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Conserved domains on  [gi|270297151|ref|NP_001161932|]
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adenylate cyclase type 5 [Canis lupus familiaris]

Protein Classification

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

protein containing domains MFS, DUF1053, and CHD

Graphical summary

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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 ...
1-461 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: 637.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151     1 MSGPRSASPPGCAAT--RGGPEHRAAWGEAEARANGHPHAAGGAtRGCSKKpggavtpqlqqqqqqqqheqqheqqqheq 78
Cdd:pfam16214    1 MSRSNSVSPPGYGAPapRGGTEHRSAWGEAESRANGYPYAPGSA-RSSTKK----------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    79 qqhvqqQQRLAKRWRGDDDPP--LGGDDPLAGGFGFSFRSRSAWQERGGDDcgrgsrrrrRGAAGGGSSRAPPAGGGGGP 156
Cdd:pfam16214   51 ------QQRLASRWRSEDDDDppLSGSDPLSGGFGFSFRSKSAWQEHGGES---------RRQRTRAPPAGGGPGSAAAA 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   157 AAAGGAEVRPRSVELGLDERRGRGRAEpepeaEAGAPGGDRGARDGDGPAGPGACCRALLQIFRSKKFPSDKLERLYQRY 236
Cdd:pfam16214  116 ASRGGGEVRPRSVELGLEERRGKGRAA-----EGGEGSGDGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRY 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   237 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQ 316
Cdd:pfam16214  191 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQ 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   317 VVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVG 396
Cdd:pfam16214  271 VVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVG 350
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270297151   397 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 461
Cdd:pfam16214  351 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1066-1260 5.41e-73

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.61  E-value: 5.41e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1066 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRVLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1145
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1146 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1225
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 270297151  1226 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1260
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
463-646 8.99e-70

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 231.36  E-value: 8.99e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   463 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 542
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   543 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGD-Y 621
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 270297151   622 EVEpgCGGErnAYLK-EHSIETFLIL 646
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
671-764 7.47e-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: 7.47e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   671 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 746
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 270297151   747 FREPDLEKKYSKQVDDRF 764
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 ...
1-461 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: 637.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151     1 MSGPRSASPPGCAAT--RGGPEHRAAWGEAEARANGHPHAAGGAtRGCSKKpggavtpqlqqqqqqqqheqqheqqqheq 78
Cdd:pfam16214    1 MSRSNSVSPPGYGAPapRGGTEHRSAWGEAESRANGYPYAPGSA-RSSTKK----------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    79 qqhvqqQQRLAKRWRGDDDPP--LGGDDPLAGGFGFSFRSRSAWQERGGDDcgrgsrrrrRGAAGGGSSRAPPAGGGGGP 156
Cdd:pfam16214   51 ------QQRLASRWRSEDDDDppLSGSDPLSGGFGFSFRSKSAWQEHGGES---------RRQRTRAPPAGGGPGSAAAA 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   157 AAAGGAEVRPRSVELGLDERRGRGRAEpepeaEAGAPGGDRGARDGDGPAGPGACCRALLQIFRSKKFPSDKLERLYQRY 236
Cdd:pfam16214  116 ASRGGGEVRPRSVELGLEERRGKGRAA-----EGGEGSGDGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRY 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   237 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQ 316
Cdd:pfam16214  191 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQ 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   317 VVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVG 396
Cdd:pfam16214  271 VVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVG 350
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270297151   397 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 461
Cdd:pfam16214  351 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1066-1260 5.41e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.61  E-value: 5.41e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1066 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRVLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1145
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1146 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1225
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 270297151  1226 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1260
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
463-646 8.99e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 231.36  E-value: 8.99e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   463 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 542
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   543 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGD-Y 621
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 270297151   622 EVEpgCGGErnAYLK-EHSIETFLIL 646
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
427-622 5.04e-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: 209.81  E-value: 5.04e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    427 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 506
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    507 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 584
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 270297151    585 FDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYE 622
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
470-608 5.38e-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: 176.01  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  470 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 549
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 270297151  550 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 608
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1074-1258 1.59e-50

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: 176.23  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1074 VAVMFASIANFSEFYVELEAnnegVECLRVLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1153
Cdd:cd07302     2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1154 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1231
Cdd:cd07302    70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                         170       180
                  ....*....|....*....|....*...
gi 270297151 1232 LAANTYQLECRGVVKVKGK-GEMMTYFL 1258
Cdd:cd07302   150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1040-1241 1.40e-48

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: 171.29  E-value: 1.40e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   1040 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRVLNEIIADFDEIISEdr 1119
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   1120 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1198
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 270297151   1199 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1241
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
671-764 7.47e-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: 7.47e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   671 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 746
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 270297151   747 FREPDLEKKYSKQVDDRF 764
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
264-625 2.78e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 148.80  E-value: 2.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  264 AARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 343
Cdd:COG2114    24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  344 TLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 423
Cdd:COG2114   104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  424 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 503
Cdd:COG2114   184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  504 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 579
Cdd:COG2114   256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 270297151  580 -LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVEP 625
Cdd:COG2114   336 sEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
988-1257 4.65e-29

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 121.45  E-value: 4.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  988 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1059
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1060 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRVLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1137
Cdd:COG2114   217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1138 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1212
Cdd:COG2114   280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 270297151 1213 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1257
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 ...
1-461 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: 637.05  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151     1 MSGPRSASPPGCAAT--RGGPEHRAAWGEAEARANGHPHAAGGAtRGCSKKpggavtpqlqqqqqqqqheqqheqqqheq 78
Cdd:pfam16214    1 MSRSNSVSPPGYGAPapRGGTEHRSAWGEAESRANGYPYAPGSA-RSSTKK----------------------------- 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    79 qqhvqqQQRLAKRWRGDDDPP--LGGDDPLAGGFGFSFRSRSAWQERGGDDcgrgsrrrrRGAAGGGSSRAPPAGGGGGP 156
Cdd:pfam16214   51 ------QQRLASRWRSEDDDDppLSGSDPLSGGFGFSFRSKSAWQEHGGES---------RRQRTRAPPAGGGPGSAAAA 115
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   157 AAAGGAEVRPRSVELGLDERRGRGRAEpepeaEAGAPGGDRGARDGDGPAGPGACCRALLQIFRSKKFPSDKLERLYQRY 236
Cdd:pfam16214  116 ASRGGGEVRPRSVELGLEERRGKGRAA-----EGGEGSGDGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRY 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   237 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQ 316
Cdd:pfam16214  191 FFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQ 270
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   317 VVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVG 396
Cdd:pfam16214  271 VVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVG 350
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 270297151   397 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 461
Cdd:pfam16214  351 VCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1066-1260 5.41e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 240.61  E-value: 5.41e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1066 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRVLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1145
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  1146 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1225
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 270297151  1226 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1260
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
463-646 8.99e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 231.36  E-value: 8.99e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   463 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 542
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   543 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGD-Y 621
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 270297151   622 EVEpgCGGErnAYLK-EHSIETFLIL 646
Cdd:pfam00211  161 EFT--ERGE--IEVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
427-622 5.04e-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: 209.81  E-value: 5.04e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    427 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 506
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151    507 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 584
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 270297151    585 FDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYE 622
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
470-608 5.38e-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: 176.01  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  470 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 549
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 270297151  550 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 608
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1074-1258 1.59e-50

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: 176.23  E-value: 1.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1074 VAVMFASIANFSEFYVELEAnnegVECLRVLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1153
Cdd:cd07302     2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1154 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1231
Cdd:cd07302    70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                         170       180
                  ....*....|....*....|....*...
gi 270297151 1232 LAANTYQLECRGVVKVKGK-GEMMTYFL 1258
Cdd:cd07302   150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
470-645 2.19e-50

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: 175.85  E-value: 2.19e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  470 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIE 549
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  550 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNG-DYEVEPg 626
Cdd:cd07302    81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                         170
                  ....*....|....*....
gi 270297151  627 cGGERNAYLKEHSIETFLI 645
Cdd:cd07302   160 -LGEVELKGKSGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1040-1241 1.40e-48

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: 171.29  E-value: 1.40e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   1040 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRVLNEIIADFDEIISEdr 1119
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   1120 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1198
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 270297151   1199 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1241
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
671-764 7.47e-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: 7.47e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151   671 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 746
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 270297151   747 FREPDLEKKYSKQVDDRF 764
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
264-625 2.78e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 148.80  E-value: 2.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  264 AARPPLRLPHLAVLAAAVGVILVMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 343
Cdd:COG2114    24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  344 TLLPVRMRAAVLSGVLLSALHLAIALRANAQDRFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 423
Cdd:COG2114   104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  424 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 503
Cdd:COG2114   184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  504 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 579
Cdd:COG2114   256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 270297151  580 -LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLSYLNGDYEVEP 625
Cdd:COG2114   336 sEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
1073-1223 7.45e-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: 126.70  E-value: 7.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1073 CVAVMFASIANFSEFYVELEAnnegVECLRVLNEIIADFDEIISEDrfrQLEKIKTIGSTYMAASGLndstydkvgkTHI 1152
Cdd:cd07556     1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGL----------DHP 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 270297151 1153 KALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARkPQYDIWGNTVNVASRMDSTGVPDRIQ 1223
Cdd:cd07556    64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
988-1257 4.65e-29

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 121.45  E-value: 4.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151  988 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1059
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1060 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRVLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1137
Cdd:COG2114   217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 270297151 1138 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1212
Cdd:COG2114   280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 270297151 1213 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1257
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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