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Conserved domains on  [gi|32565413|ref|NP_494811|]
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CYTH domain-containing protein [Caenorhabditis elegans]

Protein Classification

class IV adenylate cyclase( domain architecture ID 10167700)

class IV adenylate cyclase catalyzes the conversion of ATP to 3',5'-cyclic AMP (cAMP) and pyrophosphate (PPi)

Graphical summary

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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 ...
4-168 5.28e-43

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: 140.87  E-value: 5.28e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413   4 NVEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESP-------NGRLKMRSVEENGvahTELIWYDRSDVAG-PKLS 75
Cdd:cd07890   1 EVEIKARVDDLEALRERLAALGGAEGGREFQEDIYFDHPdrdlaatDEALRLRRMGDSG---KTLLTYKGPKLDGgPKVR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413  76 NFNKFDVPSevLDALKLSLQSSM-GVKGEVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVCLSPEETPEHGEKIAHEIRE 154
Cdd:cd07890  78 EEIETEVAD--PEAMKEILERLGfGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLG 155
                       170
                ....*....|....
gi 32565413 155 LLAVPETDLLTGAY 168
Cdd:cd07890 156 LLEYDEETLSYLEL 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 ...
4-168 5.28e-43

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: 140.87  E-value: 5.28e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413   4 NVEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESP-------NGRLKMRSVEENGvahTELIWYDRSDVAG-PKLS 75
Cdd:cd07890   1 EVEIKARVDDLEALRERLAALGGAEGGREFQEDIYFDHPdrdlaatDEALRLRRMGDSG---KTLLTYKGPKLDGgPKVR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413  76 NFNKFDVPSevLDALKLSLQSSM-GVKGEVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVCLSPEETPEHGEKIAHEIRE 154
Cdd:cd07890  78 EEIETEVAD--PEAMKEILERLGfGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLG 155
                       170
                ....*....|....
gi 32565413 155 LLAVPETDLLTGAY 168
Cdd:cd07890 156 LLEYDEETLSYLEL 169
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
3-168 1.90e-21

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: 85.67  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413     3 RNVEIKAKVQNLD-ETVRRAVEISGKQPTILKQHDIFYESPN-------GRLKMRSVEENGvahtELIWYDRSDVAGPKL 74
Cdd:pfam01928   2 IEIERKFLVSDEEyKDLLLLEKLRGKAEGPEEQRDIYFDTPDrdlartdEALRIRRFGNGA----YFLTLKGPGVDGPFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413    75 SNFNKFDVPSE-VLDALKLSLQSSMGVKGEVKKTRTLVLHGQTRIHIDRVDGL-GDFMELEVCLSPEETPEHGEKIaHEI 152
Cdd:pfam01928  78 SREEVNGEVSRdEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLgGAEVELELEVEDEEELLEAAEE-LEL 156
                         170
                  ....*....|....*.
gi 32565413   153 RELLAVPETDLLTGAY 168
Cdd:pfam01928 157 LRILGLSEESKIARFY 172
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
5-172 1.37e-10

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: 56.81  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413   5 VEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESPNGRLKMRS----VEENGvAHTELIWydrsdvAGPKLSNFNK- 79
Cdd:COG1437   3 VEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDealrIRRGG-GRATLTY------KGPKLDEGSKt 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413  80 ----------FDVPSEVLDALKLSlqssmgVKGEVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVcLSPEETPEHGEKIA 149
Cdd:COG1437  76 reeietevddGEAMEAILEALGFR------PVATVEKTREIYKLGGVTVTLDEVEGLGPFVEIEG-EAEDEVEAAREAIE 148
                       170       180
                ....*....|....*....|...
gi 32565413 150 hEIRELLAVPETDLLTGAYMDML 172
Cdd:COG1437 149 -EVLAELGLDPDDIIRKSYLELL 170
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
5-137 6.54e-03

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: 273010  Cd Length: 174  Bit Score: 35.55  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413     5 VEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESPNgrlkmrsveeNGVAHTELIWYDRSDVA-------GPKLSNF 77
Cdd:TIGR00318   4 VEVKAKIPDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPC----------RDFASTDEALRIRKLTGekfvtykGPKIDNE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565413    78 NKF--DVPSEVLDALK-LSLQSSMGVKG--EVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVCLS 137
Cdd:TIGR00318  74 SKTrkEIEFKIEDIENaLQILKKLGFKKvyEVIKKRRIYQTNELNVSIDDVEGLGFFLEIEKIIN 138
 
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 ...
4-168 5.28e-43

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: 140.87  E-value: 5.28e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413   4 NVEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESP-------NGRLKMRSVEENGvahTELIWYDRSDVAG-PKLS 75
Cdd:cd07890   1 EVEIKARVDDLEALRERLAALGGAEGGREFQEDIYFDHPdrdlaatDEALRLRRMGDSG---KTLLTYKGPKLDGgPKVR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413  76 NFNKFDVPSevLDALKLSLQSSM-GVKGEVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVCLSPEETPEHGEKIAHEIRE 154
Cdd:cd07890  78 EEIETEVAD--PEAMKEILERLGfGPVGRVKKEREIYLLGQTRVHLDRVEGLGDFVEIEVVLEDIEEAEEGLGEAAELLG 155
                       170
                ....*....|....
gi 32565413 155 LLAVPETDLLTGAY 168
Cdd:cd07890 156 LLEYDEETLSYLEL 169
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
3-168 1.90e-21

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: 85.67  E-value: 1.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413     3 RNVEIKAKVQNLD-ETVRRAVEISGKQPTILKQHDIFYESPN-------GRLKMRSVEENGvahtELIWYDRSDVAGPKL 74
Cdd:pfam01928   2 IEIERKFLVSDEEyKDLLLLEKLRGKAEGPEEQRDIYFDTPDrdlartdEALRIRRFGNGA----YFLTLKGPGVDGPFK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413    75 SNFNKFDVPSE-VLDALKLSLQSSMGVKGEVKKTRTLVLHGQTRIHIDRVDGL-GDFMELEVCLSPEETPEHGEKIaHEI 152
Cdd:pfam01928  78 SREEVNGEVSRdEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLgGAEVELELEVEDEEELLEAAEE-LEL 156
                         170
                  ....*....|....*.
gi 32565413   153 RELLAVPETDLLTGAY 168
Cdd:pfam01928 157 LRILGLSEESKIARFY 172
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
5-172 1.37e-10

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: 56.81  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413   5 VEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESPNGRLKMRS----VEENGvAHTELIWydrsdvAGPKLSNFNK- 79
Cdd:COG1437   3 VEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDealrIRRGG-GRATLTY------KGPKLDEGSKt 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413  80 ----------FDVPSEVLDALKLSlqssmgVKGEVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVcLSPEETPEHGEKIA 149
Cdd:COG1437  76 reeietevddGEAMEAILEALGFR------PVATVEKTREIYKLGGVTVTLDEVEGLGPFVEIEG-EAEDEVEAAREAIE 148
                       170       180
                ....*....|....*....|...
gi 32565413 150 hEIRELLAVPETDLLTGAYMDML 172
Cdd:COG1437 149 -EVLAELGLDPDDIIRKSYLELL 170
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
5-137 6.54e-03

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: 273010  Cd Length: 174  Bit Score: 35.55  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565413     5 VEIKAKVQNLDETVRRAVEISGKQPTILKQHDIFYESPNgrlkmrsveeNGVAHTELIWYDRSDVA-------GPKLSNF 77
Cdd:TIGR00318   4 VEVKAKIPDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPC----------RDFASTDEALRIRKLTGekfvtykGPKIDNE 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565413    78 NKF--DVPSEVLDALK-LSLQSSMGVKG--EVKKTRTLVLHGQTRIHIDRVDGLGDFMELEVCLS 137
Cdd:TIGR00318  74 SKTrkEIEFKIEDIENaLQILKKLGFKKvyEVIKKRRIYQTNELNVSIDDVEGLGFFLEIEKIIN 138
 
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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