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Conserved domains on  [gi|665407818|ref|NP_001285883|]
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adenylyl cyclase X A, isoform H [Drosophila melanogaster]

Protein Classification

nucleotidyl cyclase domain-containing protein( domain architecture ID 34085)

nucleotidyl cyclase domain-containing protein may function as a mononucleotidyl cyclase (MNC) or a diguanylate cyclase (DGC)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nucleotidyl_cyc_III super family cl11967
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
306-394 8.98e-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.


The actual alignment was detected with superfamily member pfam00211:

Pssm-ID: 448371  Cd Length: 183  Bit Score: 86.14  E-value: 8.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  306 QIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGI 385
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83

                  ....*....
gi 665407818  386 SMIANIKEV 394
Cdd:pfam00211  84 DMLEAIGEV 92
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
88-394 3.80e-16

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 79.46  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  88 INAIFDLGSLILVTGLLSINFFEDFVIRHRWVMTFTSTLSAYVVVLGDIAFNTYYYYKSNWPLNTLYDVFVLCMIYMFLP 167
Cdd:COG2114   26 LALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 168 IPSSKAAALLAISVSLTYVIYFIHFMAFNEHNVAKYVHGLDIVSIDFFHYLGFNMMGIFFRIMNDTMVRSSFLDRYQFIT 247
Cdd:COG2114  106 LALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLAL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 248 EEiwlrqaRRQESLLLDSILPPQIAkpiqksikEKIIQPDNDFYHLGTSRtaenfmsiqihnDVSILYADLVNYTQLTTT 327
Cdd:COG2114  186 RE------RERLRDLLGRYLPPEVA--------ERLLAGGEELRLGGERR------------EVTVLFADIVGFTALSER 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665407818 328 LTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIANIKEV 394
Cdd:COG2114  240 LGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
306-394 8.98e-20

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 86.14  E-value: 8.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  306 QIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGI 385
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83

                  ....*....
gi 665407818  386 SMIANIKEV 394
Cdd:pfam00211  84 DMLEAIGEV 92
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
310-394 1.92e-19

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: 84.94  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 310 DVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIA 389
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80

                 ....*
gi 665407818 390 NIKEV 394
Cdd:cd07302   81 ALAEL 85
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
262-394 5.62e-17

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: 78.45  E-value: 5.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818   262 LLDSILPPQIAKpiqksikekiiqpdndfyHLGTSRTAEnfmSIQIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLY 341
Cdd:smart00044   9 LLDQLLPASVAE------------------QLKRGGSPV---PAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLY 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 665407818   342 ARFDLAALSFKVQRIKFLGDCYYCVAGLGESD-PDHATMAVSLGISMIANIKEV 394
Cdd:smart00044  68 SRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTV 121
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
88-394 3.80e-16

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 79.46  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  88 INAIFDLGSLILVTGLLSINFFEDFVIRHRWVMTFTSTLSAYVVVLGDIAFNTYYYYKSNWPLNTLYDVFVLCMIYMFLP 167
Cdd:COG2114   26 LALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 168 IPSSKAAALLAISVSLTYVIYFIHFMAFNEHNVAKYVHGLDIVSIDFFHYLGFNMMGIFFRIMNDTMVRSSFLDRYQFIT 247
Cdd:COG2114  106 LALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLAL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 248 EEiwlrqaRRQESLLLDSILPPQIAkpiqksikEKIIQPDNDFYHLGTSRtaenfmsiqihnDVSILYADLVNYTQLTTT 327
Cdd:COG2114  186 RE------RERLRDLLGRYLPPEVA--------ERLLAGGEELRLGGERR------------EVTVLFADIVGFTALSER 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665407818 328 LTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIANIKEV 394
Cdd:COG2114  240 LGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
306-394 8.98e-20

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 86.14  E-value: 8.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  306 QIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGI 385
Cdd:pfam00211   4 QPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAEMAL 83

                  ....*....
gi 665407818  386 SMIANIKEV 394
Cdd:pfam00211  84 DMLEAIGEV 92
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
310-394 1.92e-19

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: 84.94  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 310 DVSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIA 389
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80

                 ....*
gi 665407818 390 NIKEV 394
Cdd:cd07302   81 ALAEL 85
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
262-394 5.62e-17

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: 78.45  E-value: 5.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818   262 LLDSILPPQIAKpiqksikekiiqpdndfyHLGTSRTAEnfmSIQIHNDVSILYADLVNYTQLTTTLTVEKLVKVLHDLY 341
Cdd:smart00044   9 LLDQLLPASVAE------------------QLKRGGSPV---PAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLY 67
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 665407818   342 ARFDLAALSFKVQRIKFLGDCYYCVAGLGESD-PDHATMAVSLGISMIANIKEV 394
Cdd:smart00044  68 SRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTV 121
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
88-394 3.80e-16

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 79.46  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818  88 INAIFDLGSLILVTGLLSINFFEDFVIRHRWVMTFTSTLSAYVVVLGDIAFNTYYYYKSNWPLNTLYDVFVLCMIYMFLP 167
Cdd:COG2114   26 LALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 168 IPSSKAAALLAISVSLTYVIYFIHFMAFNEHNVAKYVHGLDIVSIDFFHYLGFNMMGIFFRIMNDTMVRSSFLDRYQFIT 247
Cdd:COG2114  106 LALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLAL 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 248 EEiwlrqaRRQESLLLDSILPPQIAkpiqksikEKIIQPDNDFYHLGTSRtaenfmsiqihnDVSILYADLVNYTQLTTT 327
Cdd:COG2114  186 RE------RERLRDLLGRYLPPEVA--------ERLLAGGEELRLGGERR------------EVTVLFADIVGFTALSER 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665407818 328 LTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGLGESDPDHATMAVSLGISMIANIKEV 394
Cdd:COG2114  240 LGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAEL 306
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
311-394 1.90e-09

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: 55.44  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665407818 311 VSILYADLVNYTQLTTTLTVEKLVKVLHDLYARFDLAALSFKVQRIKFLGDCYYCVAGlgesdPDHATMAVSLGISMIAN 390
Cdd:cd07556    2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMREA 76

                 ....
gi 665407818 391 IKEV 394
Cdd:cd07556   77 VSAL 80
 
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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