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Database: UniProt
Entry: Q4QM40_HAEI8
LinkDB: Q4QM40_HAEI8
Original site: Q4QM40_HAEI8 
ID   Q4QM40_HAEI8            Unreviewed;       782 AA.
AC   Q4QM40;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   26-NOV-2014, entry version 72.
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=vacB {ECO:0000313|EMBL:AAX87907.1};
GN   Synonyms=rnr {ECO:0000256|HAMAP-Rule:MF_01895};
GN   OrderedLocusNames=NTHI1030 {ECO:0000313|EMBL:AAX87907.1};
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310 {ECO:0000313|EMBL:AAX87907.1, ECO:0000313|Proteomes:UP000002525};
RN   [1] {ECO:0000313|EMBL:AAX87907.1, ECO:0000313|Proteomes:UP000002525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP {ECO:0000313|EMBL:AAX87907.1,
RC   ECO:0000313|Proteomes:UP000002525};
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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:SAAS00061614}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
CC       ECO:0000256|SAAS:SAAS00061544}.
CC   -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01895}.
CC   -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01895}.
CC   -!- SIMILARITY: Contains S1 motif domain.
CC       {ECO:0000256|SAAS:SAAS00061579}.
CC   -!- SIMILARITY: Contains Smotif domain.
CC       {ECO:0000256|SAAS:SAAS00061579}.
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DR   EMBL; CP000057; AAX87907.1; -; Genomic_DNA.
DR   RefSeq; YP_248567.1; NC_007146.2.
DR   ProteinModelPortal; Q4QM40; -.
DR   STRING; 281310.NTHI1030; -.
DR   EnsemblBacteria; AAX87907; AAX87907; NTHI1030.
DR   GeneID; 3430330; -.
DR   KEGG; hit:NTHI1030; -.
DR   PATRIC; 20182223; VBIHaeInf100748_0956.
DR   eggNOG; COG0557; -.
DR   HOGENOM; HOG000071120; -.
DR   KO; K12573; -.
DR   OMA; GFFVRLN; -.
DR   OrthoDB; EOG6Q5NRD; -.
DR   BioCyc; HINF281310:GJ89-982-MONOMER; -.
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; 2.40.50.140; -; 1.
DR   HAMAP; MF_01895; RNase_R; 1.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
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   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; 2.
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;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002525};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061723};
KW   Exonuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061790};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061541};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061621};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01895,
KW   ECO:0000256|SAAS:SAAS00061586}.
FT   DOMAIN      651    732       S1 motif. {ECO:0000256|HAMAP-Rule:
FT                                MF_01895}.
SQ   SEQUENCE   782 AA;  89952 MW;  C0977CC85C02E3EE CRC64;
     MTKKRKNLIS QDPHYKRELE KYGNPIPSRE FILSVIRDNN APMNRDEILT ALSIRNEEQI
     EAMRRRLRAM ENDGQLVFTK RKRYALPEKL DLFKGTVIGH REGFGFLQVD GKKDDLFIPN
     HQMQRVMHGD FVLAQLAGLD RRGRREVRIV RVLESRKKQI VGRFFLENGF SYVVPDDSRI
     GRDILVPNEH RNGARMGQVV VVELQERSAS FNQPIGVITE ILGDNMAKEM EVEIALRNHD
     IPHKFPSAVE KYVKKFTEEV PEEAKKGRVD LRNLPLVTID GEDARDFDDA VYCEKHGKGW
     KLWVAIADVS YYVRLRSALD VEAHNRGNSV YFPNRVVPML PEILSNGLCS LNPQVDRLCM
     VCEMQISAKG KLIDYRFYEA VMNSHARLTY TKVAKMLEGD EELRARYSTL VPHLEDLYKL
     YQALLGARHQ RGAIDFETIE TKFIFNAMGR IERIEPVVRN DAHKIIEECM ILANIAAANF
     MEKHKEPALY RIHATPSEEK LTSFRTFLSE FGLTLEGGLK PTTKDYAALL EKVKERHDHE
     LIQTMLLRSL SQAVYHADNI GHFGLALEEY AHFTSPIRRY PDLTLHRGIK YLLAKEQGAK
     RKTTDTGGYH YSFDEMDLLG NHCSMTERRA DDATREVADW LKCEYMQDHV GGEFSGVISS
     VTGFGLFVRL DDLFIDGLVH ISTLENDYYQ FDAAKQRLIG ENSGMQYRLG DKVRIKVEAV
     HLENKMVDFS LMGSERKPRR AGKTAKEKAK KVFKELPSKT SQKRKSAVKK KDVLKKASRK
     RK
//
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