ID Q4QM40_HAEI8 Unreviewed; 782 AA.
AC Q4QM40;
DT 19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2005, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Ribonuclease R;
DE Short=RNase R;
DE EC=3.1.13.1;
GN Name=vacB; Synonyms=rnr; OrderedLocusNames=NTHI1030;
OS Haemophilus influenzae (strain 86-028NP).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=281310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=86-028NP;
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
CC direction to yield nucleoside 5'-phosphates.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the RNR ribonuclease family. RNase R
CC subfamily.
CC -!- SIMILARITY: Contains 1 S1 motif domain.
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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; FGFLIPD; -.
DR ProtClustDB; CLSK870678; -.
DR BioCyc; HINF281310:GJ89-982-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008859; F:exoribonuclease II activity; IEA:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0016070; P:RNA metabolic process; IEA: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; IPR022967; RNA-binding_domain_S1.
DR InterPro; IPR013223; RNase_B_OB_dom.
DR InterPro; IPR001900; RNase_II/R.
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 Pfam; PF08461; HTH_12; 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 SMART; SM00316; S1; 2.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 2.
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; Cytoplasm; Exonuclease; Hydrolase; Nuclease;
KW RNA-binding.
FT DOMAIN 651 732 S1 motif (By similarity).
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
//