RNB_HAEI8
ID RNB_HAEI8 Reviewed; 659 AA.
AC Q4QJL5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=NTHI2041;
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 Haemophilus
RT influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX88782.1; -; Genomic_DNA.
DR RefSeq; WP_005688061.1; NC_007146.2.
DR AlphaFoldDB; Q4QJL5; -.
DR SMR; Q4QJL5; -.
DR EnsemblBacteria; AAX88782; AAX88782; NTHI2041.
DR KEGG; hit:NTHI2041; -.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR OrthoDB; 1602988at2; -.
DR Proteomes; UP000002525; Chromosome.
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..659
FT /note="Exoribonuclease 2"
FT /id="PRO_1000063891"
FT DOMAIN 576..658
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 659 AA; 75775 MW; 1499BEE9A5235843 CRC64;
MFQDNPLLAQ LKQQIHDSKE QVEGVVKSTD KAYGFLECDK KTYFIAPPSM KKVMHGDKIK
ATIEKQGDKE QAEPEALIEP MLTRFIAKVR FNKDKKLQVL VDHPSINQPI GAQQAKSVKE
ELQEGDWVVA NLKTHPLRDD RFFYATINQF ICRADDELAP WWVTLARHEQ SRYPVQGAEH
YEMLDQKTRE NLTALHFVTI DSESTMDMDD ALYIEPIAQN STQTGWKLVV AIADPTAYIA
LDSQIEQEAK QRCFTNYLPG FNIPMLPREL SDELCSLIAN ETRPALVCYI ETDLAGNITA
KPHFVSAYVQ SKAKLAYNKV SDYLEQADNA WQPETPETAQ QIHWLHQFTK ARIQWHKTHS
LLFKEKPDYA FVLAENGKVQ EIKAEYRRIA NQIVEEAMII ANICAAQFLH EQAKTGIFNT
HSGFDKKFLE NAHHFLMANL ANEQNQTELA ERYSVENLAT LNGYCQMRHD IEPIESDYLE
LRLRRYLTFA EFKSELAPHF GLGLEGYATW TSPIRKYSDM VNHRLIKAVL AKQPYEKTQN
DVLARLQEAR RQNRLVERDI ADWLYCRYLA PKVAENVEFN AEVQDVMRGG LRVQLLENGA
SMFIPASTLH NNKEEMQVNS DEIALYIKGE RTYKIGDIVK VKLTEVKEAT RSIVGEILQ