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Conserved domains on  [gi|578802674|ref|XP_006711988|]
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adenylate cyclase type 3 isoform X3 [Homo sapiens]

Protein Classification

adenylate cyclase( domain architecture ID 11069775)

adenylate cyclase such as mammalian adenylate cyclase types 1 and 3, which catalyze the formation of the signaling molecule cAMP downstream of G protein-coupled receptors

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;
937-1144 4.47e-80

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 259.87  E-value: 4.47e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   937 LYSQTYDEIGVMFASLPNFADFYTEESinngGIECLRFLNEIISDFDSLLDNPKfrvITKIKTIGSTYMAASGVTpdvnt 1016
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP----- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  1017 ngfassnkedkseRERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASR 1096
Cdd:pfam00211   69 -------------EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASR 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 578802674  1097 MESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKG 1144
Cdd:pfam00211  136 MESTGVPGKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
310-516 3.57e-70

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.13  E-value: 3.57e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   310 MYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSIL 389
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   390 MGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptl 469
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPG----------------- 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 578802674   470 rlrweRVHISQSTMDCLKGE-FDVEPgdggsRCDY-LEEKG-IETYLIIA 516
Cdd:pfam00211  144 -----KIHVSEETYRLLKTEgFEFTE-----RGEIeVKGKGkMKTYFLNG 183
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
105-494 1.01e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 143.79  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  105 LASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLP 184
Cdd:COG2114    23 LALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  185 LSLSPIVIISVVSCVVHtLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEV 264
Cdd:COG2114   103 LLLLALLLLLLLLLLLL-LLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  265 KMNLEEQsQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQfntmymyrhenVSILFADIVGFTQLSSACSAQELVKLL 344
Cdd:COG2114   182 LLALRER-ERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------VTVLFADIVGFTALSERLGPEELVELL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  345 NELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAI----SYVREKTKTGVDMRVGVHTGTV 420
Cdd:COG2114   250 NRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEV 329
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578802674  421 LGGVLG-QKRWQYDVWSTDVTVANKMEAGGIPGGskieerlyscvvaptlrlrwerVHISQSTMDCLKGEFDVEP 494
Cdd:COG2114   330 VVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGE----------------------ILVSEATYDLLRDRFEFRE 382
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
937-1144 4.47e-80

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 259.87  E-value: 4.47e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   937 LYSQTYDEIGVMFASLPNFADFYTEESinngGIECLRFLNEIISDFDSLLDNPKfrvITKIKTIGSTYMAASGVTpdvnt 1016
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP----- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  1017 ngfassnkedkseRERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASR 1096
Cdd:pfam00211   69 -------------EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASR 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 578802674  1097 MESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKG 1144
Cdd:pfam00211  136 MESTGVPGKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
310-516 3.57e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.13  E-value: 3.57e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   310 MYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSIL 389
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   390 MGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptl 469
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPG----------------- 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 578802674   470 rlrweRVHISQSTMDCLKGE-FDVEPgdggsRCDY-LEEKG-IETYLIIA 516
Cdd:pfam00211  144 -----KIHVSEETYRLLKTEgFEFTE-----RGEIeVKGKGkMKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
906-1124 1.69e-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: 196.71  E-value: 1.69e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    906 EMRRWNEALVTNMLPEHVARHFLGSKkrdEELYSQTYDEIGVMFASLPNFADFYTEESinngGIECLRFLNEIISDFDSL 985
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLKRGG---SPVPAESYDNVTILFSDIVGFTSLCSTST----PEQVVNLLNDLYSRFDQI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    986 LDNpkfRVITKIKTIGSTYMAASGVTPDVNtngfassnkedksererWQHLADLADFALAMKDTLTNINNQ-SFNNFMLR 1064
Cdd:smart00044   74 IDR---HGGYKVKTIGDAYMVASGLPEEAL-----------------VDHAELIADEALDMVEELKTVLVQhREEGLRVR 133
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   1065 IGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVMGNIQVVEETQVILREYGFRFV 1124
Cdd:smart00044  134 IGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFV 193
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
273-490 2.10e-51

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: 179.38  E-value: 2.10e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    273 QQQENLMLSILPKHVADEMLkdmkkdesqkdqQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFD 352
Cdd:smart00044    4 KKTDRLLDQLLPASVAEQLK------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFD 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    353 KLAAKYHQLRIKILGDCYYCICGLPDYRE-DHAVCSILMGLAMVEAI-SYVREKTKTGVDMRVGVHTGTVLGGVLGQKRW 430
Cdd:smart00044   72 QIIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    431 QYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptlrlrweRVHISQSTMDCLKGEF 490
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPG----------------------QIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
317-494 1.93e-46

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: 164.67  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  317 NVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVE 396
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  397 AISYVREKTKTG--VDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptlrlrwe 474
Cdd:cd07302    81 ALAELNAEREGGppLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPG---------------------- 138
                         170       180
                  ....*....|....*....|.
gi 578802674  475 RVHISQSTMDCLKG-EFDVEP 494
Cdd:cd07302   139 QILVSEATYELLGDaGFEFEE 159
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
944-1142 1.14e-39

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: 145.03  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  944 EIGVMFASLPNFadfyTEESINNGGIECLRFLNEIISDFDSLLDnpKFRViTKIKTIGSTYMAASGVTPDVNTngfassn 1023
Cdd:cd07302     1 EVTVLFADIVGF----TALSERLGPEELVELLNEYFSAFDEIIE--RHGG-TVDKTIGDAVMAVFGLPGAHED------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674 1024 kedksererwqHLADLADFALAMKDTLTNIN--NQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTG 1101
Cdd:cd07302    67 -----------HAERAVRAALEMQEALAELNaeREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLA 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578802674 1102 VMGNIQVVEETQVILREYGFRFVRRGPIFVKGK-GELLTFFL 1142
Cdd:cd07302   136 KPGQILVSEATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
105-494 1.01e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 143.79  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  105 LASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLP 184
Cdd:COG2114    23 LALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  185 LSLSPIVIISVVSCVVHtLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEV 264
Cdd:COG2114   103 LLLLALLLLLLLLLLLL-LLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  265 KMNLEEQsQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQfntmymyrhenVSILFADIVGFTQLSSACSAQELVKLL 344
Cdd:COG2114   182 LLALRER-ERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------VTVLFADIVGFTALSERLGPEELVELL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  345 NELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAI----SYVREKTKTGVDMRVGVHTGTV 420
Cdd:COG2114   250 NRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEV 329
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578802674  421 LGGVLG-QKRWQYDVWSTDVTVANKMEAGGIPGGskieerlyscvvaptlrlrwerVHISQSTMDCLKGEFDVEP 494
Cdd:COG2114   330 VVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGE----------------------ILVSEATYDLLRDRFEFRE 382
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
44-303 4.33e-28

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: 118.57  E-value: 4.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    44 GSClC---LPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFdCYVVVMCAVVFSSDKLASLAVAGIGLVLDII 120
Cdd:pfam16214  163 GAC-ClalLQIFRSKKFQSEKLERLYQRYFFRLNQSSLTMLMAVLVLV-CLVMLAFHAARGPLQVPYVVVLSLAIGLILV 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   121 LFVLCKK-GLLPDRVTrrVLPYVLWLLITAqiFSYLGLNFARAHAASDTVGWQVFFVFSFFITLPLSLSPIVIISVVSCV 199
Cdd:pfam16214  241 LAVLCNRnAFHQDHMW--LACYAVILVVLA--VQVVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSA 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   200 VHTLVLGVTVAQQQQeelkgmqLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLM 279
Cdd:pfam16214  317 IHLAVSLRTNAQDQF-------LLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLL 389
                          250       260
                   ....*....|....*....|....
gi 578802674   280 LSILPKHVADEMLKDMkkDESQKD 303
Cdd:pfam16214  390 LSVLPRHVAMEMKADI--NAKQED 411
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
779-1146 1.06e-20

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 96.03  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  779 VAVLSLIATIMLVQVSHMVKLTLMLLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDSRLPL 858
Cdd:COG2114    57 LLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  859 VPSKYSMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKE--RVYEMRRWNEALVTNMLPEHVARHFLgsKKRDEE 936
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLllLALRERERLRDLLGRYLPPEVAERLL--AGGEEL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  937 LYSQTYDEIGVMFASLPNFADFYteESINNGGIecLRFLNEIISDFDSLLDnpKFRViTKIKTIGSTYMAASGvtpdvnt 1016
Cdd:COG2114   215 RLGGERREVTVLFADIVGFTALS--ERLGPEEL--VELLNRYFSAMVEIIE--RHGG-TVDKFIGDGVMAVFG------- 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674 1017 ngfassnkedkSERERWQHLADLADFALAMKDTLTNINNQSFNNFM----LRIGMNKGGVLAGVIGAR-KPHYDIWGNTV 1091
Cdd:COG2114   281 -----------APVAREDHAERAVRAALAMQEALAELNAELPAEGGpplrVRIGIHTGEVVVGNIGSEdRLDYTVIGDTV 349
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578802674 1092 NVASRMESTGVMGNIQVVEETQVILREyGFRFVRRGPIFVKGKGELLT-FFLKGRD 1146
Cdd:COG2114   350 NLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKAEPVEvYELLGAK 404
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
937-1144 4.47e-80

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 259.87  E-value: 4.47e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   937 LYSQTYDEIGVMFASLPNFADFYTEESinngGIECLRFLNEIISDFDSLLDNPKfrvITKIKTIGSTYMAASGVTpdvnt 1016
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP----- 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  1017 ngfassnkedkseRERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASR 1096
Cdd:pfam00211   69 -------------EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASR 135
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 578802674  1097 MESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKG 1144
Cdd:pfam00211  136 MESTGVPGKIHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFLNG 183
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
310-516 3.57e-70

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 232.13  E-value: 3.57e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   310 MYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSIL 389
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   390 MGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptl 469
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPG----------------- 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 578802674   470 rlrweRVHISQSTMDCLKGE-FDVEPgdggsRCDY-LEEKG-IETYLIIA 516
Cdd:pfam00211  144 -----KIHVSEETYRLLKTEgFEFTE-----RGEIeVKGKGkMKTYFLNG 183
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
906-1124 1.69e-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: 196.71  E-value: 1.69e-57
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    906 EMRRWNEALVTNMLPEHVARHFLGSKkrdEELYSQTYDEIGVMFASLPNFADFYTEESinngGIECLRFLNEIISDFDSL 985
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLKRGG---SPVPAESYDNVTILFSDIVGFTSLCSTST----PEQVVNLLNDLYSRFDQI 73
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    986 LDNpkfRVITKIKTIGSTYMAASGVTPDVNtngfassnkedksererWQHLADLADFALAMKDTLTNINNQ-SFNNFMLR 1064
Cdd:smart00044   74 IDR---HGGYKVKTIGDAYMVASGLPEEAL-----------------VDHAELIADEALDMVEELKTVLVQhREEGLRVR 133
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   1065 IGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVMGNIQVVEETQVILREYGFRFV 1124
Cdd:smart00044  134 IGIHTGPVVAGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGGQFV 193
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
273-490 2.10e-51

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: 179.38  E-value: 2.10e-51
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    273 QQQENLMLSILPKHVADEMLkdmkkdesqkdqQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFD 352
Cdd:smart00044    4 KKTDRLLDQLLPASVAEQLK------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNLLNDLYSRFD 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    353 KLAAKYHQLRIKILGDCYYCICGLPDYRE-DHAVCSILMGLAMVEAI-SYVREKTKTGVDMRVGVHTGTVLGGVLGQKRW 430
Cdd:smart00044   72 QIIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELkTVLVQHREEGLRVRIGIHTGPVVAGVVGIRMP 151
                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    431 QYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptlrlrweRVHISQSTMDCLKGEF 490
Cdd:smart00044  152 RYCLFGDTVNLASRMESAGDPG----------------------QIQVSEETYSLLARRG 189
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
317-494 1.93e-46

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: 164.67  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  317 NVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVE 396
Cdd:cd07302     1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  397 AISYVREKTKTG--VDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGgskieerlyscvvaptlrlrwe 474
Cdd:cd07302    81 ALAELNAEREGGppLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPG---------------------- 138
                         170       180
                  ....*....|....*....|.
gi 578802674  475 RVHISQSTMDCLKG-EFDVEP 494
Cdd:cd07302   139 QILVSEATYELLGDaGFEFEE 159
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
317-452 2.99e-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: 147.89  E-value: 2.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  317 NVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLpdyreDHAVCSILMGLAMVE 396
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL-----DHPAAAVAFAEDMRE 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578802674  397 AISYVREKTKTGVDMRVGVHTGTVLGGVLGqKRWQYDVWSTDVTVANKMEAGGIPG 452
Cdd:cd07556    76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIG-SRPQYDVWGALVNLASRMESQAKAG 130
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
944-1142 1.14e-39

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: 145.03  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  944 EIGVMFASLPNFadfyTEESINNGGIECLRFLNEIISDFDSLLDnpKFRViTKIKTIGSTYMAASGVTPDVNTngfassn 1023
Cdd:cd07302     1 EVTVLFADIVGF----TALSERLGPEELVELLNEYFSAFDEIIE--RHGG-TVDKTIGDAVMAVFGLPGAHED------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674 1024 kedksererwqHLADLADFALAMKDTLTNIN--NQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTG 1101
Cdd:cd07302    67 -----------HAERAVRAALEMQEALAELNaeREGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLA 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 578802674 1102 VMGNIQVVEETQVILREYGFRFVRRGPIFVKGK-GELLTFFL 1142
Cdd:cd07302   136 KPGQILVSEATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
105-494 1.01e-36

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 143.79  E-value: 1.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  105 LASLAVAGIGLVLDIILFVLCKKGLLPDRVTRRVLPYVLWLLITAQIFSYLGLNFARAHAASDTVGWQVFFVFSFFITLP 184
Cdd:COG2114    23 LALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  185 LSLSPIVIISVVSCVVHtLVLGVTVAQQQQEELKGMQLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEV 264
Cdd:COG2114   103 LLLLALLLLLLLLLLLL-LLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLL 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  265 KMNLEEQsQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQfntmymyrhenVSILFADIVGFTQLSSACSAQELVKLL 344
Cdd:COG2114   182 LLALRER-ERLRDLLGRYLPPEVAERLLAGGEELRLGGERRE-----------VTVLFADIVGFTALSERLGPEELVELL 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  345 NELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAI----SYVREKTKTGVDMRVGVHTGTV 420
Cdd:COG2114   250 NRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALaelnAELPAEGGPPLRVRIGIHTGEV 329
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578802674  421 LGGVLG-QKRWQYDVWSTDVTVANKMEAGGIPGGskieerlyscvvaptlrlrwerVHISQSTMDCLKGEFDVEP 494
Cdd:COG2114   330 VVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGE----------------------ILVSEATYDLLRDRFEFRE 382
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
944-1107 1.00e-28

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: 112.06  E-value: 1.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  944 EIGVMFASLPNFadfyTEESINNGGIECLRFLNEIISDFDSLLDNPKfrvITKIKTIGSTYMAASGVTpdvntngfassn 1023
Cdd:cd07556     1 PVTILFADIVGF----TSLADALGPDEGDELLNELAGRFDSLIRRSG---DLKIKTIGDEFMVVSGLD------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674 1024 kedksererwqHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARkPHYDIWGNTVNVASRMESTGVM 1103
Cdd:cd07556    62 -----------HPAAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKA 129

                  ....
gi 578802674 1104 GNIQ 1107
Cdd:cd07556   130 GQVL 133
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
44-303 4.33e-28

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: 118.57  E-value: 4.33e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674    44 GSClC---LPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFdCYVVVMCAVVFSSDKLASLAVAGIGLVLDII 120
Cdd:pfam16214  163 GAC-ClalLQIFRSKKFQSEKLERLYQRYFFRLNQSSLTMLMAVLVLV-CLVMLAFHAARGPLQVPYVVVLSLAIGLILV 240
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   121 LFVLCKK-GLLPDRVTrrVLPYVLWLLITAqiFSYLGLNFARAHAASDTVGWQVFFVFSFFITLPLSLSPIVIISVVSCV 199
Cdd:pfam16214  241 LAVLCNRnAFHQDHMW--LACYAVILVVLA--VQVVGVLLVQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSA 316
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674   200 VHTLVLGVTVAQQQQeelkgmqLLREILANVFLYLCAIAVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLM 279
Cdd:pfam16214  317 IHLAVSLRTNAQDQF-------LLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLL 389
                          250       260
                   ....*....|....*....|....
gi 578802674   280 LSILPKHVADEMLKDMkkDESQKD 303
Cdd:pfam16214  390 LSVLPRHVAMEMKADI--NAKQED 411
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
779-1146 1.06e-20

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 96.03  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  779 VAVLSLIATIMLVQVSHMVKLTLMLLVAGAVATINLYAWRPVFDEYDHKRFREHDLPMVALEQMQGFNPGLNGTDSRLPL 858
Cdd:COG2114    57 LLLAALLLLLLLLLLLGLLLLALLLGLALAALALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  859 VPSKYSMTVMVFLMMLSFYYFSRHVEKLARTLFLWKIEVHDQKE--RVYEMRRWNEALVTNMLPEHVARHFLgsKKRDEE 936
Cdd:COG2114   137 LLLALALLLLLALALLLLLLLVALLLLALLLLLLLLLLLALLLLllLALRERERLRDLLGRYLPPEVAERLL--AGGEEL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674  937 LYSQTYDEIGVMFASLPNFADFYteESINNGGIecLRFLNEIISDFDSLLDnpKFRViTKIKTIGSTYMAASGvtpdvnt 1016
Cdd:COG2114   215 RLGGERREVTVLFADIVGFTALS--ERLGPEEL--VELLNRYFSAMVEIIE--RHGG-TVDKFIGDGVMAVFG------- 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578802674 1017 ngfassnkedkSERERWQHLADLADFALAMKDTLTNINNQSFNNFM----LRIGMNKGGVLAGVIGAR-KPHYDIWGNTV 1091
Cdd:COG2114   281 -----------APVAREDHAERAVRAALAMQEALAELNAELPAEGGpplrVRIGIHTGEVVVGNIGSEdRLDYTVIGDTV 349
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 578802674 1092 NVASRMESTGVMGNIQVVEETQVILREyGFRFVRRGPIFVKGKGELLT-FFLKGRD 1146
Cdd:COG2114   350 NLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKAEPVEvYELLGAK 404
 
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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