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Conserved domains on  [gi|195639840|gb|ACG39388|]
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adenylate cyclase [Zea mays]

Protein Classification

CYTH domain-containing protein; polyphosphate polymerase domain-containing protein( domain architecture ID 10164209)

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
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-188 7.08e-25

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: 95.98  E-value: 7.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   2 EVEIKLRLPDAAAHRRLSA---FLAPRLRRTHAQRNLFFDDAARTLgaATAALRVRLYDGPDDrapsrAVLALKRrariE 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGvpgVLGVGEPETVQLRAIYFDTPDLRL--ARAGLRLRRRTGGAD-----AGWHLKL----P 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840  79 AGVSRVEEIEEPLEPALAVACTDDPARLggldspiirlvaaeYGVGGDAAPFLCLGGFGNTRAVYEYEledGGGGVVLEL 158
Cdd:cd07374   70 GGISRRTEVRAPLGDAAAVAPLLLAAAL--------------VLAVTRGLPLRPVATIETTRTVYRLL---DAGGVLAEL 132

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 195639840 159 DETRFDF------GTRYELECETAEPDRVKAVLERL 188
Cdd:cd07374  133 DLDTVTArvldggGTQYWREVEVELPDGDEALLDAL 168
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-188 7.08e-25

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: 95.98  E-value: 7.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   2 EVEIKLRLPDAAAHRRLSA---FLAPRLRRTHAQRNLFFDDAARTLgaATAALRVRLYDGPDDrapsrAVLALKRrariE 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGvpgVLGVGEPETVQLRAIYFDTPDLRL--ARAGLRLRRRTGGAD-----AGWHLKL----P 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840  79 AGVSRVEEIEEPLEPALAVACTDDPARLggldspiirlvaaeYGVGGDAAPFLCLGGFGNTRAVYEYEledGGGGVVLEL 158
Cdd:cd07374   70 GGISRRTEVRAPLGDAAAVAPLLLAAAL--------------VLAVTRGLPLRPVATIETTRTVYRLL---DAGGVLAEL 132

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 195639840 159 DETRFDF------GTRYELECETAEPDRVKAVLERL 188
Cdd:cd07374  133 DLDTVTArvldggGTQYWREVEVELPDGDEALLDAL 168
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-188 4.97e-12

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: 61.79  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840    1 MEVEIKLRLPDAAAHRRLSA----FLAPRLRRthaQRNLFFDDAARTLGAATAALRVRL---------YDGPDDRAPSra 67
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLLeklrGKAEGPEE---QRDIYFDTPDRDLARTDEALRIRRfgngayfltLKGPGVDGPF-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   68 vlalKRRARIEAGVSRVEEIEEPLepalavactddparLGGLDspiirlvaaeygvggdaapFLCLGGFGNTRAVYEYel 147
Cdd:pfam01928  77 ----KSREEVNGEVSRDEPDAVEL--------------LDGLG-------------------LQPVGSIKKERRRYKV-- 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 195639840  148 edggGGVVLELDETRFDFGTRYELECETAEPDRVKAVLERL 188
Cdd:pfam01928 118 ----KGVLIALDVVEFLGGAEVELELEVEDEEELLEAAEEL 154
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-115 2.10e-07

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 49.89  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   1 MEVEIKLRLPDAAAHRRLSAFLAPRLRRTHAQR----NLFFDDAARTLGAATAALRVRLYDGpddrapsRAVLALKRRAR 76
Cdd:COG3025    3 REIELKLLVDPEALPALRQHPLLAGLAVGEPATrrleNTYFDTPDLDLRRAGIGLRVRREGG-------RWEQTLKTAGQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 195639840  77 IEAGVSRVEEIEEPL-EPALAVACTDDPARLGGLDSPIIR 115
Cdd:COG3025   76 VVGGLHQRPEWEVPLpSPEPDLSLLPDEPLPELLDAAALG 115
 
Name Accession Description Interval E-value
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
 2-188 7.08e-25

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: 95.98  E-value: 7.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   2 EVEIKLRLPDAAAHRRLSA---FLAPRLRRTHAQRNLFFDDAARTLgaATAALRVRLYDGPDDrapsrAVLALKRrariE 78
Cdd:cd07374    1 EVERKFRVPDDAVLPLLLGvpgVLGVGEPETVQLRAIYFDTPDLRL--ARAGLRLRRRTGGAD-----AGWHLKL----P 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840  79 AGVSRVEEIEEPLEPALAVACTDDPARLggldspiirlvaaeYGVGGDAAPFLCLGGFGNTRAVYEYEledGGGGVVLEL 158
Cdd:cd07374   70 GGISRRTEVRAPLGDAAAVAPLLLAAAL--------------VLAVTRGLPLRPVATIETTRTVYRLL---DAGGVLAEL 132

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 195639840 159 DETRFDF------GTRYELECETAEPDRVKAVLERL 188
Cdd:cd07374  133 DLDTVTArvldggGTQYWREVEVELPDGDEALLDAL 168
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-188 4.97e-12

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: 61.79  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840    1 MEVEIKLRLPDAAAHRRLSA----FLAPRLRRthaQRNLFFDDAARTLGAATAALRVRL---------YDGPDDRAPSra 67
Cdd:pfam01928   2 IEIERKFLVSDEEYKDLLLLeklrGKAEGPEE---QRDIYFDTPDRDLARTDEALRIRRfgngayfltLKGPGVDGPF-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   68 vlalKRRARIEAGVSRVEEIEEPLepalavactddparLGGLDspiirlvaaeygvggdaapFLCLGGFGNTRAVYEYel 147
Cdd:pfam01928  77 ----KSREEVNGEVSRDEPDAVEL--------------LDGLG-------------------LQPVGSIKKERRRYKV-- 117

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 195639840  148 edggGGVVLELDETRFDFGTRYELECETAEPDRVKAVLERL 188
Cdd:pfam01928 118 ----KGVLIALDVVEFLGGAEVELELEVEDEEELLEAAEEL 154
CYTH-like_Pase_1 cd07762
Uncharacterized subgroup 1 of the CYTH-like superfamily; Enzymes belonging to the CYTH-like ...
 2-208 1.70e-09

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: 54.89  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   2 EVEIKLRLpDAAAHRRL-SAFlapRLRRTHAQRNLFFDDAARTLGAATAALRVRLYDGpddrapsRAVLALKRRARIEag 80
Cdd:cd07762    2 EIEFKNLL-TKEEYEQLkNAF---DLKDFFKQTNYYFDTPDFALKKKHSALRIREKEG-------KAELTLKVPQEVG-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840  81 vsrVEEIEEPLEPALAVACTDDparlGGLDSPIIRLVAAEYGVggDAAPFLCLGGFGNTRavYEYELEDGgggvVLELDE 160
Cdd:cd07762   69 ---LLETNQPLTLEEAEKLIKG----GTLPEGEILDKLKELGI--DPSELKLFGSLTTIR--AEIPYEGG----LLVLDH 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 195639840 161 TRFDFGTRYELECETAEPDRVKAVLERLLTVAGVPYEYCRsSKFACFM 208
Cdd:cd07762  134 SLYLGITDYELEYEVDDYEAGKKAFLELLKQYNIPYRPAK-NKIARFL 180
PPPi COG3025
Inorganic triphosphatase YgiF, contains CYTH and CHAD domains [Inorganic ion transport and ...
 1-115 2.10e-07

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


Pssm-ID: 442261 [Multi-domain]  Cd Length: 261  Bit Score: 49.89  E-value: 2.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   1 MEVEIKLRLPDAAAHRRLSAFLAPRLRRTHAQR----NLFFDDAARTLGAATAALRVRLYDGpddrapsRAVLALKRRAR 76
Cdd:COG3025    3 REIELKLLVDPEALPALRQHPLLAGLAVGEPATrrleNTYFDTPDLDLRRAGIGLRVRREGG-------RWEQTLKTAGQ 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 195639840  77 IEAGVSRVEEIEEPL-EPALAVACTDDPARLGGLDSPIIR 115
Cdd:COG3025   76 VVGGLHQRPEWEVPLpSPEPDLSLLPDEPLPELLDAAALG 115
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
 2-92 7.18e-07

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: 48.00  E-value: 7.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   2 EVEIKLRLPDA-----AAHRRLSAFLAPRLRRTHaQRNLFFDDAARTLGAATAALRVRlydgpddRAPSRAVLALKRRAR 76
Cdd:cd07756    1 EIELKLLLPPEdlealAAHPLLAALAAGRAQTRR-LHNTYFDTPDLALRRAGIALRVR-------REGGQWVQTLKTAGS 72

                         90
                 ....*....|....*.
gi 195639840  77 IEAGVSRVEEIEEPLE 92
Cdd:cd07756   73 VVGGLHQRPEWEVPLP 88
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 1-92 9.93e-06

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: 44.09  E-value: 9.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195639840   1 MEVEIKLRLPD-AAAHRRLSAFLAPRLRRTHaQRNLFFDDAARTLGAATAALRVRLYDGpddrapsRAVLALKRRaRIEA 79
Cdd:COG1437    1 IEVEVKVRVIDlEEVRERLEELGAELVGEEH-QIDIYYDAPDRDFAETDEALRIRRGGG-------RATLTYKGP-KLDE 71

                         90
                 ....*....|...
gi 195639840  80 GVSRVEEIEEPLE 92
Cdd:COG1437   72 GSKTREEIETEVD 84
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 2-61 1.87e-05

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: 43.41  E-value: 1.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195639840   2 EVEIKLRLPDAAAHR-RLSAFLAPRLRRTHaQRNLFFDDAARTLGAATAALRVRL----------YDGPDD 61
Cdd:cd07890    1 EVEIKARVDDLEALReRLAALGGAEGGREF-QEDIYFDHPDRDLAATDEALRLRRmgdsgktlltYKGPKL 70
 
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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