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Conserved domains on  [gi|50959205|ref|NP_001107|]
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adenylate cyclase type 9 [Homo sapiens]

Protein Classification

adenylate/guanylate cyclase domain-containing protein( domain architecture ID 10446187)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
385-573 4.58e-83

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 269.50  E-value: 4.58e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    385 FKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIE 464
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    465 MGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLddrye 544
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL----- 155
                          170       180
                   ....*....|....*....|....*....
gi 50959205    545 MEDGKVIERLGQSVVADQLKgLKTYLISG 573
Cdd:pfam00211  156 KTEGFEFTERGEIEVKGKGK-MKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1050-1241 5.37e-60

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 203.63  E-value: 5.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1050 YSKNHDSGGVIFASIVNFSEFYEEnyEGGKECYRVLNELIGDFDELLSKPDyssIEKIKTIGATYMAASGLNTAQAQdgs 1129
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSR--HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1130 hpqeHLQILFEFAKEMMRVVDDFNNNMLwFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVS 1209
Cdd:pfam00211   74 ----HARKIAEMALDMLEAIGEVNVESS-EGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 50959205   1210 EESYRVLSKMGYDFDYRGTVNVKGKGQMKTYL 1241
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYF 180
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
167-576 7.19e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.20  E-value: 7.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  167 LYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSL 246
Cdd:COG2114   29 LLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  247 CLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGkDLEVE 326
Cdd:COG2114  109 LLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLL-LALRE 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  327 KALKERMIHSVMPRIIADDLMKQGDEESENSVKRhatsspknrkkkssiqkapiafrpfkmqqieEVSILFADIVGFTKM 406
Cdd:COG2114  188 RERLRDLLGRYLPPEVAERLLAGGEELRLGGERR-------------------------------EVTVLFADIVGFTAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  407 SANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEM--- 483
Cdd:COG2114  237 SERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELNAELPAEggp 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  484 -VNMRVGVHTGTVLCGILGM-RRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMED-GKVierlgqsvva 560
Cdd:COG2114  317 pLRVRIGIHTGEVVVGNIGSeDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRElGEV---------- 386
                        410       420
                 ....*....|....*....|
gi 50959205  561 dQLKG----LKTYLISGQRA 576
Cdd:COG2114  387 -RLKGkaepVEVYELLGAKE 405
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
385-573 4.58e-83

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 269.50  E-value: 4.58e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    385 FKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIE 464
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    465 MGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLddrye 544
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL----- 155
                          170       180
                   ....*....|....*....|....*....
gi 50959205    545 MEDGKVIERLGQSVVADQLKgLKTYLISG 573
Cdd:pfam00211  156 KTEGFEFTERGEIEVKGKGK-MKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1050-1241 5.37e-60

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 203.63  E-value: 5.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1050 YSKNHDSGGVIFASIVNFSEFYEEnyEGGKECYRVLNELIGDFDELLSKPDyssIEKIKTIGATYMAASGLNTAQAQdgs 1129
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSR--HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1130 hpqeHLQILFEFAKEMMRVVDDFNNNMLwFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVS 1209
Cdd:pfam00211   74 ----HARKIAEMALDMLEAIGEVNVESS-EGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 50959205   1210 EESYRVLSKMGYDFDYRGTVNVKGKGQMKTYL 1241
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYF 180
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
326-544 4.91e-54

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: 187.08  E-value: 4.91e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205     326 EKALKERMIHSVMPRIIADDLmKQGdeesensvkrhatsspknrkkkssiqkapiaFRPFKMQQIEEVSILFADIVGFTK 405
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQL-KRG-------------------------------GSPVPAESYDNVTILFSDIVGFTS 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205     406 MSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPR-ADHAYCCIEMGLGMIKAIEQF-CQEKKEM 483
Cdd:smart00044   50 LCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTVlVQHREEG 129
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50959205     484 VNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYE 544
Cdd:smart00044  130 LRVRIGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
392-571 2.45e-52

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: 181.62  E-value: 2.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  392 EVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIK 471
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  472 AIEQFCQE--KKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYL-DDRYEMEDG 548
Cdd:cd07302   81 ALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                        170       180
                 ....*....|....*....|....*..
gi 50959205  549 KVIerlgqsvvadQLKG----LKTYLI 571
Cdd:cd07302  161 GEV----------ELKGksgpVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1059-1241 1.75e-47

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: 167.76  E-value: 1.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1059 VIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLSKPDyssIEKIKTIGATYMAASGLNTAQAqdgshpqEHLQIL 1138
Cdd:cd07302    4 VLFADIVGFTALSERL--GPEELVELLNEYFSAFDEIIERHG---GTVDKTIGDAVMAVFGLPGAHE-------DHAERA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1139 FEFAKEMMRVVDDFN-NNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLS 1217
Cdd:cd07302   72 VRAALEMQEALAELNaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLG 151
                        170       180
                 ....*....|....*....|....*
gi 50959205 1218 KMGYDFDYRGTVNVKGK-GQMKTYL 1241
Cdd:cd07302  152 DAGFEFEELGEVELKGKsGPVRVYR 176
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1024-1224 5.63e-44

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: 158.19  E-value: 5.63e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    1024 MRDQADWLLRNIIPYHVAEQLKVSQT--YSKNHDSGGVIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLSKPDy 1101
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLKRGGSpvPAESYDNVTILFSDIVGFTSLCSTS--TPEQVVNLLNDLYSRFDQIIDRHG- 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    1102 ssIEKIKTIGATYMAASGLNTAQAQDgshpqeHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTK 1181
Cdd:smart00044   79 --GYKVKTIGDAYMVASGLPEEALVD------HAELIADEALDMVEELKTVLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 50959205    1182 LLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFD 1224
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFV 193
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
167-576 7.19e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.20  E-value: 7.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  167 LYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSL 246
Cdd:COG2114   29 LLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  247 CLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGkDLEVE 326
Cdd:COG2114  109 LLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLL-LALRE 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  327 KALKERMIHSVMPRIIADDLMKQGDEESENSVKRhatsspknrkkkssiqkapiafrpfkmqqieEVSILFADIVGFTKM 406
Cdd:COG2114  188 RERLRDLLGRYLPPEVAERLLAGGEELRLGGERR-------------------------------EVTVLFADIVGFTAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  407 SANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEM--- 483
Cdd:COG2114  237 SERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELNAELPAEggp 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  484 -VNMRVGVHTGTVLCGILGM-RRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMED-GKVierlgqsvva 560
Cdd:COG2114  317 pLRVRIGIHTGEVVVGNIGSeDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRElGEV---------- 386
                        410       420
                 ....*....|....*....|
gi 50959205  561 dQLKG----LKTYLISGQRA 576
Cdd:COG2114  387 -RLKGkaepVEVYELLGAKE 405
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1021-1240 2.50e-25

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 110.28  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1021 IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGG---VIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLS 1097
Cdd:COG2114  184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERRevtVLFADIVGFTALSERL--GPEELVELLNRYFSAMVEIIE 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1098 KpdySSIEKIKTIGATYMAASGLNTAQAQDGSHpqehlqiLFEFAKEMMRVVDDFN---NNMLWFNFKLRVGFNHGPLTA 1174
Cdd:COG2114  262 R---HGGTVDKFIGDGVMAVFGAPVAREDHAER-------AVRAALAMQEALAELNaelPAEGGPPLRVRIGIHTGEVVV 331
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50959205 1175 GVIGTT-KLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKmGYDFDYRGTVNVKGKGQ-MKTY 1240
Cdd:COG2114  332 GNIGSEdRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKAEpVEVY 398
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
385-573 4.58e-83

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 269.50  E-value: 4.58e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    385 FKMQQIEEVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIE 464
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    465 MGLGMIKAIEQFCQEKKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLddrye 544
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLL----- 155
                          170       180
                   ....*....|....*....|....*....
gi 50959205    545 MEDGKVIERLGQSVVADQLKgLKTYLISG 573
Cdd:pfam00211  156 KTEGFEFTERGEIEVKGKGK-MKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
1050-1241 5.37e-60

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 203.63  E-value: 5.37e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1050 YSKNHDSGGVIFASIVNFSEFYEEnyEGGKECYRVLNELIGDFDELLSKPDyssIEKIKTIGATYMAASGLNTAQAQdgs 1129
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSR--HSPEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA--- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205   1130 hpqeHLQILFEFAKEMMRVVDDFNNNMLwFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVS 1209
Cdd:pfam00211   74 ----HARKIAEMALDMLEAIGEVNVESS-EGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVS 148
                          170       180       190
                   ....*....|....*....|....*....|..
gi 50959205   1210 EESYRVLSKMGYDFDYRGTVNVKGKGQMKTYL 1241
Cdd:pfam00211  149 EETYRLLKTEGFEFTERGEIEVKGKGKMKTYF 180
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
326-544 4.91e-54

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: 187.08  E-value: 4.91e-54
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205     326 EKALKERMIHSVMPRIIADDLmKQGdeesensvkrhatsspknrkkkssiqkapiaFRPFKMQQIEEVSILFADIVGFTK 405
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQL-KRG-------------------------------GSPVPAESYDNVTILFSDIVGFTS 49
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205     406 MSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPR-ADHAYCCIEMGLGMIKAIEQF-CQEKKEM 483
Cdd:smart00044   50 LCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEAlVDHAELIADEALDMVEELKTVlVQHREEG 129
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50959205     484 VNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYE 544
Cdd:smart00044  130 LRVRIGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
392-571 2.45e-52

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: 181.62  E-value: 2.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  392 EVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIK 471
Cdd:cd07302    1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  472 AIEQFCQE--KKEMVNMRVGVHTGTVLCGILGMRRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYL-DDRYEMEDG 548
Cdd:cd07302   81 ALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                        170       180
                 ....*....|....*....|....*..
gi 50959205  549 KVIerlgqsvvadQLKG----LKTYLI 571
Cdd:cd07302  161 GEV----------ELKGksgpVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
1059-1241 1.75e-47

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: 167.76  E-value: 1.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1059 VIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLSKPDyssIEKIKTIGATYMAASGLNTAQAqdgshpqEHLQIL 1138
Cdd:cd07302    4 VLFADIVGFTALSERL--GPEELVELLNEYFSAFDEIIERHG---GTVDKTIGDAVMAVFGLPGAHE-------DHAERA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1139 FEFAKEMMRVVDDFN-NNMLWFNFKLRVGFNHGPLTAGVIGTTKLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLS 1217
Cdd:cd07302   72 VRAALEMQEALAELNaEREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLG 151
                        170       180
                 ....*....|....*....|....*
gi 50959205 1218 KMGYDFDYRGTVNVKGK-GQMKTYL 1241
Cdd:cd07302  152 DAGFEFEELGEVELKGKsGPVRVYR 176
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
1024-1224 5.63e-44

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: 158.19  E-value: 5.63e-44
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    1024 MRDQADWLLRNIIPYHVAEQLKVSQT--YSKNHDSGGVIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLSKPDy 1101
Cdd:smart00044    2 EKKKTDRLLDQLLPASVAEQLKRGGSpvPAESYDNVTILFSDIVGFTSLCSTS--TPEQVVNLLNDLYSRFDQIIDRHG- 78
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205    1102 ssIEKIKTIGATYMAASGLNTAQAQDgshpqeHLQILFEFAKEMMRVVDDFNNNMLWFNFKLRVGFNHGPLTAGVIGTTK 1181
Cdd:smart00044   79 --GYKVKTIGDAYMVASGLPEEALVD------HAELIADEALDMVEELKTVLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|...
gi 50959205    1182 LLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKMGYDFD 1224
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFV 193
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
167-576 7.19e-42

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 159.20  E-value: 7.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  167 LYARHYAWTSLALTLLVFALTLAAQFQVLTPVSGRGDSSNLTATARPTDTCLSQVGSFSMCIEVLFLLYTVMHLPLYLSL 246
Cdd:COG2114   29 LLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLAL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  247 CLGVAYSVLFETFGYHFRDEACFPSPGAGALHWELLSRGLLHGCIHAIGVHLFVMSQVRSRSTFLKVGQSIMHGkDLEVE 326
Cdd:COG2114  109 LLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLLL-LALRE 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  327 KALKERMIHSVMPRIIADDLMKQGDEESENSVKRhatsspknrkkkssiqkapiafrpfkmqqieEVSILFADIVGFTKM 406
Cdd:COG2114  188 RERLRDLLGRYLPPEVAERLLAGGEELRLGGERR-------------------------------EVTVLFADIVGFTAL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  407 SANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGCPEPRADHAYCCIEMGLGMIKAIEQFCQEKKEM--- 483
Cdd:COG2114  237 SERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELNAELPAEggp 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  484 -VNMRVGVHTGTVLCGILGM-RRFKFDVWSNDVNLANLMEQLGVAGKVHISEATAKYLDDRYEMED-GKVierlgqsvva 560
Cdd:COG2114  317 pLRVRIGIHTGEVVVGNIGSeDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRElGEV---------- 386
                        410       420
                 ....*....|....*....|
gi 50959205  561 dQLKG----LKTYLISGQRA 576
Cdd:COG2114  387 -RLKGkaepVEVYELLGAKE 405
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
392-530 3.89e-37

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: 136.33  E-value: 3.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205  392 EVSILFADIVGFTKMSANKSAHALVGLLNDLFGRFDRLCEETKCEKISTLGDCYYCVAGcpeprADHAYCCIEMGLGMIK 471
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 50959205  472 AIEQFCQEKKEMVNMRVGVHTGTVLCGILGmRRFKFDVWSNDVNLANLMEQLGVAGKVH 530
Cdd:cd07556   76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIG-SRPQYDVWGALVNLASRMESQAKAGQVL 133
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
1058-1207 5.56e-27

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: 107.44  E-value: 5.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1058 GVIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLSKpdySSIEKIKTIGATYMAASGLntaqaqdgshpqEHLQI 1137
Cdd:cd07556    3 TILFADIVGFTSLADAL--GPDEGDELLNELAGRFDSLIRR---SGDLKIKTIGDEFMVVSGL------------DHPAA 65
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1138 LFEFAKEMMRVVDDFNNnMLWFNFKLRVGFNHGPLTAGVIGTTKLlYDIWGDTVNIASRMDTTGVECRIQ 1207
Cdd:cd07556   66 AVAFAEDMREAVSALNQ-SEGNPVRVRIGIHTGPVVVGVIGSRPQ-YDVWGALVNLASRMESQAKAGQVL 133
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
1021-1240 2.50e-25

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 110.28  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1021 IQSMRDQADWLLRNIIPYHVAEQLKVSQTYSKNHDSGG---VIFASIVNFSEFYEENyeGGKECYRVLNELIGDFDELLS 1097
Cdd:COG2114  184 ALRERERLRDLLGRYLPPEVAERLLAGGEELRLGGERRevtVLFADIVGFTALSERL--GPEELVELLNRYFSAMVEIIE 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50959205 1098 KpdySSIEKIKTIGATYMAASGLNTAQAQDGSHpqehlqiLFEFAKEMMRVVDDFN---NNMLWFNFKLRVGFNHGPLTA 1174
Cdd:COG2114  262 R---HGGTVDKFIGDGVMAVFGAPVAREDHAER-------AVRAALAMQEALAELNaelPAEGGPPLRVRIGIHTGEVVV 331
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50959205 1175 GVIGTT-KLLYDIWGDTVNIASRMDTTGVECRIQVSEESYRVLSKmGYDFDYRGTVNVKGKGQ-MKTY 1240
Cdd:COG2114  332 GNIGSEdRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKAEpVEVY 398
 
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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