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Conserved domains on  [gi|2462547296|ref|XP_054235463|]
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adenylate cyclase type 7 isoform X2 [Homo sapiens]

Protein Classification

DUF1053 and CHD domain-containing protein( domain architecture ID 11069824)

protein containing domains MFS, DUF1053, and CHD

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
871-1067 2.33e-75

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.00  E-value: 2.33e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  871 YHQSYDCVCVMFASVPDFKVFYTECDvnkeGLECLRLLNEIIADFDELLLKPKfsgVEKIKTIGSTYMAAAGLSvasghe 950
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  951 nqelERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGK 1030
Cdd:pfam00211   69 ----EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGK 144
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462547296 1031 IQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFV 1067
Cdd:pfam00211  145 IHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFL 181
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
270-453 2.18e-65

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 2.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  270 LYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVK 349
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  350 MGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHL-DKAY 428
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLkTEGF 160
                          170       180
                   ....*....|....*....|....*..
gi 2462547296  429 EVEDghgqqRDPY-LK-EMNIRTYLVI 453
Cdd:pfam00211  161 EFTE-----RGEIeVKgKGKMKTYFLN 182
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
47-432 6.48e-44

Adenylate cyclase, class 3 [Signal transduction mechanisms];


:

Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 164.98  E-value: 6.48e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   47 VALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQV 126
Cdd:COG2114      9 LLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAAL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  127 PFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASR 206
Cdd:COG2114     89 ALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  207 DLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAhismgmklAIIERLKEHGDRRCMPDnnfhslyvkRHQNVSILYADIV 286
Cdd:COG2114    169 LLLLLLLALLLLLLLALRERERLRDLLGRYLPP--------EVAERLLAGGEELRLGG---------ERREVTVLFADIV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  287 GFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQV----R 362
Cdd:COG2114    232 GFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelP 311
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462547296  363 EATGVDINMRVGIHSGNVLCGVIG-LRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVED 432
Cdd:COG2114    312 AEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
Adcy_cons_dom super family cl05691
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
485-593 8.48e-32

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: 119.54  E-value: 8.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  485 TRYLESWGAARPFAHLNHRESVSSGEThvpngrrPKSVPQRHRRTPDRSMSPKGRSEDDsYDDEMLSAIEGLSSTRPccs 564
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMT-------RIGLPLADHILQDRSASPVARLEEE-IDEFIEQAIDGRSSDKL--- 69
                           90       100
                   ....*....|....*....|....*....
gi 2462547296  565 KSDDFYTFGSIFLEKGFEREYRLAPIPRA 593
Cdd:pfam06327   70 RSEDINPFTLKFKEKSLEKKYRQLRDPRF 98
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
871-1067 2.33e-75

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.00  E-value: 2.33e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  871 YHQSYDCVCVMFASVPDFKVFYTECDvnkeGLECLRLLNEIIADFDELLLKPKfsgVEKIKTIGSTYMAAAGLSvasghe 950
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  951 nqelERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGK 1030
Cdd:pfam00211   69 ----EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGK 144
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462547296 1031 IQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFV 1067
Cdd:pfam00211  145 IHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFL 181
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
270-453 2.18e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 2.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  270 LYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVK 349
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  350 MGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHL-DKAY 428
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLkTEGF 160
                          170       180
                   ....*....|....*....|....*..
gi 2462547296  429 EVEDghgqqRDPY-LK-EMNIRTYLVI 453
Cdd:pfam00211  161 EFTE-----RGEIeVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
224-429 2.21e-60

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: 204.80  E-value: 2.21e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   224 IEKRQQENLLLSVLPAHISMGMKlaiierlkehgdrrcmpdNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVV 303
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNL 62
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   304 LNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVS-LPTHARNCVKMGLDMCQAIKQV-REATGVDINMRVGIHSGNVL 381
Cdd:smart00044   63 LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVlVQHREEGLRVRIGIHTGPVV 142
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*...
gi 2462547296   382 CGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYE 429
Cdd:smart00044  143 AGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
277-452 8.41e-53

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: 182.39  E-value: 8.41e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  277 NVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQ 356
Cdd:cd07302      1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  357 AIKQVRE--ATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHL-DKAYEVEDG 433
Cdd:cd07302     81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                          170       180
                   ....*....|....*....|.
gi 2462547296  434 HGQQrdpyLK--EMNIRTYLV 452
Cdd:cd07302    161 GEVE----LKgkSGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
878-1067 5.32e-49

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 171.61  E-value: 5.32e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  878 VCVMFASVPDFKVFYTECDvnkeGLECLRLLNEIIADFDELLLKpkfSGVEKIKTIGSTYMAAAGLSVAsghenqelerQ 957
Cdd:cd07302      2 VTVLFADIVGFTALSERLG----PEELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGA----------H 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  958 HAHIGVMVEFSIALMSKLDGINRH--SFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTE 1035
Cdd:cd07302     65 EDHAERAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSE 144
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462547296 1036 ETCTILQGLGYSCECRGLINVKGK-GELRTYFV 1067
Cdd:cd07302    145 ATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
848-1046 2.52e-48

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: 170.52  E-value: 2.52e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   848 LLENVLPAHVAAHFIGDKLNEdwYHQSYDCVCVMFASVPDFKVFYTECdvnkEGLECLRLLNEIIADFDELLLKpkfSGV 927
Cdd:smart00044    9 LLDQLLPASVAEQLKRGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLYSRFDQIIDR---HGG 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   928 EKIKTIGSTYMAAAGLsvasghenqELERQHAHIGVMVEFSIALMSKLDG-INRHSFNSFRLRVGINHGPVIAGVIGARK 1006
Cdd:smart00044   80 YKVKTIGDAYMVASGL---------PEEALVDHAELIADEALDMVEELKTvLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462547296  1007 PQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGY 1046
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
47-432 6.48e-44

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 164.98  E-value: 6.48e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   47 VALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQV 126
Cdd:COG2114      9 LLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAAL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  127 PFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASR 206
Cdd:COG2114     89 ALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  207 DLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAhismgmklAIIERLKEHGDRRCMPDnnfhslyvkRHQNVSILYADIV 286
Cdd:COG2114    169 LLLLLLLALLLLLLLALRERERLRDLLGRYLPP--------EVAERLLAGGEELRLGG---------ERREVTVLFADIV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  287 GFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQV----R 362
Cdd:COG2114    232 GFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelP 311
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462547296  363 EATGVDINMRVGIHSGNVLCGVIG-LRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVED 432
Cdd:COG2114    312 AEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
485-593 8.48e-32

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: 119.54  E-value: 8.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  485 TRYLESWGAARPFAHLNHRESVSSGEThvpngrrPKSVPQRHRRTPDRSMSPKGRSEDDsYDDEMLSAIEGLSSTRPccs 564
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMT-------RIGLPLADHILQDRSASPVARLEEE-IDEFIEQAIDGRSSDKL--- 69
                           90       100
                   ....*....|....*....|....*....
gi 2462547296  565 KSDDFYTFGSIFLEKGFEREYRLAPIPRA 593
Cdd:pfam06327   70 RSEDINPFTLKFKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
906-1067 1.07e-25

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 111.05  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  906 RLLNEIIADFDELLLKpkfSGVEKIKTIGSTYMAAAGLSVAsghenQELERQHAhigvmVEFSIALMSKLDGINR----H 981
Cdd:COG2114    247 ELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVFGAPVA-----REDHAERA-----VRAALAMQEALAELNAelpaE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  982 SFNSFRLRVGINHGPVIAGVIGAR-KPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGlGYSCECRGLINVKGKG 1060
Cdd:COG2114    314 GGPPLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKA 392

                   ....*...
gi 2462547296 1061 E-LRTYFV 1067
Cdd:COG2114    393 EpVEVYEL 400
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
47-249 1.79e-21

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: 98.54  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   47 VALIIIAFSQGDPsrHQAILGMAFLVLAVFaaLSVLMYVECllRR--------WLRALALLtwACLVALGYVLVFDAWTK 118
Cdd:pfam16214  209 VCLVMLAFHAARG--PLQVPYVVVLSLAIG--LILVLAVLC--NRnafhqdhmWLACYAVI--LVVLAVQVVGVLLVQPR 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  119 AACawEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVlgSLMggFTTPSVRVGLQLLANAVIFLCGNLTGAFHK 198
Cdd:pfam16214  281 SAS--EGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV--SLR--TNAQDQFLLKQLVSNVLIFSCTNIVGVCTH 354
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462547296  199 HQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAI 249
Cdd:pfam16214  355 YPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADI 405
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
65-120 6.28e-03

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 40.25  E-value: 6.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462547296   65 ILGMAFLVLAVFAALSVLmyveCLLRRWLRALALLTWACLVALGYVLVFDAWTKAA 120
Cdd:PRK00302   164 VYGLSFLVVLVNALLALA----LIKRRWRLALLALLLLLLAALGYGLRRLQWTTPA 215
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
871-1067 2.33e-75

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 246.00  E-value: 2.33e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  871 YHQSYDCVCVMFASVPDFKVFYTECDvnkeGLECLRLLNEIIADFDELLLKPKfsgVEKIKTIGSTYMAAAGLSvasghe 950
Cdd:pfam00211    2 YAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLP------ 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  951 nqelERQHAHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGK 1030
Cdd:pfam00211   69 ----EPSPAHARKIAEMALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGK 144
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2462547296 1031 IQVTEETCTILQGLGYSCECRGLINVKGKGELRTYFV 1067
Cdd:pfam00211  145 IHVSEETYRLLKTEGFEFTERGEIEVKGKGKMKTYFL 181
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
270-453 2.18e-65

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 218.27  E-value: 2.18e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  270 LYVKRHQNVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVK 349
Cdd:pfam00211    1 VYAQPYDNVTILFADIVGFTALSSRHSPEQVVRLLNELYTRFDRLLDKHKVYKVKTIGDAYMVVSGLPEPSPAHARKIAE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  350 MGLDMCQAIKQVREATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHL-DKAY 428
Cdd:pfam00211   81 MALDMLEAIGEVNVESSEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYRLLkTEGF 160
                          170       180
                   ....*....|....*....|....*..
gi 2462547296  429 EVEDghgqqRDPY-LK-EMNIRTYLVI 453
Cdd:pfam00211  161 EFTE-----RGEIeVKgKGKMKTYFLN 182
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
224-429 2.21e-60

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: 204.80  E-value: 2.21e-60
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   224 IEKRQQENLLLSVLPAHISMGMKlaiierlkehgdrrcmpdNNFHSLYVKRHQNVSILYADIVGFTQLASDCSPKELVVV 303
Cdd:smart00044    1 EEKKKTDRLLDQLLPASVAEQLK------------------RGGSPVPAESYDNVTILFSDIVGFTSLCSTSTPEQVVNL 62
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   304 LNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVS-LPTHARNCVKMGLDMCQAIKQV-REATGVDINMRVGIHSGNVL 381
Cdd:smart00044   63 LNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEaLVDHAELIADEALDMVEELKTVlVQHREEGLRVRIGIHTGPVV 142
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*...
gi 2462547296   382 CGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYE 429
Cdd:smart00044  143 AGVVGIRMPRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
277-452 8.41e-53

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: 182.39  E-value: 8.41e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  277 NVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQ 356
Cdd:cd07302      1 EVTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  357 AIKQVRE--ATGVDINMRVGIHSGNVLCGVIGLRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHL-DKAYEVEDG 433
Cdd:cd07302     81 ALAELNAerEGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLgDAGFEFEEL 160
                          170       180
                   ....*....|....*....|.
gi 2462547296  434 HGQQrdpyLK--EMNIRTYLV 452
Cdd:cd07302    161 GEVE----LKgkSGPVRVYRL 177
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
878-1067 5.32e-49

cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.


Pssm-ID: 143636 [Multi-domain]  Cd Length: 177  Bit Score: 171.61  E-value: 5.32e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  878 VCVMFASVPDFKVFYTECDvnkeGLECLRLLNEIIADFDELLLKpkfSGVEKIKTIGSTYMAAAGLSVAsghenqelerQ 957
Cdd:cd07302      2 VTVLFADIVGFTALSERLG----PEELVELLNEYFSAFDEIIER---HGGTVDKTIGDAVMAVFGLPGA----------H 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  958 HAHIGVMVEFSIALMSKLDGINRH--SFNSFRLRVGINHGPVIAGVIGARKPQYDIWGNTVNVASRMESTGELGKIQVTE 1035
Cdd:cd07302     65 EDHAERAVRAALEMQEALAELNAEreGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSE 144
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2462547296 1036 ETCTILQGLGYSCECRGLINVKGK-GELRTYFV 1067
Cdd:cd07302    145 ATYELLGDAGFEFEELGEVELKGKsGPVRVYRL 177
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
848-1046 2.52e-48

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: 170.52  E-value: 2.52e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   848 LLENVLPAHVAAHFIGDKLNEdwYHQSYDCVCVMFASVPDFKVFYTECdvnkEGLECLRLLNEIIADFDELLLKpkfSGV 927
Cdd:smart00044    9 LLDQLLPASVAEQLKRGGSPV--PAESYDNVTILFSDIVGFTSLCSTS----TPEQVVNLLNDLYSRFDQIIDR---HGG 79
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   928 EKIKTIGSTYMAAAGLsvasghenqELERQHAHIGVMVEFSIALMSKLDG-INRHSFNSFRLRVGINHGPVIAGVIGARK 1006
Cdd:smart00044   80 YKVKTIGDAYMVASGL---------PEEALVDHAELIADEALDMVEELKTvLVQHREEGLRVRIGIHTGPVVAGVVGIRM 150
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|
gi 2462547296  1007 PQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGLGY 1046
Cdd:smart00044  151 PRYCLFGDTVNLASRMESAGDPGQIQVSEETYSLLARRGG 190
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
47-432 6.48e-44

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 164.98  E-value: 6.48e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   47 VALIIIAFSQGDPSRHQAILGMAFLVLAVFAALSVLMYVECLLRRWLRALALLTWACLVALGYVLVFDAWTKAACAWEQV 126
Cdd:COG2114      9 LLLLLLLLLLLLLLLALLALLLLLAALLLVLLLLLAALLLLLLLLLALLLLAALLLLLLLLLLLGLLLLALLLGLALAAL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  127 PFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVLGSLMGGFTTPSVRVGLQLLANAVIFLCGNLTGAFHKHQMQDASR 206
Cdd:COG2114     89 ALALLAAAALLLLLLLLLALLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLALALLLLLALALLLLLLLVALLLLALLLL 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  207 DLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAhismgmklAIIERLKEHGDRRCMPDnnfhslyvkRHQNVSILYADIV 286
Cdd:COG2114    169 LLLLLLLALLLLLLLALRERERLRDLLGRYLPP--------EVAERLLAGGEELRLGG---------ERREVTVLFADIV 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  287 GFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGLPVSLPTHARNCVKMGLDMCQAIKQV----R 362
Cdd:COG2114    232 GFTALSERLGPEELVELLNRYFSAMVEIIERHGGTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQEALAELnaelP 311
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462547296  363 EATGVDINMRVGIHSGNVLCGVIG-LRKWQYDVWSHDVSLANRMEAAGVPGRVHITEATLKHLDKAYEVED 432
Cdd:COG2114    312 AEGGPPLRVRIGIHTGEVVVGNIGsEDRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRDRFEFRE 382
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
277-415 1.30e-40

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: 145.96  E-value: 1.30e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  277 NVSILYADIVGFTQLASDCSPKELVVVLNELFGKFDQIAKANECMRIKILGDCYYCVSGlpvslPTHARNCVKMGLDMCQ 356
Cdd:cd07556      1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSG-----LDHPAAAVAFAEDMRE 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462547296  357 AIKQVREATGVDINMRVGIHSGNVLCGVIGLRkWQYDVWSHDVSLANRMEAAGVPGRVH 415
Cdd:cd07556     76 AVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
877-1032 4.05e-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: 135.95  E-value: 4.05e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  877 CVCVMFASVPDFKVFYTECdvnkEGLECLRLLNEIIADFDELLLKpkfSGVEKIKTIGSTYMAAAGLSvasghenqeler 956
Cdd:cd07556      1 PVTILFADIVGFTSLADAL----GPDEGDELLNELAGRFDSLIRR---SGDLKIKTIGDEFMVVSGLD------------ 61
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462547296  957 qhaHIGVMVEFSIALMSKLDGINRHSFNSFRLRVGINHGPVIAGVIGARkPQYDIWGNTVNVASRMESTGELGKIQ 1032
Cdd:cd07556     62 ---HPAAAVAFAEDMREAVSALNQSEGNPVRVRIGIHTGPVVVGVIGSR-PQYDVWGALVNLASRMESQAKAGQVL 133
Adcy_cons_dom pfam06327
Adenylate cyclase, conserved domain; Adenylate cyclase (AC) enzyme uses ATP as its substrate ...
485-593 8.48e-32

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: 119.54  E-value: 8.48e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  485 TRYLESWGAARPFAHLNHRESVSSGEThvpngrrPKSVPQRHRRTPDRSMSPKGRSEDDsYDDEMLSAIEGLSSTRPccs 564
Cdd:pfam06327    1 TRYLESWGAERPFANLNHRESVSSEMT-------RIGLPLADHILQDRSASPVARLEEE-IDEFIEQAIDGRSSDKL--- 69
                           90       100
                   ....*....|....*....|....*....
gi 2462547296  565 KSDDFYTFGSIFLEKGFEREYRLAPIPRA 593
Cdd:pfam06327   70 RSEDINPFTLKFKEKSLEKKYRQLRDPRF 98
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
906-1067 1.07e-25

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 111.05  E-value: 1.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  906 RLLNEIIADFDELLLKpkfSGVEKIKTIGSTYMAAAGLSVAsghenQELERQHAhigvmVEFSIALMSKLDGINR----H 981
Cdd:COG2114    247 ELLNRYFSAMVEIIER---HGGTVDKFIGDGVMAVFGAPVA-----REDHAERA-----VRAALAMQEALAELNAelpaE 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  982 SFNSFRLRVGINHGPVIAGVIGAR-KPQYDIWGNTVNVASRMESTGELGKIQVTEETCTILQGlGYSCECRGLINVKGKG 1060
Cdd:COG2114    314 GGPPLRVRIGIHTGEVVVGNIGSEdRLDYTVIGDTVNLAARLESLAKPGEILVSEATYDLLRD-RFEFRELGEVRLKGKA 392

                   ....*...
gi 2462547296 1061 E-LRTYFV 1067
Cdd:COG2114    393 EpVEVYEL 400
AC_N pfam16214
Adenylyl cyclase N-terminal extracellular and transmembrane region; This family covers the ...
47-249 1.79e-21

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: 98.54  E-value: 1.79e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296   47 VALIIIAFSQGDPsrHQAILGMAFLVLAVFaaLSVLMYVECllRR--------WLRALALLtwACLVALGYVLVFDAWTK 118
Cdd:pfam16214  209 VCLVMLAFHAARG--PLQVPYVVVLSLAIG--LILVLAVLC--NRnafhqdhmWLACYAVI--LVVLAVQVVGVLLVQPR 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462547296  119 AACawEQVPFFLFIVFVVYTLLPFSMRGAVAVGAVSTASHLLVlgSLMggFTTPSVRVGLQLLANAVIFLCGNLTGAFHK 198
Cdd:pfam16214  281 SAS--EGIWWTVFFIYTIYTLLPVRMRAAVISGVLLSAIHLAV--SLR--TNAQDQFLLKQLVSNVLIFSCTNIVGVCTH 354
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2462547296  199 HQMQDASRDLFTYTVKCIQIRRKLRIEKRQQENLLLSVLPAHISMGMKLAI 249
Cdd:pfam16214  355 YPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADI 405
lnt PRK00302
apolipoprotein N-acyltransferase; Reviewed
65-120 6.28e-03

apolipoprotein N-acyltransferase; Reviewed


Pssm-ID: 234721 [Multi-domain]  Cd Length: 505  Bit Score: 40.25  E-value: 6.28e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462547296   65 ILGMAFLVLAVFAALSVLmyveCLLRRWLRALALLTWACLVALGYVLVFDAWTKAA 120
Cdd:PRK00302   164 VYGLSFLVVLVNALLALA----LIKRRWRLALLALLLLLLAALGYGLRRLQWTTPA 215
 
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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