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Conserved domains on  [gi|23346499|ref|NP_694723|]
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thiamine-triphosphatase [Mus musculus]

Protein Classification

ThTPase domain-containing protein( domain architecture ID 10166812)

ThTPase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 6-198 6.25e-79

Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine triphosphate (ThTP) to thiamine diphosphate. This catalytic activity depends on a divalent metal cofactor, for example Mg++. ThTPase regulates the intracellular concentration of ThTP, maintaining it at a low concentration in vivo. ThTP acts as a messenger in cell signaling in response to cellular stress, and in addition, can phosphorylate proteins in certain tissues. There is another class of membrane-associated enzymes in animal tissues which also convert ThTP to thiamine diphosphate, however they do not belong to this subgroup. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


:

Pssm-ID: 143625  Cd Length: 196  Bit Score: 234.96  E-value: 6.25e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFAPGPDTEERLQELGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWELKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758   1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  82 VTSEAAIVAQLFELLGSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLalsgahgqEPQLTIDLDSADFGYAVGEVEAM 161
Cdd:cd07758  80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWKL--------DGAFRVDLDRTDFGYSVGEVELL 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23346499 162 VHE---KAEVPAALEKIITVSSMLGVPA-----QEEAPAKLMVYL 198
Cdd:cd07758 152 VEEednEAEVPAALAKIDELISALMERYlwafkQGRPPGKLTAYL 196
 
Name Accession Description Interval E-value
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 6-198 6.25e-79

Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine triphosphate (ThTP) to thiamine diphosphate. This catalytic activity depends on a divalent metal cofactor, for example Mg++. ThTPase regulates the intracellular concentration of ThTP, maintaining it at a low concentration in vivo. ThTP acts as a messenger in cell signaling in response to cellular stress, and in addition, can phosphorylate proteins in certain tissues. There is another class of membrane-associated enzymes in animal tissues which also convert ThTP to thiamine diphosphate, however they do not belong to this subgroup. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143625  Cd Length: 196  Bit Score: 234.96  E-value: 6.25e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFAPGPDTEERLQELGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWELKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758   1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  82 VTSEAAIVAQLFELLGSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLalsgahgqEPQLTIDLDSADFGYAVGEVEAM 161
Cdd:cd07758  80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWKL--------DGAFRVDLDRTDFGYSVGEVELL 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23346499 162 VHE---KAEVPAALEKIITVSSMLGVPA-----QEEAPAKLMVYL 198
Cdd:cd07758 152 VEEednEAEVPAALAKIDELISALMERYlwafkQGRPPGKLTAYL 196
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 5-191 2.34e-24

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyzes the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Six distinct non-homologous classes of AC have been identified. The structure of three classes of adenylyl cyclases have been solved.


Pssm-ID: 396490  Cd Length: 172  Bit Score: 94.91  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499     5 LIEVERKFAPGP---DTEERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQR-EGSGWE---LKCPGVTGVSGPHN 77
Cdd:pfam01928   1 MIEIERKFLVSDeeyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRrFGNGAYfltLKGPGVDGPFKSRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499    78 EY-VEVTSEAAIVAQLFELLGsgeqkpagvaavlgslkLQEVASFITTRSSWKLAlsgahgqepQLTIDLDSADF-GYAV 155
Cdd:pfam01928  81 EVnGEVSRDEPDAVELLDGLG-----------------LQPVGSIKKERRRYKVK---------GVLIALDVVEFlGGAE 134

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 23346499   156 GEVEAMVHEKAEVPAALEKiITVSSMLGVPAQEEAP 191
Cdd:pfam01928 135 VELELEVEDEEELLEAAEE-LELLRILGLSEESKIA 169
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 6-185 7.00e-18

Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441046  Cd Length: 173  Bit Score: 77.61  E-value: 7.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFaPGPDTE---ERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE-GSGWEL--KCPGVTGVSGPHNEY 79
Cdd:COG1437   1 IEVEVKV-RVIDLEevrERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRgGGRATLtyKGPKLDEGSKTREEI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  80 -VEVTSEAAiVAQLFELLGsgeqkpagvaavlgslkLQEVASFITTRSSWKLalsgahgqePQLTIDLDSADFGYAVGEV 158
Cdd:COG1437  80 eTEVDDGEA-MEAILEALG-----------------FRPVATVEKTREIYKL---------GGVTVTLDEVEGLGPFVEI 132

                       170       180
                ....*....|....*....|....*..
gi 23346499 159 EAMVheKAEVPAALEKIITVSSMLGVP 185
Cdd:COG1437 133 EGEA--EDEVEAAREAIEEVLAELGLD 157
 
Name Accession Description Interval E-value
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 6-198 6.25e-79

Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine triphosphate (ThTP) to thiamine diphosphate. This catalytic activity depends on a divalent metal cofactor, for example Mg++. ThTPase regulates the intracellular concentration of ThTP, maintaining it at a low concentration in vivo. ThTP acts as a messenger in cell signaling in response to cellular stress, and in addition, can phosphorylate proteins in certain tissues. There is another class of membrane-associated enzymes in animal tissues which also convert ThTP to thiamine diphosphate, however they do not belong to this subgroup. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143625  Cd Length: 196  Bit Score: 234.96  E-value: 6.25e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFAPGPDTEERLQELGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWELKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758   1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  82 VTSEAAIVAQLFELLGSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLalsgahgqEPQLTIDLDSADFGYAVGEVEAM 161
Cdd:cd07758  80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWKL--------DGAFRVDLDRTDFGYSVGEVELL 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23346499 162 VHE---KAEVPAALEKIITVSSMLGVPA-----QEEAPAKLMVYL 198
Cdd:cd07758 152 VEEednEAEVPAALAKIDELISALMERYlwafkQGRPPGKLTAYL 196
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 5-191 2.34e-24

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyzes the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Six distinct non-homologous classes of AC have been identified. The structure of three classes of adenylyl cyclases have been solved.


Pssm-ID: 396490  Cd Length: 172  Bit Score: 94.91  E-value: 2.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499     5 LIEVERKFAPGP---DTEERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQR-EGSGWE---LKCPGVTGVSGPHN 77
Cdd:pfam01928   1 MIEIERKFLVSDeeyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRrFGNGAYfltLKGPGVDGPFKSRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499    78 EY-VEVTSEAAIVAQLFELLGsgeqkpagvaavlgslkLQEVASFITTRSSWKLAlsgahgqepQLTIDLDSADF-GYAV 155
Cdd:pfam01928  81 EVnGEVSRDEPDAVELLDGLG-----------------LQPVGSIKKERRRYKVK---------GVLIALDVVEFlGGAE 134

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 23346499   156 GEVEAMVHEKAEVPAALEKiITVSSMLGVPAQEEAP 191
Cdd:pfam01928 135 VELELEVEDEEELLEAAEE-LELLRILGLSEESKIA 169
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 7-177 6.93e-18

CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like superfamily enzymes hydrolyze triphosphate-containing substrates and require metal cations as cofactors. They have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB), and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions.


Pssm-ID: 143620  Cd Length: 174  Bit Score: 77.88  E-value: 6.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   7 EVERKFAPGPDTEERLQE-----LGATLEHRVTFRDTYYDTSELSLMLSDHWLRQREGS---GWELKCPGVTGVsgpHNE 78
Cdd:cd07374   1 EVERKFRVPDDAVLPLLLgvpgvLGVGEPETVQLRAIYFDTPDLRLARAGLRLRRRTGGadaGWHLKLPGGISR---RTE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  79 YVEVTSEAAIVAQLfellgsgEQKPAGVAAVLGSLKLQEVASFITTRSSWKLALSGAHGQEpqltIDLDSADFG------ 152
Cdd:cd07374  78 VRAPLGDAAAVAPL-------LLAAALVLAVTRGLPLRPVATIETTRTVYRLLDAGGVLAE----LDLDTVTARvldggg 146

                       170       180
                ....*....|....*....|....*..
gi 23346499 153 -YAVGEVEAMVHEKAE-VPAALEKIIT 177
Cdd:cd07374 147 tQYWREVEVELPDGDEaLLDALERRLT 173
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 6-185 7.00e-18

Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) [Signal transduction mechanisms, General function prediction only];


Pssm-ID: 441046  Cd Length: 173  Bit Score: 77.61  E-value: 7.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFaPGPDTE---ERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE-GSGWEL--KCPGVTGVSGPHNEY 79
Cdd:COG1437   1 IEVEVKV-RVIDLEevrERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRgGGRATLtyKGPKLDEGSKTREEI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  80 -VEVTSEAAiVAQLFELLGsgeqkpagvaavlgslkLQEVASFITTRSSWKLalsgahgqePQLTIDLDSADFGYAVGEV 158
Cdd:COG1437  80 eTEVDDGEA-MEAILEALG-----------------FRPVATVEKTREIYKL---------GGVTVTLDEVEGLGPFVEI 132

                       170       180
                ....*....|....*....|....*..
gi 23346499 159 EAMVheKAEVPAALEKIITVSSMLGVP 185
Cdd:COG1437 133 EGEA--EDEVEAAREAIEEVLAELGLD 157
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 7-175 1.17e-08

Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup contains class IV ACs and similar proteins. AC catalyzes the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. cAMP is a key signaling molecule which conveys a variety of signals in different cell types. In prokaryotes, cAMP is a catabolite derepression signal which triggers the expression of metabolic pathways including the lactose operon. Six non-homologous classes of ACs have been identified (I-VI). Class IV ACs are found in this group. In bacteria, the gene encoding Class IV AC has been designated cyaB and the protein as AC2. AC-IV occurs in addition to AC-I in bacterial pathogens such as Yersinia pestis (plague disease). The role of AC-IV is unknown but it has been speculated that it may be a factor in pathogenesis, perhaps providing cAMP for a secondary internal signaling function, or for secretion and uptake into host cells, where it may disrupt normal cellular processes. This subgroup belongs to the CYTH/triphosphate tunnel metalloenzyme (TTM)-like superfamily, whose enzymes have a unique active site located within an eight-stranded beta barrel.


Pssm-ID: 143628  Cd Length: 169  Bit Score: 52.66  E-value: 1.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   7 EVERKF-APGPDT-EERLQELGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE---GSGWEL--KCPGVTGVSgPHNEY 79
Cdd:cd07890   1 EVEIKArVDDLEAlRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRmgdSGKTLLtyKGPKLDGGP-KVREE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499  80 VEVTseaaiVAqlfellgsgeqKPAGVAAVLGSLKLQEVASFITTRSSWKLalsgahgqePQLTIDLDS-ADFGYAVgEV 158
Cdd:cd07890  80 IETE-----VA-----------DPEAMKEILERLGFGPVGRVKKEREIYLL---------GQTRVHLDRvEGLGDFV-EI 133

                       170
                ....*....|....*..
gi 23346499 159 EAMVHEKAEVPAALEKI 175
Cdd:cd07890 134 EVVLEDIEEAEEGLGEA 150
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 7-136 1.18e-06

Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This subgroup belongs to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily. Members of this superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). A number of proteins in this subgroup also contain a C-terminal CHAD (Conserved Histidine Alpha-helical Domain) domain which may participate in metal chelation or act as a phosphor-acceptor. The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup have not been characterized.


Pssm-ID: 143624 [Multi-domain]  Cd Length: 197  Bit Score: 47.23  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   7 EVERKFAPGPDTEER------LQELGATLEHRVTFRDTYYDTSelslmlsDHWLRQ--------REGSGWE--LKCPGvT 70
Cdd:cd07756   1 EIELKLLLPPEDLEAlaahplLAALAAGRAQTRRLHNTYFDTP-------DLALRRagialrvrREGGQWVqtLKTAG-S 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23346499  71 GVSGPH--NEY-VEVTSEAAIVAQLfellgsgEQKPAG--VAAVLGSLKLQEVasFIT--TRSSWKLALSGAH 136
Cdd:cd07756  73 VVGGLHqrPEWeVPLPGPAPDLDLA-------SILPDGelLEALAALAALVPL--FTTdfERTVWLLRLGGSE 136
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 6-134 5.58e-06

Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and metabolism];


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 46.04  E-value: 5.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23346499   6 IEVERKFAPGPDTEERLQELGATLEHRV------TFRDTYYDTSELSLMLSDHWLRQR-EGSGWE--LKCPGvTGVSGPH 76
Cdd:COG3025   3 REIELKLLVDPEALPALRQHPLLAGLAVgepatrRLENTYFDTPDLDLRRAGIGLRVRrEGGRWEqtLKTAG-QVVGGLH 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23346499  77 --NEY-VEVTSEAAIVAQLfellgSGEQKPAGVAAVLGSLKLQEVASFITTRSSWKLALSG 134
Cdd:COG3025  82 qrPEWeVPLPSPEPDLSLL-----PDEPLPELLDAAALGAALQPVFTTDFERTTWLLTLAD 137
 
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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