NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1084634770|gb|OGO83830|]
View 

hypothetical protein A2Y18_03610 [Clostridiales bacterium GWD2_32_19]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CyaB super family cl42670
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
10-172 1.59e-15

Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) [Signal transduction mechanisms, General function prediction only];


The actual alignment was detected with superfamily member COG1437:

Pssm-ID: 441046  Cd Length: 173  Bit Score: 72.60  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  10 VEIEEKFFcDNDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTiDDKELEITYKGKSEVfSSFYAKK 89
Cdd:COG1437     1 IEVEVKVR-VIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRR-GGGRATLTYKGPKLD-EGSKTRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  90 EsnIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTEneitYNILIDSILNIGEFLEFEIIIHDDSSEGEKYFLEFI 169
Cdd:COG1437    78 E--IETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGG----VTVTLDEVEGLGPFVEIEGEAEDEVEAAREAIEEVL 151

                  ...
gi 1084634770 170 DKF 172
Cdd:COG1437   152 AEL 154
 
Name Accession Description Interval E-value
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
10-172 1.59e-15

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: 72.60  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  10 VEIEEKFFcDNDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTiDDKELEITYKGKSEVfSSFYAKK 89
Cdd:COG1437     1 IEVEVKVR-VIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRR-GGGRATLTYKGPKLD-EGSKTRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  90 EsnIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTEneitYNILIDSILNIGEFLEFEIIIHDDSSEGEKYFLEFI 169
Cdd:COG1437    78 E--IETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGG----VTVTLDEVEGLGPFVEIEGEAEDEVEAAREAIEEVL 151

                  ...
gi 1084634770 170 DKF 172
Cdd:COG1437   152 AEL 154
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
11-185 5.28e-13

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: 65.37  E-value: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  11 EIEEKFFCDnDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTIDD-KELEITYKGKsEVFSSFYAKK 89
Cdd:cd07890     1 EVEIKARVD-DLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDsGKTLLTYKGP-KLDGGPKVRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  90 EsnIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTENEITynilIDSILNIGEFLEFEIIIhDDSSEGEKYFLEFI 169
Cdd:cd07890    79 E--IETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVH----LDRVEGLGDFVEIEVVL-EDIEEAEEGLGEAA 151
                         170
                  ....*....|....*.
gi 1084634770 170 DKFKSLKLNKADLPYR 185
Cdd:cd07890   152 ELLGLLEYDEETLSYL 167
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
9-156 3.04e-05

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: 43.64  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770   9 VVEIEEKFFCDnDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTiDDKELEITYKGKSEVFSSfyaK 88
Cdd:TIGR00318   1 MIEVEVKAKIP-DKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIRK-LTGEKFVTYKGPKIDNES---K 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084634770  89 KESNIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTEneitYNILIDSILNIGEFLEFEIIIHD 156
Cdd:TIGR00318  76 TRKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNE----LNVSIDDVEGLGFFLEIEKIINN 139
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
11-157 3.54e-03

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: 37.52  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  11 EIEEKFFCDNDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTIDDKELEITYKGkSEVFSSFYAKKE 90
Cdd:pfam01928   3 EIERKFLVSDEEYKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYFLTLKG-PGVDGPFKSREE 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084634770  91 SNIISEvKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTENEITYNilIDSILNiGEFLEFEIIIHDD 157
Cdd:pfam01928  82 VNGEVS-RDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALD--VVEFLG-GAEVELELEVEDE 144
 
Name Accession Description Interval E-value
CyaB COG1437
Adenylate cyclase class IV, CYTH domain (includes archaeal enzymes of unknown function) ...
10-172 1.59e-15

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: 72.60  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  10 VEIEEKFFcDNDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTiDDKELEITYKGKSEVfSSFYAKK 89
Cdd:COG1437     1 IEVEVKVR-VIDLEEVRERLEELGAELVGEEHQIDIYYDAPDRDFAETDEALRIRR-GGGRATLTYKGPKLD-EGSKTRE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  90 EsnIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTEneitYNILIDSILNIGEFLEFEIIIHDDSSEGEKYFLEFI 169
Cdd:COG1437    78 E--IETEVDDGEAMEAILEALGFRPVATVEKTREIYKLGG----VTVTLDEVEGLGPFVEIEGEAEDEVEAAREAIEEVL 151

                  ...
gi 1084634770 170 DKF 172
Cdd:COG1437   152 AEL 154
CYTH-like_AC_IV-like cd07890
Adenylyl cyclase (AC) class IV-like, a subgroup of the CYTH-like superfamily; This subgroup ...
11-185 5.28e-13

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: 65.37  E-value: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  11 EIEEKFFCDnDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTIDD-KELEITYKGKsEVFSSFYAKK 89
Cdd:cd07890     1 EVEIKARVD-DLEALRERLAALGGAEGGREFQEDIYFDHPDRDLAATDEALRLRRMGDsGKTLLTYKGP-KLDGGPKVRE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  90 EsnIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTENEITynilIDSILNIGEFLEFEIIIhDDSSEGEKYFLEFI 169
Cdd:cd07890    79 E--IETEVADPEAMKEILERLGFGPVGRVKKEREIYLLGQTRVH----LDRVEGLGDFVEIEVVL-EDIEEAEEGLGEAA 151
                         170
                  ....*....|....*.
gi 1084634770 170 DKFKSLKLNKADLPYR 185
Cdd:cd07890   152 ELLGLLEYDEETLSYL 167
cyaB TIGR00318
adenylyl cyclase CyaB, putative; The protein CyaB from Aeromonas hydrophila is a second ...
9-156 3.04e-05

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: 43.64  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770   9 VVEIEEKFFCDnDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTiDDKELEITYKGKSEVFSSfyaK 88
Cdd:TIGR00318   1 MIEVEVKAKIP-DKEKVVEKLKNKGFKFIKKEFQHDIYFSNPCRDFASTDEALRIRK-LTGEKFVTYKGPKIDNES---K 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084634770  89 KESNIISEVKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTEneitYNILIDSILNIGEFLEFEIIIHD 156
Cdd:TIGR00318  76 TRKEIEFKIEDIENALQILKKLGFKKVYEVIKKRRIYQTNE----LNVSIDDVEGLGFFLEIEKIINN 139
CYTH pfam01928
CYTH domain; These sequences are functionally identified as members of the adenylate cyclase ...
11-157 3.54e-03

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: 37.52  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084634770  11 EIEEKFFCDNDIETIKDEIEREGFKFIKRINEKDEYFTDLAGEYIKNRTCLRTRTIDDKELEITYKGkSEVFSSFYAKKE 90
Cdd:pfam01928   3 EIERKFLVSDEEYKDLLLLEKLRGKAEGPEEQRDIYFDTPDRDLARTDEALRIRRFGNGAYFLTLKG-PGVDGPFKSREE 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084634770  91 SNIISEvKSYENIVDLFKVFGYHSYVVVDKIRDYYSKTENEITYNilIDSILNiGEFLEFEIIIHDD 157
Cdd:pfam01928  82 VNGEVS-RDEPDAVELLDGLGLQPVGSIKKERRRYKVKGVLIALD--VVEFLG-GAEVELELEVEDE 144
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH