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Conserved domains on  [gi|985331391|gb|KXA14949|]
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putative adenylyl cyclase CyaB [Clostridium perfringens]

Protein Classification

class IV adenylate cyclase( domain architecture ID 10787662)

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
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 2-176 4.04e-43

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: 141.55  E-value: 4.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   2 KELETRIIDIDVEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDlinnkiVYFMTTKKMLSQDKFK 81
Cdd:COG1437    1 IEVEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGG------RATLTYKGPKLDEGSK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391  82 VMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPsfcPFPYIEIET-------SSEEKLNEIL 154
Cdd:COG1437   75 TREEIETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGGVTVTLDEVEG---LGPFVEIEGeaedeveAAREAIEEVL 151

                        170       180
                 ....*....|....*....|..
gi 985331391 155 IDLGYSMEDTTSKTIYEILKDK 176
Cdd:COG1437  152 AELGLDPDDIIRKSYLELLLEK 173
 
Name Accession Description Interval E-value
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 2-176 4.04e-43

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: 141.55  E-value: 4.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   2 KELETRIIDIDVEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDlinnkiVYFMTTKKMLSQDKFK 81
Cdd:COG1437    1 IEVEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGG------RATLTYKGPKLDEGSK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391  82 VMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPsfcPFPYIEIET-------SSEEKLNEIL 154
Cdd:COG1437   75 TREEIETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGGVTVTLDEVEG---LGPFVEIEGeaedeveAAREAIEEVL 151

                        170       180
                 ....*....|....*....|..
gi 985331391 155 IDLGYSMEDTTSKTIYEILKDK 176
Cdd:COG1437  152 AELGLDPDDIIRKSYLELLLEK 173
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-169 3.13e-30

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: 108.78  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391    1 MKELETRIIDIDVE-KLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDlinnkIVYFMTTKKMLSQDK 79
Cdd:pfam01928   1 MIEIERKFLVSDEEyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGN-----GAYFLTLKGPGVDGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   80 FKVMEENETIIE-DGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPSFCPFPYIEIETSSEEKLNEILID-- 156
Cdd:pfam01928  76 FKSREEVNGEVSrDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELELEVEDEEELLEAAEEle 155

                         170
                  ....*....|....*..
gi 985331391  157 ----LGYSMEDTTSKTI 169
Cdd:pfam01928 156 llriLGLSEESKIARFY 172
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 2-172 6.88e-29

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: 105.04  E-value: 6.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   2 KELETRIIDIdvEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDLINNKIVYfmttKKMLSQDKFK 81
Cdd:cd07890    2 VEIKARVDDL--EALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTY----KGPKLDGGPK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391  82 VMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPsfcPFPYIEIETS------SEEKLNEILI 155
Cdd:cd07890   76 VREEIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEG---LGDFVEIEVVledieeAEEGLGEAAE 152

                        170
                 ....*....|....*..
gi 985331391 156 DLGYSMEDTTSKTIYEI 172
Cdd:cd07890  153 LLGLLEYDEETLSYLEL 169
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
 1-128 2.63e-04

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: 39.78  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391    1 MKELETRIIDIDVEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRtveDLINNKIVyfmTTKKMLSQDKF 80
Cdd:TIGR00318   1 MIEVEVKAKIPDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIR---KLTGEKFV---TYKGPKIDNES 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 985331391   81 KVMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEID 128
Cdd:TIGR00318  75 KTRKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNELNVSID 122
 
Name Accession Description Interval E-value
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
 2-176 4.04e-43

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: 141.55  E-value: 4.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   2 KELETRIIDIDVEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDlinnkiVYFMTTKKMLSQDKFK 81
Cdd:COG1437    1 IEVEVKVRVIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRRGGG------RATLTYKGPKLDEGSK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391  82 VMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPsfcPFPYIEIET-------SSEEKLNEIL 154
Cdd:COG1437   75 TREEIETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGGVTVTLDEVEG---LGPFVEIEGeaedeveAAREAIEEVL 151

                        170       180
                 ....*....|....*....|..
gi 985331391 155 IDLGYSMEDTTSKTIYEILKDK 176
Cdd:COG1437  152 AELGLDPDDIIRKSYLELLLEK 173
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
 1-169 3.13e-30

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: 108.78  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391    1 MKELETRIIDIDVE-KLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDlinnkIVYFMTTKKMLSQDK 79
Cdd:pfam01928   1 MIEIERKFLVSDEEyKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGN-----GAYFLTLKGPGVDGP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   80 FKVMEENETIIE-DGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPSFCPFPYIEIETSSEEKLNEILID-- 156
Cdd:pfam01928  76 FKSREEVNGEVSrDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALDVVEFLGGAEVELELEVEDEEELLEAAEEle 155

                         170
                  ....*....|....*..
gi 985331391  157 ----LGYSMEDTTSKTI 169
Cdd:pfam01928 156 llriLGLSEESKIARFY 172
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
 2-172 6.88e-29

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: 105.04  E-value: 6.88e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391   2 KELETRIIDIdvEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRTVEDLINNKIVYfmttKKMLSQDKFK 81
Cdd:cd07890    2 VEIKARVDDL--EALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDSGKTLLTY----KGPKLDGGPK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391  82 VMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEIDINDPsfcPFPYIEIETS------SEEKLNEILI 155
Cdd:cd07890   76 VREEIETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVHLDRVEG---LGDFVEIEVVledieeAEEGLGEAAE 152

                        170
                 ....*....|....*..
gi 985331391 156 DLGYSMEDTTSKTIYEI 172
Cdd:cd07890  153 LLGLLEYDEETLSYLEL 169
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
 1-128 2.63e-04

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: 39.78  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 985331391    1 MKELETRIIDIDVEKLRETLSKLGAENIKRENQTNDIFDFPDRKLLDKKGYARIRtveDLINNKIVyfmTTKKMLSQDKF 80
Cdd:TIGR00318   1 MIEVEVKAKIPDKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIR---KLTGEKFV---TYKGPKIDNES 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 985331391   81 KVMEENETIIEDGAMGKNIFKSLGLELFETIKKYRESYKYKDSLIEID 128
Cdd:TIGR00318  75 KTRKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNELNVSID 122
 
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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