ID J9R0S5_RIEAN Unreviewed; 721 AA.
AC J9R0S5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=B739_0712 {ECO:0000313|EMBL:AFR35314.1};
OS Riemerella anatipestifer RA-CH-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=1228997 {ECO:0000313|EMBL:AFR35314.1, ECO:0000313|Proteomes:UP000006276};
RN [1] {ECO:0000313|EMBL:AFR35314.1, ECO:0000313|Proteomes:UP000006276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RA-CH-1 {ECO:0000313|EMBL:AFR35314.1,
RC ECO:0000313|Proteomes:UP000006276};
RA Chun C.A., Shu W.M., Kang Z.D., Jia W.X.;
RT "Riemerella anatipestifer vaccine strains.";
RL Submitted (SEP-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|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; CP003787; AFR35314.1; -; Genomic_DNA.
DR RefSeq; WP_014937723.1; NC_018609.1.
DR AlphaFoldDB; J9R0S5; -.
DR STRING; 34085.AB406_1061; -.
DR KEGG; rag:B739_0712; -.
DR PATRIC; fig|1228997.3.peg.708; -.
DR HOGENOM; CLU_002333_7_3_10; -.
DR Proteomes; UP000006276; Chromosome.
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; 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; 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; SM00955; RNB; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
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:UP000006276};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT DOMAIN 635..716
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 721 AA; 82974 MW; 36997426393DFA43 CRC64;
MAKKKKYISK KNEGKLKDLG RQILSFMNKQ SAKIYNYKQI ADGIDYKNPR QREQVIQALH
KLLADERIKE VEKGKYIIDL KIKDTLTGFI DFNHSGNAYV RVEDLEEDIF IHSKNVKDAL
QGDKVLIVTY HFKSKKLEGS VVEVLERNRK EFVGTFEFIK HKDFGFVVCD KKQINTDIFV
PRNKINGAKD GDKVVVKMVE WNPTEKNPHG EIVKVLGTPG SHETEIHSIL AEYGLPYAFP
EEVEQEADAI DREIRDDEVK KRWDMRGICT FTIDPKDAKD FDDALSIRKL ENGNWEIGVH
IADVSHYVVP NTLLDQEAYQ RATSVYLVDR VVPMLPEVLS NEVCSLRPNE DKYTFSAVFE
LNDKAEIKKQ WFGRTVIHSD RRFTYEEAQE RIETGKGDLA DEILTLDKLA KILREERIRK
GAITFDRSEV RFNLDENNEP IGVYFKVSKD SNHLIEEFML LANRKVSEFI SLNKKGSPTG
KTFIYRVHDD PDPTKLEALR DFVATFGYKM NLANSQKVAE SMNELLKSVK GKGEENMIET
LAMRSMSKAI YSTEPIGHYG LGFEYYTHFT SPIRRYPDLI AHRLLQHYLD QGKSPDKAEY
EEKSKHCSAM ERLAADAERD SIKFMQVKFM EKHLGEVFTG VISGVAEFGF WVQIPENGAE
GLIKLRDLMD DSYQYDAKTH AVYGSRTGNS YQLGDTVKIK VMKANLIQKQ LDFKIIEKAE
N
//
