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Conserved domains on  [gi|489327515|ref|WP_003234807|]
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MULTISPECIES: anti-TRAP regulator [Bacillus]

Protein Classification

anti-TRAP domain-containing protein( domain architecture ID 10180536)

anti-TRAP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
anti-TRAP cd10748
anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT ...
 2-53 3.84e-30

anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT binds to the TRAP protein, (tryptophan-activated trp RNA-binding attenuation protein), effectively disrupting interaction of TRAP with mRNAs. Upon binding of tryptophan, TRAP (which forms a complex of 11 identical subunits) interacts with a specific location in the leader RNA and blocks translation of the tryptophan biosynthetic operon. AT, in turn, recognizes the tryptophan-activated TRAP complex and prevents RNA binding. AT is expressed in response to high levels of uncharged tryptophan tRNA. AT contains a zinc-binding motif that closely resembles the zinc-binding motifs in the zinc-finger region of DnaJ/Hsp40. AT has been shown to form homo-dodecameric assemblies, and can actually do that in two different relative orientations, resulting in two different dodecamers. Recent data suggest that the trimeric form of AT may be the biologically relevant active complex.


:

Pssm-ID: 199910 [Multi-domain]  Cd Length: 52  Bit Score: 99.23  E-value: 3.84e-30
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 489327515  2 VIATDDLEVACPKCERAGEIEGTPCPACSGKGVILTAQGYTLLDFIQKHLNK 53
Cdd:cd10748   1 VIATDDLEVTCPKCERAGEEEGTPCPKCSGKGVILTAQGYTLLHFIKKHLNE 52
 
Name Accession Description Interval E-value
anti-TRAP cd10748
anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT ...
 2-53 3.84e-30

anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT binds to the TRAP protein, (tryptophan-activated trp RNA-binding attenuation protein), effectively disrupting interaction of TRAP with mRNAs. Upon binding of tryptophan, TRAP (which forms a complex of 11 identical subunits) interacts with a specific location in the leader RNA and blocks translation of the tryptophan biosynthetic operon. AT, in turn, recognizes the tryptophan-activated TRAP complex and prevents RNA binding. AT is expressed in response to high levels of uncharged tryptophan tRNA. AT contains a zinc-binding motif that closely resembles the zinc-binding motifs in the zinc-finger region of DnaJ/Hsp40. AT has been shown to form homo-dodecameric assemblies, and can actually do that in two different relative orientations, resulting in two different dodecamers. Recent data suggest that the trimeric form of AT may be the biologically relevant active complex.


Pssm-ID: 199910 [Multi-domain]  Cd Length: 52  Bit Score: 99.23  E-value: 3.84e-30
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 489327515  2 VIATDDLEVACPKCERAGEIEGTPCPACSGKGVILTAQGYTLLDFIQKHLNK 53
Cdd:cd10748   1 VIATDDLEVTCPKCERAGEEEGTPCPKCSGKGVILTAQGYTLLHFIKKHLNE 52
Anti-TRAP pfam15777
Tryptophan RNA-binding attenuator protein inhibitory protein;
3-52 1.85e-22

Tryptophan RNA-binding attenuator protein inhibitory protein;


Pssm-ID: 406260 [Multi-domain]  Cd Length: 59  Bit Score: 80.33  E-value: 1.85e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489327515   3 IATDDLEVACPKCERAGEIEGT------PCPACSGKGVILTAQGYTLLDFIQKHLN 52
Cdd:pfam15777  4 IALPELETPCPACNGSGDIEPEtpyaslPCPKCKGKGVIPTAQGQTLLDFIKRHLN 59
PRK14293 PRK14293
molecular chaperone DnaJ;
11-34 1.32e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 36.89  E-value: 1.32e-04
                         10        20
                 ....*....|....*....|....
gi 489327515  11 ACPKCERAGEIEGTPCPACSGKGV 34
Cdd:PRK14293 188 ECPTCNGTGQVIEDPCDACGGQGV 211
CafA COG1530
Ribonuclease G or E [Translation, ribosomal structure and biogenesis];
19-53 2.16e-03

Ribonuclease G or E [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441139 [Multi-domain]  Cd Length: 490  Bit Score: 33.58  E-value: 2.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489327515  19 GEIEGTPCPACSGKGVILTAQ--GYTLLDFIQKHLNK 53
Cdd:COG1530  395 GESLCEPCPRCEGRGTIKSVEtvALEILREIEREARK 431
RNaseEG TIGR00757
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic ...
 19-40 5.41e-03

ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome. [Transcription, Degradation of RNA]


Pssm-ID: 273254 [Multi-domain]  Cd Length: 414  Bit Score: 32.29  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|..
gi 489327515   19 GEIEGTPCPACSGKGVILTAQG 40
Cdd:TIGR00757 386 MEVLGTVCPHCSGTGIVKTSES 407
 
Name Accession Description Interval E-value
anti-TRAP cd10748
anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT ...
 2-53 3.84e-30

anti-TRAP (AT) protein specific to Bacilli; In Bacillus subtilis and related bacteria, AT binds to the TRAP protein, (tryptophan-activated trp RNA-binding attenuation protein), effectively disrupting interaction of TRAP with mRNAs. Upon binding of tryptophan, TRAP (which forms a complex of 11 identical subunits) interacts with a specific location in the leader RNA and blocks translation of the tryptophan biosynthetic operon. AT, in turn, recognizes the tryptophan-activated TRAP complex and prevents RNA binding. AT is expressed in response to high levels of uncharged tryptophan tRNA. AT contains a zinc-binding motif that closely resembles the zinc-binding motifs in the zinc-finger region of DnaJ/Hsp40. AT has been shown to form homo-dodecameric assemblies, and can actually do that in two different relative orientations, resulting in two different dodecamers. Recent data suggest that the trimeric form of AT may be the biologically relevant active complex.


Pssm-ID: 199910 [Multi-domain]  Cd Length: 52  Bit Score: 99.23  E-value: 3.84e-30
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 489327515  2 VIATDDLEVACPKCERAGEIEGTPCPACSGKGVILTAQGYTLLDFIQKHLNK 53
Cdd:cd10748   1 VIATDDLEVTCPKCERAGEEEGTPCPKCSGKGVILTAQGYTLLHFIKKHLNE 52
Anti-TRAP pfam15777
Tryptophan RNA-binding attenuator protein inhibitory protein;
3-52 1.85e-22

Tryptophan RNA-binding attenuator protein inhibitory protein;


Pssm-ID: 406260 [Multi-domain]  Cd Length: 59  Bit Score: 80.33  E-value: 1.85e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489327515   3 IATDDLEVACPKCERAGEIEGT------PCPACSGKGVILTAQGYTLLDFIQKHLN 52
Cdd:pfam15777  4 IALPELETPCPACNGSGDIEPEtpyaslPCPKCKGKGVIPTAQGQTLLDFIKRHLN 59
PRK14293 PRK14293
molecular chaperone DnaJ;
11-34 1.32e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 36.89  E-value: 1.32e-04
                         10        20
                 ....*....|....*....|....
gi 489327515  11 ACPKCERAGEIEGTPCPACSGKGV 34
Cdd:PRK14293 188 ECPTCNGTGQVIEDPCDACGGQGV 211
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 10-35 6.09e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 35.10  E-value: 6.09e-04
                         10        20
                 ....*....|....*....|....*.
gi 489327515  10 VACPKCERAGEIEGTPCPACSGKGVI 35
Cdd:PRK14301 184 VPCPVCRGEGRVITHPCPKCKGSGIV 209
PRK14289 PRK14289
molecular chaperone DnaJ;
12-36 1.13e-03

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 34.42  E-value: 1.13e-03
                         10        20
                 ....*....|....*....|....*
gi 489327515  12 CPKCERAGEIEGTPCPACSGKGVIL 36
Cdd:PRK14289 200 CPTCNGEGKIIKKKCKKCGGEGIVY 224
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 12-33 1.37e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 33.87  E-value: 1.37e-03
                         10        20
                 ....*....|....*....|..
gi 489327515  12 CPKCERAGEIEGTPCPACSGKG 33
Cdd:PRK14278 185 CPTCRGVGEVIPDPCHECAGDG 206
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 12-33 1.69e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 33.67  E-value: 1.69e-03
                         10        20
                 ....*....|....*....|..
gi 489327515  12 CPKCERAGEIEGTPCPACSGKG 33
Cdd:PRK14298 187 CSTCHGRGQVIESPCPVCSGTG 208
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 12-35 2.04e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 33.81  E-value: 2.04e-03
                         10        20
                 ....*....|....*....|....
gi 489327515  12 CPKCERAGEIEGTPCPACSGKGVI 35
Cdd:PRK14285 188 CPKCYGNGKIISNPCKSCKGKGSL 211
CafA COG1530
Ribonuclease G or E [Translation, ribosomal structure and biogenesis];
19-53 2.16e-03

Ribonuclease G or E [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441139 [Multi-domain]  Cd Length: 490  Bit Score: 33.58  E-value: 2.16e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 489327515  19 GEIEGTPCPACSGKGVILTAQ--GYTLLDFIQKHLNK 53
Cdd:COG1530  395 GESLCEPCPRCEGRGTIKSVEtvALEILREIEREARK 431
PRK14295 PRK14295
molecular chaperone DnaJ;
9-40 2.69e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 33.28  E-value: 2.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 489327515   9 EVACPKCERAGEIEGTP---CPACSGKGVILTAQG 40
Cdd:PRK14295 166 QAPCPACSGTGAKNGTTprvCPTCSGTGQVSRNSG 200
PRK14280 PRK14280
molecular chaperone DnaJ;
9-33 3.72e-03

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 32.77  E-value: 3.72e-03
                         10        20
                 ....*....|....*....|....*
gi 489327515   9 EVACPKCERAGEIEGTPCPACSGKG 33
Cdd:PRK14280 186 RQTCPHCNGTGQEIKEKCPTCHGKG 210
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 12-35 4.01e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 32.85  E-value: 4.01e-03
                         10        20
                 ....*....|....*....|....
gi 489327515  12 CPKCERAGEIEGTPCPACSGKGVI 35
Cdd:PRK14277 201 CDRCHGEGKIITDPCNKCGGTGRI 224
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 12-39 4.59e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 32.55  E-value: 4.59e-03
                         10        20
                 ....*....|....*....|....*...
gi 489327515  12 CPKCERAGEIEGTPCPACSGKGVILTAQ 39
Cdd:PRK14292 186 CPTCRGEGQIITDPCTVCRGRGRTLKAE 213
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 8-35 5.22e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 32.42  E-value: 5.22e-03
                         10        20
                 ....*....|....*....|....*...
gi 489327515   8 LEVACPKCERAGEIEGTPCPACSGKGVI 35
Cdd:PRK10767 180 VQQTCPTCHGRGKIIKDPCKKCHGQGRV 207
RNaseEG TIGR00757
ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic ...
 19-40 5.41e-03

ribonuclease, Rne/Rng family; This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome. [Transcription, Degradation of RNA]


Pssm-ID: 273254 [Multi-domain]  Cd Length: 414  Bit Score: 32.29  E-value: 5.41e-03
                          10        20
                  ....*....|....*....|..
gi 489327515   19 GEIEGTPCPACSGKGVILTAQG 40
Cdd:TIGR00757 386 MEVLGTVCPHCSGTGIVKTSES 407
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 10-35 5.79e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 32.49  E-value: 5.79e-03
                         10        20
                 ....*....|....*....|....*.
gi 489327515  10 VACPKCERAGEIEGTPCPACSGKGVI 35
Cdd:PRK14283 190 TTCPDCQGEGKIVEKPCSNCHGKGVV 215
PRK07219 PRK07219
DNA topoisomerase I; Validated
 9-35 9.07e-03

DNA topoisomerase I; Validated


Pssm-ID: 235971 [Multi-domain]  Cd Length: 822  Bit Score: 31.89  E-value: 9.07e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 489327515   9 EVACPKC------ERAGEIEGtPCPACSGKGVI 35
Cdd:PRK07219 669 VVGCPDCeaekeeEDPDEVIG-PCPKCGGELAI 700
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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