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Conserved domains on  [gi|76802186|ref|YP_327194|]
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adenylate cyclase [Natronomonas pharaonis DSM 2160]

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List of domain hits

Name Accession Description Interval E-value
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
3-172 3.03e-47

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: 153.96  E-value: 3.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   3 EVELKVQ-TDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRERQDGdaEARVTYKGPLVEAASKTRR 81
Cdd:cd07890   1 EVEIKARvDDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSG--KTLLTYKGPKLDGGPKVRE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  82 ELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEAGEIEPAREGAVAVLTALGLDA 161
Cdd:cd07890  79 EIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLGLLE 158
                       170
                ....*....|.
gi 76802186 162 DEQVRTSYLGL 172
Cdd:cd07890 159 YDEETLSYLEL 169
 
Name Accession Description Interval E-value
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
3-172 3.03e-47

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: 153.96  E-value: 3.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   3 EVELKVQ-TDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRERQDGdaEARVTYKGPLVEAASKTRR 81
Cdd:cd07890   1 EVEIKARvDDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSG--KTLLTYKGPKLDGGPKVRE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  82 ELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEAGEIEPAREGAVAVLTALGLDA 161
Cdd:cd07890  79 EIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLGLLE 158
                       170
                ....*....|.
gi 76802186 162 DEQVRTSYLGL 172
Cdd:cd07890 159 YDEETLSYLEL 169
CyaB COG1437
Adenylate cyclase, class 2 (thermophilic) [Nucleotide transport and metabolism]
1-176 1.66e-48

Adenylate cyclase, class 2 (thermophilic) [Nucleotide transport and metabolism]


Pssm-ID: 224354  Cd Length: 178  Bit Score: 157.50  E-value: 1.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   1 MYEVELKVQ-TDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRERqdgDAEARVTYKGPLVEAASKT 79
Cdd:COG1437   1 MYEVEVKFRvRDLEEIRERLASLGAKFIKEEEQEDIYFDHPCRDFADTDEALRIRRIN---GGEVFLTYKGPKLDRESKT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  80 RRELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEA---GEIEPAREGAVAVLTA 156
Cdd:COG1437  78 REEIEIEVSDVEKALEILKRLGFKEVAVVKKTREIYKVGNVTIELDAVEGLGDFLEIEVMVddeNEIDGAKEEIEEIARQ 157
                       170       180
                ....*....|....*....|
gi 76802186 157 LGLDADEQVRTSYLGLLLDE 176
Cdd:COG1437 158 LGLKEEDLERRSYLELLLEK 177
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
1-174 2.34e-29

adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second adenylyl cyclase from that species, as demonstrated by complementation in E. coli and by assay of the enzymatic properties of purified recombinant protein. It has no detectable homology to any other protein of known function, and has several unusual properties, including an optimal temperature of 65 degrees and an optimal pH of 9.5. A cluster of uncharaterized archaeal homologs may be orthologous and serve (under certain circumstances) to produce the regulatory metabolite cyclic AMP (cAMP) [Regulatory functions, Small molecule interactions].


Pssm-ID: 232916  Cd Length: 174  Bit Score: 107.59  E-value: 2.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186     1 MYEVELKVQT-DHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRErqdgDAEARVTYKGPLVEAASKT 79
Cdd:TIGR00318   1 MIEVEVKAKIpDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIRKL----TGEKFVTYKGPKIDNESKT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186    80 RRELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEA---GEIEPAREGAVAVLTA 156
Cdd:TIGR00318  77 RKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNELNVSIDDVEGLGFFLEIEKIInniNDKDLALEEIFEIINQ 156
                         170
                  ....*....|....*...
gi 76802186   157 LGLDaDEQVRTSYLGLLL 174
Cdd:TIGR00318 157 LGIK-DNIERRSYLELLS 173
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
1-175 2.53e-24

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyses 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: 250975  Cd Length: 177  Bit Score: 94.52  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186     1 MYEVELK--VQTDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRErqdGDAEARVTYKGPLVeAASK 78
Cdd:pfam01928   1 MIEIERKflVSDEEYKDLLLLEKLRGKAEGPEEQRDTYFDTPDRDLARTDEALRIRRF---GNGAYFLTLKGPGV-DGPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186    79 TRRELETAVE-DGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGL-GEFVEVETEAGEIEPAREGA--VAVL 154
Cdd:pfam01928  77 SREEVNGELSrDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLgGAEVELELEVEDEEELLEAAeeLELL 156
                         170       180
                  ....*....|....*....|.
gi 76802186   155 TALGLDADEQVRTSYLGLLLD 175
Cdd:pfam01928 157 RILGLSEESKIARFYLELLAL 177
 
Name Accession Description Interval E-value
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
3-172 3.03e-47

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: 153.96  E-value: 3.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   3 EVELKVQ-TDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRERQDGdaEARVTYKGPLVEAASKTRR 81
Cdd:cd07890   1 EVEIKARvDDLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSG--KTLLTYKGPKLDGGPKVRE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  82 ELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEAGEIEPAREGAVAVLTALGLDA 161
Cdd:cd07890  79 EIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLGLLE 158
                       170
                ....*....|.
gi 76802186 162 DEQVRTSYLGL 172
Cdd:cd07890 159 YDEETLSYLEL 169
CyaB COG1437
Adenylate cyclase, class 2 (thermophilic) [Nucleotide transport and metabolism]
1-176 1.66e-48

Adenylate cyclase, class 2 (thermophilic) [Nucleotide transport and metabolism]


Pssm-ID: 224354  Cd Length: 178  Bit Score: 157.50  E-value: 1.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   1 MYEVELKVQ-TDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRERqdgDAEARVTYKGPLVEAASKT 79
Cdd:COG1437   1 MYEVEVKFRvRDLEEIRERLASLGAKFIKEEEQEDIYFDHPCRDFADTDEALRIRRIN---GGEVFLTYKGPKLDRESKT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  80 RRELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEA---GEIEPAREGAVAVLTA 156
Cdd:COG1437  78 REEIEIEVSDVEKALEILKRLGFKEVAVVKKTREIYKVGNVTIELDAVEGLGDFLEIEVMVddeNEIDGAKEEIEEIARQ 157
                       170       180
                ....*....|....*....|
gi 76802186 157 LGLDADEQVRTSYLGLLLDE 176
Cdd:COG1437 158 LGLKEEDLERRSYLELLLEK 177
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
1-174 2.34e-29

adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second adenylyl cyclase from that species, as demonstrated by complementation in E. coli and by assay of the enzymatic properties of purified recombinant protein. It has no detectable homology to any other protein of known function, and has several unusual properties, including an optimal temperature of 65 degrees and an optimal pH of 9.5. A cluster of uncharaterized archaeal homologs may be orthologous and serve (under certain circumstances) to produce the regulatory metabolite cyclic AMP (cAMP) [Regulatory functions, Small molecule interactions].


Pssm-ID: 232916  Cd Length: 174  Bit Score: 107.59  E-value: 2.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186     1 MYEVELKVQT-DHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRErqdgDAEARVTYKGPLVEAASKT 79
Cdd:TIGR00318   1 MIEVEVKAKIpDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIRKL----TGEKFVTYKGPKIDNESKT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186    80 RRELETAVEDGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGLGEFVEVETEA---GEIEPAREGAVAVLTA 156
Cdd:TIGR00318  77 RKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNELNVSIDDVEGLGFFLEIEKIInniNDKDLALEEIFEIINQ 156
                         170
                  ....*....|....*...
gi 76802186   157 LGLDaDEQVRTSYLGLLL 174
Cdd:TIGR00318 157 LGIK-DNIERRSYLELLS 173
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
1-175 2.53e-24

CYTH domain; These sequences are functionally identified as members of the adenylate cyclase family, which catalyses 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: 250975  Cd Length: 177  Bit Score: 94.52  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186     1 MYEVELK--VQTDHEPVRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRErqdGDAEARVTYKGPLVeAASK 78
Cdd:pfam01928   1 MIEIERKflVSDEEYKDLLLLEKLRGKAEGPEEQRDTYFDTPDRDLARTDEALRIRRF---GNGAYFLTLKGPGV-DGPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186    79 TRRELETAVE-DGETMAGVLEAVGFEPAATVEKTRERFEYDGYTVTLDSVTGL-GEFVEVETEAGEIEPAREGA--VAVL 154
Cdd:pfam01928  77 SREEVNGELSrDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLgGAEVELELEVEDEEELLEAAeeLELL 156
                         170       180
                  ....*....|....*....|.
gi 76802186   155 TALGLDADEQVRTSYLGLLLD 175
Cdd:pfam01928 157 RILGLSEESKIARFYLELLAL 177
CYTH-like_Pase cd07374
CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) Phosphatases; CYTH-like ...
3-142 1.08e-04

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: 39.74  E-value: 1.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186   3 EVELKVQTDHEPVRSRLSELEA----EPLGAVTQVDTYYDHPvrEFGETDEALRIRRerQDGDAEARVTYKGPlveAASK 78
Cdd:cd07374   1 EVERKFRVPDDAVLPLLLGVPGvlgvGEPETVQLRAIYFDTP--DLRLARAGLRLRR--RTGGADAGWHLKLP---GGIS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76802186  79 TRRELETAVEDGETMAGVLEAV----------GFEPAATVEKTRERFEYDGY-----TVTLDSVTG-------LGEFVEV 136
Cdd:cd07374  74 RRTEVRAPLGDAAAVAPLLLAAalvlavtrglPLRPVATIETTRTVYRLLDAggvlaELDLDTVTArvldgggTQYWREV 153

                ....*.
gi 76802186 137 ETEAGE 142
Cdd:cd07374 154 EVELPD 159
CYTH-like_Pase_CHAD cd07756
Uncharacterized subgroup of the CYTH-like superfamily having an associated CHAD domain; This ...
3-56 8.03e-03

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  Cd Length: 197  Bit Score: 34.52  E-value: 8.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76802186   3 EVELKVQTDHEP-----VRSRLSELEAEPLGAVTQVDTYYDHPVREFGETDEALRIRRE 56
Cdd:cd07756   1 EIELKLLLPPEDlealaAHPLLAALAAGRAQTRRLHNTYFDTPDLALRRAGIALRVRRE 59
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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