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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
 
 
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