RNB_VIBCH
ID RNB_VIBCH Reviewed; 678 AA.
AC Q9KLE1;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=VC_A0805;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003853; AAF96703.1; -; Genomic_DNA.
DR PIR; D82415; D82415.
DR RefSeq; NP_233191.1; NC_002506.1.
DR RefSeq; WP_000484954.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KLE1; -.
DR SMR; Q9KLE1; -.
DR STRING; 243277.VC_A0805; -.
DR DNASU; 2612319; -.
DR EnsemblBacteria; AAF96703; AAF96703; VC_A0805.
DR GeneID; 57742185; -.
DR KEGG; vch:VC_A0805; -.
DR PATRIC; fig|243277.26.peg.3426; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR BioCyc; VCHO:VCA0805-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 InterPro; IPR003029; S1_domain.
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 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..678
FT /note="Exoribonuclease 2"
FT /id="PRO_0000166390"
FT DOMAIN 568..650
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
FT REGION 659..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76149 MW; F1F3E282087CA5EB CRC64;
MFQDNPLLAQ LKQKIQETLP KKEGTIKASD KGFGFLEVDS KTSYFVPPPY MKKCMHGDKV
VAFIRTENER EVAEPSELIE QSLTRFIGRV KLFKGKLNVA PDHPQLKKLS LKAKTKKGLN
EADFQEGDWV VAHLVRHPLK GDDGFFVQIS HKITDANDKI APWWVTLAEN DLPNSEPAGI
DDWQLKDDAD LVREDLTALP FVTIDGESTK DMDDALYAQQ LPNGDFALTI AIADPTAYIT
PEDEMDKVAR ERGFTIYLPG RNIPMLPRDL ADELCSLMEN QVRPALCCSV TIRKDGVIGD
DIRFFAANIK SHARLVYDHV SDWLETGSSE QWQPSEEIAQ VVRDLYAFSQ ARANWRETHA
VVFPDRPDYR FELSADNDVV AIHADMRRTA NRLVEESMIT ANICAGKTLQ TTFGFGVFNT
HAGFKAEKMA DVVELMAVNG APNADAETLA TVEGFAALRR WLATQETSYL DNRIRKYQSY
SEIGNQPLPH FAMGLDVYAT WTSPIRKYGD MINHRLLKAH ILGKAPVQTP DETVGEELAL
HRKHHKIAER NVADWLYART LADEPAKETR FQAEIFDINR PGMRVRLLEN GAMAFIPGAL
ILDNKERIEC NGEDGTVLID KEVVYKLGDV LEIVLTEVNQ ENRSLVGKPT QVFADLVSET
QTSAEQPAEG AENNEPQV