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Conserved domains on  [gi|149064013|gb|EDM14283|]
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adenylate cyclase 4, isoform CRA_b [Rattus norvegicus]

Protein Classification

CHD and DUF1053 domain-containing protein( domain architecture ID 11069821)

protein containing domains AC_N, CHD, and DUF1053

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;
264-430 5.50e-66

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 5.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL--AGA 421
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLktEGF 160

                  ....*....
gi 149064013  422 YAVERADME 430
Cdd:pfam00211 161 EFTERGEIE 169
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 1.01e-43

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 163.82  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  40 AIVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWAALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWRPESQRDLLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQssrpentnnfhslyvkrHQGVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGE-----------------RREVT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 149064013 429 MEHrdpyLRELGEP--TYLVIDPWAEE 453
Cdd:COG2114  385 EVR----LKGKAEPveVYELLGAKEAA 407
Adcy_cons_dom super family cl05691
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-581 4.04e-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: 125.71  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  479 TRYLESWGAAKPFAHLSHVDSPASTSTP--LPEKAFSPQwslDRSRTPRG-LHDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 149064013  556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-430 5.50e-66

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 5.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL--AGA 421
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLktEGF 160

                  ....*....
gi 149064013  422 YAVERADME 430
Cdd:pfam00211 161 EFTERGEIE 169
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 6.45e-58

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: 196.71  E-value: 6.45e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013   219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqssrpentNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013   299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIRKLRV-ATGVDINMRVGVHSGSVLC 376
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 149064013   377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-446 1.64e-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: 1.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 352 IRKL--RVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAyaveRADM 429
Cdd:cd07302   82 LAELnaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA----GFEF 157
                        170       180
                 ....*....|....*....|
gi 149064013 430 EHRDPY-LRELGEP--TYLV 446
Cdd:cd07302  158 EELGEVeLKGKSGPvrVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 1.01e-43

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 163.82  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  40 AIVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWAALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWRPESQRDLLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQssrpentnnfhslyvkrHQGVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGE-----------------RREVT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 149064013 429 MEHrdpyLRELGEP--TYLVIDPWAEE 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 4.04e-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: 125.71  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  479 TRYLESWGAAKPFAHLSHVDSPASTSTP--LPEKAFSPQwslDRSRTPRG-LHDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 149064013  556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 4.20e-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: 90.84  E-value: 4.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  115 SAWDQVSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVlglylGWRPESQRD-LLPQLAANAVLFLCGNVVGAYHKA 193
Cdd:pfam16214 281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-----SLRTNAQDQfLLKQLVSNVLIFSCTNIVGVCTHY 355
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 149064013  194 LMERALRATFREALSSLHSRRRLDTEKKHQEHLLLSILPAYLAREMKAEIMAR 246
Cdd:pfam16214 356 PAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAK 408
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
264-430 5.50e-66

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 5.50e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  264 LYVKRHQGVSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVR 343
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  344 MGLDMCRAIRKLRVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALL--AGA 421
Cdd:pfam00211  81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLktEGF 160

                  ....*....
gi 149064013  422 YAVERADME 430
Cdd:pfam00211 161 EFTERGEIE 169
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
219-422 6.45e-58

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: 196.71  E-value: 6.45e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013   219 EKKHQEHLLLSILPAYLAREMKaeimarlqagqssrpentNNFHSLYVKRHQGVSVLYADIVGFTRLASECSPKELVLML 298
Cdd:smart00044   2 EKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLL 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013   299 NELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLS-LPDHAINCVRMGLDMCRAIRKLRV-ATGVDINMRVGVHSGSVLC 376
Cdd:smart00044  64 NDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVLVqHREEGLRVRIGIHTGPVVA 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 149064013   377 GVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAY 422
Cdd:smart00044 144 GVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
272-446 1.64e-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: 1.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRA 351
Cdd:cd07302    2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 352 IRKL--RVATGVDINMRVGVHSGSVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAyaveRADM 429
Cdd:cd07302   82 LAELnaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDA----GFEF 157
                        170       180
                 ....*....|....*....|
gi 149064013 430 EHRDPY-LRELGEP--TYLV 446
Cdd:cd07302  158 EELGEVeLKGKSGPvrVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
40-453 1.01e-43

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 163.82  E-value: 1.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  40 AIVALPAVAWASGRELTSDPSFLTTVLCALGGFSLLLGLASREQQLQRWTRPLSGLIWAALLALGYGFLFTGGVVSAWDQ 119
Cdd:COG2114    2 ALAALLLLLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 120 VSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVLGLYLGWRPESQRDLLPQLAANAVLFLCGNVVGAYHKALMERAL 199
Cdd:COG2114   82 GLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 200 RATFREALSSLHSRRRLDT------EKKHQEHLLLSILPAYLAREMKAEIMARLQAGQssrpentnnfhslyvkrHQGVS 273
Cdd:COG2114  162 LLALLLLLLLLLLLALLLLlllalrERERLRDLLGRYLPPEVAERLLAGGEELRLGGE-----------------RREVT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 274 VLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGLPLSLPDHAINCVRMGLDMCRAIR 353
Cdd:COG2114  225 VLFADIVGFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 354 KLRVAT----GVDINMRVGVHSGSVLCGVIG-LQKWQYDVWSHDVTLANHMEAGGVPGRVHITGATLALLAGAYAVERAD 428
Cdd:COG2114  305 ELNAELpaegGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRELG 384
                        410       420
                 ....*....|....*....|....*..
gi 149064013 429 MEHrdpyLRELGEP--TYLVIDPWAEE 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 3.26e-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: 3.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013 272 VSVLYADIVGFTRLASECSPKELVLMLNELFGKFDQIAKEHECMRIKILGDCYYCVSGlplslPDHAINCVRMGLDMCRA 351
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149064013 352 IRKLRVATGVDINMRVGVHSGSVLCGVIGLqKWQYDVWSHDVTLANHMEAGGVPGRVH 409
Cdd:cd07556   77 VSALNQSEGNPVRVRIGIHTGPVVVGVIGS-RPQYDVWGALVNLASRMESQAKAGQVL 133
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
479-581 4.04e-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: 125.71  E-value: 4.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  479 TRYLESWGAAKPFAHLSHVDSPASTSTP--LPEKAFSPQwslDRSRTPRG-LHDELdtgDAKFFQVIEQLNSQKQwkQSK 555
Cdd:pfam06327   1 TRYLESWGAERPFANLNHRESVSSEMTRigLPLADHILQ---DRSASPVArLEEEI---DEFIEQAIDGRSSDKL--RSE 72
                          90       100
                  ....*....|....*....|....*.
gi 149064013  556 DFNLLTLYFREKEMEKQYRLSALPAF 581
Cdd:pfam06327  73 DINPFTLKFKEKSLEKKYRQLRDPRF 98
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
115-246 4.20e-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: 90.84  E-value: 4.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149064013  115 SAWDQVSFFLFIIFTVYAMLPLGMRDAAAAGVISSLSHLLVlglylGWRPESQRD-LLPQLAANAVLFLCGNVVGAYHKA 193
Cdd:pfam16214 281 SASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV-----SLRTNAQDQfLLKQLVSNVLIFSCTNIVGVCTHY 355
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 149064013  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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