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Conserved domains on  [gi|1805791150|ref|NP_001365188|]
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adenylate cyclase type 5 isoform 3 [Homo sapiens]

Protein Classification

DUF1053 and CHD domain-containing protein( domain architecture ID 11069824)

protein containing domains MFS, DUF1053, and CHD

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
AC_N super family cl24704
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
1-458 0e+00

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: 704.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150    1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791150  401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1087-1281 1.01e-73

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.92  E-value: 1.01e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1087 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1166
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1167 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1246
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1805791150 1247 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1281
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.28e-69

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.59  E-value: 2.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 1805791150  619 EVEpgCGGErnAYLK-EHSIETFLIL 643
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
668-761 7.59e-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: 7.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 1805791150  744 FREPDLEKKYSKQVDDRF 761
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
1-458 0e+00

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: 704.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150    1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791150  401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1087-1281 1.01e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.92  E-value: 1.01e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1087 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1166
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1167 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1246
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1805791150 1247 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1281
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.28e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.59  E-value: 2.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 1805791150  619 EVEpgCGGErnAYLK-EHSIETFLIL 643
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
424-619 4.78e-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: 210.19  E-value: 4.78e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   424 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 503
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   504 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 581
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1805791150   582 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 619
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
467-605 1.73e-51

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: 177.16  E-value: 1.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 546
Cdd:cd07556      1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791150  547 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 605
Cdd:cd07556     76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1095-1279 2.12e-51

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: 178.93  E-value: 2.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1095 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1174
Cdd:cd07302      2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1175 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1252
Cdd:cd07302     70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                          170       180
                   ....*....|....*....|....*...
gi 1805791150 1253 LAANTYQLECRGVVKVKGK-GEMMTYFL 1279
Cdd:cd07302    150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1061-1262 4.43e-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: 172.83  E-value: 4.43e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  1061 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 1140
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  1141 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1219
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 1805791150  1220 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1262
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
668-761 7.59e-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: 7.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 1805791150  744 FREPDLEKKYSKQVDDRF 761
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
261-622 1.24e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 149.95  E-value: 1.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  261 AARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 340
Cdd:COG2114     24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  341 TLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 420
Cdd:COG2114    104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  421 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 500
Cdd:COG2114    184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  501 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 576
Cdd:COG2114    256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1805791150  577 -LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEP 622
Cdd:COG2114    336 sEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1009-1278 4.56e-30

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 124.53  E-value: 4.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1009 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1080
Cdd:COG2114    137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1081 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1158
Cdd:COG2114    217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1159 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1233
Cdd:COG2114    280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1805791150 1234 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1278
Cdd:COG2114    355 LESLAKPGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEPVEVY 398
 
Name Accession Description Interval E-value
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
1-458 0e+00

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: 704.84  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150    1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1805791150  401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1087-1281 1.01e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.92  E-value: 1.01e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1087 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1166
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1167 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1246
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1805791150 1247 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1281
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.28e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.59  E-value: 2.28e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 1805791150  619 EVEpgCGGErnAYLK-EHSIETFLIL 643
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
424-619 4.78e-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: 210.19  E-value: 4.78e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   424 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 503
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150   504 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 581
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1805791150   582 FDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYE 619
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
467-605 1.73e-51

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: 177.16  E-value: 1.73e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 546
Cdd:cd07556      1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1805791150  547 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 605
Cdd:cd07556     76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1095-1279 2.12e-51

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: 178.93  E-value: 2.12e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1095 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1174
Cdd:cd07302      2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1175 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1252
Cdd:cd07302     70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                          170       180
                   ....*....|....*....|....*...
gi 1805791150 1253 LAANTYQLECRGVVKVKGK-GEMMTYFL 1279
Cdd:cd07302    150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
467-642 4.14e-51

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: 178.16  E-value: 4.14e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIE 546
Cdd:cd07302      1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  547 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNG-DYEVEPg 623
Cdd:cd07302     81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                          170
                   ....*....|....*....
gi 1805791150  624 cGGERNAYLKEHSIETFLI 642
Cdd:cd07302    160 -LGEVELKGKSGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1061-1262 4.43e-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: 172.83  E-value: 4.43e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  1061 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 1140
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  1141 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1219
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 1805791150  1220 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1262
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
668-761 7.59e-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: 7.59e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 1805791150  744 FREPDLEKKYSKQVDDRF 761
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
261-622 1.24e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 149.95  E-value: 1.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  261 AARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 340
Cdd:COG2114     24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  341 TLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 420
Cdd:COG2114    104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  421 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 500
Cdd:COG2114    184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150  501 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 576
Cdd:COG2114    256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1805791150  577 -LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEP 622
Cdd:COG2114    336 sEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
1094-1244 2.01e-34

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: 128.63  E-value: 2.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1094 CVAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEDrfrQLEKIKTIGSTYMAASGLndstydkvgkTHI 1173
Cdd:cd07556      1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGL----------DHP 63
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1805791150 1174 KALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARkPQYDIWGNTVNVASRMDSTGVPDRIQ 1244
Cdd:cd07556     64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1009-1278 4.56e-30

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 124.53  E-value: 4.56e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1009 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1080
Cdd:COG2114    137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1081 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1158
Cdd:COG2114    217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1805791150 1159 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1233
Cdd:COG2114    280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1805791150 1234 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1278
Cdd:COG2114    355 LESLAKPGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEPVEVY 398
 
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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