NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|76882889|gb|ABA57570|]
View 

Adenylyl cyclase class-3/4/guanylyl cyclase [Nitrosococcus oceani ATCC 19707]

Protein Classification

adenylate/guanylate cyclase domain-containing protein (domain architecture ID 10660917)

adenylate/guanylate cyclase domain-containing protein with a CHASE2 sensor domain, similar to Myxococcus xanthus CyaA and CyaB adenylate cyclases

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
38-392 1.33e-45

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


:

Pssm-ID: 215016  Cd Length: 303  Bit Score: 166.01  E-value: 1.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889     38 WLFELRGSRAAPEEVVIVTIDRESSDWLGLPNepdkWPRELHAHLVQRLVQEGAAVIAFDIIFDEP--RDPVQDRLFAEA 115
Cdd:smart01080  10 ARFRLRPRRAPDPDIVIVAIDEASLAALGRWP----WPRSVLARLLDRLAAAGAKAIGFDILFDEPdrDSPDGDAALAAA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    116 IRKAGNVVLFEYL---KKHRKWVAIGGRQAEIeieeRVPPVPEFASAAVTLAPFPLPKVPARVSQAWLFkfgvptlpvaa 192
Cdd:smart01080  86 LARAPNVVLLAKLsreAGGGVLPSPPLPLPEL----PLPPLPGLADAAAGLGHVNEPDADGVVRRVPLL----------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    193 lqvyarpyygdlfrllkevtpekirwLKNDWRSVPSQPAliALARHLREWFQGDAQLPQSLLARLQSPEALSRfqgqsiv 272
Cdd:smart01080 151 --------------------------LRYGGKAYPSLAL--ELARVALGTPPLRLRLGGLGGPALTLGDGGYP------- 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    273 aalirgLSQEESFFLDFYGPPH--SIVTFPYYQLLkeNGGAPLPVS-FKGKAVFVGFSEqfqPEQKDGFYTVYSQPdgld 349
Cdd:smart01080 196 ------GDRAGRLLIPFDGPGRggTFPTVSAADVL--DGEVPALPElLRGKIVLIGATA---AGLGDLFPTPFSRV---- 260
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 76882889    350 ISGVEIAATAFANLLEQRSVTPLPLPLHYLIILLWGAGIGFFF 392
Cdd:smart01080 261 MPGVEIHANAIDNLLDGRFLRPAPPWWALLLLLLLWLLLGLLL 303
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
483-656 6.00e-44

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: 157.36  E-value: 6.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 483 CLATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDIREQACLAALDIEKAVA 562
Cdd:cd07302   4 VLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEALA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 563 EFN-RCTPEAPLPTRIGLHYGKIVIGSVGsSEHLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVV--VGLESIFTREL 639
Cdd:cd07302  84 ELNaEREGGPPLRLRIGIHTGPVVAGVVG-SERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYelLGDAGFEFEEL 160
                       170
                ....*....|....*..
gi 76882889 640 GEFCVKGRQQPLAIYEL 656
Cdd:cd07302 161 GEVELKGKSGPVRVYRL 177
 
Name Accession Description Interval E-value
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
38-392 1.33e-45

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 166.01  E-value: 1.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889     38 WLFELRGSRAAPEEVVIVTIDRESSDWLGLPNepdkWPRELHAHLVQRLVQEGAAVIAFDIIFDEP--RDPVQDRLFAEA 115
Cdd:smart01080  10 ARFRLRPRRAPDPDIVIVAIDEASLAALGRWP----WPRSVLARLLDRLAAAGAKAIGFDILFDEPdrDSPDGDAALAAA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    116 IRKAGNVVLFEYL---KKHRKWVAIGGRQAEIeieeRVPPVPEFASAAVTLAPFPLPKVPARVSQAWLFkfgvptlpvaa 192
Cdd:smart01080  86 LARAPNVVLLAKLsreAGGGVLPSPPLPLPEL----PLPPLPGLADAAAGLGHVNEPDADGVVRRVPLL----------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    193 lqvyarpyygdlfrllkevtpekirwLKNDWRSVPSQPAliALARHLREWFQGDAQLPQSLLARLQSPEALSRfqgqsiv 272
Cdd:smart01080 151 --------------------------LRYGGKAYPSLAL--ELARVALGTPPLRLRLGGLGGPALTLGDGGYP------- 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    273 aalirgLSQEESFFLDFYGPPH--SIVTFPYYQLLkeNGGAPLPVS-FKGKAVFVGFSEqfqPEQKDGFYTVYSQPdgld 349
Cdd:smart01080 196 ------GDRAGRLLIPFDGPGRggTFPTVSAADVL--DGEVPALPElLRGKIVLIGATA---AGLGDLFPTPFSRV---- 260
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 76882889    350 ISGVEIAATAFANLLEQRSVTPLPLPLHYLIILLWGAGIGFFF 392
Cdd:smart01080 261 MPGVEIHANAIDNLLDGRFLRPAPPWWALLLLLLLWLLLGLLL 303
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
483-656 6.00e-44

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: 157.36  E-value: 6.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 483 CLATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDIREQACLAALDIEKAVA 562
Cdd:cd07302   4 VLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEALA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 563 EFN-RCTPEAPLPTRIGLHYGKIVIGSVGsSEHLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVV--VGLESIFTREL 639
Cdd:cd07302  84 ELNaEREGGPPLRLRIGIHTGPVVAGVVG-SERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYelLGDAGFEFEEL 160
                       170
                ....*....|....*..
gi 76882889 640 GEFCVKGRQQPLAIYEL 656
Cdd:cd07302 161 GEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
484-660 5.49e-28

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 114.17  E-value: 5.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 484 LATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDireqACLAALDIEKAVAE 563
Cdd:COG2114  50 LFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLED----AVACALDLQLALRN 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 564 FNRCTPEAPLPTRIGLHYGKIVIGSVGSsehleYRAVGDVVNTASRIENLNKllGTRVLVSHEVV--VGLESIFTRELGE 641
Cdd:COG2114 126 PLARLRRESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAK--PGQVLLSEATYdlVRDLVDLFSGLGS 198
                       170
                ....*....|....*....
gi 76882889 642 FCVKGRQQPLAIYELIGRA 660
Cdd:COG2114 199 HRLKGLARPVRVYQLCHRS 217
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
3-428 1.61e-25

Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 226703  Cd Length: 400  Bit Score: 109.79  E-value: 1.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   3 RLAKAIMLGLLTAWVGFLATMVPPLGRLEvELGLAWLFELRGSRAAPEEVVIVTIDRESSDWLGlpnePDKWPRELHAHL 82
Cdd:COG4252  14 RLRVILLLALLVALLVLLLRLLGLLQLLE-LAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLG----QWPWPRAALARL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889  83 VQRLVQEGAAVIAFDIIFDEPRDPvQDRLFAEAIRKAGNVVLFEylkkhrkwvAIGGRQAeieieERVPPVPEFASAA-V 161
Cdd:COG4252  89 LDKLAAAQPRAIGLDIYRDLPSSP-GDRALAAVLQRAPNLIGVE---------KLSGDPG-----IAVNPPPELPRQAqI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 162 TLAPFPLPkvPARVSQAWLFKFGVPTLPVAAL-QVYARPYYgdlfrllkevTPEKIrwlkndwrsvpsQPALIAlarhlr 240
Cdd:COG4252 154 GFSDLILD--SDGKVRRLLLAATPGPEPKYSLaLKLALQYL----------ASLGI------------SPKYPD------ 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 241 ewfQGDAQLPQSLLARLQSPEalsrfqgqsivAALIRGLSQEESFFLDFYGPPHSIVTFPYYQLLkeNGGAPlPVSFKGK 320
Cdd:COG4252 204 ---PERLRLGKTTLPRLLGNS-----------GGYQGADAGGYQILLNYRSSSSDFRTVSLRDVL--NGKVP-AELIRGR 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 321 AVFVGFSeqfQPEQKDGFYTVYSQPDGLDISGVEIAATAFANL----LEQRSVTP-LPLPLHYLIILLWGAGIGFF---- 391
Cdd:COG4252 267 IVLIGAT---APSLNDYFATPYSSSLKELVPGVEIHANIVSQIlsalLDGRPLLPvWPDGAELLWIFAWSLLGGLLawrl 343
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 76882889 392 --FLYLPIYALLPSAAVLGMGYMSVAHhlftgnGLWLPV 428
Cdd:COG4252 344 rsPLRLLLAVGLALAGLLLISYLLFLA------GWWIPL 376
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
486-654 1.21e-16

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 79.98  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   486 TDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDIREQACLAALDIEKAVAEFN 565
Cdd:pfam00211  14 ADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAEMALDMLEAIGSVN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   566 RCTPEaPLPTRIGLHYGKIVIGSVGSSEhLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVVVGL--ESIFTRELGEFC 643
Cdd:pfam00211  94 VDSSE-GLRVRIGIHTGPVVAGVIGARR-PRYDVWGDTVNVASRMESTGV--PGKIHVSESTYRLLktEGFEFTERGEVE 169
                         170
                  ....*....|.
gi 76882889   644 VKGRQQPLAIY 654
Cdd:pfam00211 170 VKGKGKMETYF 180
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
15-386 1.91e-16

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 310087  Cd Length: 234  Bit Score: 80.06  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    15 AWVGFLATMVPPLGRLEvELGLAWLFELRgSRAAPEEVVIVTIDRESSDWLGlpNEPdkWPRELHAHLVQRLVQEGAAVI 94
Cdd:pfam05226   2 ALLALLLLRLLGLLQLE-LKAYDLLFRLR-RPPPDEDIVIVAIDEASLQRLG--RWP--WPRAVLARLLDKLAAAGPRAI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    95 AFDIIFDEPRDPV--QDRLFAEAirkagnvvlfeylkkhrkwvaiggrqaeieieervppvpefasaavtlapfplpkvp 172
Cdd:pfam05226  76 GLDILFDEPDRDVppGDEALAQS--------------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   173 arvsqawlfkfgvptLPVAALQVYarpyygdlfrLLKEVTPEkirwlkndwrsvpsqpalialarhlrewfqgdaqLPQS 252
Cdd:pfam05226  99 ---------------LALALALLY----------LKAEISPE----------------------------------LGKT 119
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   253 LLARLQSPEAlsrfqgqsivaalirglsqeESFFLDFYGPPHSIVTFPYYQLLkeNGGAPlPVSFKGKAVFVGFSEqfqP 332
Cdd:pfam05226 120 VFLRIPTDND--------------------GGILLNYRGPPGTFPTVSAADVL--EGKVP-PELFKDKIVLIGATA---P 173
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76882889   333 EQKDGFYTVYSQPdgldISGVEIAATAFANLLEQRSVTP--------LPLPLHYLIILLWGA 386
Cdd:pfam05226 174 GLGDLFPTPFSQV----MPGVEIHANALSQILDGSAVGRppwfliwvWPEWGELLWILLWLL 231
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
486-642 1.59e-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: 64.20  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    486 TDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKE-DIREQACLAALDIEKAVAEF 564
Cdd:smart00044  42 SDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTV 121
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76882889    565 NRCTPEAPLPTRIGLHYGKIVIGSVGsSEHLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVVvgleSIFTRELGEF 642
Cdd:smart00044 122 LVQHREEGLRVRIGIHTGPVVAGVVG-IRMPRYCLFGDTVNLASRMESAGD--PGQIQVSEETY----SLLARRGGQF 192
 
Name Accession Description Interval E-value
CHASE2 smart01080
CHASE2 is an extracellular sensory domain, which is present in various classes of ...
38-392 1.33e-45

CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria; Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognised by CHASE2 domains are not known at this time.


Pssm-ID: 215016  Cd Length: 303  Bit Score: 166.01  E-value: 1.33e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889     38 WLFELRGSRAAPEEVVIVTIDRESSDWLGLPNepdkWPRELHAHLVQRLVQEGAAVIAFDIIFDEP--RDPVQDRLFAEA 115
Cdd:smart01080  10 ARFRLRPRRAPDPDIVIVAIDEASLAALGRWP----WPRSVLARLLDRLAAAGAKAIGFDILFDEPdrDSPDGDAALAAA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    116 IRKAGNVVLFEYL---KKHRKWVAIGGRQAEIeieeRVPPVPEFASAAVTLAPFPLPKVPARVSQAWLFkfgvptlpvaa 192
Cdd:smart01080  86 LARAPNVVLLAKLsreAGGGVLPSPPLPLPEL----PLPPLPGLADAAAGLGHVNEPDADGVVRRVPLL----------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    193 lqvyarpyygdlfrllkevtpekirwLKNDWRSVPSQPAliALARHLREWFQGDAQLPQSLLARLQSPEALSRfqgqsiv 272
Cdd:smart01080 151 --------------------------LRYGGKAYPSLAL--ELARVALGTPPLRLRLGGLGGPALTLGDGGYP------- 195
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    273 aalirgLSQEESFFLDFYGPPH--SIVTFPYYQLLkeNGGAPLPVS-FKGKAVFVGFSEqfqPEQKDGFYTVYSQPdgld 349
Cdd:smart01080 196 ------GDRAGRLLIPFDGPGRggTFPTVSAADVL--DGEVPALPElLRGKIVLIGATA---AGLGDLFPTPFSRV---- 260
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 76882889    350 ISGVEIAATAFANLLEQRSVTPLPLPLHYLIILLWGAGIGFFF 392
Cdd:smart01080 261 MPGVEIHANAIDNLLDGRFLRPAPPWWALLLLLLLWLLLGLLL 303
CHD cd07302
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ...
483-656 6.00e-44

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: 157.36  E-value: 6.00e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 483 CLATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDIREQACLAALDIEKAVA 562
Cdd:cd07302   4 VLFADIVGFTALSERLGPEELVELLNEYFSAFDEIIERHGGTVDKTIGDAVMAVFGLPGAHEDHAERAVRAALEMQEALA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 563 EFN-RCTPEAPLPTRIGLHYGKIVIGSVGsSEHLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVV--VGLESIFTREL 639
Cdd:cd07302  84 ELNaEREGGPPLRLRIGIHTGPVVAGVVG-SERPEYTVIGDTVNLAARLESLAK--PGQILVSEATYelLGDAGFEFEEL 160
                       170
                ....*....|....*..
gi 76882889 640 GEFCVKGRQQPLAIYEL 656
Cdd:cd07302 161 GEVELKGKSGPVRVYRL 177
AcyC COG2114
Adenylate cyclase, class 3 [Signal transduction mechanisms];
484-660 5.49e-28

Adenylate cyclase, class 3 [Signal transduction mechanisms];


Pssm-ID: 225025  Cd Length: 227  Bit Score: 114.17  E-value: 5.49e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 484 LATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDireqACLAALDIEKAVAE 563
Cdd:COG2114  50 LFADIVGSTELSESLGDEALVELLNLYFDAVAEVVARHGGRVVKFIGDGFLAVFGRPSPLED----AVACALDLQLALRN 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 564 FNRCTPEAPLPTRIGLHYGKIVIGSVGSsehleYRAVGDVVNTASRIENLNKllGTRVLVSHEVV--VGLESIFTRELGE 641
Cdd:COG2114 126 PLARLRRESLRVRIGIHTGEVVVGNTGG-----YTVVGSAVNQAARLESLAK--PGQVLLSEATYdlVRDLVDLFSGLGS 198
                       170
                ....*....|....*....
gi 76882889 642 FCVKGRQQPLAIYELIGRA 660
Cdd:COG2114 199 HRLKGLARPVRVYQLCHRS 217
CHASE2 COG4252
Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction ...
3-428 1.61e-25

Extracellular (periplasmic) sensor domain CHASE2 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 226703  Cd Length: 400  Bit Score: 109.79  E-value: 1.61e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   3 RLAKAIMLGLLTAWVGFLATMVPPLGRLEvELGLAWLFELRGSRAAPEEVVIVTIDRESSDWLGlpnePDKWPRELHAHL 82
Cdd:COG4252  14 RLRVILLLALLVALLVLLLRLLGLLQLLE-LAAFDQLLRLRPSEPPDDRILIVAIDEQDLESLG----QWPWPRAALARL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889  83 VQRLVQEGAAVIAFDIIFDEPRDPvQDRLFAEAIRKAGNVVLFEylkkhrkwvAIGGRQAeieieERVPPVPEFASAA-V 161
Cdd:COG4252  89 LDKLAAAQPRAIGLDIYRDLPSSP-GDRALAAVLQRAPNLIGVE---------KLSGDPG-----IAVNPPPELPRQAqI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 162 TLAPFPLPkvPARVSQAWLFKFGVPTLPVAAL-QVYARPYYgdlfrllkevTPEKIrwlkndwrsvpsQPALIAlarhlr 240
Cdd:COG4252 154 GFSDLILD--SDGKVRRLLLAATPGPEPKYSLaLKLALQYL----------ASLGI------------SPKYPD------ 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 241 ewfQGDAQLPQSLLARLQSPEalsrfqgqsivAALIRGLSQEESFFLDFYGPPHSIVTFPYYQLLkeNGGAPlPVSFKGK 320
Cdd:COG4252 204 ---PERLRLGKTTLPRLLGNS-----------GGYQGADAGGYQILLNYRSSSSDFRTVSLRDVL--NGKVP-AELIRGR 266
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 321 AVFVGFSeqfQPEQKDGFYTVYSQPDGLDISGVEIAATAFANL----LEQRSVTP-LPLPLHYLIILLWGAGIGFF---- 391
Cdd:COG4252 267 IVLIGAT---APSLNDYFATPYSSSLKELVPGVEIHANIVSQIlsalLDGRPLLPvWPDGAELLWIFAWSLLGGLLawrl 343
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 76882889 392 --FLYLPIYALLPSAAVLGMGYMSVAHhlftgnGLWLPV 428
Cdd:COG4252 344 rsPLRLLLAVGLALAGLLLISYLLFLA------GWWIPL 376
Guanylate_cyc pfam00211
Adenylate and Guanylate cyclase catalytic domain;
486-654 1.21e-16

Adenylate and Guanylate cyclase catalytic domain;


Pssm-ID: 306677  Cd Length: 183  Bit Score: 79.98  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   486 TDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKEDIREQACLAALDIEKAVAEFN 565
Cdd:pfam00211  14 ADIVGFTALSSAHSPIEVVRLLNDLYARFDELLDEHGVYKVKTIGDAYMAASGLPEPSPAHARKIAEMALDMLEAIGSVN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   566 RCTPEaPLPTRIGLHYGKIVIGSVGSSEhLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVVVGL--ESIFTRELGEFC 643
Cdd:pfam00211  94 VDSSE-GLRVRIGIHTGPVVAGVIGARR-PRYDVWGDTVNVASRMESTGV--PGKIHVSESTYRLLktEGFEFTERGEVE 169
                         170
                  ....*....|.
gi 76882889   644 VKGRQQPLAIY 654
Cdd:pfam00211 170 VKGKGKMETYF 180
CHASE2 pfam05226
CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes ...
15-386 1.91e-16

CHASE2 domain; CHASE2 is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in bacteria. Specifically, CHASE2 domains are found in histidine kinases, adenylate cyclases, serine/threonine kinases and predicted diguanylate cyclases/phosphodiesterases. Environmental factors that are recognized by CHASE2 domains are not known at this time.


Pssm-ID: 310087  Cd Length: 234  Bit Score: 80.06  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    15 AWVGFLATMVPPLGRLEvELGLAWLFELRgSRAAPEEVVIVTIDRESSDWLGlpNEPdkWPRELHAHLVQRLVQEGAAVI 94
Cdd:pfam05226   2 ALLALLLLRLLGLLQLE-LKAYDLLFRLR-RPPPDEDIVIVAIDEASLQRLG--RWP--WPRAVLARLLDKLAAAGPRAI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    95 AFDIIFDEPRDPV--QDRLFAEAirkagnvvlfeylkkhrkwvaiggrqaeieieervppvpefasaavtlapfplpkvp 172
Cdd:pfam05226  76 GLDILFDEPDRDVppGDEALAQS--------------------------------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   173 arvsqawlfkfgvptLPVAALQVYarpyygdlfrLLKEVTPEkirwlkndwrsvpsqpalialarhlrewfqgdaqLPQS 252
Cdd:pfam05226  99 ---------------LALALALLY----------LKAEISPE----------------------------------LGKT 119
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889   253 LLARLQSPEAlsrfqgqsivaalirglsqeESFFLDFYGPPHSIVTFPYYQLLkeNGGAPlPVSFKGKAVFVGFSEqfqP 332
Cdd:pfam05226 120 VFLRIPTDND--------------------GGILLNYRGPPGTFPTVSAADVL--EGKVP-PELFKDKIVLIGATA---P 173
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76882889   333 EQKDGFYTVYSQPdgldISGVEIAATAFANLLEQRSVTP--------LPLPLHYLIILLWGA 386
Cdd:pfam05226 174 GLGDLFPTPFSQV----MPGVEIHANALSQILDGSAVGRppwfliwvWPEWGELLWILLWLL 231
CYCc smart00044
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ...
486-642 1.59e-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: 64.20  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889    486 TDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADLISKE-DIREQACLAALDIEKAVAEF 564
Cdd:smart00044  42 SDIVGFTSLCSTSTPEQVVNLLNDLYSRFDQIIDRHGGYKVKTIGDAYMVASGLPEEALvDHAELIADEALDMVEELKTV 121
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76882889    565 NRCTPEAPLPTRIGLHYGKIVIGSVGsSEHLEYRAVGDVVNTASRIENLNKllGTRVLVSHEVVvgleSIFTRELGEF 642
Cdd:smart00044 122 LVQHREEGLRVRIGIHTGPVVAGVVG-IRMPRYCLFGDTVNLASRMESAGD--PGQIQVSEETY----SLLARRGGQF 192
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
484-611 4.84e-10

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: 59.29  E-value: 4.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76882889 484 LATDVQQYTALAERFDLERLRPLLNRYFRSIFEPVKYRGGFIADIKGDAIMAIWADliskEDIreQACLA-ALDIEKAVA 562
Cdd:cd07556   5 LFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGL----DHP--AAAVAfAEDMREAVS 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 76882889 563 EFNRcTPEAPLPTRIGLHYGKIVIGSVGSSEhlEYRAVGDVVNTASRIE 611
Cdd:cd07556  79 ALNQ-SEGNPVRVRIGIHTGPVVVGVIGSRP--QYDVWGALVNLASRME 124
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH