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Database: UniProt
Entry: C6C4D3_DICP7
LinkDB: C6C4D3_DICP7
Original site: C6C4D3_DICP7 
ID   C6C4D3_DICP7            Unreviewed;       657 AA.
AC   C6C4D3;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=Exoribonuclease 2 {ECO:0000256|HAMAP-Rule:MF_01036};
DE            EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01036};
DE   AltName: Full=Exoribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
DE            Short=RNase II {ECO:0000256|HAMAP-Rule:MF_01036};
DE            Short=Ribonuclease II {ECO:0000256|HAMAP-Rule:MF_01036};
GN   Name=rnb {ECO:0000256|HAMAP-Rule:MF_01036};
GN   OrderedLocusNames=Dd703_1710 {ECO:0000313|EMBL:ACS85507.1};
OS   Dickeya paradisiaca (strain Ech703) (Dickeya dadantii (strain
OS   Ech703)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=579405 {ECO:0000313|EMBL:ACS85507.1, ECO:0000313|Proteomes:UP000002734};
RN   [1] {ECO:0000313|EMBL:ACS85507.1, ECO:0000313|Proteomes:UP000002734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ech703 {ECO:0000313|EMBL:ACS85507.1,
RC   ECO:0000313|Proteomes:UP000002734};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Dickeya dadantii Ech703.";
RL   Submitted (JUN-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:0000256|HAMAP-Rule:MF_01036, ECO:0000256|SAAS:SAAS00050085}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to
CC         yield nucleoside 5'-phosphates.; EC=3.1.13.1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01036,
CC         ECO:0000256|SAAS:SAAS01124678};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01036,
CC       ECO:0000256|SAAS:SAAS00089931}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase II
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01036,
CC       ECO:0000256|SAAS:SAAS00555034}.
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DR   EMBL; CP001654; ACS85507.1; -; Genomic_DNA.
DR   STRING; 579405.Dd703_1710; -.
DR   EnsemblBacteria; ACS85507; ACS85507; Dd703_1710.
DR   KEGG; dda:Dd703_1710; -.
DR   eggNOG; ENOG4108IEC; Bacteria.
DR   eggNOG; COG4776; LUCA.
DR   HOGENOM; HOG000271427; -.
DR   KO; K01147; -.
DR   OMA; CFTNYLP; -.
DR   Proteomes; UP000002734; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   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; 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   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   Complete proteome {ECO:0000313|Proteomes:UP000002734};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01036,
KW   ECO:0000256|SAAS:SAAS00462075};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01036,
KW   ECO:0000256|SAAS:SAAS00089915};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01036,
KW   ECO:0000256|SAAS:SAAS00446781, ECO:0000313|EMBL:ACS85507.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01036,
KW   ECO:0000256|SAAS:SAAS00462054};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01036,
KW   ECO:0000256|SAAS:SAAS00462035}.
FT   DOMAIN       37     93       CSP. {ECO:0000259|SMART:SM00357}.
FT   DOMAIN      203    530       RNB. {ECO:0000259|SMART:SM00955}.
SQ   SEQUENCE   657 AA;  73804 MW;  F045D39D0E12FDC7 CRC64;
     MSAAKATNNP ILDAMFQDNP LLAQLKQQLH SQTPRVEGTV KATDKGFGFL EADAQKSYFI
     PPPHMKKVMH GDRIIATLHT EKEREIAEPE SLVEPFLSRF VGRVQKKDDR LSIIPDHPLL
     KDAIPCRPAR ELEQDFKEGD WAVAEMRRHP LKGDRGFYAE LTQYITTGDD PLVPWWVTLS
     RHNLERTAPQ ADAADLNDGD LVREDLTGLD FVTIDSASTE DMDDALYVQD NGDGTWQLIV
     AIADPTAYVP VGSELDNIAR QRAFTNYLPG FNIPMLPRHL SDDICSLRPN ERRPVLACRV
     TLAADGAMSD IRFFAAWIQS RAKLVYDEVS DWLEQQGGWQ PENDAIANQI RLLHRICLAR
     GEWRAKHALV FRDRPDYRFL LGEHGEVLDI VVEQRRIANR IVEEAMIAAN LCAAQVLRDR
     LGFGIYNVHN GFEPATIDQA VAVLESNGVQ ATAEQLLTLD GFCTLRRELD AMPTQFLDSR
     IRRFQTFAEV STTPGPHFGL GLEAYATWTS PIRKYGDMIN HRLLKAIITG AGAEKPQDDI
     TVQLAERRRL NRMAERDVGD WLYARFLKDK AGTDARFSAE IIDVNRGGLR VRLLENGAVA
     FIPASFVHAV RDELVCSQDT GIVTVKGEPV YRQSDTLQVV LTEVRIETRS IIAKPAA
//
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