RNB_ACTP2
ID RNB_ACTP2 Reviewed; 658 AA.
AC A3N0B9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=APL_0757;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73855.1; -; Genomic_DNA.
DR RefSeq; WP_009874880.1; NC_009053.1.
DR AlphaFoldDB; A3N0B9; -.
DR SMR; A3N0B9; -.
DR STRING; 416269.APL_0757; -.
DR EnsemblBacteria; ABN73855; ABN73855; APL_0757.
DR KEGG; apl:APL_0757; -.
DR PATRIC; fig|416269.6.peg.792; -.
DR eggNOG; COG4776; Bacteria.
DR HOGENOM; CLU_002333_7_3_6; -.
DR OMA; CFTNYLP; -.
DR Proteomes; UP000001432; 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; 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; 2.
DR SUPFAM; SSF50249; SSF50249; 4.
DR TIGRFAMs; TIGR00358; 3_prime_RNase; 1.
DR TIGRFAMs; TIGR02062; RNase_B; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Exonuclease; Hydrolase; Nuclease; Reference proteome;
KW RNA-binding.
FT CHAIN 1..658
FT /note="Exoribonuclease 2"
FT /id="PRO_1000063881"
FT DOMAIN 576..658
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01036"
SQ SEQUENCE 658 AA; 75767 MW; 19F52AB8EF17D469 CRC64;
MFQNNPLLAQ LKQQIEANKE YVEGTVKASD KAFGFLECDK KSYFIPPMEM KKVMHGDKVK
AVVKREDDKE QVEIDSLLEP MLDRFIAQVR FNKDNKLQLI VDHPSIKNII PANTHKKVTE
TLESGDWVVA QLKTHPLRDD RFLFAQVTQF ICKADDNFAP WWVTLARHEQ PREPVANEKS
YELHDELDRE DLTSLYFTTI DSPSTQDMDD ALYIEPIKQG EVQTGWRLVV AIADPTAYIP
ENSNLEKAAR QRCFTNYLPG FNIPMLPREL SDDLCSLVPN KKRPALVGYI ETDLAGNITG
DTRFVSAWVE SKAKLAYDNV SDYLEQVENA WQPESAETKQ QIDWLHQFTL ARIEWRRNNA
LLFKESGDYS FELNEDGSVR DIHVEYRRIA NQMIEESMII ANICCAKFLA DNAKTGVFNT
HAGFDPKNLE LAQKFLLDTL STDENRDALT AFYAPEKLAT LEGYCEMRRS IDEFPEKFLE
LRLRRYLTFA EFKSEVAPHL GLGISHYATW TSPIRKYGDM VNHRLIKQVL LGKQAKTVEE
GILVRLQEAR RQNRLVERDI ADWLYARYLF PMVEQAVEFD CEIADVSRGG VRAKVIANGA
QIFVPFSTLH DKKEEMEFRP EEIALYIKGE KAYQIGQAVK VKLTEVRLET RSIVGNII