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Conserved domains on  [gi|564386161|ref|XP_006252032|]
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thiamine-triphosphatase isoform X2 [Rattus norvegicus]

Protein Classification

CYTH domain-containing protein; polyphosphate polymerase domain-containing protein( domain architecture ID 10166812)

CYTH domain-containing protein such as inorganic triphosphatase, which catalyzes the hydrolysis of inorganic or nucleoside-linked triphosphate-containing substrates| polyphosphate (polyP) polymerase domain-containing protein similar to yeast vacuolar transport chaperone (VTC) proteins VTC-2, -3 and- 4, which are components of the integral membrane VTC complex; the polyP polymerase domain generates polyP from ATP by a phosphotransfer reaction releasing ADP

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 ...
 6-184 1.77e-70

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: 212.62  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFTPGPDTEERLQKLGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWEFKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758    1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  82 VTSESAIVTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKlaLSGAheeeslLTVDLDSTDFGYAVGEVEAV 161
Cdd:cd07758   80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWK--LDGA------FRVDLDRTDFGYSVGEVELL 151

                        170       180
                 ....*....|....*....|....*.
gi 564386161 162 VHE---KAEVPAALEKIISVSSMLGE 184
Cdd:cd07758  152 VEEednEAEVPAALAKIDELISALME 177
 
Name Accession Description Interval E-value
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 6-184 1.77e-70

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: 212.62  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFTPGPDTEERLQKLGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWEFKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758    1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  82 VTSESAIVTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKlaLSGAheeeslLTVDLDSTDFGYAVGEVEAV 161
Cdd:cd07758   80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWK--LDGA------FRVDLDRTDFGYSVGEVELL 151

                        170       180
                 ....*....|....*....|....*.
gi 564386161 162 VHE---KAEVPAALEKIISVSSMLGE 184
Cdd:cd07758  152 VEEednEAEVPAALAKIDELISALME 177
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 5-186 1.18e-19

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: 81.82  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161    5 LIEVERKFTPGP---DTEERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQR-EGSGWE---FKCPGVTGVSgphn 77
Cdd:pfam01928   1 MIEIERKFLVSDeeyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRrFGNGAYfltLKGPGVDGPF---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   78 eyvevtsesaivTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKLalsgaheEESLLTVDLDStDFGYAVGE 157
Cdd:pfam01928  77 ------------KSREEVNGEVSRDEPDAVELLDGLGLQPVGSIKKERRRYKV-------KGVLIALDVVE-FLGGAEVE 136

                         170       180
                  ....*....|....*....|....*....
gi 564386161  158 VEAVVHEKAEVPAALEKiISVSSMLGEGD 186
Cdd:pfam01928 137 LELEVEDEEELLEAAEE-LELLRILGLSE 164
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 6-183 3.20e-15

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: 70.29  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFtPGPDTE---ERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE-GSGWE--FKCPGVTGVSGpHNEY 79
Cdd:COG1437    1 IEVEVKV-RVIDLEevrERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRgGGRATltYKGPKLDEGSK-TREE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  80 VEVTsesaivtqlfelLGSGEQetagVAAVLGRLKLQEVASFITTRSSWKLalsgahEEeslLTVDLDSTDFGYAVGEVE 159
Cdd:COG1437   79 IETE------------VDDGEA----MEAILEALGFRPVATVEKTREIYKL------GG---VTVTLDEVEGLGPFVEIE 133

                        170       180
                 ....*....|....*....|....
gi 564386161 160 AVVheKAEVPAALEKIISVSSMLG 183
Cdd:COG1437  134 GEA--EDEVEAAREAIEEVLAELG 155
 
Name Accession Description Interval E-value
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 6-184 1.77e-70

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: 212.62  E-value: 1.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFTPGPDTEERLQKLGA--TLEHRVTFRDTYYDTSELSLMLSDHWLRQREGsGWEFKCPGVTGVS--GPHNEYVE 81
Cdd:cd07758    1 LEVERKFRCGPSAEERLRKLGAllELLGRRTFHDTYYDTPDNTLSLNDVWLRQRNG-QWELKIPPGGDPPtaGANTRYEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  82 VTSESAIVTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKlaLSGAheeeslLTVDLDSTDFGYAVGEVEAV 161
Cdd:cd07758   80 LTGEAAIAAALRKLLGGALPSAGGLGDELANLGLREFASFVTKRESWK--LDGA------FRVDLDRTDFGYSVGEVELL 151

                        170       180
                 ....*....|....*....|....*.
gi 564386161 162 VHE---KAEVPAALEKIISVSSMLGE 184
Cdd:cd07758  152 VEEednEAEVPAALAKIDELISALME 177
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 5-186 1.18e-19

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: 81.82  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161    5 LIEVERKFTPGP---DTEERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQR-EGSGWE---FKCPGVTGVSgphn 77
Cdd:pfam01928   1 MIEIERKFLVSDeeyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRrFGNGAYfltLKGPGVDGPF---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   78 eyvevtsesaivTQLFELLGSGEQETAGVAAVLGRLKLQEVASFITTRSSWKLalsgaheEESLLTVDLDStDFGYAVGE 157
Cdd:pfam01928  77 ------------KSREEVNGEVSRDEPDAVELLDGLGLQPVGSIKKERRRYKV-------KGVLIALDVVE-FLGGAEVE 136

                         170       180
                  ....*....|....*....|....*....
gi 564386161  158 VEAVVHEKAEVPAALEKiISVSSMLGEGD 186
Cdd:pfam01928 137 LELEVEDEEELLEAAEE-LELLRILGLSE 164
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 6-183 3.20e-15

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: 70.29  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFtPGPDTE---ERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE-GSGWE--FKCPGVTGVSGpHNEY 79
Cdd:COG1437    1 IEVEVKV-RVIDLEevrERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRgGGRATltYKGPKLDEGSK-TREE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  80 VEVTsesaivtqlfelLGSGEQetagVAAVLGRLKLQEVASFITTRSSWKLalsgahEEeslLTVDLDSTDFGYAVGEVE 159
Cdd:COG1437   79 IETE------------VDDGEA----MEAILEALGFRPVATVEKTREIYKL------GG---VTVTLDEVEGLGPFVEIE 133

                        170       180
                 ....*....|....*....|....
gi 564386161 160 AVVheKAEVPAALEKIISVSSMLG 183
Cdd:COG1437  134 GEA--EDEVEAAREAIEEVLAELG 155
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 7-177 1.95e-14

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: 68.25  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   7 EVERKFTPGPDTEERLQK-----LGATLEHRVTFRDTYYDTSELSLMLSDHWLRQREGS---GWEFKCPGVTGVsgphNE 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLgvpgvLGVGEPETVQLRAIYFDTPDLRLARAGLRLRRRTGGadaGWHLKLPGGISR----RT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  79 YVEVTSESAIVTQlfellgSGEQETAGVAAVLGRLKLQEVASFITTRSSWKLALSGAHeeesLLTVDLDSTDFG------ 152
Cdd:cd07374   77 EVRAPLGDAAAVA------PLLLAAALVLAVTRGLPLRPVATIETTRTVYRLLDAGGV----LAELDLDTVTARvldggg 146

                        170       180
                 ....*....|....*....|....*..
gi 564386161 153 -YAVGEVEAVVHEKAE-VPAALEKIIS 177
Cdd:cd07374  147 tQYWREVEVELPDGDEaLLDALERRLT 173
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 7-175 5.87e-07

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: 47.65  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   7 EVERKFtPGPDTE---ERLQKLGATLEHRVTFRDTYYDTSELSLMLSDHWLRQRE-----GSGWEFKCPGVTGVSgPHNE 78
Cdd:cd07890    1 EVEIKA-RVDDLEalrERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRmgdsgKTLLTYKGPKLDGGP-KVRE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  79 YVEVTSESAIVTqlfellgsgeqetagvAAVLGRLKLQEVASFITTRSSWKLAlsGAHeeeslltVDLDSTD-FGYAVgE 157
Cdd:cd07890   79 EIETEVADPEAM----------------KEILERLGFGPVGRVKKEREIYLLG--QTR-------VHLDRVEgLGDFV-E 132

                        170
                 ....*....|....*...
gi 564386161 158 VEAVVHEKAEVPAALEKI 175
Cdd:cd07890  133 IEVVLEDIEEAEEGLGEA 150
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 7-160 2.93e-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: 46.07  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   7 EVERKFTPGPDTEER------LQKLGATLEHRVTFRDTYYDTSelslmlsDHWLRQ--------REGSGWE--FKCPGvT 70
Cdd:cd07756    1 EIELKLLLPPEDLEAlaahplLAALAAGRAQTRRLHNTYFDTP-------DLALRRagialrvrREGGQWVqtLKTAG-S 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  71 GVSGPH--NEY-VEVTSESAIVTQLFELLgsgeqETAGVAAVLGRLKLQEVasFIT--TRSSWKLALSGAHEEeslltVD 145
Cdd:cd07756   73 VVGGLHqrPEWeVPLPGPAPDLDLASILP-----DGELLEALAALAALVPL--FTTdfERTVWLLRLGGSEIE-----VA 140

                        170
                 ....*....|....*
gi 564386161 146 LDStdfgyavGEVEA 160
Cdd:cd07756  141 LDQ-------GEIRA 148
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 6-160 3.84e-05

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 42.96  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161   6 IEVERKFTPGPDTEERLQKLGATLEHRV------TFRDTYYDTSELSLMLSDHWLRQR-EGSGWE--FKCPGvTGVSGPH 76
Cdd:COG3025    3 REIELKLLVDPEALPALRQHPLLAGLAVgepatrRLENTYFDTPDLDLRRAGIGLRVRrEGGRWEqtLKTAG-QVVGGLH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564386161  77 --NEY-VEVTSESAIVTQLfellgSGEQETAGVAAVLGRLKLQEVASFITTRSSWKLALsgahEEESLLTVDLDstdfgy 153
Cdd:COG3025   82 qrPEWeVPLPSPEPDLSLL-----PDEPLPELLDAAALGAALQPVFTTDFERTTWLLTL----ADGSLIEVALD------ 146


                 ....*..
gi 564386161 154 aVGEVEA 160
Cdd:COG3025  147 -QGEIRA 152
 
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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