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Conserved domains on  [gi|1571052980|ref|NP_001355342|]
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adenylate cyclase type 6 isoform 2 [Mus musculus]

Protein Classification

adenylate/guanylate cyclase domain-containing protein( domain architecture ID 11069805)

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

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

Graphical summary

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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 ...
14-366 2.29e-120

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: 377.81  E-value: 2.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   14 ERKTAWGER----NGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHT------------RCPWQDE---------- 67
Cdd:pfam16214   22 EHRSAWGEAesraNGYPYAPGSARSSTKKQQRLASRWRSEDDDDPPLSGSDplsggfgfsfrsKSAWQEHggesrrqrtr 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   68 --------AFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGP-------SCWHRLVQVFQSKQFRSA 132
Cdd:pfam16214  102 appagggpGSAAAAASRGGGEVRPRSVELGLEERRGKGRAAEGGEGSGDGGSSAPevvfslgACCLALLQIFRSKKFQSE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  133 KLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYV 212
Cdd:pfam16214  182 KLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYA 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  213 VLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVV 292
Cdd:pfam16214  262 VILVVLAVQVVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVL 341
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571052980  293 LFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFH 366
Cdd:pfam16214  342 IFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
968-1162 1.33e-71

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 236.37  E-value: 1.33e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  968 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEerfRQLEKIKTIGSTYMAASGLnastyD 1047
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDK---HKVYKVKTIGDAYMVVSGL-----P 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1048 QVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVT 1127
Cdd:pfam00211   69 EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1571052980 1128 TDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNG 1162
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
368-552 2.15e-70

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.90  E-value: 2.15e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  368 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 447
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  448 MGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLN---- 523
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1571052980  524 -----GDYEVePGRGGernaylkeqcIETFLILG 552
Cdd:pfam00211  161 efterGEIEV-KGKGK----------MKTYFLNG 183
Adcy_cons_dom super family cl05691
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
580-667 1.38e-19

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.


The actual alignment was detected with superfamily member pfam06327:

Pssm-ID: 461877  Cd Length: 98  Bit Score: 84.88  E-value: 1.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  580 PRWVPDRAF----SRTKDSKAFRQMGID--DSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQRE 653
Cdd:pfam06327    5 ESWGAERPFanlnHRESVSSEMTRIGLPlaDHILQDRSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLKFKEK 84
                           90
                   ....*....|....
gi 1571052980  654 DLEKKYSRKVDPRF 667
Cdd:pfam06327   85 SLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
14-366 2.29e-120

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: 377.81  E-value: 2.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   14 ERKTAWGER----NGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHT------------RCPWQDE---------- 67
Cdd:pfam16214   22 EHRSAWGEAesraNGYPYAPGSARSSTKKQQRLASRWRSEDDDDPPLSGSDplsggfgfsfrsKSAWQEHggesrrqrtr 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   68 --------AFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGP-------SCWHRLVQVFQSKQFRSA 132
Cdd:pfam16214  102 appagggpGSAAAAASRGGGEVRPRSVELGLEERRGKGRAAEGGEGSGDGGSSAPevvfslgACCLALLQIFRSKKFQSE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  133 KLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYV 212
Cdd:pfam16214  182 KLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYA 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  213 VLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVV 292
Cdd:pfam16214  262 VILVVLAVQVVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVL 341
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571052980  293 LFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFH 366
Cdd:pfam16214  342 IFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
968-1162 1.33e-71

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 236.37  E-value: 1.33e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  968 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEerfRQLEKIKTIGSTYMAASGLnastyD 1047
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDK---HKVYKVKTIGDAYMVVSGL-----P 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1048 QVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVT 1127
Cdd:pfam00211   69 EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1571052980 1128 TDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNG 1162
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
368-552 2.15e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.90  E-value: 2.15e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  368 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 447
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  448 MGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLN---- 523
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1571052980  524 -----GDYEVePGRGGernaylkeqcIETFLILG 552
Cdd:pfam00211  161 efterGEIEV-KGKGK----------MKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
332-527 9.17e-60

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: 203.26  E-value: 9.17e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   332 ENRQQERLLLSVLPQHVAMEMKEdintkkedmMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 411
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLKR---------GGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   412 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGVDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 489
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1571052980   490 FDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYE 527
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
375-550 6.25e-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: 6.25e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  375 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIE 454
Cdd:cd07302      1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  455 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNG-DYEVEPg 531
Cdd:cd07302     81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                          170
                   ....*....|....*....
gi 1571052980  532 rGGERNAYLKEQCIETFLI 550
Cdd:cd07302    160 -LGEVELKGKSGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
976-1160 2.64e-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: 175.46  E-value: 2.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  976 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEerfRQLEKIKTIGSTYMAASGLNASTYDqvgrsHIT 1055
Cdd:cd07302      2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1056 ALADYAMRLMEQMKHINEH--SFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQV 1133
Cdd:cd07302     70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                          170       180
                   ....*....|....*....|....*...
gi 1571052980 1134 LAAKGYQLECRGVVKVKGK-GEMTTYFL 1160
Cdd:cd07302    150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
942-1143 1.00e-46

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: 165.89  E-value: 1.00e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   942 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEer 1021
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  1022 fRQLEKIKTIGSTYMAASGL-NASTYDqvgrsHITALADYAMRLMEQMK-HINEHSFNNFQMKIGLNMGPVVAGVIGARK 1099
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLpEEALVD-----HAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1571052980  1100 PQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLEC 1143
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
208-555 1.27e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 143.79  E-value: 1.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  208 VVSYVVLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQL 287
Cdd:COG2114     64 LLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALAL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  288 GANVVLFLcTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHk 367
Cdd:COG2114    144 LLLLALAL-LLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR- 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  368 iyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 447
Cdd:COG2114    222 -------EVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVR 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  448 MGVDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYL 522
Cdd:COG2114    295 AALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLL 374
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1571052980  523 NGDYEVEPgrGGERNAYLKEQCIETFLILGASQ 555
Cdd:COG2114    375 RDRFEFRE--LGEVRLKGKAEPVEVYELLGAKE 405
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
814-1162 6.37e-31

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 126.84  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  814 FVGNVLLSLLASSVFLHISSIGKLAMTFILGFTYLVLLLLGPPAAIFDNYDLLLGVHGLASSNETFDGLDCPAVGRVALK 893
Cdd:COG2114     63 LLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  894 YMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLAR--------ERRN 965
Cdd:COG2114    143 LLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeelrlggERRE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  966 delyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEERfrqLEKIKTIGSTYMAASGLNAST 1045
Cdd:COG2114    223 ----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIERHG---GTVDKFIGDGVMAVFGAPVAR 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1046 YDqvgrsHITALADYAMRLMEQMKHINEHSFNN----FQMKIGLNMGPVVAGVIGAR-KPQYDIWGNTVNVSSRMDSTGV 1120
Cdd:COG2114    286 ED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESLAK 360
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1571052980 1121 PDRIQVTTDLYQvLAAKGYQLECRGVVKVKGKGE-MTTYFLNG 1162
Cdd:COG2114    361 PGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEpVEVYELLG 402
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
580-667 1.38e-19

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: 84.88  E-value: 1.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  580 PRWVPDRAF----SRTKDSKAFRQMGID--DSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQRE 653
Cdd:pfam06327    5 ESWGAERPFanlnHRESVSSEMTRIGLPlaDHILQDRSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLKFKEK 84
                           90
                   ....*....|....
gi 1571052980  654 DLEKKYSRKVDPRF 667
Cdd:pfam06327   85 SLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
14-366 2.29e-120

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: 377.81  E-value: 2.29e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   14 ERKTAWGER----NGQKRPRHANRASGFCAPRYMSCLKNAEPPSPTPAAHT------------RCPWQDE---------- 67
Cdd:pfam16214   22 EHRSAWGEAesraNGYPYAPGSARSSTKKQQRLASRWRSEDDDDPPLSGSDplsggfgfsfrsKSAWQEHggesrrqrtr 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   68 --------AFIRRAGPGRGVELGLRSVALGFDDTEVTTPMGTAEVAPDTSPRSGP-------SCWHRLVQVFQSKQFRSA 132
Cdd:pfam16214  102 appagggpGSAAAAASRGGGEVRPRSVELGLEERRGKGRAAEGGEGSGDGGSSAPevvfslgACCLALLQIFRSKKFQSE 181
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  133 KLERLYQRYFFQMNQSSLTLLMAVLVLLMAVLLTFHAAPAQPQPAYVALLTCASVLFVVLMVVCNRHSFRQDSMWVVSYV 212
Cdd:pfam16214  182 KLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARGPLQVPYVVVLSLAIGLILVLAVLCNRNAFHQDHMWLACYA 261
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  213 VLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQLGANVV 292
Cdd:pfam16214  262 VILVVLAVQVVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAVSLRTNAQDQFLLKQLVSNVL 341
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1571052980  293 LFLCTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFH 366
Cdd:pfam16214  342 IFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFH 415
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
968-1162 1.33e-71

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 236.37  E-value: 1.33e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  968 LYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEerfRQLEKIKTIGSTYMAASGLnastyD 1047
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALS----SRHSPEQVVRLLNELYTRFDRLLDK---HKVYKVKTIGDAYMVVSGL-----P 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1048 QVGRSHITALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVT 1127
Cdd:pfam00211   69 EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1571052980 1128 TDLYQVLAAKGYQLECRGVVKVKGKGEMTTYFLNG 1162
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
368-552 2.15e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.90  E-value: 2.15e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  368 IYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 447
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  448 MGVDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLN---- 523
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKtegf 160
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1571052980  524 -----GDYEVePGRGGernaylkeqcIETFLILG 552
Cdd:pfam00211  161 efterGEIEV-KGKGK----------MKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
332-527 9.17e-60

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: 203.26  E-value: 9.17e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   332 ENRQQERLLLSVLPQHVAMEMKEdintkkedmMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDK 411
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLKR---------GGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQ 72
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   412 LAAENHCLRIKILGDCYYCVSGLPEAR-ADHAHCCVEMGVDMIEAI-SLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQ 489
Cdd:smart00044   73 IIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMPR 152
                           170       180       190
                    ....*....|....*....|....*....|....*...
gi 1571052980   490 FDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNGDYE 527
Cdd:smart00044  153 YCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
375-550 6.25e-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: 6.25e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  375 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGVDMIE 454
Cdd:cd07302      1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  455 AISLVRE--VTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYLNG-DYEVEPg 531
Cdd:cd07302     81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDaGFEFEE- 159
                          170
                   ....*....|....*....
gi 1571052980  532 rGGERNAYLKEQCIETFLI 550
Cdd:cd07302    160 -LGEVELKGKSGPVRVYRL 177
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
375-513 1.11e-50

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: 174.85  E-value: 1.11e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  375 NVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGlpearADHAHCCVEMGVDMIE 454
Cdd:cd07556      1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1571052980  455 AISLVREVTGVNVNMRVGIHSGRVHCGVLGLRkWQFDVWSNDVTLANHMEAGGRAGRIH 513
Cdd:cd07556     76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
976-1160 2.64e-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: 175.46  E-value: 2.64e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  976 VAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEerfRQLEKIKTIGSTYMAASGLNASTYDqvgrsHIT 1055
Cdd:cd07302      2 VTVLFADIVGFTALSERLGP----EELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHED-----HAE 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1056 ALADYAMRLMEQMKHINEH--SFNNFQMKIGLNMGPVVAGVIGARKPQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQV 1133
Cdd:cd07302     70 RAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYEL 149
                          170       180
                   ....*....|....*....|....*...
gi 1571052980 1134 LAAKGYQLECRGVVKVKGK-GEMTTYFL 1160
Cdd:cd07302    150 LGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
942-1143 1.00e-46

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: 165.89  E-value: 1.00e-46
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980   942 NRRLLHNILPKDVAAHFLARERRndeLYYQSCECVAVMFASIANFSEFYveleANNEGVECLRLLNEIIADFDEIISEer 1021
Cdd:smart00044    6 TDRLLDQLLPASVAEQLKRGGSP---VPAESYDNVTILFSDIVGFTSLC----STSTPEQVVNLLNDLYSRFDQIIDR-- 76
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  1022 fRQLEKIKTIGSTYMAASGL-NASTYDqvgrsHITALADYAMRLMEQMK-HINEHSFNNFQMKIGLNMGPVVAGVIGARK 1099
Cdd:smart00044   77 -HGGYKVKTIGDAYMVASGLpEEALVD-----HAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....
gi 1571052980  1100 PQYDIWGNTVNVSSRMDSTGVPDRIQVTTDLYQVLAAKGYQLEC 1143
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFVF 194
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
208-555 1.27e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 143.79  E-value: 1.27e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  208 VVSYVVLGILAAVQVGGALAANPHSPSAGLWCPVFFVYITYTLLPIRMRAAVLSGLGLSTLHLILAWQLNSSDPFLWKQL 287
Cdd:COG2114     64 LLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALAL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  288 GANVVLFLcTNAIGVCTHYPAEVSQRQAFQETRGYIQARLHLQHENRQQERLLLSVLPQHVAMEMKEDINTKKEDMMFHk 367
Cdd:COG2114    144 LLLLALAL-LLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERR- 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  368 iyiqkhdNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVE 447
Cdd:COG2114    222 -------EVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVR 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  448 MGVDMIEAI----SLVREVTGVNVNMRVGIHSGRVHCGVLG-LRKWQFDVWSNDVTLANHMEAGGRAGRIHITRATLQYL 522
Cdd:COG2114    295 AALAMQEALaelnAELPAEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLL 374
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1571052980  523 NGDYEVEPgrGGERNAYLKEQCIETFLILGASQ 555
Cdd:COG2114    375 RDRFEFRE--LGEVRLKGKAEPVEVYELLGAKE 405
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
975-1125 1.38e-32

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: 123.24  E-value: 1.38e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  975 CVAVMFASIANFSEFYVELEAnnegVECLRLLNEIIADFDEIISEErfrQLEKIKTIGSTYMAASGLNastydqvgrsHI 1054
Cdd:cd07556      1 PVTILFADIVGFTSLADALGP----DEGDELLNELAGRFDSLIRRS---GDLKIKTIGDEFMVVSGLD----------HP 63
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1571052980 1055 TALADYAMRLMEQMKHINEHSFNNFQMKIGLNMGPVVAGVIGARkPQYDIWGNTVNVSSRMDSTGVPDRIQ 1125
Cdd:cd07556     64 AAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
814-1162 6.37e-31

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 126.84  E-value: 6.37e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  814 FVGNVLLSLLASSVFLHISSIGKLAMTFILGFTYLVLLLLGPPAAIFDNYDLLLGVHGLASSNETFDGLDCPAVGRVALK 893
Cdd:COG2114     63 LLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALA 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  894 YMTPVILLVFALALYLHAQQVESTARLDFLWKLQATGEKEEMEELQAYNRRLLHNILPKDVAAHFLAR--------ERRN 965
Cdd:COG2114    143 LLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeelrlggERRE 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  966 delyyqscecVAVMFASIANFSEFYVELEAnnEGVecLRLLNEIIADFDEIISEERfrqLEKIKTIGSTYMAASGLNAST 1045
Cdd:COG2114    223 ----------VTVLFADIVGFTALSERLGP--EEL--VELLNRYFSAMVEIIERHG---GTVDKFIGDGVMAVFGAPVAR 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980 1046 YDqvgrsHITALADYAMRLMEQMKHINEHSFNN----FQMKIGLNMGPVVAGVIGAR-KPQYDIWGNTVNVSSRMDSTGV 1120
Cdd:COG2114    286 ED-----HAERAVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESLAK 360
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1571052980 1121 PDRIQVTTDLYQvLAAKGYQLECRGVVKVKGKGE-MTTYFLNG 1162
Cdd:COG2114    361 PGEILVSEATYD-LLRDRFEFRELGEVRLKGKAEpVEVYELLG 402
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
580-667 1.38e-19

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: 84.88  E-value: 1.38e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1571052980  580 PRWVPDRAF----SRTKDSKAFRQMGID--DSSKDNRGAQDALNPEDEVDEFLGRAIDARSIDQLRKDHVRRFLLTFQRE 653
Cdd:pfam06327    5 ESWGAERPFanlnHRESVSSEMTRIGLPlaDHILQDRSASPVARLEEEIDEFIEQAIDGRSSDKLRSEDINPFTLKFKEK 84
                           90
                   ....*....|....
gi 1571052980  654 DLEKKYSRKVDPRF 667
Cdd:pfam06327   85 SLEKKYRQLRDPRF 98
 
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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