(data stored in SCRATCH zone)

SWISSPROT: C5BF70_EDWI9

ID   C5BF70_EDWI9            Unreviewed;       816 AA.
AC   C5BF70;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 65.
DE   RecName: Full=Ribonuclease R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            Short=RNase R {ECO:0000256|HAMAP-Rule:MF_01895};
DE            EC=3.1.13.1 {ECO:0000256|HAMAP-Rule:MF_01895};
GN   Name=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   OrderedLocusNames=NT01EI_0418 {ECO:0000313|EMBL:ACR67656.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67656.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: 3'-5' exoribonuclease that releases 5'-nucleoside
CC       monophosphates and is involved in maturation of structured RNAs.
CC       {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC       direction to yield nucleoside 5'-phosphates. {ECO:0000256|HAMAP-
CC       Rule:MF_01895, ECO:0000256|SAAS:SAAS00385302}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00385373}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
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DR   EMBL; CP001600; ACR67656.1; -; Genomic_DNA.
DR   RefSeq; WP_015869860.1; NC_012779.2.
DR   ProteinModelPortal; C5BF70; -.
DR   STRING; 634503.NT01EI_0418; -.
DR   EnsemblBacteria; ACR67656; ACR67656; NT01EI_0418.
DR   GeneID; 7961243; -.
DR   KEGG; eic:NT01EI_0418; -.
DR   PATRIC; fig|634503.3.peg.377; -.
DR   eggNOG; ENOG4105C40; Bacteria.
DR   eggNOG; COG0557; LUCA.
DR   HOGENOM; HOG000071120; -.
DR   KO; K12573; -.
DR   OMA; DWYEYRS; -.
DR   OrthoDB; POG091H0219; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008859; F:exoribonuclease II activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.10.10; -; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR013223; RNase_B_OB_dom.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   InterPro; IPR004476; RNase_II/RNase_R.
DR   InterPro; IPR011805; RNase_R.
DR   InterPro; IPR013668; RNase_R_HTH_12.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF08461; HTH_12; 1.
DR   Pfam; PF08206; OB_RNB; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 4.
DR   TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR   TIGRFAMs; TIGR02063; RNase_R; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5BF70.
DR   SWISS-2DPAGE; C5BF70.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089898};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00462115};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061541, ECO:0000313|EMBL:ACR67656.1};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089881};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00089904}.
FT   DOMAIN      644    725       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED       37     65       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   816 AA;  91536 MW;  049E941B9BE8CA79 CRC64;
     MSQDPYLERE AEKYASPIPS REFILMHLAK RKTPASREEL AQELALSSEE ALEALRRRLR
     AMERDGQLIF TRRQCYALPE RLDLIKGTVI GHRDGFGFLR SEGQKEDLYL SPEQMKMCMH
     GDEILAQVTG TDRRGRKEVR VVRVVESRTG LIVGRYFTDA GTGFVVPDDG RLSFDILIPS
     DAIAGARMGY VVVVELTQRP TRRTKAVGKI VEVLGDNMGT GMAVDIALRS HDIPHAWPDL
     VERQVAELCE EVPEAAKVGR IDLRDLPLVT IDGEDARDFD DAVYCEKKRG GGWRLWVAIA
     DVSYYVRPNT ALDHEARSRG NSVYFPSQVV PMLPEVLSNG LCSLNPQVDR LCMVCEMTIA
     ASGRLSSYKF YEAVMSSHAR LTYTKVAHIL AGDPDLRAQY HALVKPLEEL HALYKALDHA
     RAERGGISFE TEEAKFIFNA ERRIERIEPT VRNDAHKLIE ECMILANISA ARFMEKNHEP
     VLFRIHDKPS EDHVMALRSV LAELGLSLGG GTQPEPKDYA LLMDKVADRP DHEMLQTMLL
     RSMKQAVYDP ENRGHFGLAL QAYAHFTSPI RRYPDLSLHR GIKYLLASEH GHAERWTPSG
     GWHYHTEDML QLGEHCSMTE RRADEATRDV SDWLKCDFMQ DHVGQTYGGI ITSVTGFGFF
     VRLDDLFIDG LVHVSTLDND YYRFDQIGQR LIGESSGQVY RLGDKVEVKV DAVHLDERKI
     DFALISTARG VRGAGKTARN KARQANGGAE KKPSRSARRG GKMPANFASD SVQRRGDEAA
     PAKKGRGKGK GKKPSVQTRN IAASTKAKRA RKKTTD
//

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