RNR_VIBPA
ID RNR_VIBPA Reviewed; 835 AA.
AC P40611;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Ribonuclease R {ECO:0000255|HAMAP-Rule:MF_01895};
DE Short=RNase R {ECO:0000255|HAMAP-Rule:MF_01895};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01895};
DE AltName: Full=VacB protein homolog;
GN Name=rnr {ECO:0000255|HAMAP-Rule:MF_01895}; Synonyms=vacB;
GN OrderedLocusNames=VP2807;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-383.
RC STRAIN=BB22;
RA McCarter L.L.;
RL Submitted (APR-1994) 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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01895};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01895}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01895}.
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DR EMBL; BA000031; BAC61070.1; -; Genomic_DNA.
DR EMBL; U09005; AAA62192.1; -; Genomic_DNA.
DR RefSeq; NP_799186.1; NC_004603.1.
DR RefSeq; WP_005480076.1; NC_004603.1.
DR AlphaFoldDB; P40611; -.
DR SMR; P40611; -.
DR STRING; 223926.28807817; -.
DR PRIDE; P40611; -.
DR EnsemblBacteria; BAC61070; BAC61070; BAC61070.
DR GeneID; 1190357; -.
DR KEGG; vpa:VP2807; -.
DR PATRIC; fig|223926.6.peg.2699; -.
DR eggNOG; COG0557; Bacteria.
DR HOGENOM; CLU_002333_7_0_6; -.
DR OMA; DWYEYRS; -.
DR Proteomes; UP000002493; Chromosome 1.
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 Gene3D; 2.40.50.140; -; 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; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
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; SSF50249; 4.
DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR TIGRFAMs; TIGR02063; RNase_R; 1.
DR PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..835
FT /note="Ribonuclease R"
FT /id="PRO_0000166416"
FT DOMAIN 652..733
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01895"
FT REGION 739..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..828
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 95037 MW; FA0674C937407F5F CRC64;
MSDNIPNDPF ADRESQNYEN PIPSREFILE FLEQAGVPMN RNDLFEALKL AGEEQYEGLR
RRLRAMERDG QLVFTRRQCY ALPEKLEMVK GYVIGHKDGH GWVRPEGSVG KDDDILLPHH
QMKNIIHGDF VLVQPTDNSK RGRREGRLVR VLEERNSQIV GRFFLEYGYS YVVPDDSRIS
QDILIPNEHK AGARMGNVVV IEITDRGSRS RGMMGKVVEV LGENMAPGME TQIAIRTHQI
PYEWPEAVEK QIVNLGEEVP EEAKVGRVDL RELPLVTIDG EDARDFDDAV FCEKKKDGGW
RLWVAIADVS YYVRPDSALD KEAINRGNSV YFPSQVVPML PEVLSNGLCS LNPQVDRLCM
VCEMTISESG KLSSYKHYEA VMNSHARLTY SKVSAILEGD EELRERYQPL VSHLEELHAM
YKVLKEARDQ RGAIEFETVE TKFIFNAERK IESIEPVIRN DAHKIIEECM ILANIASASL
VEKAKEPALY RIHESPGELR LQGFRDFLSE LGLELKGGLE PSPTDYADLA RQIAGRQDQE
LIQTMLLRSM KQAVYNADNA GHFGLALKRY AHFTSPIRRY PDLLLHRAIK YLIAKEEGRN
QDRWTPTGGY HYSFDDMDFY GEQCSMTERR ADDATREVAD WLKCEYMQDH VGDELEGVIA
NVTSFGFFVR LTDLHIDGLV HISTLANDYY QFDPIGQRLI GESFGNIYRL GDAVKVKVLA
VNLDDKQIDF ELVETSRKLR GEGKTAKKRA AEAKRKAKEK KRAATRSSSK ESATARAVPA
IEPTKRPEQT DSGRKRKGPK RGDDDSAKKP KVKKAHKKKP HSKPKKTKRT KQDAQ
