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Conserved domains on  [gi|528866030|ref|NP_001268697|]
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adenylate cyclase type 1 isoform 2 [Homo sapiens]

Protein Classification

adenylate/guanylate cyclase domain-containing protein( domain architecture ID 10446187)

adenylate/guanylate cyclase domain-containing protein may function as an adenylate cyclase, catalyzing the synthesis of 3',5'-cyclic AMP, or as a guanylate cyclase, catalyzing the synthesis of 3',5'-cyclic GMP

CATH:  3.30.70.1230
EC:  2.7.7.-
Gene Ontology:  GO:0046872|GO:0016779
PubMed:  17236651|9914257
SCOP:  4001316

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
69-251 6.94e-82

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.39  E-value: 6.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030   69 IYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVE 148
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  149 MGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLN---- 224
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 528866030  225 -----GDYEVePGYGhernsflkthNIETFFI 251
Cdd:pfam00211 161 efterGEIEV-KGKG----------KMKTYFL 181
AC_N super family cl24704
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
3-67 2.54e-15

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: 76.20  E-value: 2.54e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528866030    3 GVFVRILTERSQRKAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDF-LKPPERIFH 67
Cdd:pfam16214 350 GVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADInAKQEDMMFH 415
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
69-251 6.94e-82

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.39  E-value: 6.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030   69 IYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVE 148
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  149 MGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLN---- 224
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 528866030  225 -----GDYEVePGYGhernsflkthNIETFFI 251
Cdd:pfam00211 161 efterGEIEV-KGKG----------KMKTYFL 181
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
33-228 4.48e-75

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: 229.45  E-value: 4.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030    33 DENEKQERLLMSLLPRNVAMEMKEDFlkpperifHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDE 112
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGG--------SPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030   113 LATENHCRRIKILGDCYYCVSGLTQPKT-DHAHCCVEMGLDMIDTITSV-AEATEVDLNMRVGLHTGRVLCGVLGLRKWQ 190
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTVlVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 528866030   191 YDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYE 228
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
76-251 1.01e-54

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: 176.62  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  76 NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMID 155
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030 156 TITSVAE--ATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNG-DYEVEPG 232
Cdd:cd07302   81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEEL 160
                        170       180
                 ....*....|....*....|
gi 528866030 233 YGHE-RNsflKTHNIETFFI 251
Cdd:cd07302  161 GEVElKG---KSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
17-231 3.98e-41

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 148.41  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  17 AFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERifhkiyiQRHDNVSILFADIVGFTGLASQCTA 96
Cdd:COG2114  170 LLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLG-------GERREVTVLFADIVGFTALSERLGP 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  97 QELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATE----VDLNMRV 172
Cdd:COG2114  243 EELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELNAELPaeggPPLRVRI 322
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030 173 GLHTGRVLCGVLG-LRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEP 231
Cdd:COG2114  323 GIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
3-67 2.54e-15

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: 76.20  E-value: 2.54e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528866030    3 GVFVRILTERSQRKAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDF-LKPPERIFH 67
Cdd:pfam16214 350 GVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADInAKQEDMMFH 415
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
69-251 6.94e-82

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.39  E-value: 6.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030   69 IYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVE 148
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  149 MGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLN---- 224
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 528866030  225 -----GDYEVePGYGhernsflkthNIETFFI 251
Cdd:pfam00211 161 efterGEIEV-KGKG----------KMKTYFL 181
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
33-228 4.48e-75

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: 229.45  E-value: 4.48e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030    33 DENEKQERLLMSLLPRNVAMEMKEDFlkpperifHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDE 112
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGG--------SPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030   113 LATENHCRRIKILGDCYYCVSGLTQPKT-DHAHCCVEMGLDMIDTITSV-AEATEVDLNMRVGLHTGRVLCGVLGLRKWQ 190
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTVlVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 528866030   191 YDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYE 228
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
76-251 1.01e-54

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: 176.62  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  76 NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMID 155
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030 156 TITSVAE--ATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNG-DYEVEPG 232
Cdd:cd07302   81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEEL 160
                        170       180
                 ....*....|....*....|
gi 528866030 233 YGHE-RNsflKTHNIETFFI 251
Cdd:cd07302  161 GEVElKG---KSGPVRVYRL 177
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
76-214 1.47e-49

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: 162.14  E-value: 1.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  76 NVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLtqpktDHAHCCVEMGLDMID 155
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-----DHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 528866030 156 TITSVAEATEVDLNMRVGLHTGRVLCGVLGLRkWQYDVWSNDVTLANVMEAAGLPGKVH 214
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
17-231 3.98e-41

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 148.41  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  17 AFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERifhkiyiQRHDNVSILFADIVGFTGLASQCTA 96
Cdd:COG2114  170 LLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLG-------GERREVTVLFADIVGFTALSERLGP 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030  97 QELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATE----VDLNMRV 172
Cdd:COG2114  243 EELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELNAELPaeggPPLRVRI 322
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 528866030 173 GLHTGRVLCGVLG-LRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEP 231
Cdd:COG2114  323 GIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
3-67 2.54e-15

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: 76.20  E-value: 2.54e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 528866030    3 GVFVRILTERSQRKAFLQARSCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDF-LKPPERIFH 67
Cdd:pfam16214 350 GVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADInAKQEDMMFH 415
 
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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