RNB_VIBA3
ID RNB_VIBA3 Reviewed; 668 AA.
AC B7VSB8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Exoribonuclease 2 {ECO:0000255|HAMAP-Rule:MF_01036};
DE EC=3.1.13.1 {ECO:0000255|HAMAP-Rule:MF_01036};
DE AltName: Full=Exoribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
DE Short=RNase II {ECO:0000255|HAMAP-Rule:MF_01036};
DE Short=Ribonuclease II {ECO:0000255|HAMAP-Rule:MF_01036};
GN Name=rnb {ECO:0000255|HAMAP-Rule:MF_01036}; OrderedLocusNames=VS_II1138;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in mRNA degradation. Hydrolyzes single-stranded
CC polyribonucleotides processively in the 3' to 5' direction.
CC {ECO:0000255|HAMAP-Rule:MF_01036}.
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_01036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01036}.
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01036}.
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DR EMBL; FM954973; CAV27060.1; -; Genomic_DNA.
DR RefSeq; WP_012600986.1; NC_011744.2.
DR AlphaFoldDB; B7VSB8; -.
DR SMR; B7VSB8; -.
DR STRING; 575788.VS_II1138; -.
DR EnsemblBacteria; CAV27060; CAV27060; VS_II1138.
DR KEGG; vsp:VS_II1138; -.
DR PATRIC; fig|575788.5.peg.1072; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000009100; Chromosome 2.
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-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_01036; RNase_II; 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; IPR011804; RNase_II.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR004476; RNase_II/RNase_R.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR Pfam; PF17876; CSD2; 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; TIGR02062; RNase_B; 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..668
FT /note="Exoribonuclease 2"
FT /id="PRO_1000149461"
FT DOMAIN 568..650
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 668 AA; 75202 MW; 1F3A3F0837DA33AC CRC64;
MFQDNPLLAQ LKQQIQETLP KKEGTIKATE KGFGFLEVDS KTSFFIPPPY MKKCVHGDKV
IAIIRTEKER EVAEPEELIE QGLTRFIARV KLFKGRLNVV PDHPQLKKLQ LKAKAKKGLN
PETLKEGDWV VAHIVQHPLK GDNGFLAQIS EKITDADDKI APWWVTLAQN DLPNSEPEGI
DDWQIKDDAD LERVDMTHVP FVTIDGESTK DMDDALYAKK KENGDFELTI AIADPTAYIS
PDDAMDKVAR ERGFTIYLPG RNIPMLPRDL ADNLCSLIEN EVRPALCCTV TVSKDGVIGD
DINFFAANIK SHARLAYDHV SDWLETGASE KWQPSEEIAA IVSDLHQFAQ ARSAWRSANA
VVFPDRPDYR FELSEDNDVV AIHADMRRSA NKLVEESMIS ANICAGRVLK ESFNQGVFNC
HSGFKAEKLT DVLELVNPEA ETPFTEEQIV SLEGFATLRR WLGSLDNSYY DNRIRKFQAY
SEISNEPAPH YAMGLDIYAT WTSPIRKYGD MINHRMLKAH ILRKTPTQTP DETIGDELAL
HRRHHGMAER NVGDWLYART LANAPVEETR FQAEIFDINR AGMRVRLLEN GAAAFIPGSL
ILNNKERIEC NGDMGTVSID KEMVYKLGDV LEVVLSEVNQ ENRNLVAKPT QVFADLPSGP
ETTNETEA