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Database: UniProt
Entry: A0A1V9F8P8_9BACT
LinkDB: A0A1V9F8P8_9BACT
Original site: A0A1V9F8P8_9BACT 
ID   A0A1V9F8P8_9BACT        Unreviewed;       679 AA.
AC   A0A1V9F8P8;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=A4H97_21875 {ECO:0000313|EMBL:OQP54617.1};
OS   Niastella yeongjuensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=354355 {ECO:0000313|EMBL:OQP54617.1, ECO:0000313|Proteomes:UP000192610};
RN   [1] {ECO:0000313|Proteomes:UP000192610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17621 {ECO:0000313|Proteomes:UP000192610};
RA   Chen L., Zhuang W., Wang G.;
RL   Submitted (APR-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQP54617.1}.
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DR   EMBL; LVXG01000003; OQP54617.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V9F8P8; -.
DR   STRING; 354355.SAMN05660816_01889; -.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000192610; 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   SMART; SM00357; CSP; 2.
DR   SMART; SM00955; RNB; 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:UP000192610};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT   DOMAIN          567..649
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          658..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   679 AA;  77200 MW;  996D8743DFF2C729 CRC64;
     MSRKPAKKKK KKEASSQHTL KGVLDITRSG IGYVIVDNLP NDILVRPADF NTALHGDTVR
     VRVLGGSAKK SGRQQGAVVD VLQRKQMEFL GKIEIGKNAA FFTADTEKPM PDFFIPETAL
     NGAKDGDRVI VRITEWEKQK KPVGAVIQIM EAGNEGDMAM KEILMENGFP LFFPEEVIEE
     TERIPDTISQ DEINKRKDVR DVLTFTIDPV DARDFDDALS IRLLKNGMYE IGVHIADVSH
     FVEPDTALDK EAYDRATSVY LPDRVAPMLP ERISNELCSL RPHEDKLTFS AIFQITEAGE
     VNQYWLGKTV IHSNHRFTYE EVQEIIEKGE GLYQGEIMLL NKLAQQFRAK RFRKGAINFS
     SQEVRFKLDE TGKPIGIMVK ESKEAHQLIE EFMLLANRIV AENVSKVKVN KKDLPFPYRV
     HDTPDEQKLA PFVEFAKKYG HTFDTSTPEG IAASFNQMLQ DVQGKPEQHV LEQLGIRTMA
     KAIYTTENIG HYGLGFKHYC HFTSPIRRYP DVLVHRILQE VLTGDVEPEK KLEQKCKHCS
     EKERSAMEAE RAANKYKQVE YMKEFLGEEF EGVISGVASF GFWVETIEHK CEGLVSMNSL
     LEYDDFRHVE SDYSLVGLRS GRKFGMGDKV RIRVVAANLT KRQLDYEWVI TKSLKEEGET
     KKPAGGKSKY IPAKKGKRK
//
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