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Conserved domains on  [gi|496535306|ref|WP_009241997|]
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MULTISPECIES: CYTH domain-containing protein [Ralstonia]

Protein Classification

CYTH domain-containing protein( domain architecture ID 10166798)

CYTH domain-containing protein such as inorganic triphosphatase, which catalyzes the hydrolysis of inorganic or nucleoside-linked triphosphate-containing substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-210 2.80e-60

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: 187.44  E-value: 2.80e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAG-----AHDALVGWLdaNAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVSTSGLS 78
Cdd:cd07756    1 EIELKLLLPPEdlealAAHPLLAAL--AAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  79 ARHEWEVPLQNDALSVDA---FVANNAAEAADyvrpHAAALAPLFRTDFTRRLWHVGAEGGEIEIALDAGAILIPGtqAR 155
Cdd:cd07756   79 QRPEWEVPLPGPAPDLDLasiLPDGELLEALA----ALAALVPLFTTDFERTVWLLRLGGSEIEVALDQGEIRAGD--RS 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496535306 156 EPIDELELEWKPADDSTLgeDAIAERLHAWTqtlraavpGLTPLDISKAQRGYQL 210
Cdd:cd07756  153 EPICEIELELKSGDPAAL--FALARRLAERL--------PLRLSNRSKAERGYRL 197
 
Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-210 2.80e-60

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: 187.44  E-value: 2.80e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAG-----AHDALVGWLdaNAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVSTSGLS 78
Cdd:cd07756    1 EIELKLLLPPEdlealAAHPLLAAL--AAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  79 ARHEWEVPLQNDALSVDA---FVANNAAEAADyvrpHAAALAPLFRTDFTRRLWHVGAEGGEIEIALDAGAILIPGtqAR 155
Cdd:cd07756   79 QRPEWEVPLPGPAPDLDLasiLPDGELLEALA----ALAALVPLFTTDFERTVWLLRLGGSEIEVALDQGEIRAGD--RS 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496535306 156 EPIDELELEWKPADDSTLgeDAIAERLHAWTqtlraavpGLTPLDISKAQRGYQL 210
Cdd:cd07756  153 EPICEIELELKSGDPAAL--FALARRLAERL--------PLRLSNRSKAERGYRL 197
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-214 1.21e-55

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 177.78  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   1 MAREIELKLAVSAGAHDALVGWL---DANAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVSTSGL 77
Cdd:COG3025    1 MAREIELKLLVDPEALPALRQHPllaGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  78 SARHEWEVPLQNDALSVDAFVANNAAEAADyVRPHAAALAPLFRTDFTRRLWHVGAEGG-EIEIALDAGAIlIPGTQaRE 156
Cdd:COG3025   81 HQRPEWEVPLPSPEPDLSLLPDEPLPELLD-AAALGAALQPVFTTDFERTTWLLTLADGsLIEVALDQGEI-RAGER-RE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496535306 157 PIDELELEWKPADDSTLgeDAIAERLhawtqtlrAAVPGLTPLDISKAQRGYQLREKA 214
Cdd:COG3025  158 PICELELELKSGDPAAL--FALALEL--------AEALPLRLSSLSKAERGYRLAAGA 205
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-208 6.52e-28

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: 103.77  E-value: 6.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306    2 AREIELKLAVSAGAHDALVGWLDANAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQW-LQTLKTAAVSTSGLSaR 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAyFLTLKGPGVDGPFKS-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   81 HEWEVPLQNDALSVDAFVAnnaaeaadyvrphAAALAPLFRTDFTRRLWHVgaegGEIEIALDAGAILipgtqarePIDE 160
Cdd:pfam01928  80 EEVNGEVSRDEPDAVELLD-------------GLGLQPVGSIKKERRRYKV----KGVLIALDVVEFL--------GGAE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 496535306  161 LELEWKPADDSTLgedaiaerlhAWTQTLRAAVPGLTPLDISKAQRGY 208
Cdd:pfam01928 135 VELELEVEDEEEL----------LEAAEELELLRILGLSEESKIARFY 172
 
Name Accession Description Interval E-value
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 4-210 2.80e-60

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: 187.44  E-value: 2.80e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAG-----AHDALVGWLdaNAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVSTSGLS 78
Cdd:cd07756    1 EIELKLLLPPEdlealAAHPLLAAL--AAGRAQTRRLHNTYFDTPDLALRRAGIALRVRREGGQWVQTLKTAGSVVGGLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  79 ARHEWEVPLQNDALSVDA---FVANNAAEAADyvrpHAAALAPLFRTDFTRRLWHVGAEGGEIEIALDAGAILIPGtqAR 155
Cdd:cd07756   79 QRPEWEVPLPGPAPDLDLasiLPDGELLEALA----ALAALVPLFTTDFERTVWLLRLGGSEIEVALDQGEIRAGD--RS 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496535306 156 EPIDELELEWKPADDSTLgeDAIAERLHAWTqtlraavpGLTPLDISKAQRGYQL 210
Cdd:cd07756  153 EPICEIELELKSGDPAAL--FALARRLAERL--------PLRLSNRSKAERGYRL 197
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-214 1.21e-55

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 177.78  E-value: 1.21e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   1 MAREIELKLAVSAGAHDALVGWL---DANAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVSTSGL 77
Cdd:COG3025    1 MAREIELKLLVDPEALPALRQHPllaGLAVGEPATRRLENTYFDTPDLDLRRAGIGLRVRREGGRWEQTLKTAGQVVGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  78 SARHEWEVPLQNDALSVDAFVANNAAEAADyVRPHAAALAPLFRTDFTRRLWHVGAEGG-EIEIALDAGAIlIPGTQaRE 156
Cdd:COG3025   81 HQRPEWEVPLPSPEPDLSLLPDEPLPELLD-AAALGAALQPVFTTDFERTTWLLTLADGsLIEVALDQGEI-RAGER-RE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496535306 157 PIDELELEWKPADDSTLgeDAIAERLhawtqtlrAAVPGLTPLDISKAQRGYQLREKA 214
Cdd:COG3025  158 PICELELELKSGDPAAL--FALALEL--------AEALPLRLSSLSKAERGYRLAAGA 205
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 2-208 6.52e-28

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: 103.77  E-value: 6.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306    2 AREIELKLAVSAGAHDALVGWLDANAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQW-LQTLKTAAVSTSGLSaR 80
Cdd:pfam01928   1 MIEIERKFLVSDEEYKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAyFLTLKGPGVDGPFKS-R 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   81 HEWEVPLQNDALSVDAFVAnnaaeaadyvrphAAALAPLFRTDFTRRLWHVgaegGEIEIALDAGAILipgtqarePIDE 160
Cdd:pfam01928  80 EEVNGEVSRDEPDAVELLD-------------GLGLQPVGSIKKERRRYKV----KGVLIALDVVEFL--------GGAE 134

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 496535306  161 LELEWKPADDSTLgedaiaerlhAWTQTLRAAVPGLTPLDISKAQRGY 208
Cdd:pfam01928 135 VELELEVEDEEEL----------LEAAEELELLRILGLSEESKIARFY 172
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 4-182 4.30e-12

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: 62.09  E-value: 4.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAGAHDALVGWLDANAQAA--GSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAvstsGLSARH 81
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVPGVLGVGepETVQLRAIYFDTPDLRLARAGLRLRRRTGGADAGWHLKLPG----GISRRT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  82 EWEVPLqnDALSVDAFVANNAAEAADYVRPHaaALAPLFRTDFTRRLWHVGAEGGE-IEIALDAGAILipGTQAREPIDE 160
Cdd:cd07374   77 EVRAPL--GDAAAVAPLLLAAALVLAVTRGL--PLRPVATIETTRTVYRLLDAGGVlAELDLDTVTAR--VLDGGGTQYW 150

                        170       180
                 ....*....|....*....|..
gi 496535306 161 LELEWKPADDSTLGEDAIAERL 182
Cdd:cd07374  151 REVEVELPDGDEALLDALERRL 172
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 3-183 1.00e-08

Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) 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). 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 are of bacterial origin and have not been characterized.


Pssm-ID: 143627  Cd Length: 180  Bit Score: 52.97  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   3 REIELKLAVSAGAHDALVGWLDANAqaagSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAvsTSGLsarHE 82
Cdd:cd07762    1 LEIEFKNLLTKEEYEQLKNAFDLKD----FFKQTNYYFDTPDFALKKKHSALRIREKEGKAELTLKVPQ--EVGL---LE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  83 WEVPLQ----NDALSVDAFVANnaaEAADYVRPHAAALAPL--FRTDFTRRLWHVGAEGgeiEIALDAGaiLIPGTQare 156
Cdd:cd07762   72 TNQPLTleeaEKLIKGGTLPEG---EILDKLKELGIDPSELklFGSLTTIRAEIPYEGG---LLVLDHS--LYLGIT--- 140

                        170       180
                 ....*....|....*....|....*...
gi 496535306 157 piD-ELELEwkpADDSTLGEDAIAERLH 183
Cdd:cd07762  141 --DyELEYE---VDDYEAGKKAFLELLK 163
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 3-143 4.36e-08

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: 51.03  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   3 REIELKLAVsaGAHDALVGWL-DANAQAAGSVELANVYYDTRDQALARNRAALRVRRQGSQWLQTLKTAAVStSGLSARH 81
Cdd:COG1437    1 IEVEVKVRV--IDLEEVRERLeELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGGRATLTYKGPKLD-EGSKTRE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496535306  82 EWEVPLqNDALSVDAFVannaaEAADYVrphaaalaPLFRTDFTRRLWHVgaegGEIEIALD 143
Cdd:COG1437   78 EIETEV-DDGEAMEAIL-----EALGFR--------PVATVEKTREIYKL----GGVTVTLD 121
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 4-89 3.72e-04

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: 39.56  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAgaHDALVGWLDANAQAAGSVEL-ANVYYDTRDQALARNRAALRVRRQG--SQWLQTLKTAAVStSGLSAR 80
Cdd:cd07890    1 EVEIKARVDD--LEALRERLAALGGAEGGREFqEDIYFDHPDRDLAATDEALRLRRMGdsGKTLLTYKGPKLD-GGPKVR 77


                 ....*....
gi 496535306  81 HEWEVPLQN 89
Cdd:cd07890   78 EEIETEVAD 86
ThTPase cd07758
Thiamine Triphosphatase; ThTPase is a soluble cytosolic enzyme which converts thiamine ...
 4-161 7.89e-03

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: 36.20  E-value: 7.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306   4 EIELKLAVSAGAHDALVGwLDANAQAAGSVELANVYYDTRDQALARNRAALRvRRQGsQW-LQTLKTAAVSTSGLSARHE 82
Cdd:cd07758    2 EVERKFRCGPSAEERLRK-LGALLELLGRRTFHDTYYDTPDNTLSLNDVWLR-QRNG-QWeLKIPPGGDPPTAGANTRYE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496535306  83 wEVplqNDALSVDAFVANNAAEAADYVRPHAAALAPL-------FRTdfTRRLWHV-------------GAEGGEIEIAL 142
Cdd:cd07758   79 -EL---TGEAAIAAALRKLLGGALPSAGGLGDELANLglrefasFVT--KRESWKLdgafrvdldrtdfGYSVGEVELLV 152

                        170
                 ....*....|....*....
gi 496535306 143 DAGAILIPGTQAREPIDEL 161
Cdd:cd07758  153 EEEDNEAEVPAALAKIDEL 171
 
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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