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Conserved domains on  [gi|34486092|ref|NP_899200|]
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adenylate cyclase type 5 isoform 1 [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: 705.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092      1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34486092    401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1062-1256 1.11e-73

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.53  E-value: 1.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1062 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1141
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1142 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1221
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 34486092   1222 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1256
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.58e-69

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.21  E-value: 2.58e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 34486092    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 7.44e-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: 7.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 34486092    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: 705.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092      1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34486092    401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1062-1256 1.11e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.53  E-value: 1.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1062 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1141
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1142 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1221
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 34486092   1222 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1256
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.58e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.21  E-value: 2.58e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 34486092    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 5.11e-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: 5.11e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     424 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 503
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     504 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 581
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 34486092     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 2.07e-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: 2.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 546
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34486092  547 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 605
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1070-1254 2.78e-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: 178.54  E-value: 2.78e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1070 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1149
Cdd:cd07302    2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1150 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1227
Cdd:cd07302   70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                        170       180
                 ....*....|....*....|....*...
gi 34486092 1228 LAANTYQLECRGVVKVKGK-GEMMTYFL 1254
Cdd:cd07302  150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1036-1237 4.73e-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: 4.73e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    1036 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 1115
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    1116 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1194
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 34486092    1195 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1237
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
668-761 7.44e-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: 7.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 34486092    744 FREPDLEKKYSKQVDDRF 761
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
261-622 1.40e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 149.57  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  261 AARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 340
Cdd:COG2114   24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  341 TLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 420
Cdd:COG2114  104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  421 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 500
Cdd:COG2114  184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  501 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 576
Cdd:COG2114  256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 34486092  577 -LRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEP 622
Cdd:COG2114  336 sEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
984-1253 5.35e-30

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 124.15  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  984 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1055
Cdd:COG2114  137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1056 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1133
Cdd:COG2114  217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1134 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1208
Cdd:COG2114  280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 34486092 1209 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1253
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: 705.23  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092      1 MSGSKSVSPPGYAAqktaaPAPRGGPEHRSAWGEADSRANGYPHAPGgSARGSTKKpggavtpqqQQRLASRWRSDDDDD 80
Cdd:pfam16214    1 MSRSNSVSPPGYGA-----PAPRGGTEHRSAWGEAESRANGYPYAPG-SARSSTKK---------QQRLASRWRSEDDDD 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     81 PPLSGDDPLAGGFGFSFRSKSAWQERGgDDCGRGSRRQRRGAASGGSTRAPPAGGGggsaaaaasaggTEVRPRSVEVGL 160
Cdd:pfam16214   66 PPLSGSDPLSGGFGFSFRSKSAWQEHG-GESRRQRTRAPPAGGGPGSAAAAASRGG------------GEVRPRSVELGL 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    161 EERRGKGRAADELEAGAveggegsgdggssadSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQS 240
Cdd:pfam16214  133 EERRGKGRAAEGGEGSG---------------DGGSSAPEVVFSLGACCLALLQIFRSKKFQSEKLERLYQRYFFRLNQS 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    241 SLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLP 320
Cdd:pfam16214  198 SLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYAVILVVLAVQVVGVLLV 277
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    321 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 400
Cdd:pfam16214  278 QPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPA 357
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 34486092    401 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 458
Cdd:pfam16214  358 EVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1062-1256 1.11e-73

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 242.53  E-value: 1.11e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1062 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEDRfrqLEKIKTIGSTYMAASGLNDSTYD 1141
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092   1142 kvgktHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVT 1221
Cdd:pfam00211   74 -----HARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 34486092   1222 TDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNG 1256
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
460-643 2.58e-69

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 230.21  E-value: 2.58e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    460 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 539
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    540 MGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGD-Y 618
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKTEgF 160
                          170       180
                   ....*....|....*....|....*.
gi 34486092    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 5.11e-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: 5.11e-62
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     424 ENQQQERLLLSVLPRHVAMEMKadinakqedMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 503
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK---------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092     504 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGMDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 581
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 34486092     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 2.07e-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: 2.07e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGMDMIE 546
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 34486092  547 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGKAGRIH 605
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1070-1254 2.78e-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: 178.54  E-value: 2.78e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1070 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAASGLNDSTYDkvgktHIK 1149
Cdd:cd07302    2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1150 ALADFAMKLMDQMKYINEH--SFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQV 1227
Cdd:cd07302   70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                        170       180
                 ....*....|....*....|....*...
gi 34486092 1228 LAANTYQLECRGVVKVKGK-GEMMTYFL 1254
Cdd:cd07302  150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
467-642 5.74e-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: 177.39  E-value: 5.74e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  467 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIE 546
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  547 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNG-DYEVEPg 623
Cdd:cd07302   81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                        170
                 ....*....|....*....
gi 34486092  624 cGGERNAYLKEHSIETFLI 642
Cdd:cd07302  160 -LGEVELKGKSGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1036-1237 4.73e-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: 4.73e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    1036 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEdr 1115
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    1116 fRQLEKIKTIGSTYMAASGLNDSTydkvGKTHIKALADFAMKLMDQMK-YINEHSFNNFQMKIGLNIGPVVAGVIGARKP 1194
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLPEEA----LVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 34486092    1195 QYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLEC 1237
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
668-761 7.44e-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: 7.44e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092    668 GHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDK----NAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLT 743
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRIGLPLADHIlqdrSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLK 80
                           90
                   ....*....|....*...
gi 34486092    744 FREPDLEKKYSKQVDDRF 761
Cdd:pfam06327   81 FKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
261-622 1.40e-38

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 149.57  E-value: 1.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  261 AARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIY 340
Cdd:COG2114   24 ALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  341 TLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLH 420
Cdd:COG2114  104 LLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  421 SQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHkiyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFAR 500
Cdd:COG2114  184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR--------EVTVLFADIVGFTALSERLGPEELVELLNRYFSA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  501 FDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG 576
Cdd:COG2114  256 MVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIG 335
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 34486092  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 ...
1069-1219 2.30e-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: 128.24  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1069 CVAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEDrfrQLEKIKTIGSTYMAASGLndstydkvgkTHI 1148
Cdd:cd07556    1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGL----------DHP 63
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34486092 1149 KALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARkPQYDIWGNTVNVASRMDSTGVPDRIQ 1219
Cdd:cd07556   64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
984-1253 5.35e-30

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 124.15  E-value: 5.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092  984 VALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNR--RLLHNILPKDVAAHFLAR------ 1055
Cdd:COG2114  137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERlrDLLGRYLPPEVAERLLAGgeelrl 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1056 --ERRNdelyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEdrfRQLEKIKTIGSTYMAAS 1133
Cdd:COG2114  217 ggERRE----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVF 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34486092 1134 GLNDSTYDkvgktHIKALADFAMKLMDQMKYINEHSFNN----FQMKIGLNIGPVVAGVIGAR-KPQYDIWGNTVNVASR 1208
Cdd:COG2114  280 GAPVARED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAAR 354
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 34486092 1209 MDSTGVPDRIQVTTDMYQvLAANTYQLECRGVVKVKGKGEMMTYF 1253
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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