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Conserved domains on  [gi|82946979|dbj|BAE51843|]
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hypothetical protein amb3039 [Magnetospirillum magneticum AMB-1]

Protein Classification

adenylate/guanylate cyclase domain-containing protein (domain architecture ID 10163659)

adenylate/guanylate cyclase domain-containing protein similar to Glutamicibacter nicotianae adenylate cyclase and mammalian type 10 adenylate cyclase, which catalyze the formation of the signaling molecule cAMP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
421-580 4.06e-34

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  Cd Length: 177  Bit Score: 128.47  E-value: 4.06e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 421 MTVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASF-------ASAANAVEATVQIQRQ 493
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 494 VTAHNEK-QPNLPLHLRIGLNAGEPI-------QEEDDLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGGTG-AFTDGG 564
Cdd:cd07302  82 LAELNAErEGGPPLRLRIGIHTGPVVagvvgseRPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAGfEFEELG 161
                       170
                ....*....|....*.
gi 82946979 565 MHALKGFRDKFQLWEV 580
Cdd:cd07302 162 EVELKGKSGPVRVYRL 177
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
421-580 4.06e-34

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  Cd Length: 177  Bit Score: 128.47  E-value: 4.06e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 421 MTVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASF-------ASAANAVEATVQIQRQ 493
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 494 VTAHNEK-QPNLPLHLRIGLNAGEPI-------QEEDDLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGGTG-AFTDGG 564
Cdd:cd07302  82 LAELNAErEGGPPLRLRIGIHTGPVVagvvgseRPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAGfEFEELG 161
                       170
                ....*....|....*.
gi 82946979 565 MHALKGFRDKFQLWEV 580
Cdd:cd07302 162 EVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
422-581 4.32e-27

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 110.32  E-value: 4.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 422 TVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASFASA---ANAVEATVQIQRQVTAHN 498
Cdd:COG2114  48 TLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPsplEDAVACALDLQLALRNPL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 499 EKQPNLPLHLRIGLNAGEPIQEED---DLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGG-TGAFTDGGMHALKGFRDK 574
Cdd:COG2114 128 ARLRRESLRVRIGIHTGEVVVGNTggyTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDlVDLFSGLGSHRLKGLARP 207

                ....*..
gi 82946979 575 FQLWEVL 581
Cdd:COG2114 208 VRVYQLC 214
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
422-560 1.07e-11

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: 64.59  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979    422 TVMFTDMVGSTDLTQARgdqAAQEIVR---KHNAIVRTALTQFAGREVKHTGDGIMASF-----------ASAANAVEAT 487
Cdd:smart00044  38 TILFSDIVGFTSLCSTS---TPEQVVNllnDLYSRFDQIIDRHGGYKVKTIGDAYMVASglpeealvdhaELIADEALDM 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979    488 VQIQRQVTA-HNEKqpnlPLHLRIGLNAGEPIQEED-------DLFGSTVQLAARVCAATDSDQTLCTQVVKD-LAGGTG 558
Cdd:smart00044 115 VEELKTVLVqHREE----GLRVRIGIHTGPVVAGVVgirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYSlLARRGG 190

                   ..
gi 82946979    559 AF 560
Cdd:smart00044 191 QF 192
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
421-570 3.61e-10

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 59.56  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   421 MTVMFTDMVGSTDLTQArgdQAAQEIVR---KHNAIVRTALTQFAGREVKHTGDGIMASFASAANAVEATVQIQ------ 491
Cdd:pfam00211   9 VTILFADIVGFTALSSA---HSPIEVVRllnDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAemaldm 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   492 RQVTAHNEKQPNLPLHLRIGLNAGEPIQEED-------DLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGGTG-AFTDG 563
Cdd:pfam00211  86 LEAIGSVNVDSSEGLRVRIGIHTGPVVAGVIgarrpryDVWGDTVNVASRMESTGVPGKIHVSESTYRLLKTEGfEFTER 165

                  ....*..
gi 82946979   564 GMHALKG 570
Cdd:pfam00211 166 GEVEVKG 172
mod_pep_cyc TIGR04510
putative peptide modification system cyclase; Members of this family show homology to ...
418-516 6.62e-05

putative peptide modification system cyclase; Members of this family show homology to mononucleotidyl cyclases and to tetratricopeptide repeat (TPR) proteins. Members occur in next to two other markers of ribosomal peptide modification systems. One is a dehydrogenase related to SagB proteins from thiazole/oxazole modification systems. The other is the putative precursor, related to the nitrile hydratase-related leader peptide (NHLP) and nitrile hydratase alpha subunit families. These systems occur in many species of Xanthomonas and Stenotrophomonas, among others.


Pssm-ID: 275303  Cd Length: 814  Bit Score: 45.81  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   418 PSLMTVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTgDGIMASFASAANAVEATVQIQRQVTAH 497
Cdd:TIGR04510   3 PQLRTLLFTDLCDSLALVERIGDAAAAELFQEHDRLVLALQQRWRGRLIDRS-DGLLLLFERPIDALGFALDYQRGLQPL 81
                          90
                  ....*....|....*....
gi 82946979   498 NEkQPNLPLHLRIGLNAGE 516
Cdd:TIGR04510  82 GQ-ARKLELRARAGLHVGE 99
 
Name Accession Description Interval E-value
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
421-580 4.06e-34

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  Cd Length: 177  Bit Score: 128.47  E-value: 4.06e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 421 MTVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASF-------ASAANAVEATVQIQRQ 493
Cdd:cd07302   2 VTVLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFglpgaheDHAERAVRAALEMQEA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 494 VTAHNEK-QPNLPLHLRIGLNAGEPI-------QEEDDLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGGTG-AFTDGG 564
Cdd:cd07302  82 LAELNAErEGGPPLRLRIGIHTGPVVagvvgseRPEYTVIGDTVNLAARLESLAKPGQILVSEATYELLGDAGfEFEELG 161
                       170
                ....*....|....*.
gi 82946979 565 MHALKGFRDKFQLWEV 580
Cdd:cd07302 162 EVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
422-581 4.32e-27

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 110.32  E-value: 4.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 422 TVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASFASA---ANAVEATVQIQRQVTAHN 498
Cdd:COG2114  48 TLLFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPsplEDAVACALDLQLALRNPL 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 499 EKQPNLPLHLRIGLNAGEPIQEED---DLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGG-TGAFTDGGMHALKGFRDK 574
Cdd:COG2114 128 ARLRRESLRVRIGIHTGEVVVGNTggyTVVGSAVNQAARLESLAKPGQVLLSEATYDLVRDlVDLFSGLGSHRLKGLARP 207

                ....*..
gi 82946979 575 FQLWEVL 581
Cdd:COG2114 208 VRVYQLC 214
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
422-545 9.94e-17

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  Cd Length: 133  Bit Score: 78.17  E-value: 9.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979 422 TVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTGDGIMASF--ASAANAVEATVQIQRQVTAHNe 499
Cdd:cd07556   3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSglDHPAAAVAFAEDMREAVSALN- 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 82946979 500 KQPNLPLHLRIGLNAGEPI------QEEDDLFGSTVQLAARVCAATDSDQTL 545
Cdd:cd07556  82 QSEGNPVRVRIGIHTGPVVvgvigsRPQYDVWGALVNLASRMESQAKAGQVL 133
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
422-560 1.07e-11

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: 64.59  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979    422 TVMFTDMVGSTDLTQARgdqAAQEIVR---KHNAIVRTALTQFAGREVKHTGDGIMASF-----------ASAANAVEAT 487
Cdd:smart00044  38 TILFSDIVGFTSLCSTS---TPEQVVNllnDLYSRFDQIIDRHGGYKVKTIGDAYMVASglpeealvdhaELIADEALDM 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979    488 VQIQRQVTA-HNEKqpnlPLHLRIGLNAGEPIQEED-------DLFGSTVQLAARVCAATDSDQTLCTQVVKD-LAGGTG 558
Cdd:smart00044 115 VEELKTVLVqHREE----GLRVRIGIHTGPVVAGVVgirmpryCLFGDTVNLASRMESAGDPGQIQVSEETYSlLARRGG 190

                   ..
gi 82946979    559 AF 560
Cdd:smart00044 191 QF 192
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
421-570 3.61e-10

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 59.56  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   421 MTVMFTDMVGSTDLTQArgdQAAQEIVR---KHNAIVRTALTQFAGREVKHTGDGIMASFASAANAVEATVQIQ------ 491
Cdd:pfam00211   9 VTILFADIVGFTALSSA---HSPIEVVRllnDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAemaldm 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   492 RQVTAHNEKQPNLPLHLRIGLNAGEPIQEED-------DLFGSTVQLAARVCAATDSDQTLCTQVVKDLAGGTG-AFTDG 563
Cdd:pfam00211  86 LEAIGSVNVDSSEGLRVRIGIHTGPVVAGVIgarrpryDVWGDTVNVASRMESTGVPGKIHVSESTYRLLKTEGfEFTER 165

                  ....*..
gi 82946979   564 GMHALKG 570
Cdd:pfam00211 166 GEVEVKG 172
mod_pep_cyc TIGR04510
putative peptide modification system cyclase; Members of this family show homology to ...
418-516 6.62e-05

putative peptide modification system cyclase; Members of this family show homology to mononucleotidyl cyclases and to tetratricopeptide repeat (TPR) proteins. Members occur in next to two other markers of ribosomal peptide modification systems. One is a dehydrogenase related to SagB proteins from thiazole/oxazole modification systems. The other is the putative precursor, related to the nitrile hydratase-related leader peptide (NHLP) and nitrile hydratase alpha subunit families. These systems occur in many species of Xanthomonas and Stenotrophomonas, among others.


Pssm-ID: 275303  Cd Length: 814  Bit Score: 45.81  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82946979   418 PSLMTVMFTDMVGSTDLTQARGDQAAQEIVRKHNAIVRTALTQFAGREVKHTgDGIMASFASAANAVEATVQIQRQVTAH 497
Cdd:TIGR04510   3 PQLRTLLFTDLCDSLALVERIGDAAAAELFQEHDRLVLALQQRWRGRLIDRS-DGLLLLFERPIDALGFALDYQRGLQPL 81
                          90
                  ....*....|....*....
gi 82946979   498 NEkQPNLPLHLRIGLNAGE 516
Cdd:TIGR04510  82 GQ-ARKLELRARAGLHVGE 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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