RNB_VIBVU
ID RNB_VIBVU Reviewed; 664 AA.
AC Q8D7K6;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=VV2_0146;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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; AE016796; AAO07119.1; -; Genomic_DNA.
DR RefSeq; WP_011081128.1; NC_004460.2.
DR AlphaFoldDB; Q8D7K6; -.
DR SMR; Q8D7K6; -.
DR EnsemblBacteria; AAO07119; AAO07119; VV2_0146.
DR KEGG; vvu:VV2_0146; -.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR Proteomes; UP000002275; 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; 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; 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; RNA-binding.
FT CHAIN 1..664
FT /note="Exoribonuclease 2"
FT /id="PRO_0000166392"
FT DOMAIN 568..650
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 664 AA; 75055 MW; 8EFF359610CEF002 CRC64;
MFQDNPLLAQ LKQQIQENLP KKEGTIKATE KGFGFLEVDS KTSFFIPPAY MKKCMHGDKV
IAIIRTENER EVAEPQELVE QMLNRFIGRV KMFKGKLNVV PDHPQLKKMS LKAKTKKGLN
PQEFAEGDWV VGHLIRHPLK DDNGFFVEIS EKITDADDKI APWWVTLAEN DLPNSEPAGI
DDWQIKDDAD LERIDMTHIP FVTIDGESTK DMDDALYAKK NDAGDFELTI AIADPTAYIT
PDDEMDKVAR ERGFTIYLPG RNIPMLPRDL ADELCSLIEG EIRPALCCTV TVSKDGVIGD
DIQFFAANIK SHARLAYDNV SDWLETGSCE KWQPSEEIAA IVRDLYEFSQ ARAEWREKNA
VVFPDRPDYR FELSEDNDVV AIHADMRRSA NRLVEESMIT ANICAGKTLQ GHFGTGVFNC
HAGFKPEKIA DVVELVNPEG TLEFTAESIA TREGFAALRR WLSKQETTYL DNRIRKFQTY
SEVSNQPLPH YAMGLDIYAT WTSPIRKYGD MINHRMLKAL ILNKEPVQKP DDSVGEELAL
HRKHHKIAER NVADWLYART LADAPENQTL FTGEIFDINR AGMRIRLLEN GAAAFIPGSL
IIDNKERIEC NGDLGTVSID KEVVYKLGDV LEVVLADVNQ ENRSLVAKPT QVFAELPVVE
ETQN