ID A0A1B1VAB3_9VIBR Unreviewed; 821 AA.
AC A0A1B1VAB3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=F0224_18930 {ECO:0000313|EMBL:NOI77761.1};
OS Vibrio coralliilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=190893 {ECO:0000313|EMBL:NOI77761.1, ECO:0000313|Proteomes:UP000528382};
RN [1] {ECO:0000313|EMBL:NOI77761.1, ECO:0000313|Proteomes:UP000528382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AIC-5 {ECO:0000313|EMBL:NOI77761.1,
RC ECO:0000313|Proteomes:UP000528382};
RA Kehlet-Delgado H., Mueller R.S.;
RT "Draft genome sequencing and comparative genomics of hatchery-associated
RT Vibrios.";
RL Submitted (SEP-2019) 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:NOI77761.1}.
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DR EMBL; VTXB01000009; NOI77761.1; -; Genomic_DNA.
DR RefSeq; WP_064488778.1; NZ_VTXB01000009.1.
DR STRING; 190893.BA953_07625; -.
DR Proteomes; UP000528382; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; 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; IPR013668; RNase_R_HTH_12.
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; PF08461; HTH_12; 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; 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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895}.
FT REGION 739..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..821
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 93383 MW; 336B9FBDE738FDCF CRC64;
MSESTPNDPF AARESENYEN PVPSREFILE FLEQAGVPLN RNDLFEALHL EGEEQYEGLR
RRLRAMERDG QLVFTRRQCY ALPEKLEMVK GYVIGHKDGH GWVRPEGSVG KDNDVVLPHH
QMKSVLHGDY VLVQPTQNSK RGRKEGRLVR VLEERQTQIV GRFFMEYGYS YVVPDDSRIS
QDILIPNELR AGARMGNVVV IEITERGSRS RGMMGKVIEV LGENMAPGME TQIAIRTHQI
PHEWPEEVDK QIEGLGEEVP EEAKQGRVDL RELPLVTIDG EDARDFDDAV YCEAKKSGGW
RLWVAIADVS YYVRPDSALD KEAINRGNSV YFPSQVVPML PEVLSNGLCS LNPQVDRLCM
VCEMTISESG KLSGYKHYEA VMNSHARLTY NKVHHILEGD EELRQRYQPL VPHLEELHKM
YKVLKHARDN RGAIEFETVE TKFIFNAERK IDSIEPVIRN DAHKIIEECM ILANIASASL
VEKAKEPALY RIHESPGEQR LTGFRDFLSE LGLDLKGGLE PSPTDYADLV RQIGQRQDKE
LIQTMLLRSM KQAVYNADNC GHFGLALKRY AHFTSPIRRY PDLLLHRAIK YLIAKENGTL
KDRWTPTGGF HYSFDDMDFY GEQCSMTERR ADDATREVSD WLKCEYMQDH VGEELEGVIA
NVTGFGFFVR LTELHIDGLV HISTLANDYY QFDPIGQRLI GESFGAIYRL GDAVKVKVLS
VNLDDRQIDF ELVETSRKLR GKGKTAKKRA AEAQKKAKAK KNAAANGRRS VDKAKPMVEP
TKRPDGSQEE GKGSKASKKP SDKARKKKPR NKAKKARGKK Q
//
