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Database: UniProt
Entry: V5F5P4_9VIBR
LinkDB: V5F5P4_9VIBR
Original site: V5F5P4_9VIBR 
ID   V5F5P4_9VIBR            Unreviewed;       819 AA.
AC   V5F5P4;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
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   ECO:0000313|EMBL:GAD90889.1};
GN   ORFNames=VHA01S_059_00140 {ECO:0000313|EMBL:GAD90889.1};
OS   Vibrio halioticoli NBRC 102217.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1219072 {ECO:0000313|EMBL:GAD90889.1, ECO:0000313|Proteomes:UP000017800};
RN   [1] {ECO:0000313|EMBL:GAD90889.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90889.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Ichikawa N., Kimura A., Ohji S., Hosoyama A., Fujita N.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAD90889.1, ECO:0000313|Proteomes:UP000017800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102217 {ECO:0000313|EMBL:GAD90889.1,
RC   ECO:0000313|Proteomes:UP000017800};
RA   Isaki S., Kimura A., Ohji S., Hosoyama A., Fujita N., Hashimoto M.,
RA   Hosoyama Y., Yamazoe A.;
RT   "Whole genome shotgun sequence of Vibrio halioticoli NBRC 102217.";
RL   Submitted (NOV-2013) 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:GAD90889.1}.
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DR   EMBL; BAUJ01000059; GAD90889.1; -; Genomic_DNA.
DR   RefSeq; WP_023405200.1; NZ_BAUJ01000059.1.
DR   AlphaFoldDB; V5F5P4; -.
DR   eggNOG; COG0557; Bacteria.
DR   OrthoDB; 9764149at2; -.
DR   Proteomes; UP000017800; 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   DOMAIN          652..733
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          734..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..796
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        797..819
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   819 AA;  92903 MW;  93E4B176EF8C6D66 CRC64;
     MSDSKSLDPH ADREAKNYEN PVPSREFLLS FLESAGVPMN RNDLFTALEL AGEDQYEGLR
     RRLNAMLRDG QLVFTRRQCY ALPDKLEMIK GYVIGHKDGF GWVRPEGVIG KEQDLVLPFH
     QMRSIIHGDY VLAQQSGTDK RGRKEARIVR VLEERAMKIV GRFFLEFGHA YVVADDSRIH
     HDILIPKEHR MGARMGNVVV IEVTDRGNRS RGMSGKVVEV LGENLAPGME TQIAIRTHQI
     PNEWPEEVTK QIASLAEEVP EEAKKGRVDL RELPLVTIDG EDARDFDDAV YCEKKKSGGW
     RLWVAIADVS YYVRPDSALD KEAINRGNSV YFPSQVVPML PEVLSNGLCS LNPQVDRLCM
     VCEMTVSESG KLSGYKHYEA VMNSHARLTY NKVNDILNGD QELNQRYETL VPHLQELHNM
     YRTLKQSRDL RGAIEFETVE TKFIFNADRK IDRIEPVVRN DAHKLIEECM ILANIASASL
     VEKLKEPALY RVHETPGEQR LVGFKDFLSE LGLTLNGGLA PSPTDYADLM HIVTQRPDKE
     LIQTMLLRSM KQAVYNPDNA GHFGLALKRY AHFTSPIRRY PDLLLHRAIK YLIAKQEGRN
     TDRWTPTGGY HYSFDDMDVF GEQCSMTERR ADDATRDVTD WLKCEYMQDH VGEELDGVIA
     NVTGFGFFVR LTELHIDGLV HISTLANDYY RYDAISQRLV GESSGQIYRL GDTVKVKVLA
     VNLNDKQIDF EMVGSQRTPR GKGKTAKKRL VEDAKRFDDK KKSGSSEGRR SRRAKAKVEP
     TVRPDGSKDS APAPKKPKSN KAKKNKARGK KNTARAPKK
//
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