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Figure 6.
Figure 6. Analysis of RNB amino acid sequence. (a) Schematic
representation of the domains found in prokaryotic
exoribonuclease II: CSD, cold shock domain; RNB, conserved
central region of about 400 amino acid residues that contains
four sequence motifs (I–IV); S1, RNA-binding domain. (b)
Multiple amino acid sequence alignment (CLUSTAL X^43) of the
residues comprising the motifs I to IV of the RNB domain (upper
part) and the N-terminal part of the RNB domain (*) containing a
new conserved region (lower part). The consensus sequence is
represented bellow the alignment. Bacterial genus and species
are abbreviated as follows: Esco, Escherichia coli K12 (acession
number: NP_415802.1); Vich, Vibrio cholerae O395
(ZP_00754758.1); Vivu, Vibrio vulnificus CMCP6 (NP_762129.1);
Shfl, Shigella flexneri 2a str. 2457T (NP_836978.1); Saty,
Salmonella typhimurium LT2 (AAL20620.1); Yepe, Yersinia pestis
biovar Medievalis str. 91001 (AAS62250.1); Erca, Erwinia
carotovora subsp. atroseptica SCRI1043 (CAG74865.1); Phlu,
Photorhabdus luminescens subsp. laumondii TTO1 (NP_929629.1);
Hain, Haemophilus influenzae Rd KW20 (NP_439875.1); Haso,
Haemophilus somnus 2336 (ZP_00133292.2); Pamu, Pasteurella
multocida subsp. multocida str. Pm70 (AAK02265.1); Acpl,
Actinobacillus pleuropneumoniae serovar 1 str. 4074
(ZP_00134345.1). Numbers of intervening amino acids are given in
brackets. (c) Secondary structure prediction of the N-terminal
part (residues from 85 to 156) of the RNB domain of E.coli RNase
II. β-Sheet elements are illustrated as arrows. The secondary
structure prediction was made using 3D-PSSM program, Folding
Recognition Server. Figure 6. Analysis of RNB amino acid
sequence. (a) Schematic representation of the domains found in
prokaryotic exoribonuclease II: CSD, cold shock domain; RNB,
conserved central region of about 400 amino acid residues that
contains four sequence motifs (I–IV); S1, RNA-binding domain.
(b) Multiple amino acid sequence alignment (CLUSTAL X[3]^43) of
the residues comprising the motifs I to IV of the RNB domain
(upper part) and the N-terminal part of the RNB domain (*)
containing a new conserved region (lower part). The consensus
sequence is represented bellow the alignment. Bacterial genus
and species are abbreviated as follows: Esco, Escherichia coli
K12 (acession number: NP_415802.1); Vich, Vibrio cholerae O395
(ZP_00754758.1); Vivu, Vibrio vulnificus CMCP6 (NP_762129.1);
Shfl, Shigella flexneri 2a str. 2457T (NP_836978.1); Saty,
Salmonella typhimurium LT2 (AAL20620.1); Yepe, Yersinia pestis
biovar Medievalis str. 91001 (AAS62250.1); Erca, Erwinia
carotovora subsp. atroseptica SCRI1043 (CAG74865.1); Phlu,
Photorhabdus luminescens subsp. laumondii TTO1 (NP_929629.1);
Hain, Haemophilus influenzae Rd KW20 (NP_439875.1); Haso,
Haemophilus somnus 2336 (ZP_00133292.2); Pamu, Pasteurella
multocida subsp. multocida str. Pm70 (AAK02265.1); Acpl,
Actinobacillus pleuropneumoniae serovar 1 str. 4074
(ZP_00134345.1). Numbers of intervening amino acids are given in
brackets. (c) Secondary structure prediction of the N-terminal
part (residues from 85 to 156) of the RNB domain of E.coli RNase
II. β-Sheet elements are illustrated as arrows. The secondary
structure prediction was made using 3D-PSSM program, Folding
Recognition Server. [4]^44
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