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Conserved domains on  [gi|2462586755|ref|XP_054201034|]
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adenylate cyclase type 5 isoform X1 [Homo sapiens]

Protein Classification

DUF1053 and CHD domain-containing protein( domain architecture ID 11087281)

DUF1053 and CHD domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
754-948 1.06e-73

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 754 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 833
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 834 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 913
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462586755 914 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 948
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
127-289 3.28e-69

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 3.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 127 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 206
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 207 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 285
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 2462586755 286 EVEP 289
Cdd:pfam00211 161 EFTE 164
AC_N super family cl24704
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
46-125 1.45e-56

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


The actual alignment was detected with superfamily member pfam16214:

Pssm-ID: 318454  Cd Length: 415  Bit Score: 201.39  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  46 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 125
Cdd:pfam16214 336 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
335-428 5.52e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


:

Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.43  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 335 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 410
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 2462586755 411 FREPDLEKKYSKQVDDRF 428
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
754-948 1.06e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 754 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 833
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 834 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 913
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462586755 914 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 948
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
127-289 3.28e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 3.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 127 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 206
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 207 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 285
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 2462586755 286 EVEP 289
Cdd:pfam00211 161 EFTE 164
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
91-286 5.50e-62

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 208.65  E-value: 5.50e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755   91 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 170
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  171 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 248
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462586755  249 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 286
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
46-125 1.45e-56

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 201.39  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  46 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 125
Cdd:pfam16214 336 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
134-272 3.49e-52

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 178.70  E-value: 3.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 134 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 213
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462586755 214 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 272
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
762-946 4.43e-52

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 180.08  E-value: 4.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 762 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 841
Cdd:cd07302     2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 842 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 919
Cdd:cd07302    70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                         170       180
                  ....*....|....*....|....*...
gi 2462586755 920 LAANTYQLECRGVVKVKGK-GEMMTYFL 946
Cdd:cd07302   150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
728-929 7.53e-49

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 171.67  E-value: 7.53e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  728 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 807
Cdd:smart00044   6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  808 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 886
Cdd:smart00044  77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462586755  887 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 929
Cdd:smart00044 152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
335-428 5.52e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.43  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 335 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 410
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 2462586755 411 FREPDLEKKYSKQVDDRF 428
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
66-311 3.65e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 144.95  E-value: 3.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  66 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGF 145
Cdd:COG2114   162 LLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGF 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 146 TSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREV 221
Cdd:COG2114   234 TALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 222 TGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPgcGGERNAYLK 300
Cdd:COG2114   314 GGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE--LGEVRLKGK 391
                         250
                  ....*....|.
gi 2462586755 301 EHSIETFLILR 311
Cdd:COG2114   392 AEPVEVYELLG 402
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
676-951 4.30e-32

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 129.92  E-value: 4.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 676 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 747
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 748 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 825
Cdd:COG2114   217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 826 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 900
Cdd:COG2114   280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462586755 901 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGE-MMTYFLNGGPP 951
Cdd:COG2114   355 LESLAKPGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEpVEVYELLGAKE 405
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
754-948 1.06e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 754 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 833
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 834 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 913
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2462586755 914 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 948
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
127-289 3.28e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 3.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 127 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 206
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 207 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 285
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 2462586755 286 EVEP 289
Cdd:pfam00211 161 EFTE 164
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
91-286 5.50e-62

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 208.65  E-value: 5.50e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755   91 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 170
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  171 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 248
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2462586755  249 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 286
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
46-125 1.45e-56

Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the N-terminal extracellular region and the first transmembrane 5-6 pass region of adenylate cyclase.


Pssm-ID: 318454  Cd Length: 415  Bit Score: 201.39  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  46 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 125
Cdd:pfam16214 336 LVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
134-272 3.49e-52

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 178.70  E-value: 3.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 134 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 213
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462586755 214 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 272
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
762-946 4.43e-52

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 180.08  E-value: 4.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 762 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 841
Cdd:cd07302     2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 842 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 919
Cdd:cd07302    70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                         170       180
                  ....*....|....*....|....*...
gi 2462586755 920 LAANTYQLECRGVVKVKGK-GEMMTYFL 946
Cdd:cd07302   150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
134-309 9.16e-52

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 179.31  E-value: 9.16e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 134 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIE 213
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 214 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNG-DYEVEPg 290
Cdd:cd07302    81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                         170
                  ....*....|....*....
gi 2462586755 291 cGGERNAYLKEHSIETFLI 309
Cdd:cd07302   160 -LGEVELKGKSGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
728-929 7.53e-49

Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes.


Pssm-ID: 214485  Cd Length: 194  Bit Score: 171.67  E-value: 7.53e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  728 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 807
Cdd:smart00044   6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  808 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 886
Cdd:smart00044  77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2462586755  887 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 929
Cdd:smart00044 152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
335-428 5.52e-42

Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate to produce Cyclic AMP (cAMP), a ubiquitous signalling molecule that mediates many cellular processes by activating cAMP- dependent kinases and also inducing protein-protein interactions. Mammalian adenylate cyclase has nine closely related membrane-bound isoforms (AC1-9) showing significant sequence homology and sharing the same overall structure: two hydrophobic transmembrane domains, and two cytoplasmic domains that are responsible for the catalytic activity. These isoforms differ in both their tissue specificity and their regulation. This entry represents a region of unknown function found in many of these isoforms. It is part of the N-terminal cytoplasmic domain but its presence is not necessary for catalytic activity.


Pssm-ID: 461877  Cd Length: 98  Bit Score: 148.43  E-value: 5.52e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 335 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 410
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 2462586755 411 FREPDLEKKYSKQVDDRF 428
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
66-311 3.65e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 144.95  E-value: 3.65e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755  66 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGF 145
Cdd:COG2114   162 LLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGF 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 146 TSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREV 221
Cdd:COG2114   234 TALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAE 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 222 TGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPgcGGERNAYLK 300
Cdd:COG2114   314 GGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE--LGEVRLKGK 391
                         250
                  ....*....|.
gi 2462586755 301 EHSIETFLILR 311
Cdd:COG2114   392 AEPVEVYELLG 402
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
761-911 6.33e-35

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 129.40  E-value: 6.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 761 CVAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEDrfrQLEKIKTIGSTYMAASGLndstydkvgkTHI 840
Cdd:cd07556     1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGL----------DHP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462586755 841 KALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARkPQYDIWGNTVNVASRMDSTGVPDRIQ 911
Cdd:cd07556    64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
676-951 4.30e-32

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 129.92  E-value: 4.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 676 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 747
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 748 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 825
Cdd:COG2114   217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462586755 826 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 900
Cdd:COG2114   280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462586755 901 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGE-MMTYFLNGGPP 951
Cdd:COG2114   355 LESLAKPGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEpVEVYELLGAKE 405
 
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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