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Conserved domains on  [gi|489176347|ref|WP_003085869|]
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MULTISPECIES: TenA family transcriptional regulator [Pseudomonas]

Protein Classification

TenA family transcriptional regulator( domain architecture ID 10009274)

TenA family transcriptional regulator similar to Chlamydia trachomatis Chlamydia protein associating with death domains (CADD), a Chlamydia specific toxin that associates with death domains of tumor necrosis factor family (TNF) receptors and induces apoptosis in mammalian cell lines through a Caspase-dependent mechanism

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
19-250 1.07e-49

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


:

Pssm-ID: 444176  Cd Length: 228  Bit Score: 163.14  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  19 QWAQQLIVDCQasKDRVSGHELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSQNLlktrfARHPgEDMARRWLMRNI 98
Cdd:COG5424    6 EFEARLRAEIA--RRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAIL-----SRCP-DEELRRALLENL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  99 RVEL------NHADYWLHWAEAHGVSLAEIQAQDVPAELHALSHWCWHTCASDSLPVAMAATnYAIEGVTGEWSALVCSN 172
Cdd:COG5424   78 YEEDgegpeeGHIELWLRFAEALGLDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAAS-LTAEGFAPEISRERLEG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489176347 173 GVYENAFPKEgrkRAMKWLKLHAQYDDAHPWEALEIICTLAGTnpsAELRRQLRDAICKSYDYMYLFLERCMQLEEAR 250
Cdd:COG5424  157 LLEHYGLPDE---EALEYFRLHAELDPRHAEEALELVLRLADT---PEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
 
Name Accession Description Interval E-value
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
19-250 1.07e-49

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


Pssm-ID: 444176  Cd Length: 228  Bit Score: 163.14  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  19 QWAQQLIVDCQasKDRVSGHELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSQNLlktrfARHPgEDMARRWLMRNI 98
Cdd:COG5424    6 EFEARLRAEIA--RRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAIL-----SRCP-DEELRRALLENL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  99 RVEL------NHADYWLHWAEAHGVSLAEIQAQDVPAELHALSHWCWHTCASDSLPVAMAATnYAIEGVTGEWSALVCSN 172
Cdd:COG5424   78 YEEDgegpeeGHIELWLRFAEALGLDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAAS-LTAEGFAPEISRERLEG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489176347 173 GVYENAFPKEgrkRAMKWLKLHAQYDDAHPWEALEIICTLAGTnpsAELRRQLRDAICKSYDYMYLFLERCMQLEEAR 250
Cdd:COG5424  157 LLEHYGLPDE---EALEYFRLHAELDPRHAEEALELVLRLADT---PEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
Haem_oxygenas_2 pfam14518
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ...
55-234 3.00e-09

Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase.


Pssm-ID: 434009  Cd Length: 178  Bit Score: 55.09  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347   55 RLYLIGGWPVVEQFPLYMSQNLLKTRFARhpgedmARRWLMRNI-------RVELNHADYWLHWAEAHGVSLAEIQAQDV 127
Cdd:pfam14518   1 REFLRQRYPYVLVFADWLALVIPRLPDGR------AKAALVENLweelgdgDPERNHVELFRRLLAALGLDPEYLEYLPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  128 PAELHALSHWCWHTCASDSLPVAMAATNYAIEGVTGEwsalvcSNGVYENAFPKEG-RKRAMKWLKLHAQYDDAHPWEAL 206
Cdd:pfam14518  75 LPETLALVNLMSLFGLHRRLRGALLGALAALELTSPP------PALRLAKGLRRLGlDDEALYYFDEHVEIDAAHAQMAL 148
                         170       180
                  ....*....|....*....|....*....
gi 489176347  207 EIIC-TLAGTNPsaELRRQLRDAICKSYD 234
Cdd:pfam14518 149 EDVLePLADEEP--ELAQDVLFGARRRLD 175
TenA_PqqC cd19370
TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to ...
38-241 3.19e-03

TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to TenA, and includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C or PQQC proteins. PQQ is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. The exact molecular function of members of this family is unclear. Also belonging to this family is Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), a redox protein toxin unique to Chlamydia species, which modulates host cell apoptosis; its redox activity and death domain binding ability may be required for this biological activity. CADD may have a role in folate metabolism.


Pssm-ID: 381705  Cd Length: 219  Bit Score: 37.96  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  38 HELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSQNLLKTrfarhpGEDMARRWLMRNIRVEL------NHADYWLHW 111
Cdd:cd19370   19 HPFHVAMHNGTLTKEQLQGYVANRYYYQKTIPKKLSAIMARC------DDAQTRRKWLQNILDEDgghgepGHIELWLRL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347 112 AEAHGVSLAEIQAQDV-PAELHALSHWCwHTCASDSLpVAMAATNYAIEGVTGEWSALVCSNGVYENAFpkEGRKRAMKW 190
Cdd:cd19370   93 GEALGLTRELLSERHPlPATRFAVDTYL-NFARRASW-LEAAASSLSEEFAPQRIQSRLDSWLQHYNSP--WIKEEGYFF 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489176347 191 LKLHAQYDDAHPWEALEIICTLAGTnpsAELRRQLRDAICKSYDYMYLFLE 241
Cdd:cd19370  169 FRSELSQDVRHAREGLALAEAYCDS---AEKQNRVLEALQFKLDILWSMLD 216
 
Name Accession Description Interval E-value
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
19-250 1.07e-49

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


Pssm-ID: 444176  Cd Length: 228  Bit Score: 163.14  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  19 QWAQQLIVDCQasKDRVSGHELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSQNLlktrfARHPgEDMARRWLMRNI 98
Cdd:COG5424    6 EFEARLRAEIA--RRYLLKHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAIL-----SRCP-DEELRRALLENL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  99 RVEL------NHADYWLHWAEAHGVSLAEIQAQDVPAELHALSHWCWHTCASDSLPVAMAATnYAIEGVTGEWSALVCSN 172
Cdd:COG5424   78 YEEDgegpeeGHIELWLRFAEALGLDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAAS-LTAEGFAPEISRERLEG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489176347 173 GVYENAFPKEgrkRAMKWLKLHAQYDDAHPWEALEIICTLAGTnpsAELRRQLRDAICKSYDYMYLFLERCMQLEEAR 250
Cdd:COG5424  157 LLEHYGLPDE---EALEYFRLHAELDPRHAEEALELVLRLADT---PEDQEAALEAARFKLDLLWAFLDALYRAYVAP 228
Haem_oxygenas_2 pfam14518
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ...
55-234 3.00e-09

Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase.


Pssm-ID: 434009  Cd Length: 178  Bit Score: 55.09  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347   55 RLYLIGGWPVVEQFPLYMSQNLLKTRFARhpgedmARRWLMRNI-------RVELNHADYWLHWAEAHGVSLAEIQAQDV 127
Cdd:pfam14518   1 REFLRQRYPYVLVFADWLALVIPRLPDGR------AKAALVENLweelgdgDPERNHVELFRRLLAALGLDPEYLEYLPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  128 PAELHALSHWCWHTCASDSLPVAMAATNYAIEGVTGEwsalvcSNGVYENAFPKEG-RKRAMKWLKLHAQYDDAHPWEAL 206
Cdd:pfam14518  75 LPETLALVNLMSLFGLHRRLRGALLGALAALELTSPP------PALRLAKGLRRLGlDDEALYYFDEHVEIDAAHAQMAL 148
                         170       180
                  ....*....|....*....|....*....
gi 489176347  207 EIIC-TLAGTNPsaELRRQLRDAICKSYD 234
Cdd:pfam14518 149 EDVLePLADEEP--ELAQDVLFGARRRLD 175
TenA_PqqC cd19370
TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to ...
38-241 3.19e-03

TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to TenA, and includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C or PQQC proteins. PQQ is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. The exact molecular function of members of this family is unclear. Also belonging to this family is Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), a redox protein toxin unique to Chlamydia species, which modulates host cell apoptosis; its redox activity and death domain binding ability may be required for this biological activity. CADD may have a role in folate metabolism.


Pssm-ID: 381705  Cd Length: 219  Bit Score: 37.96  E-value: 3.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347  38 HELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSQNLLKTrfarhpGEDMARRWLMRNIRVEL------NHADYWLHW 111
Cdd:cd19370   19 HPFHVAMHNGTLTKEQLQGYVANRYYYQKTIPKKLSAIMARC------DDAQTRRKWLQNILDEDgghgepGHIELWLRL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347 112 AEAHGVSLAEIQAQDV-PAELHALSHWCwHTCASDSLpVAMAATNYAIEGVTGEWSALVCSNGVYENAFpkEGRKRAMKW 190
Cdd:cd19370   93 GEALGLTRELLSERHPlPATRFAVDTYL-NFARRASW-LEAAASSLSEEFAPQRIQSRLDSWLQHYNSP--WIKEEGYFF 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 489176347 191 LKLHAQYDDAHPWEALEIICTLAGTnpsAELRRQLRDAICKSYDYMYLFLE 241
Cdd:cd19370  169 FRSELSQDVRHAREGLALAEAYCDS---AEKQNRVLEALQFKLDILWSMLD 216
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
38-153 9.40e-03

TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain.


Pssm-ID: 397272 [Multi-domain]  Cd Length: 210  Bit Score: 36.18  E-value: 9.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489176347   38 HELYRRMRDAELSPALMRLYLIGGWPVVEQFPLYMSqnllkTRFARHPGEDMARRWLMRNIRVELNHADYWLHWAEAHGV 117
Cdd:pfam03070  14 HPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLA-----IIASKSPDLEVRREWENRIVDHDGNEIELHLRLAEALGL 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489176347  118 SLAEIQAQDVPAELHALSHWCWHTCASDSLPVAMAA 153
Cdd:pfam03070  89 SREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAA 124
 
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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