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Conserved domains on  [gi|530373840|ref|XP_005247135|]
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adenylate cyclase type 5 isoform X3 [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;
737-931 8.81e-74

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 8.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  737 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 816
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  817 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 896
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530373840  897 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 931
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
110-272 2.79e-69

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 2.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  110 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 189
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  190 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 268
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 530373840  269 EVEP 272
Cdd:pfam00211 161 EFTE 164
AC_N super family cl24704
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
27-108 5.42e-57

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: 202.16  E-value: 5.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   27 RRLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 106
Cdd:pfam16214 334 KQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 413

                  ..
gi 530373840  107 FH 108
Cdd:pfam16214 414 FH 415
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
318-411 5.39e-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: 5.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  318 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 393
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 530373840  394 FREPDLEKKYSKQVDDRF 411
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
737-931 8.81e-74

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 8.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  737 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 816
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  817 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 896
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530373840  897 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 931
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
110-272 2.79e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 2.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  110 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 189
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  190 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 268
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 530373840  269 EVEP 272
Cdd:pfam00211 161 EFTE 164
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
74-269 4.70e-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: 4.70e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840    74 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 153
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   154 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 231
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 530373840   232 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 269
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
27-108 5.42e-57

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: 202.16  E-value: 5.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   27 RRLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 106
Cdd:pfam16214 334 KQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 413

                  ..
gi 530373840  107 FH 108
Cdd:pfam16214 414 FH 415
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
117-255 3.30e-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: 3.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 117 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 196
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530373840 197 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 255
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
745-929 4.30e-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: 4.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 745 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 824
Cdd:cd07302    2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 825 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 902
Cdd:cd07302   70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                        170       180
                 ....*....|....*....|....*...
gi 530373840 903 LAANTYQLECRGVVKVKGK-GEMMTYFL 929
Cdd:cd07302  150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
711-912 6.78e-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: 6.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   711 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 790
Cdd:smart00044   6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   791 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 869
Cdd:smart00044  77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 530373840   870 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 912
Cdd:smart00044 152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
318-411 5.39e-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: 5.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  318 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 393
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 530373840  394 FREPDLEKKYSKQVDDRF 411
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
49-294 3.83e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 144.95  E-value: 3.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  49 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGF 128
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGF 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 129 TSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREV 204
Cdd:COG2114  234 TALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAE 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 205 TGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPgcGGERNAYLK 283
Cdd:COG2114  314 GGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE--LGEVRLKGK 391
                        250
                 ....*....|.
gi 530373840 284 EHSIETFLILR 294
Cdd:COG2114  392 AEPVEVYELLG 402
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
659-934 4.34e-32

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 129.92  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 659 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 730
Cdd:COG2114  137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 731 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 808
Cdd:COG2114  217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 809 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 883
Cdd:COG2114  280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530373840 884 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGE-MMTYFLNGGPP 934
Cdd:COG2114  355 LESLAKPGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEpVEVYELLGAKE 405
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
737-931 8.81e-74

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.22  E-value: 8.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  737 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 816
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  817 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 896
Cdd:pfam00211  74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 530373840  897 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 931
Cdd:pfam00211 149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
110-272 2.79e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 227.90  E-value: 2.79e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  110 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 189
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  190 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 268
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160

                  ....
gi 530373840  269 EVEP 272
Cdd:pfam00211 161 EFTE 164
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
74-269 4.70e-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: 4.70e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840    74 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 153
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   154 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 231
Cdd:smart00044  73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 530373840   232 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 269
Cdd:smart00044 153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
27-108 5.42e-57

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: 202.16  E-value: 5.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   27 RRLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 106
Cdd:pfam16214 334 KQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMM 413

                  ..
gi 530373840  107 FH 108
Cdd:pfam16214 414 FH 415
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
117-255 3.30e-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: 3.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 117 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 196
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530373840 197 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 255
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
745-929 4.30e-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: 4.30e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 745 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 824
Cdd:cd07302    2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 825 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 902
Cdd:cd07302   70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                        170       180
                 ....*....|....*....|....*...
gi 530373840 903 LAANTYQLECRGVVKVKGK-GEMMTYFL 929
Cdd:cd07302  150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
117-292 8.81e-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: 8.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 117 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIE 196
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 197 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNG-DYEVEPg 273
Cdd:cd07302   81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                        170
                 ....*....|....*....
gi 530373840 274 cGGERNAYLKEHSIETFLI 292
Cdd:cd07302  160 -LGEVELKGKSGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
711-912 6.78e-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: 6.78e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   711 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 790
Cdd:smart00044   6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840   791 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 869
Cdd:smart00044  77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 530373840   870 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 912
Cdd:smart00044 152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
318-411 5.39e-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: 5.39e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  318 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 393
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                          90
                  ....*....|....*...
gi 530373840  394 FREPDLEKKYSKQVDDRF 411
Cdd:pfam06327  81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
49-294 3.83e-37

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 144.95  E-value: 3.83e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840  49 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGF 128
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGF 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 129 TSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREV 204
Cdd:COG2114  234 TALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAE 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 205 TGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPgcGGERNAYLK 283
Cdd:COG2114  314 GGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE--LGEVRLKGK 391
                        250
                 ....*....|.
gi 530373840 284 EHSIETFLILR 294
Cdd:COG2114  392 AEPVEVYELLG 402
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
744-894 6.21e-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: 6.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 744 CVAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEDrfrQLEKIKTIGSTYMAASGLndstydkvgkTHI 823
Cdd:cd07556    1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGL----------DHP 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373840 824 KALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARkPQYDIWGNTVNVASRMDSTGVPDRIQ 894
Cdd:cd07556   64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
659-934 4.34e-32

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 129.92  E-value: 4.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 659 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 730
Cdd:COG2114  137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 731 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 808
Cdd:COG2114  217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373840 809 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 883
Cdd:COG2114  280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530373840 884 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGE-MMTYFLNGGPP 934
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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