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Conserved domains on  [gi|702484451|ref|XP_010033982|]
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triphosphate tunnel metalloenzyme 3 isoform X1 [Eucalyptus grandis]

Protein Classification

CYTH-like_Pase domain-containing protein( domain architecture ID 10164209)

CYTH-like_Pase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 56-231 5.34e-28

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: 105.23  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLPDSTAHQQLSDA---LSPFHVKTLAQENVFFDGEGSELVKnlAALRLRFYDLDSHCVLSLKAKPvissGISR 132
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTPDLRLAR--AGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 133 VEEQEESVDPSVGRACVDDPGRLllfgssdiikrVREEYNVKGLVCLGGFRNVRAVYDW---KGLKLELDETVYDF---- 205
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAAL-----------VLAVTRGLPLRPVATIETTRTVYRLldaGGVLAELDLDTVTArvld 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 702484451 206 --GTSYEIECESAEPERD---KILIERFLEE 231
Cdd:cd07374  144 ggGTQYWREVEVELPDGDealLDALERRLTA 174
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 56-231 5.34e-28

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: 105.23  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLPDSTAHQQLSDA---LSPFHVKTLAQENVFFDGEGSELVKnlAALRLRFYDLDSHCVLSLKAKPvissGISR 132
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTPDLRLAR--AGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 133 VEEQEESVDPSVGRACVDDPGRLllfgssdiikrVREEYNVKGLVCLGGFRNVRAVYDW---KGLKLELDETVYDF---- 205
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAAL-----------VLAVTRGLPLRPVATIETTRTVYRLldaGGVLAELDLDTVTArvld 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 702484451 206 --GTSYEIECESAEPERD---KILIERFLEE 231
Cdd:cd07374  144 ggGTQYWREVEVELPDGDealLDALERRLTA 174
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 55-237 7.96e-17

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: 75.65  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451   55 MEVEIKLRLPDSTAHQQLS-DALSPFHVKTLAQENVFFDGEGSELVKNLAALRLRFYDlDSHCVLSLK-AKPVISSGISR 132
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLlEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFG-NGAYFLTLKgPGVDGPFKSRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  133 VEEQEESVDPsvgRACVDDPGRLllfgssdiikrvreeynvkGLVCLGGFRNVRAVYDWKGLKLELDETVYDFGTSYEIE 212
Cdd:pfam01928  81 EVNGEVSRDE---PDAVELLDGL-------------------GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELE 138

                         170       180
                  ....*....|....*....|....*
gi 702484451  213 CESAEPERDKILIERFLEENGIMYS 237
Cdd:pfam01928 139 LEVEDEEELLEAAEELELLRILGLS 163
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 55-234 1.55e-07

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: 49.87  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  55 MEVEIKLRLPD-STAHQQLsDALSPFHVKTLAQENVFFDGEGSELVKNLAALRLRfyDLDSHCVLSLKAKPVISSGISRV 133
Cdd:COG1437    1 IEVEVKVRVIDlEEVRERL-EELGAELVGEEHQIDIYYDAPDRDFAETDEALRIR--RGGGRATLTYKGPKLDEGSKTRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 134 EEQEEsvdpsvgracVDDPGRLllfgsSDIIKRVreeynvkGLVCLGGFRNVRAVYDWKGLKLELDEtVYDFGTSYEIEC 213
Cdd:COG1437   78 EIETE----------VDDGEAM-----EAILEAL-------GFRPVATVEKTREIYKLGGVTVTLDE-VEGLGPFVEIEG 134

                        170       180
                 ....*....|....*....|..
gi 702484451 214 ES-AEPERDKILIERFLEENGI 234
Cdd:COG1437  135 EAeDEVEAAREAIEEVLAELGL 156
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 56-231 5.34e-28

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: 105.23  E-value: 5.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLPDSTAHQQLSDA---LSPFHVKTLAQENVFFDGEGSELVKnlAALRLRFYDLDSHCVLSLKAKPvissGISR 132
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGVpgvLGVGEPETVQLRAIYFDTPDLRLAR--AGLRLRRRTGGADAGWHLKLPG----GISR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 133 VEEQEESVDPSVGRACVDDPGRLllfgssdiikrVREEYNVKGLVCLGGFRNVRAVYDW---KGLKLELDETVYDF---- 205
Cdd:cd07374   75 RTEVRAPLGDAAAVAPLLLAAAL-----------VLAVTRGLPLRPVATIETTRTVYRLldaGGVLAELDLDTVTArvld 143

                        170       180       190
                 ....*....|....*....|....*....|.
gi 702484451 206 --GTSYEIECESAEPERD---KILIERFLEE 231
Cdd:cd07374  144 ggGTQYWREVEVELPDGDealLDALERRLTA 174
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 55-237 7.96e-17

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: 75.65  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451   55 MEVEIKLRLPDSTAHQQLS-DALSPFHVKTLAQENVFFDGEGSELVKNLAALRLRFYDlDSHCVLSLK-AKPVISSGISR 132
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLlEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFG-NGAYFLTLKgPGVDGPFKSRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  133 VEEQEESVDPsvgRACVDDPGRLllfgssdiikrvreeynvkGLVCLGGFRNVRAVYDWKGLKLELDETVYDFGTSYEIE 212
Cdd:pfam01928  81 EVNGEVSRDE---PDAVELLDGL-------------------GLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELE 138

                         170       180
                  ....*....|....*....|....*
gi 702484451  213 CESAEPERDKILIERFLEENGIMYS 237
Cdd:pfam01928 139 LEVEDEEELLEAAEELELLRILGLS 163
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 56-247 2.39e-10

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: 57.98  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLpDSTAHQQLSDALspFHVKTLAQENVFFDGEGSELVKNLAALRLRFYDlDSHcVLSLKAKpvISSGisrVEE 135
Cdd:cd07762    2 EIEFKNLL-TKEEYEQLKNAF--DLKDFFKQTNYYFDTPDFALKKKHSALRIREKE-GKA-ELTLKVP--QEVG---LLE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 136 QEESVDPsvgracvdDPGRLLLFGSSDIIKRVREEYNVKG-----LVCLGGFRNVRAVYDWKGLKLELDETVYdFGTS-Y 209
Cdd:cd07762   72 TNQPLTL--------EEAEKLIKGGTLPEGEILDKLKELGidpseLKLFGSLTTIRAEIPYEGGLLVLDHSLY-LGITdY 142

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 702484451 210 EIECESAEPERDKILIERFLEENGIMYSySNVNKFAVF 247
Cdd:cd07762  143 ELEYEVDDYEAGKKAFLELLKQYNIPYR-PAKNKIARF 179
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 56-235 2.85e-09

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: 54.58  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLPDSTAHQQLSDALSPFHVKTLAQENVFFDGEGSELVKNLAALRLRFYDLDSHCVLSLKAKPVisSGISRVEE 135
Cdd:cd07890    1 EVEIKARVDDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTYKGPKL--DGGPKVRE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 136 QEESvdpsvgraCVDDPGRL------LLFGSSDIIKRVREEYNvkglvcLGGFRnvravydwkglkLELDEtVYDFGTSY 209
Cdd:cd07890   79 EIET--------EVADPEAMkeilerLGFGPVGRVKKEREIYL------LGQTR------------VHLDR-VEGLGDFV 131

                        170       180
                 ....*....|....*....|....*.
gi 702484451 210 EIECESAEPERDKILIERFLEENGIM 235
Cdd:cd07890  132 EIEVVLEDIEEAEEGLGEAAELLGLL 157
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 55-234 1.55e-07

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: 49.87  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  55 MEVEIKLRLPD-STAHQQLsDALSPFHVKTLAQENVFFDGEGSELVKNLAALRLRfyDLDSHCVLSLKAKPVISSGISRV 133
Cdd:COG1437    1 IEVEVKVRVIDlEEVRERL-EELGAELVGEEHQIDIYYDAPDRDFAETDEALRIR--RGGGRATLTYKGPKLDEGSKTRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451 134 EEQEEsvdpsvgracVDDPGRLllfgsSDIIKRVreeynvkGLVCLGGFRNVRAVYDWKGLKLELDEtVYDFGTSYEIEC 213
Cdd:COG1437   78 EIETE----------VDDGEAM-----EAILEAL-------GFRPVATVEKTREIYKLGGVTVTLDE-VEGLGPFVEIEG 134

                        170       180
                 ....*....|....*....|..
gi 702484451 214 ES-AEPERDKILIERFLEENGI 234
Cdd:COG1437  135 EAeDEVEAAREAIEEVLAELGL 156
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 56-141 5.33e-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: 45.69  E-value: 5.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  56 EVEIKLRLPDSTAHQQLSDAL------SPFHVKTLaqENVFFDGEGSELVKNLAALRLRfyDLDSHCVLSLKAKPVISSG 129
Cdd:cd07756    1 EIELKLLLPPEDLEALAAHPLlaalaaGRAQTRRL--HNTYFDTPDLALRRAGIALRVR--REGGQWVQTLKTAGSVVGG 76

                         90
                 ....*....|..
gi 702484451 130 ISRVEEQEESVD 141
Cdd:cd07756   77 LHQRPEWEVPLP 88
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 53-141 2.61e-03

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 38.34  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 702484451  53 APMEVEIKLRLPDSTA-----HQQLSD-ALSPFHVKTLaqENVFFDGEGSELVKNLAALRLRFYdlDSHCVLSLKAKPVI 126
Cdd:COG3025    1 MAREIELKLLVDPEALpalrqHPLLAGlAVGEPATRRL--ENTYFDTPDLDLRRAGIGLRVRRE--GGRWEQTLKTAGQV 76

                         90
                 ....*....|....*
gi 702484451 127 SSGISRVEEQEESVD 141
Cdd:COG3025   77 VGGLHQRPEWEVPLP 91
 
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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