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Conserved domains on  [gi|1034103813|ref|XP_016781416|]
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adenylate cyclase type 4 isoform X3 [Pan troglodytes]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-418 1.15e-64

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 215.95  E-value: 1.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034103813 344 MGLDMCRAIRKLRAATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL 418
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL 155
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
68-453 1.99e-45

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 169.21  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  68 ALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLA 147
Cdd:COG2114    39 LLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 148 SSLSHLLVLGLYLGPQPDSRPALLPQLAANAVLFLCGNVAGVYHKALMERALRATFREALSSLHSRRRldtEKKHQEHLL 227
Cdd:COG2114   119 LLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALR---ERERLRDLL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 228 LSILPAYLAREMKAEIMARLQAGQgsrpestnnfhslyvkrHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQ 307
Cdd:COG2114   196 GRYLPPEVAERLLAGGEELRLGGE-----------------RREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVE 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 308 IAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKL----RAATGVDINMRVGVHSGSVLCGVIG-LQ 382
Cdd:COG2114   259 IIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsED 338
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034103813 383 KWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVEDAGMEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114   339 RLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELGEVR----LKGKAEPveVYELLGAKEAA 407
Nucleotidyl_cyc_III super family cl11967
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
864-986 1.13e-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.


The actual alignment was detected with superfamily member pfam00211:

Pssm-ID: 448371  Cd Length: 183  Bit Score: 130.83  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 864 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 943
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034103813 944 daqqdAERSCSHLGTMVEFAMALGSKLDVINKHSFNNFRLRVG 986
Cdd:pfam00211  68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVG 105
Adcy_cons_dom super family cl05691
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-584 3.02e-34

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: 126.48  E-value: 3.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 479 TRYLESWGAAKPFAHLSHGDSPVSTSTPLPeKTLASFSTQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQS 557
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIG-LPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RS 71
                          90       100
                  ....*....|....*....|....*..
gi 1034103813 558 KDFNPLTLYFREKEMEKEYRLSAIPAF 584
Cdd:pfam06327  72 EDINPFTLKFKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-418 1.15e-64

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 215.95  E-value: 1.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034103813 344 MGLDMCRAIRKLRAATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL 418
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL 155
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 1.92e-57

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: 195.94  E-value: 1.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqgsrpestNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIR-KLRAATGVDINMRVGVHSGSVLC 376
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034103813  377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-428 1.01e-54

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: 187.79  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302     2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 352 IRKLRA--ATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGA-YAVEDAG 428
Cdd:cd07302    82 LAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEFEELG 161
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
68-453 1.99e-45

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 169.21  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  68 ALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLA 147
Cdd:COG2114    39 LLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 148 SSLSHLLVLGLYLGPQPDSRPALLPQLAANAVLFLCGNVAGVYHKALMERALRATFREALSSLHSRRRldtEKKHQEHLL 227
Cdd:COG2114   119 LLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALR---ERERLRDLL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 228 LSILPAYLAREMKAEIMARLQAGQgsrpestnnfhslyvkrHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQ 307
Cdd:COG2114   196 GRYLPPEVAERLLAGGEELRLGGE-----------------RREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVE 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 308 IAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKL----RAATGVDINMRVGVHSGSVLCGVIG-LQ 382
Cdd:COG2114   259 IIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsED 338
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034103813 383 KWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVEDAGMEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114   339 RLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELGEVR----LKGKAEPveVYELLGAKEAA 407
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
864-986 1.13e-34

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 130.83  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 864 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 943
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034103813 944 daqqdAERSCSHLGTMVEFAMALGSKLDVINKHSFNNFRLRVG 986
Cdd:pfam00211  68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVG 105
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-584 3.02e-34

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: 126.48  E-value: 3.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 479 TRYLESWGAAKPFAHLSHGDSPVSTSTPLPeKTLASFSTQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQS 557
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIG-LPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RS 71
                          90       100
                  ....*....|....*....|....*..
gi 1034103813 558 KDFNPLTLYFREKEMEKEYRLSAIPAF 584
Cdd:pfam06327  72 EDINPFTLKFKEKSLEKKYRQLRDPRF 98
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
871-986 1.57e-20

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: 88.57  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 871 CVCVLFASVPDFKEFYSESNinheGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNatsgqdaqqdae 950
Cdd:cd07556     1 PVTILFADIVGFTSLADALG----PDEGDELLNELAGRFDSLIRR---SGDLKIKTIGDEFMVVSGLD------------ 61
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034103813 951 rscsHLGTMVEFAMALGSKLDVINKHSFNNFRLRVG 986
Cdd:cd07556    62 ----HPAAAVAFAEDMREAVSALNQSEGNPVRVRIG 93
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
827-986 9.65e-20

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: 88.08  E-value: 9.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  827 EREETETmenltrlLLENVLPAHVAPQFIgQNRRNEdlYHQSYECVCVLFASVPDFKEFYSESninhEGLECLRLLNEII 906
Cdd:smart00044   2 EKKKTDR-------LLDQLLPASVAEQLK-RGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  907 ADFDELLSKpkfSGVEKIKTIGSTYMAATGL-NATSGQDAQQDAERScshLGtMVEFAMAlgskldVINKHSFNNFRLRV 985
Cdd:smart00044  68 SRFDQIIDR---HGGYKVKTIGDAYMVASGLpEEALVDHAELIADEA---LD-MVEELKT------VLVQHREEGLRVRI 134

                   .
gi 1034103813  986 G 986
Cdd:smart00044 135 G 135
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 3.88e-17

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: 85.06  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 115 SAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVlGLYLGPQpDSrpALLPQLAANAVLFLCGNVAGVYHKAL 194
Cdd:pfam16214 281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-SLRTNAQ-DQ--FLLKQLVSNVLIFSCTNIVGVCTHYP 356
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034103813 195 MERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMAR 246
Cdd:pfam16214 357 AEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAK 408
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
763-986 6.00e-03

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 40.17  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 763 AWLSECLIVRLYLGPLDSRPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRLLL 842
Cdd:COG2114   116 LLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 843 ENVLPAHVApQFIGQNRRNEDLYHQSYEcVCVLFAsvpDFKEF--YSESnINHEGLecLRLLNEIIADFDELLSKpkfSG 920
Cdd:COG2114   196 GRYLPPEVA-ERLLAGGEELRLGGERRE-VTVLFA---DIVGFtaLSER-LGPEEL--VELLNRYFSAMVEIIER---HG 264
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 921 VEKIKTIGSTYMAATGLNATSGQDAQQdaerscshlgtMVEFAMALGSKLDVINKHSFNN----FRLRVG 986
Cdd:COG2114   265 GTVDKFIGDGVMAVFGAPVAREDHAER-----------AVRAALAMQEALAELNAELPAEggppLRVRIG 323
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-418 1.15e-64

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 215.95  E-value: 1.15e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034103813 344 MGLDMCRAIRKLRAATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL 418
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL 155
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 1.92e-57

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: 195.94  E-value: 1.92e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqgsrpestNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIR-KLRAATGVDINMRVGVHSGSVLC 376
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKtVLVQHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034103813  377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-428 1.01e-54

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: 187.79  E-value: 1.01e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302     2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 352 IRKLRA--ATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGA-YAVEDAG 428
Cdd:cd07302    82 LAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAgFEFEELG 161
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
68-453 1.99e-45

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 169.21  E-value: 1.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  68 ALGGFSLLLGLASREQRLQRWTRPLSGLVWVALLALGHAFLFTGGVVSAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLA 147
Cdd:COG2114    39 LLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 148 SSLSHLLVLGLYLGPQPDSRPALLPQLAANAVLFLCGNVAGVYHKALMERALRATFREALSSLHSRRRldtEKKHQEHLL 227
Cdd:COG2114   119 LLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALR---ERERLRDLL 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 228 LSILPAYLAREMKAEIMARLQAGQgsrpestnnfhslyvkrHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQ 307
Cdd:COG2114   196 GRYLPPEVAERLLAGGEELRLGGE-----------------RREVTVLFADIVGFTALSERLGPEELVELLNRYFSAMVE 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 308 IAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIRKL----RAATGVDINMRVGVHSGSVLCGVIG-LQ 382
Cdd:COG2114   259 IIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelPAEGGPPLRVRIGIHTGEVVVGNIGsED 338
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034103813 383 KWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVEDAGMEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114   339 RLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELGEVR----LKGKAEPveVYELLGAKEAA 407
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
272-409 1.66e-41

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: 148.27  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGlplslPDHAINCVRMGLDMCRA 351
Cdd:cd07556     2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034103813 352 IRKLRAATGVDINMRVGVHSGSVLCGVIGLqKWQYDVWSHDVTLANHMEAGGVPGRVH 409
Cdd:cd07556    77 VSALNQSEGNPVRVRIGIHTGPVVVGVIGS-RPQYDVWGALVNLASRMESQAKAGQVL 133
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
864-986 1.13e-34

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 130.83  E-value: 1.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 864 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 943
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034103813 944 daqqdAERSCSHLGTMVEFAMALGSKLDVINKHSFNNFRLRVG 986
Cdd:pfam00211  68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVG 105
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-584 3.02e-34

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: 126.48  E-value: 3.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 479 TRYLESWGAAKPFAHLSHGDSPVSTSTPLPeKTLASFSTQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQS 557
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRIG-LPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RS 71
                          90       100
                  ....*....|....*....|....*..
gi 1034103813 558 KDFNPLTLYFREKEMEKEYRLSAIPAF 584
Cdd:pfam06327  72 EDINPFTLKFKEKSLEKKYRQLRDPRF 98
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
871-986 1.57e-20

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: 88.57  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 871 CVCVLFASVPDFKEFYSESNinheGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNatsgqdaqqdae 950
Cdd:cd07556     1 PVTILFADIVGFTSLADALG----PDEGDELLNELAGRFDSLIRR---SGDLKIKTIGDEFMVVSGLD------------ 61
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034103813 951 rscsHLGTMVEFAMALGSKLDVINKHSFNNFRLRVG 986
Cdd:cd07556    62 ----HPAAAVAFAEDMREAVSALNQSEGNPVRVRIG 93
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
827-986 9.65e-20

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: 88.08  E-value: 9.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  827 EREETETmenltrlLLENVLPAHVAPQFIgQNRRNEdlYHQSYECVCVLFASVPDFKEFYSESninhEGLECLRLLNEII 906
Cdd:smart00044   2 EKKKTDR-------LLDQLLPASVAEQLK-RGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLY 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813  907 ADFDELLSKpkfSGVEKIKTIGSTYMAATGL-NATSGQDAQQDAERScshLGtMVEFAMAlgskldVINKHSFNNFRLRV 985
Cdd:smart00044  68 SRFDQIIDR---HGGYKVKTIGDAYMVASGLpEEALVDHAELIADEA---LD-MVEELKT------VLVQHREEGLRVRI 134

                   .
gi 1034103813  986 G 986
Cdd:smart00044 135 G 135
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 3.88e-17

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: 85.06  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 115 SAWDQVSYFLFVIFTAYAMLPLGMRDAAVAGLASSLSHLLVlGLYLGPQpDSrpALLPQLAANAVLFLCGNVAGVYHKAL 194
Cdd:pfam16214 281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-SLRTNAQ-DQ--FLLKQLVSNVLIFSCTNIVGVCTHYP 356
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034103813 195 MERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMAR 246
Cdd:pfam16214 357 AEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAK 408
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
872-986 1.02e-13

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: 70.30  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 872 VCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNATSGQDAQQdaer 951
Cdd:cd07302     2 VTVLFADIVGFTALSER----LGPEELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHEDHAER---- 70
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1034103813 952 scshlgtMVEFAMALGSKLDVINKH--SFNNFRLRVG 986
Cdd:cd07302    71 -------AVRAALEMQEALAELNAEreGGPPLRLRIG 100
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
763-986 6.00e-03

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 40.17  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 763 AWLSECLIVRLYLGPLDSRPGVLKEPKLMGAISFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRLLL 842
Cdd:COG2114   116 LLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 843 ENVLPAHVApQFIGQNRRNEDLYHQSYEcVCVLFAsvpDFKEF--YSESnINHEGLecLRLLNEIIADFDELLSKpkfSG 920
Cdd:COG2114   196 GRYLPPEVA-ERLLAGGEELRLGGERRE-VTVLFA---DIVGFtaLSER-LGPEEL--VELLNRYFSAMVEIIER---HG 264
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034103813 921 VEKIKTIGSTYMAATGLNATSGQDAQQdaerscshlgtMVEFAMALGSKLDVINKHSFNN----FRLRVG 986
Cdd:COG2114   265 GTVDKFIGDGVMAVFGAPVAREDHAER-----------AVRAALAMQEALAELNAELPAEggppLRVRIG 323
 
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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