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Conserved domains on  [gi|1907178236|ref|XP_036008663|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
215-320 5.13e-13

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.28  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGD 294
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                          90       100
                  ....*....|....*....|....*.
gi 1907178236 295 NIQQNVKIIPVIGQGGKIRHYVSIIR 320
Cdd:COG2202    95 LFWVELSISPVRDEDGEITGFVGIAR 120
PDEase_I super family cl47516
3'5'-cyclic nucleotide phosphodiesterase;
550-574 4.18e-05

3'5'-cyclic nucleotide phosphodiesterase;


The actual alignment was detected with superfamily member pfam00233:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 45.23  E-value: 4.18e-05
                          10        20
                  ....*....|....*....|....*
gi 1907178236 550 YHNSTHAADVLHATAYFLSRDKIKR 574
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKE 25
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 78-165 8.19e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


The actual alignment was detected with superfamily member COG3706:

Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236  78 VLLVftkEDSQCNGFH--RACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPrQMDAETLCRSIRSSKFSENTVIV 155
Cdd:COG3706     4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79

                          90
                  ....*....|
gi 1907178236 156 GVVRRVDKEE 165
Cdd:COG3706    80 FLTALDDEED 89
 
Name Accession Description Interval E-value
PAS COG2202
PAS domain [Signal transduction mechanisms];
215-320 5.13e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.28  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGD 294
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                          90       100
                  ....*....|....*....|....*.
gi 1907178236 295 NIQQNVKIIPVIGQGGKIRHYVSIIR 320
Cdd:COG2202    95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 230-320 1.49e-09

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 55.16  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 230 DHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAInsCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQG 309
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|.
gi 1907178236 310 GKIRHYVSIIR 320
Cdd:pfam13426  79 GELVGIIAILR 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 226-320 2.78e-07

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 49.17  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 226 ITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPV 305
Cdd:cd00130     7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                          90
                  ....*....|....*
gi 1907178236 306 IGQGGKIRHYVSIIR 320
Cdd:cd00130    87 RDEGGEVIGLLGVVR 101
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 215-320 2.97e-06

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 46.52  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHT-QKKNG 293
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 1907178236 294 DNIQQNVKIIPVIGQGGkIRHYVSIIR 320
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
550-574 4.18e-05

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 45.23  E-value: 4.18e-05
                          10        20
                  ....*....|....*....|....*
gi 1907178236 550 YHNSTHAADVLHATAYFLSRDKIKR 574
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKE 25
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 215-259 2.79e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 39.30  E-value: 2.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907178236  215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQV 259
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 78-165 8.19e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236  78 VLLVftkEDSQCNGFH--RACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPrQMDAETLCRSIRSSKFSENTVIV 155
Cdd:COG3706     4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79

                          90
                  ....*....|
gi 1907178236 156 GVVRRVDKEE 165
Cdd:COG3706    80 FLTALDDEED 89
 
Name Accession Description Interval E-value
PAS COG2202
PAS domain [Signal transduction mechanisms];
215-320 5.13e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.28  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGD 294
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                          90       100
                  ....*....|....*....|....*.
gi 1907178236 295 NIQQNVKIIPVIGQGGKIRHYVSIIR 320
Cdd:COG2202    95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 230-320 1.49e-09

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 55.16  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 230 DHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAInsCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQG 309
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|.
gi 1907178236 310 GKIRHYVSIIR 320
Cdd:pfam13426  79 GELVGIIAILR 89
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 215-320 8.23e-09

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 53.58  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQK-KNG 293
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRvPDG 84

                          90       100
                  ....*....|....*....|....*..
gi 1907178236 294 DNIQQNVKIIPVIGQGGKIRHYVSIIR 320
Cdd:pfam00989  85 RPRHVEVRASPVRDAGGEILGFLGVLR 111
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 215-320 2.10e-07

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 53.62  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVpinEKKGDLLDAINSCVTVdkewqgVYHTQKKNGD 294
Cdd:COG3829    15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL---IPNSPLLEVLKTGKPV------TGVIQKTGGK 85

                          90       100
                  ....*....|....*....|....*.
gi 1907178236 295 NIQQNVKIIPVIgQGGKIRHYVSIIR 320
Cdd:COG3829    86 GKTVIVTAIPIF-EDGEVIGAVETFR 110
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
215-320 2.10e-07

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 53.31  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKkgDLLDAINSCVTVDKE-WQGVYHTQKKNG 293
Cdd:COG3852    11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPvTEREVTLRRKDG 88

                          90       100
                  ....*....|....*....|....*..
gi 1907178236 294 DNIQQNVKIIPVIGQGGKIrHYVSIIR 320
Cdd:COG3852    89 EERPVDVSVSPLRDAEGEG-GVLLVLR 114
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 226-320 2.78e-07

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 49.17  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 226 ITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPV 305
Cdd:cd00130     7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                          90
                  ....*....|....*
gi 1907178236 306 IGQGGKIRHYVSIIR 320
Cdd:cd00130    87 RDEGGEVIGLLGVVR 101
PAS COG2202
PAS domain [Signal transduction mechanisms];
202-320 9.12e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.41  E-value: 9.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 202 RSQLKLRAcnsvftALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKE 281
Cdd:COG2202   134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1907178236 282 -WQGVYHTQKKNGDNIQQNVKIIPVIGqGGKIRHYVSIIR 320
Cdd:COG2202   208 sYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVR 246
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 215-320 2.97e-06

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 46.52  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHT-QKKNG 293
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRvRRKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 1907178236 294 DNIQQNVKIIPVIGQGGkIRHYVSIIR 320
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 203-320 3.11e-05

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 46.89  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 203 SQLKLRacnsvfTALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEW 282
Cdd:COG5809   139 SEEKFR------LIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIA 212

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907178236 283 QGVYHTQKKNGDNIQQNVKIIPvIGQGGKIRHYVSIIR 320
Cdd:COG5809   213 QGEVRFWTKDGRWRLLEASGAP-IKKNGEVDGIVIIFR 249
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
550-574 4.18e-05

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 45.23  E-value: 4.18e-05
                          10        20
                  ....*....|....*....|....*
gi 1907178236 550 YHNSTHAADVLHATAYFLSRDKIKR 574
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKE 25
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 217-320 1.71e-04

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 44.34  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 217 LEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINScvtVDKEWQ-GVYHTQK--KNG 293
Cdd:COG5805   163 IENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIES---ITEVWQeFIIEREIitKDG 239

                          90       100
                  ....*....|....*....|....*..
gi 1907178236 294 DNIQQNVKIIPVIGQGGKIRHYVSIIR 320
Cdd:COG5805   240 RIRYFEAVIVPLIDTDGSVKGILVILR 266
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 215-259 2.79e-04

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 39.30  E-value: 2.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907178236  215 TALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQV 259
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 214-318 5.43e-04

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 42.80  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 214 FTALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVpINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNG 293
Cdd:COG5805    37 ETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDF-LEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDG 115

                          90       100
                  ....*....|....*....|....*
gi 1907178236 294 DNIQQNVKIIPVIGQGGKIRHYVSI 318
Cdd:COG5805   116 ELIYVEVKLFPIYNQNGQAAILALR 140
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 78-165 8.19e-04

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 40.66  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236  78 VLLVftkEDSQCNGFH--RACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPrQMDAETLCRSIRSSKFSENTVIV 155
Cdd:COG3706     4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79

                          90
                  ....*....|
gi 1907178236 156 GVVRRVDKEE 165
Cdd:COG3706    80 FLTALDDEED 89
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 69-233 1.46e-03

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 40.53  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236  69 MRFHQdQLQVLLVftkEDSQCN--GFHRACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPRqMDAETLCRSIRSS 146
Cdd:COG3437     1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907178236 147 KFSENTVIVGVVRRVDKEEssLMPFLAAGFTrRFIENPNVMAcynELLQLacgeVRSQLKLRACNsvfTALEKSQEAIEI 226
Cdd:COG3437    76 PSTRDIPVIFLTALADPED--RERALEAGAD-DYLTKPFDPE---ELLAR----VRNALELRRLQ---RELDDLVLYLKL 142


                  ....*..
gi 1907178236 227 TSEDHII 233
Cdd:COG3437   143 AAPLHDI 149
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 217-273 8.94e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 36.24  E-value: 8.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907178236 217 LEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAIN 273
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALR 57
 
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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