ID   RNB_PSYIN               Reviewed;         656 AA.
AC   A1SWZ6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Ping_2270;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) 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; CP000510; ABM04011.1; -; Genomic_DNA.
DR   RefSeq; WP_011770571.1; NC_008709.1.
DR   AlphaFoldDB; A1SWZ6; -.
DR   SMR; A1SWZ6; -.
DR   STRING; 357804.Ping_2270; -.
DR   EnsemblBacteria; ABM04011; ABM04011; Ping_2270.
DR   KEGG; pin:Ping_2270; -.
DR   eggNOG; COG4776; Bacteria.
DR   HOGENOM; CLU_002333_7_3_6; -.
DR   OMA; CFTNYLP; -.
DR   OrthoDB; 1602988at2; -.
DR   Proteomes; UP000000639; Chromosome.
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; 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   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00955; RNB; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..656
FT                   /note="Exoribonuclease 2"
FT                   /id="PRO_0000409536"
FT   DOMAIN          564..649
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ   SEQUENCE   656 AA;  74164 MW;  6D95CDD8CE37DDB0 CRC64;
     MFQNNPLLSQ LKKQIQEDIP KRQGKVKATD RGYGFLETDK GKRFFIPPSE MKKVLHGDQI
     NAFIRGKGDK STAEPNQLKK TGSAVFIARL VIKQKNISII PKNPLLKGFF KIKGSQSLQS
     RGYQDGDWVK VELVSHALEG NGFLTQIIEK IADASDPFAY RLLTVATHNL ANKAPEFDHP
     WKIIDPQLSR SDLTKTPFFT IDGVNTQDMD DALYIEADEN GWKLTVAISD PSAYVPENSD
     MDAEAKRRAF TLYLPNFNVP MLPRDLSDSL CSLKEGEKRA TLCCTIHINK KGEIEGEPAF
     YGAWIKSHYR LNYTDVSNYL ENEELSNDCW KPSTQLAEQL RTLDSLSLKR LQWRTDNNAV
     FKNQPDYTLK LNNKGEISEI LCEPRRSANR LVEESMIAAN ICAGDFLAKH KQQGVFNTHS
     GFSSERLGKV VSLLSEFGIE SDIQTLATVT GYTKIRQQTN LLHNSYLDHR LRKLLSYADI
     KNTPEAHFTL GVDHYATWTS PIRKYGDLLN HRLIKSVLLK EDNIQIDNEI GQVLNAARKL
     QRLAERDVNN ILYSQYLKNQ VESKWRYKAE IFDIIKAGIR VKIQENGATF FIPCSLLCKD
     SSDATKIDCN QALGKVIIAQ QTELQLGDVI DVMLNNVKVE SGQLIGKLAE SLTISE