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Conserved domains on  [gi|17978250|ref|NP_536683|]
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adenylate cyclase type 4 [Mus musculus]

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
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
866-1065 3.18e-78

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 254.09  E-value: 3.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    866 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 945
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    946 dtqqdSERSCSHLGTMVEFAVALGSKLGVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVL 1025
Cdd:pfam00211   68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVP 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 17978250   1026 GKIQVTEETARALQSLGYTCYSRGSIKVKGKGELCTYFLN 1065
Cdd:pfam00211  143 GKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLN 182
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-447 4.44e-65

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 217.50  E-value: 4.44e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGaya 423
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKT--- 157
                          170       180
                   ....*....|....*....|....*.
gi 17978250    424 vERADTEHRDPY-LRELGEP-TYLVI 447
Cdd:pfam00211  158 -EGFEFTERGEIeVKGKGKMkTYFLN 182
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 3.54e-46

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 171.53  E-value: 3.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250   40 ALVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWVALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWQPESQRALLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQRSRpentnnfhslyvkrhqgVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------------VT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 17978250  429 TEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114  385 EVR----LKGKAEPveVYELLGAKEAA 407
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-581 1.09e-35

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: 130.71  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    479 TRYLESWGAAKPFAHLSHLDSPVSTSTP--LPEKAFSPQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                           90       100
                   ....*....|....*....|....*.
gi 17978250    556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327   73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
866-1065 3.18e-78

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 254.09  E-value: 3.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    866 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 945
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    946 dtqqdSERSCSHLGTMVEFAVALGSKLGVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVL 1025
Cdd:pfam00211   68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVP 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 17978250   1026 GKIQVTEETARALQSLGYTCYSRGSIKVKGKGELCTYFLN 1065
Cdd:pfam00211  143 GKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLN 182
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-447 4.44e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 217.50  E-value: 4.44e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGaya 423
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKT--- 157
                          170       180
                   ....*....|....*....|....*.
gi 17978250    424 vERADTEHRDPY-LRELGEP-TYLVI 447
Cdd:pfam00211  158 -EGFEFTERGEIeVKGKGKMkTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 1.83e-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: 196.32  E-value: 1.83e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqrsrpentNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIRKLRV-ATGVDINMRVGVHSGSVLC 376
Cdd:smart00044   64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 17978250     377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044  144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-446 3.04e-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: 186.63  E-value: 3.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  352 IRKL--RVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAyaveRADT 429
Cdd:cd07302   82 LAELnaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA----GFEF 157
                        170       180
                 ....*....|....*....|
gi 17978250  430 EHRDPY-LRELGEP--TYLV 446
Cdd:cd07302  158 EELGEVeLKGKSGPvrVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
829-1044 2.60e-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: 173.21  E-value: 2.60e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     829 EREETETmenltrlLLENVLPAHVAPQFIgQNRRNEdlYHQSYECVCVLFASVPDFKEFYSESninhEGLECLRLLNEII 908
Cdd:smart00044    2 EKKKTDR-------LLDQLLPASVAEQLK-RGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLY 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     909 ADFDELLSKpkfSGVEKIKTIGSTYMAATGLnATSgqDTQQDSERSCSHLGTMVEFAValgsklGVINKHSFNNFRLRVG 988
Cdd:smart00044   68 SRFDQIIDR---HGGYKVKTIGDAYMVASGL-PEE--ALVDHAELIADEALDMVEELK------TVLVQHREEGLRVRIG 135
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 17978250     989 LNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVTEETARALQSLGYT 1044
Cdd:smart00044  136 IHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQ 191
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
874-1064 2.91e-49

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: 172.38  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  874 VCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNATSGQDTQQdser 953
Cdd:cd07302    2 VTVLFADIVGFTALSER----LGPEELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHEDHAER---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  954 scshlgtMVEFAVALGSKLGVINKH--SFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVT 1031
Cdd:cd07302   71 -------AVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVS 143
                        170       180       190
                 ....*....|....*....|....*....|....
gi 17978250 1032 EETARALQSLGYTCYSRGSIKVKGK-GELCTYFL 1064
Cdd:cd07302  144 EATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 3.54e-46

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 171.53  E-value: 3.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250   40 ALVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWVALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWQPESQRALLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQRSRpentnnfhslyvkrhqgVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------------VT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 17978250  429 TEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114  385 EVR----LKGKAEPveVYELLGAKEAA 407
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-581 1.09e-35

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: 130.71  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    479 TRYLESWGAAKPFAHLSHLDSPVSTSTP--LPEKAFSPQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                           90       100
                   ....*....|....*....|....*.
gi 17978250    556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327   73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
792-1058 3.18e-26

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 112.59  E-value: 3.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  792 LMGAIYFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRLLLENVLPAHVApQFIGQNRRNEDLYHQSY 871
Cdd:COG2114  143 LLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVA-ERLLAGGEELRLGGERR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  872 EcVCVLFAsvpDFKEF--YSESnINHEGLecLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGlnatSGQDTQQ 949
Cdd:COG2114  222 E-VTVLFA---DIVGFtaLSER-LGPEEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVFG----APVARED 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  950 DSERscshlgtMVEFAVALGSKLGVINKHSFNN----FRLRVGLNHGPVVAGVIGA-QKPQYDIWGNTVNVASRMESTGV 1024
Cdd:COG2114  288 HAER-------AVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSeDRLDYTVIGDTVNLAARLESLAK 360
                        250       260       270
                 ....*....|....*....|....*....|....
gi 17978250 1025 LGKIQVTEETARALQSlGYTCYSRGSIKVKGKGE 1058
Cdd:COG2114  361 PGEILVSEATYDLLRD-RFEFRELGEVRLKGKAE 393
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 7.36e-19

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: 90.45  E-value: 7.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    115 SAWDQVSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVlglylGWQPESQ-RALLPQLAANAVLFLCGNVVGAYHKA 193
Cdd:pfam16214  281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-----SLRTNAQdQFLLKQLVSNVLIFSCTNIVGVCTHY 355
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17978250    194 LMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMAR 246
Cdd:pfam16214  356 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAK 408
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
866-1065 3.18e-78

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 254.09  E-value: 3.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    866 LYHQSYECVCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKPKfsgVEKIKTIGSTYMAATGLnatsgq 945
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSR----HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGL------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    946 dtqqdSERSCSHLGTMVEFAVALGSKLGVINKHSFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVL 1025
Cdd:pfam00211   68 -----PEPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVP 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 17978250   1026 GKIQVTEETARALQSLGYTCYSRGSIKVKGKGELCTYFLN 1065
Cdd:pfam00211  143 GKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLN 182
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-447 4.44e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 217.50  E-value: 4.44e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGaya 423
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLKT--- 157
                          170       180
                   ....*....|....*....|....*.
gi 17978250    424 vERADTEHRDPY-LRELGEP-TYLVI 447
Cdd:pfam00211  158 -EGFEFTERGEIeVKGKGKMkTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 1.83e-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: 196.32  E-value: 1.83e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqrsrpentNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIRKLRV-ATGVDINMRVGVHSGSVLC 376
Cdd:smart00044   64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*.
gi 17978250     377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044  144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-446 3.04e-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: 186.63  E-value: 3.04e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  352 IRKL--RVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAyaveRADT 429
Cdd:cd07302   82 LAELnaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA----GFEF 157
                        170       180
                 ....*....|....*....|
gi 17978250  430 EHRDPY-LRELGEP--TYLV 446
Cdd:cd07302  158 EELGEVeLKGKSGPvrVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
829-1044 2.60e-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: 173.21  E-value: 2.60e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     829 EREETETmenltrlLLENVLPAHVAPQFIgQNRRNEdlYHQSYECVCVLFASVPDFKEFYSESninhEGLECLRLLNEII 908
Cdd:smart00044    2 EKKKTDR-------LLDQLLPASVAEQLK-RGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLY 67
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250     909 ADFDELLSKpkfSGVEKIKTIGSTYMAATGLnATSgqDTQQDSERSCSHLGTMVEFAValgsklGVINKHSFNNFRLRVG 988
Cdd:smart00044   68 SRFDQIIDR---HGGYKVKTIGDAYMVASGL-PEE--ALVDHAELIADEALDMVEELK------TVLVQHREEGLRVRIG 135
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 17978250     989 LNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVTEETARALQSLGYT 1044
Cdd:smart00044  136 IHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQ 191
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
874-1064 2.91e-49

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: 172.38  E-value: 2.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  874 VCVLFASVPDFKEFYSEsninHEGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNATSGQDTQQdser 953
Cdd:cd07302    2 VTVLFADIVGFTALSER----LGPEELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGAHEDHAER---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  954 scshlgtMVEFAVALGSKLGVINKH--SFNNFRLRVGLNHGPVVAGVIGAQKPQYDIWGNTVNVASRMESTGVLGKIQVT 1031
Cdd:cd07302   71 -------AVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVS 143
                        170       180       190
                 ....*....|....*....|....*....|....
gi 17978250 1032 EETARALQSLGYTCYSRGSIKVKGK-GELCTYFL 1064
Cdd:cd07302  144 EATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 3.54e-46

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 171.53  E-value: 3.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250   40 ALVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWVALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWQPESQRALLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQRSRpentnnfhslyvkrhqgVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------------VT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 17978250  429 TEHrdpyLRELGEP--TYLVIDPRAEE 453
Cdd:COG2114  385 EVR----LKGKAEPveVYELLGAKEAA 407
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
272-409 4.17e-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: 147.50  E-value: 4.17e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGlplslPDHAINCVRMGLDMCRA 351
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 17978250  352 IRKLRVATGVDINMRVGVHSGSVLCGVIGLqKWQYDVWSHDVTLANHMEAGGVPGRVH 409
Cdd:cd07556   77 VSALNQSEGNPVRVRIGIHTGPVVVGVIGS-RPQYDVWGALVNLASRMESQAKAGQVL 133
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
873-1029 1.07e-39

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: 143.27  E-value: 1.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  873 CVCVLFASVPDFKEFYSESNinheGLECLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGLNatsgqdtqqdse 952
Cdd:cd07556    1 PVTILFADIVGFTSLADALG----PDEGDELLNELAGRFDSLIRR---SGDLKIKTIGDEFMVVSGLD------------ 61
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17978250  953 rscsHLGTMVEFAVALGSKLGVINKHSFNNFRLRVGLNHGPVVAGVIGAqKPQYDIWGNTVNVASRMESTGVLGKIQ 1029
Cdd:cd07556   62 ----HPAAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGS-RPQYDVWGALVNLASRMESQAKAGQVL 133
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-581 1.09e-35

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: 130.71  E-value: 1.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    479 TRYLESWGAAKPFAHLSHLDSPVSTSTP--LPEKAFSPQwslDRSRTPRG-LDDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                           90       100
                   ....*....|....*....|....*.
gi 17978250    556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327   73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
792-1058 3.18e-26

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 112.59  E-value: 3.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  792 LMGAIYFFIFFFTLLVLARQNEYYCRLDFLWKKKLRQEREETETMENLTRLLLENVLPAHVApQFIGQNRRNEDLYHQSY 871
Cdd:COG2114  143 LLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVA-ERLLAGGEELRLGGERR 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  872 EcVCVLFAsvpDFKEF--YSESnINHEGLecLRLLNEIIADFDELLSKpkfSGVEKIKTIGSTYMAATGlnatSGQDTQQ 949
Cdd:COG2114  222 E-VTVLFA---DIVGFtaLSER-LGPEEL--VELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVFG----APVARED 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250  950 DSERscshlgtMVEFAVALGSKLGVINKHSFNN----FRLRVGLNHGPVVAGVIGA-QKPQYDIWGNTVNVASRMESTGV 1024
Cdd:COG2114  288 HAER-------AVRAALAMQEALAELNAELPAEggppLRVRIGIHTGEVVVGNIGSeDRLDYTVIGDTVNLAARLESLAK 360
                        250       260       270
                 ....*....|....*....|....*....|....
gi 17978250 1025 LGKIQVTEETARALQSlGYTCYSRGSIKVKGKGE 1058
Cdd:COG2114  361 PGEILVSEATYDLLRD-RFEFRELGEVRLKGKAE 393
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 7.36e-19

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: 90.45  E-value: 7.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17978250    115 SAWDQVSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVlglylGWQPESQ-RALLPQLAANAVLFLCGNVVGAYHKA 193
Cdd:pfam16214  281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-----SLRTNAQdQFLLKQLVSNVLIFSCTNIVGVCTHY 355
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 17978250    194 LMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMAR 246
Cdd:pfam16214  356 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAK 408
 
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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