete genome sequence of of a novel Thermoleptolyngbya strain isolated
RT from hot springs of Ganzi, Sichuan China.";
RL Submitted (MAY-2020) 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; CP053661; QKD83731.1; -; Genomic_DNA.
DR RefSeq; WP_172357677.1; NZ_CP053661.1.
DR AlphaFoldDB; A0A6M8BJ75; -.
DR KEGG; theu:HPC62_17385; -.
DR Proteomes; UP000505210; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:TreeGrafter.
DR CDD; cd04471; S1_RNase_R; 1.
DR FunFam; 2.40.50.140:FF:000408; Ribonuclease R; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 2.
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; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR011805; RNase_R.
DR InterPro; IPR050180; RNR_Ribonuclease.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00358; 3_prime_RNase; 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; 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:UP000505210};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 685..766
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 797 AA; 90064 MW; 5A952C10D7E5849F CRC64;
MDFSIASLLS NFPDDKLVAP KALEKKLNCE DDASLRRLQI ALDALEKIGI LVKERGKYRR
VFEDDVVEGK LRCSSKGFCF AIQDIEGSED IYIRESQLNT AWNGDRVLVR VTKEGSRRRS
PEGEVRLILE RSNSSVLARV KKTEDGQYRA LPLDDRLLFE LELTPDGEPL EESVDQLVHV
EIARYPLGQH PPIGRVAQIL GSDAQAASDI DIVCCKHDLP RGFSEAVLEA AKALPTKLRK
TDLKKRLDLR EQLTVTIDGP DHPHSPAIDD ALSVEKVGDD EWRLGIHIAD VSYYVAARSP
VDLEAQKRGT SVFLGELVVP MLPEHLHRCC SLLPGEDRLA ISVLVTLNAA GEVQDFEIQP
SVVRVDQHLD YQQAQAVLLR DDPEAAAEAR YPLPSAKELK HLEPVFELVD NLFAISQAVA
AQRLARGAFD LNLPESIFPD EHNPELGKFL STNFQYDDEG ELGAMVVSSL LPARTIVTEL
MLLANQLVAL HLQCLQVPAI YRVHRTPDPS DVQELVKLVN NMDIEYQLED EEVVHPRDYQ
RLTQQFAESY AERVLTYLLL ETLKPAVYST TPGTHFGLAL DNGYTHFTSP LRRYPDLLVH
RALHAVFEHG RDRKSTRSKD KVNLFSSECH GAIDWKVLPP EVHDELEEYF NSIVNHLTER
EKLAQEAESD LEGLKKAEYM QERTGETFHG LITGVQSYGF FVEIEELLVE GLVHVSSLKD
DWYEYRSRQQ KLVGRKNRKQ YRLGDRVEVQ VKSVDYYRQQ IDLVAVGGGS EATDDDEDLL
ETEADLLETE DLSEEEE
//
