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Conserved domains on  [gi|4504215|ref|NP_000848|]
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guanylate cyclase soluble subunit beta-1 isoform 2 [Homo sapiens]

Protein Classification

guanylate cyclase soluble subunit beta-1-like( domain architecture ID 11169715)

soluble guanylate cyclase beta subunit, similar to the beta-1 or beta-2 subunits of mammalian soluble guanylate cyclase, which is active a heterodimer of alpha and beta subunits and catalyzes the conversion of GTP to the second messenger cGMP in response to nitric oxide

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;
412-605 1.62e-85

Adenylate and Guanylate cyclase catalytic domain;


:

Pssm-ID: 425528  Cd Length: 183  Bit Score: 264.88  E-value: 1.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    412 VPAKRYDNVTILFSGIVGFNAFCSKHAsgegAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIH 491
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    492 HARSICHLALDMMEIAGQVQVDG-ESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYR 570
Cdd:pfam00211  74 HARKIAEMALDMLEAIGEVNVESsEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYR 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4504215    571 CLMspensDPQFHLEHRGPVSMKGKKEPMQVWFLS 605
Cdd:pfam00211 154 LLK-----TEGFEFTERGEIEVKGKGKMKTYFLNG 183
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
207-406 1.54e-84

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


:

Pssm-ID: 462234  Cd Length: 214  Bit Score: 263.28  E-value: 1.54e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    207 RISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLD 286
Cdd:pfam07701   2 PISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKKLTDVFRLRRPLIEFTFDNILQHINVVFELQTKRPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    287 VEK------------LECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVL 354
Cdd:pfam07701  82 KEEeaklsaaldaseEESSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4504215    355 LGEQFREEYKLTQE-LEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANEL 406
Cdd:pfam07701 162 AGQQQSAELKLALDqLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
HNOB pfam07700
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
2-166 8.93e-68

Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.


:

Pssm-ID: 462233  Cd Length: 162  Bit Score: 217.75  E-value: 8.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215      2 YGFVNHALELLVIRNYGPEVWEDIKKEAQLdEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQES 81
Cdd:pfam07700   1 YGIVFEALQDLVEEKYGEEVWDEILEKAGL-EEGVFTPHETYDDEETLKLVEAAAKVTGLSVDELLEAFGRFFIKFFAES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     82 GYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDaEKGKGLILHYYSEREGLQDIVIGIIKTVAqQIHGTE 161
Cdd:pfam07700  80 GYPRFFKVLGRNLFDFLNNLDNLHEVLKLSYPGMKPPSFRCEE-ESDGGLVLHYYSKRKGLFPYVLGLLEGAA-EFFNED 157

                  ....*
gi 4504215    162 IDMKV 166
Cdd:pfam07700 158 VEIEV 162
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
412-605 1.62e-85

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 264.88  E-value: 1.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    412 VPAKRYDNVTILFSGIVGFNAFCSKHAsgegAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIH 491
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    492 HARSICHLALDMMEIAGQVQVDG-ESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYR 570
Cdd:pfam00211  74 HARKIAEMALDMLEAIGEVNVESsEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYR 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4504215    571 CLMspensDPQFHLEHRGPVSMKGKKEPMQVWFLS 605
Cdd:pfam00211 154 LLK-----TEGFEFTERGEIEVKGKGKMKTYFLNG 183
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
207-406 1.54e-84

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


Pssm-ID: 462234  Cd Length: 214  Bit Score: 263.28  E-value: 1.54e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    207 RISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLD 286
Cdd:pfam07701   2 PISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKKLTDVFRLRRPLIEFTFDNILQHINVVFELQTKRPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    287 VEK------------LECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVL 354
Cdd:pfam07701  82 KEEeaklsaaldaseEESSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4504215    355 LGEQFREEYKLTQE-LEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANEL 406
Cdd:pfam07701 162 AGQQQSAELKLALDqLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
385-584 5.86e-80

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: 250.64  E-value: 5.86e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     385 DEKKKTDTLLYSVLPPSVANELRHKR-PVPAKRYDNVTILFSGIVGFNAFCSKhasgEGAMKIVNLLNDLYTRFDTLTDS 463
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGGsPVPAESYDNVTILFSDIVGFTSLCST----STPEQVVNLLNDLYSRFDQIIDR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     464 RKnpfVYKVETVGDKYMTVSGLPEPCIH-HARSICHLALDMMEIAGQV--QVDGESVQITIGIHTGEVVTGVIGQRMPRY 540
Cdd:smart00044  77 HG---GYKVKTIGDAYMVASGLPEEALVdHAELIADEALDMVEELKTVlvQHREEGLRVRIGIHTGPVVAGVVGIRMPRY 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 4504215     541 CLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmspENSDPQFHL 584
Cdd:smart00044 154 CLFGDTVNLASRMESAGDPGQIQVSEETYSLL---ARRGGQFVF 194
HNOB pfam07700
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
2-166 8.93e-68

Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.


Pssm-ID: 462233  Cd Length: 162  Bit Score: 217.75  E-value: 8.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215      2 YGFVNHALELLVIRNYGPEVWEDIKKEAQLdEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQES 81
Cdd:pfam07700   1 YGIVFEALQDLVEEKYGEEVWDEILEKAGL-EEGVFTPHETYDDEETLKLVEAAAKVTGLSVDELLEAFGRFFIKFFAES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     82 GYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDaEKGKGLILHYYSEREGLQDIVIGIIKTVAqQIHGTE 161
Cdd:pfam07700  80 GYPRFFKVLGRNLFDFLNNLDNLHEVLKLSYPGMKPPSFRCEE-ESDGGLVLHYYSKRKGLFPYVLGLLEGAA-EFFNED 157

                  ....*
gi 4504215    162 IDMKV 166
Cdd:pfam07700 158 VEIEV 162
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
419-604 4.04e-61

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: 200.88  E-value: 4.04e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  419 NVTILFSGIVGFNAFCSKHasgeGAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIHHARSICH 498
Cdd:cd07302   1 EVTVLFADIVGFTALSERL----GPEELVELLNEYFSAFDEIIERHG---GTVDKTIGDAVMAVFGLPGAHEDHAERAVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  499 LALDMMEIAGQVQV---DGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmsp 575
Cdd:cd07302  74 AALEMQEALAELNAereGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELL--- 150
                       170       180
                ....*....|....*....|....*....
gi 4504215  576 enSDPQFHLEHRGPVSMKGKKEPMQVWFL 604
Cdd:cd07302 151 --GDAGFEFEELGEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
348-604 5.91e-41

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 153.81  E-value: 5.91e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  348 ATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHK--RPVPAKRYDNVTILFS 425
Cdd:COG2114 149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  426 GIVGFNAFCSKHasgeGAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMME 505
Cdd:COG2114 229 DIVGFTALSERL----GPEELVELLNRYFSAMVEIIERHG---GTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQE 301
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  506 IAGQV-----QVDGESVQITIGIHTGEVVTGVIG--QRMPrYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmspens 578
Cdd:COG2114 302 ALAELnaelpAEGGPPLRVRIGIHTGEVVVGNIGseDRLD-YTVIGDTVNLAARLESLAKPGEILVSEATYDLL------ 374
                       250       260
                ....*....|....*....|....*.
gi 4504215  579 DPQFHLEHRGPVSMKGKKEPMQVWFL 604
Cdd:COG2114 375 RDRFEFRELGEVRLKGKAEPVEVYEL 400
 
Name Accession Description Interval E-value
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
412-605 1.62e-85

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 425528  Cd Length: 183  Bit Score: 264.88  E-value: 1.62e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    412 VPAKRYDNVTILFSGIVGFNAFCSKHAsgegAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIH 491
Cdd:pfam00211   1 VYAQPYDNVTILFADIVGFTALSSRHS----PEQVVRLLNELYTRFDRLLDKHK---VYKVKTIGDAYMVVSGLPEPSPA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    492 HARSICHLALDMMEIAGQVQVDG-ESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYR 570
Cdd:pfam00211  74 HARKIAEMALDMLEAIGEVNVESsEGLRVRVGIHTGPVVAGVIGARMPRYDLWGNTVNLASRMESTGVPGKIHVSEETYR 153
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 4504215    571 CLMspensDPQFHLEHRGPVSMKGKKEPMQVWFLS 605
Cdd:pfam00211 154 LLK-----TEGFEFTERGEIEVKGKGKMKTYFLNG 183
HNOBA pfam07701
Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and ...
207-406 1.54e-84

Heme NO binding associated; The HNOBA domain is found associated with the HNOB domain and pfam00211 in soluble cyclases and signalling proteins. The HNOB domain is predicted to function as a heme-dependent sensor for gaseous ligands, and transduce diverse downstream signals, in both bacteria and animals.


Pssm-ID: 462234  Cd Length: 214  Bit Score: 263.28  E-value: 1.54e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    207 RISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLD 286
Cdd:pfam07701   2 PISSDVFFRLFPFHVVFDRDMKIVSAGSSLARVFPDPDLIGKKLTDVFRLRRPLIEFTFDNILQHINVVFELQTKRPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215    287 VEK------------LECEDELTGTEISCLRLKGQMIYLPEADSILFLCSPSVMNLDDLTRRGLYLSDIPLHDATRDLVL 354
Cdd:pfam07701  82 KEEeaklsaaldaseEESSSDLSEESSRNLKLKGQMRYLPEWDSILFLCSPVVDNLEELRKQGLYLSDLPLHDASRDLVL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 4504215    355 LGEQFREEYKLTQE-LEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANEL 406
Cdd:pfam07701 162 AGQQQSAELKLALDqLEQKSAELEESMRELEEEKKKTDELLYSMLPKSVADRL 214
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
385-584 5.86e-80

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: 250.64  E-value: 5.86e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     385 DEKKKTDTLLYSVLPPSVANELRHKR-PVPAKRYDNVTILFSGIVGFNAFCSKhasgEGAMKIVNLLNDLYTRFDTLTDS 463
Cdd:smart00044   1 EEKKKTDRLLDQLLPASVAEQLKRGGsPVPAESYDNVTILFSDIVGFTSLCST----STPEQVVNLLNDLYSRFDQIIDR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     464 RKnpfVYKVETVGDKYMTVSGLPEPCIH-HARSICHLALDMMEIAGQV--QVDGESVQITIGIHTGEVVTGVIGQRMPRY 540
Cdd:smart00044  77 HG---GYKVKTIGDAYMVASGLPEEALVdHAELIADEALDMVEELKTVlvQHREEGLRVRIGIHTGPVVAGVVGIRMPRY 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 4504215     541 CLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmspENSDPQFHL 584
Cdd:smart00044 154 CLFGDTVNLASRMESAGDPGQIQVSEETYSLL---ARRGGQFVF 194
HNOB pfam07700
Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain ...
2-166 8.93e-68

Haem-NO-binding; The HNOB (Haem NO Binding) domain, is a predominantly alpha-helical domain and binds heme via a covalent linkage to histidine. It is a haem protein sensor (SONO) that displays femtomolar affinity for nitrous oxide, NO. It is predicted to function as a haem-dependent sensor for gaseous ligands and to transduce diverse downstream signals in both bacteria and animals.


Pssm-ID: 462233  Cd Length: 162  Bit Score: 217.75  E-value: 8.93e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215      2 YGFVNHALELLVIRNYGPEVWEDIKKEAQLdEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQES 81
Cdd:pfam07700   1 YGIVFEALQDLVEEKYGEEVWDEILEKAGL-EEGVFTPHETYDDEETLKLVEAAAKVTGLSVDELLEAFGRFFIKFFAES 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215     82 GYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDaEKGKGLILHYYSEREGLQDIVIGIIKTVAqQIHGTE 161
Cdd:pfam07700  80 GYPRFFKVLGRNLFDFLNNLDNLHEVLKLSYPGMKPPSFRCEE-ESDGGLVLHYYSKRKGLFPYVLGLLEGAA-EFFNED 157

                  ....*
gi 4504215    162 IDMKV 166
Cdd:pfam07700 158 VEIEV 162
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
419-604 4.04e-61

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: 200.88  E-value: 4.04e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  419 NVTILFSGIVGFNAFCSKHasgeGAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIHHARSICH 498
Cdd:cd07302   1 EVTVLFADIVGFTALSERL----GPEELVELLNEYFSAFDEIIERHG---GTVDKTIGDAVMAVFGLPGAHEDHAERAVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  499 LALDMMEIAGQVQV---DGESVQITIGIHTGEVVTGVIGQRMPRYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmsp 575
Cdd:cd07302  74 AALEMQEALAELNAereGGPPLRLRIGIHTGPVVAGVVGSERPEYTVIGDTVNLAARLESLAKPGQILVSEATYELL--- 150
                       170       180
                ....*....|....*....|....*....
gi 4504215  576 enSDPQFHLEHRGPVSMKGKKEPMQVWFL 604
Cdd:cd07302 151 --GDAGFEFEELGEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
348-604 5.91e-41

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 441717 [Multi-domain]  Cd Length: 407  Bit Score: 153.81  E-value: 5.91e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  348 ATRDLVLLGEQFREEYKLTQELEILTDRLQLTLRALEDEKKKTDTLLYSVLPPSVANELRHK--RPVPAKRYDNVTILFS 425
Cdd:COG2114 149 LALLLLLLLVALLLLALLLLLLLLLLLALLLLLLLALRERERLRDLLGRYLPPEVAERLLAGgeELRLGGERREVTVLFA 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  426 GIVGFNAFCSKHasgeGAMKIVNLLNDLYTRFDTLTDSRKnpfVYKVETVGDKYMTVSGLPEPCIHHARSICHLALDMME 505
Cdd:COG2114 229 DIVGFTALSERL----GPEELVELLNRYFSAMVEIIERHG---GTVDKFIGDGVMAVFGAPVAREDHAERAVRAALAMQE 301
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  506 IAGQV-----QVDGESVQITIGIHTGEVVTGVIG--QRMPrYCLFGNTVNLTSRTETTGEKGKINVSEYTYRCLmspens 578
Cdd:COG2114 302 ALAELnaelpAEGGPPLRVRIGIHTGEVVVGNIGseDRLD-YTVIGDTVNLAARLESLAKPGEILVSEATYDLL------ 374
                       250       260
                ....*....|....*....|....*.
gi 4504215  579 DPQFHLEHRGPVSMKGKKEPMQVWFL 604
Cdd:COG2114 375 RDRFEFRELGEVRLKGKAEPVEVYEL 400
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
419-562 2.52e-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: 107.06  E-value: 2.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504215  419 NVTILFSGIVGFnafcSKHASGEGAMKIVNLLNDLYTRFDTLTdsRKNPfVYKVETVGDKYMTVSGLPepcihHARSICH 498
Cdd:cd07556   1 PVTILFADIVGF----TSLADALGPDEGDELLNELAGRFDSLI--RRSG-DLKIKTIGDEFMVVSGLD-----HPAAAVA 68
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4504215  499 LALDM-MEIAGQVQVDGESVQITIGIHTGEVVTGVIGqRMPRYCLFGNTVNLTSRTETTGEKGKI 562
Cdd:cd07556  69 FAEDMrEAVSALNQSEGNPVRVRIGIHTGPVVVGVIG-SRPQYDVWGALVNLASRMESQAKAGQV 132
 
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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