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Conserved domains on  [gi|516060608|ref|WP_017491191|]
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TenA family protein [Rouxiella badensis]

Protein Classification

TenA family protein( domain architecture ID 14443657)

TenA family protein such as Bacillus halodurans aminopyrimidine aminohydrolase, which catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, as part of the thiamine salvage pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TenA_E_Spr0628-like cd19358
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ...
 7-215 6.43e-74

TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Many proteins in this family have yet to be characterized.


:

Pssm-ID: 381693 [Multi-domain]  Cd Length: 209  Bit Score: 222.45  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQ 86
Cdd:cd19358    1 FSDRLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLARFLGFLANDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  87 MAYFECVMTKRNISLDGYR--RSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNEIESPDVKDWVAM 164
Cdd:cd19358   81 NDYFERAFAALGVSEADREapPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDWASRAAAAAPLRFKHQEWIDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516060608 165 HAEETFISQANWLKIELDCCAENMPEREkiQLSELYAQVLQWEIDFHSAAY 215
Cdd:cd19358  161 HSGPEFEAWVDFLRDEVDRVGPTEEERE--RLEAVFARAVELEIAFFDAAY 209
 
Name Accession Description Interval E-value
TenA_E_Spr0628-like cd19358
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ...
 7-215 6.43e-74

TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Many proteins in this family have yet to be characterized.


Pssm-ID: 381693 [Multi-domain]  Cd Length: 209  Bit Score: 222.45  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQ 86
Cdd:cd19358    1 FSDRLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLARFLGFLANDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  87 MAYFECVMTKRNISLDGYR--RSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNEIESPDVKDWVAM 164
Cdd:cd19358   81 NDYFERAFAALGVSEADREapPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDWASRAAAAAPLRFKHQEWIDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516060608 165 HAEETFISQANWLKIELDCCAENMPEREkiQLSELYAQVLQWEIDFHSAAY 215
Cdd:cd19358  161 HSGPEFEAWVDFLRDEVDRVGPTEEERE--RLEAVFARAVELEIAFFDAAY 209
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 5-216 1.80e-49

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 160.43  E-value: 1.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   5 TSFTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALAN 84
Cdd:COG0819    1 MSFSERLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  85 EQMAYFECVMTKRNISLDGYRRS--SPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQN-EIESPDVKDW 161
Cdd:COG0819   81 VELALHERYAAELGISEEELEATppSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAERpLPPDHPYAEW 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516060608 162 VAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAYE 216
Cdd:COG0819  161 IETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYR 215
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 8-215 1.39e-09

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 56.89  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   8 TERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLI----GVLDALA 83
Cdd:PTZ00347  14 SEALWKENQDLAMMSLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLellkGVLEELK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  84 NEQMAYFEcvmtkrNISLDGYRRSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEwmYYHWCARVSQNEIESPD---VKD 160
Cdd:PTZ00347  94 NCHHHYID------NPDAAGPEAACRKYVDFLLASGNADTLGPSVVIAAVIPCAR--LYAWVGQELTNEVELTEshpFRR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516060608 161 WVAMHAEETFISQANWLKIELDCCAENMPEREKIQlseLYAQVLQWEIDFHSAAY 215
Cdd:PTZ00347 166 WLLSYSDEPINTSVEQLESLLDKYIRPGEFSEVAQ---AYRRAMELEYDFFDSFG 217
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 16-216 3.51e-08

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: 51.97  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   16 QELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQMAYFECVMT 95
Cdd:pfam03070   5 RPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRREWENRIVDHDGNEIELHLRLAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   96 KRNISLD--GYRRSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQ--NEIESPDVKDWVAMHAEETFI 171
Cdd:pfam03070  85 ALGLSREdlSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEkiRALEGPEYYEWVKTYASEYFR 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 516060608  172 SQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAYE 216
Cdd:pfam03070 165 AAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALD 209
 
Name Accession Description Interval E-value
TenA_E_Spr0628-like cd19358
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ...
 7-215 6.43e-74

TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Many proteins in this family have yet to be characterized.


Pssm-ID: 381693 [Multi-domain]  Cd Length: 209  Bit Score: 222.45  E-value: 6.43e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQ 86
Cdd:cd19358    1 FSDRLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLARFLGFLANDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  87 MAYFECVMTKRNISLDGYR--RSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNEIESPDVKDWVAM 164
Cdd:cd19358   81 NDYFERAFAALGVSEADREapPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDWASRAAAAAPLRFKHQEWIDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516060608 165 HAEETFISQANWLKIELDCCAENMPEREkiQLSELYAQVLQWEIDFHSAAY 215
Cdd:cd19358  161 HSGPEFEAWVDFLRDEVDRVGPTEEERE--RLEAVFARAVELEIAFFDAAY 209
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 5-216 1.80e-49

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 160.43  E-value: 1.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   5 TSFTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALAN 84
Cdd:COG0819    1 MSFSERLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  85 EQMAYFECVMTKRNISLDGYRRS--SPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQN-EIESPDVKDW 161
Cdd:COG0819   81 VELALHERYAAELGISEEELEATppSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAERpLPPDHPYAEW 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516060608 162 VAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAYE 216
Cdd:COG0819  161 IETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYR 215
TenA_C_BhTenA-like cd19366
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ...
 7-215 2.50e-23

TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus halodurans TenA which participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.


Pssm-ID: 381701 [Multi-domain]  Cd Length: 213  Bit Score: 93.00  E-value: 2.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYL----VFEGDFVataiKIFSYAVIKAPEIRQQRWLIGVLDAL 82
Cdd:cd19366    1 FSERLREKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLkqdyLYLIDYA----RVFALGAAKADDLETMGRFAELLHGT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  83 ANEQMAYFECVMTKRNISLDGYR--RSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNE--IESPDV 158
Cdd:cd19366   77 LNTEMDLHRQYAAEFGITEEELEatEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGgaLEHNPY 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 516060608 159 KDWVAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAY 215
Cdd:cd19366  157 REWIEMYSSDEFTELADWLIDLLDELAEGKSEAELERLEEIFLTSSRYEYMFWDMAY 213
TenA_C_HP1287-like cd19361
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ...
 7-210 2.73e-15

TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Helicobacter pylori TenA (HP1287) protein which is thought to catalyze a salvage reaction in thiamin metabolism, however its pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. HP1287 may contribute to stomach colonization and persistence.


Pssm-ID: 381696 [Multi-domain]  Cd Length: 212  Bit Score: 71.46  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQ 86
Cdd:cd19361    1 LSERLYEAVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFADLINAILNEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  87 MAYFECVMTKRNISLDGYRRS--SPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQN---EIESPDVKDW 161
Cdd:cd19361   81 MDIHRGYMKRLGITEEEIENTkpALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYIAKKLVERypaALEHEFYGEW 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516060608 162 VAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDF 210
Cdd:cd19361  161 VKGYSSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKF 209
TenA_PqqC-like cd16099
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ...
 18-210 1.31e-13

TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C; TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors.


Pssm-ID: 381691 [Multi-domain]  Cd Length: 196  Bit Score: 66.60  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  18 LWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEqMAYFECVMTKR 97
Cdd:cd16099    1 IWDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAELINVLDDE-LELHEKLLAEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  98 NISLDGYRRS--SPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNEIESPDVKDWVAMHAEETFISQAN 175
Cdd:cd16099   80 GISEEDLSEAepNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAASLPEHPPYRFWIDFYASDEYQELVE 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 516060608 176 WLKIELDCCAENMPErEKIQLSELYAQVLQWEIDF 210
Cdd:cd16099  160 ELLQLLDQLAAAGEE-EKEELKEIFLTSLRYELMF 193
TenA_E_At3g16990-like cd19357
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ...
 8-210 2.39e-12

TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Members of this family include Arabidopsis thaliana At3g16990, Zea mays GRMZM2G080501, and Pyrococcus furiosus PF1337, among others. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin; nor does it have activity with other thiamine degradation products such as thiamine mono- or diphosphate, oxythiamine, oxothiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates. Structural studies of P. furiosus PF1337 strongly support its enzymatic function in thiamine biosynthesis. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.


Pssm-ID: 381692 [Multi-domain]  Cd Length: 217  Bit Score: 63.49  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   8 TERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAP------EIRQQRWLIGVLDA 81
Cdd:cd19357    1 TSHLLSLHPALYTAATQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRFLGSLLARAPlpssslNQRLLDVLLGALAN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  82 LaNEQMAYFECVMTKRNISLDG-YRRSSPEVYRFSQGMLRAAETG-SYAEILTLMFAAEWMYYHWCARVSQNEIESPDVK 159
Cdd:cd19357   81 L-RRELAFFEETAAEYGLDLPGlGVPPSPATRAYVDFLASLASEGvSYLEGLVVLWATEKVYLDAWSYARSFLPSDADGG 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516060608 160 dwvAMHAE-------ETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDF 210
Cdd:cd19357  160 ---ALYREfipnwtsPEFAAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLELEEAF 214
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 8-215 1.39e-09

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 56.89  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   8 TERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLI----GVLDALA 83
Cdd:PTZ00347  14 SEALWKENQDLAMMSLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLellkGVLEELK 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  84 NEQMAYFEcvmtkrNISLDGYRRSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEwmYYHWCARVSQNEIESPD---VKD 160
Cdd:PTZ00347  94 NCHHHYID------NPDAAGPEAACRKYVDFLLASGNADTLGPSVVIAAVIPCAR--LYAWVGQELTNEVELTEshpFRR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516060608 161 WVAMHAEETFISQANWLKIELDCCAENMPEREKIQlseLYAQVLQWEIDFHSAAY 215
Cdd:PTZ00347 166 WLLSYSDEPINTSVEQLESLLDKYIRPGEFSEVAQ---AYRRAMELEYDFFDSFG 217
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 16-216 3.51e-08

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: 51.97  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   16 QELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQMAYFECVMT 95
Cdd:pfam03070   5 RPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRREWENRIVDHDGNEIELHLRLAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   96 KRNISLD--GYRRSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQ--NEIESPDVKDWVAMHAEETFI 171
Cdd:pfam03070  85 ALGLSREdlSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEkiRALEGPEYYEWVKTYASEYFR 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 516060608  172 SQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAYE 216
Cdd:pfam03070 165 AAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALD 209
TenA_C_SaTenA-like cd19360
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ...
 7-210 6.16e-08

TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins.


Pssm-ID: 381695 [Multi-domain]  Cd Length: 211  Bit Score: 51.05  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLvfEGDF--VATAIKIFSYAVIKAPEIRQQRWLIGVLDALAN 84
Cdd:cd19360    1 FSEELREEAQPILEAIYAHPFVQGIAAGELPKEALIHYV--QQDYeyLNAFLKVYALAIAKSDTREDMRFFLEQIGFILN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  85 EQMAYFECVMTKRNIS---LDGYRRsSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYhWCAR--VSQNEIEsPD-- 157
Cdd:cd19360   79 GESHAHQNLCEVAGVDyeeLQGAPW-APTADHYIKHMYYAARTGDLGDILAALLPCPWTYV-ELAKrlIEEGKPT-PDnp 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516060608 158 VKDWVAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDF 210
Cdd:cd19360  156 FYEWIDFYADDEMDGLTDQLFARLDRLAEKASEEERERAKQAFLKSCQLEWRF 208
TenA_C_PH1161-like cd19363
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ...
 8-215 6.18e-08

uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes functionally uncharacterized TenA like proteins such as Pyrococcus horikoshii PH1161 protein.


Pssm-ID: 381698 [Multi-domain]  Cd Length: 210  Bit Score: 51.17  E-value: 6.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   8 TERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRWLIGVLDALANEQM 87
Cdd:cd19363    2 TGKLRRDADDIWKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELLELAYGEATTEF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  88 AYFECVMTKRNISLDGYR--RSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMY-----YHwCARVSQNEIesPDVKD 160
Cdd:cd19363   82 ANYEELLDELGLSLEDAIkvEPFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYleiaeYH-KDKLSENPN--DIYRD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 516060608 161 WVAMHAEETFISQANWLKIELDCCAENMPEREkiqLSELYAQVLQWEIDFHSAAY 215
Cdd:cd19363  159 WASVYLSKEYKELVERLRRIVDKYGEGEPFEK---LKRIFKTASKYEYMFWDAAY 210
TenA_C-like cd19369
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 17-210 7.47e-07

uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins.


Pssm-ID: 381704 [Multi-domain]  Cd Length: 202  Bit Score: 47.99  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  17 ELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAPEIRQQRW----LIGVLDALANEQMAYFEc 92
Cdd:cd19369    1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFfyssLSFVNEDETATRIKYLK- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  93 vmtKRNISLDGYRRSS--PEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYY---HWCARVSQNEIESPDVKDWVAMHAE 167
Cdd:cd19369   80 ---EFGLTDEDIEKIEplPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYyifKELVKKYKDNLESNPYKDWIEDYAS 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 516060608 168 ETFISQAN-WLKIELDCCaENMPEREKIQLSELYAQVLQWEIDF 210
Cdd:cd19369  157 EEYAEYCKeWIDFADRLC-ENLSEEEKEKLKEIFRKASLYELKF 199
TenA_C-like cd19365
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 8-214 2.80e-05

uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins.


Pssm-ID: 381700 [Multi-domain]  Cd Length: 205  Bit Score: 43.27  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   8 TERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLV----FEGDFVataiKIFSYAVIKAPEIR-QQRWLIGVLDAL 82
Cdd:cd19365    1 TEALWEAIAPIYAAILAHPFIRELADGTLPREKFRFYLAqdalYLRDYA----RALALLAARAPDPEeQVFFARFAAGAI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  83 ANEQmAYFECVMTKRNISLDGyrRSSPEVYRFSQGMLRAAETGSYAEILtlmfAAE----WMYYHWCARVSQNEIESPDV 158
Cdd:cd19365   77 EVER-ELHRSFLGEFGIDAAA--EPSPVTLAYTSFLLATAATGPYAVAV----AAVlpcfWIYAEVGKRLAAAASPNHPY 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516060608 159 KDWVAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAA 214
Cdd:cd19365  150 QDWIDTYSDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWDAA 205
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-214 4.91e-05

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 43.62  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVFNQYLVFEGDFVATAIKIFSYAVIKAP-EIRQQRWLIGVLDALANE 85
Cdd:PRK14713 320 FTAALWQASGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAPdPAEQVFWAQSAQACLEVE 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  86 qMAYFECVMTKRNISLDgyrrSSPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYYHWCARVSQNEIESPD--VKDWVA 163
Cdd:PRK14713 400 -SELHRSWLGDRDADTA----PSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHARAGNPDDhpYAEWLQ 474

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516060608 164 MHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAA 214
Cdd:PRK14713 475 TYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQA 525
TenA_C_BsTenA-like cd19364
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ...
 7-216 7.14e-04

TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus subtilis TenA which has been shown to be a thiaminase II, catalyzing the hydrolysis of thiamine into HMP and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine metabolism. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.


Pssm-ID: 381699 [Multi-domain]  Cd Length: 212  Bit Score: 39.09  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608   7 FTERLLAENQELWQGMQQHRFVTDIEQGALTARVF-------NQYLVfegDFVataiKIFSYAVIKAPEIRQQRWLIGVL 79
Cdd:cd19364    1 FTEELREAADPLWQKSFEHPFIQGLADGTLPLETFryyliqdAYYLK---HFA----KLHALAAAKADDPAIKALLLEGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516060608  80 DALANEQMAYFECVMTKRNISLDGYRRS--SPEVYRFSQGMLRAAETGSYAEILTLMFAAEWMYY----HWCARVSQNEI 153
Cdd:cd19364   74 QGLAEGELALRETFFKELGITEEEIAQTppAPTAYHYVSHMYRQLNEGSVAEAVAALLPCYWLYQeigeRLADAGSPVPL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516060608 154 espdVKDWVAMHAEETFISQANWLKIELDCCAENMPEREKIQLSELYAQVLQWEIDFHSAAYE 216
Cdd:cd19364  154 ----YQRWIDTYASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMAYT 212
 
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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