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Conserved domains on  [gi|341823698|ref|NP_001230066|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A isoform 3 [Homo sapiens]

Protein Classification

high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8 family protein( domain architecture ID 12816628)

high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8 family protein hydrolyzes the second messenger cAMP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
483-734 1.14e-105

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 1.14e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  483 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 562
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  563 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 642
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  643 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 721
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 341823698  722 DAFV-DLPDLMQHL 734
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
147-252 1.38e-14

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 226
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                         90       100
                 ....*....|....*....|....*.
gi 341823698 227 NIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:COG2202   95 LFWVELSISPVRDEDGEITGFVGIAR 120
RpfG super family cl34613
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-97 5.43e-04

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


The actual alignment was detected with superfamily member COG3437:

Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 42.07  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698   1 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 78
Cdd:COG3437    1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                         90
                 ....*....|....*....
gi 341823698  79 KLSENTVIVGVVRRVDREE 97
Cdd:COG3437   76 PSTRDIPVIFLTALADPED 94
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
483-734 1.14e-105

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 1.14e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  483 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 562
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  563 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 642
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  643 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 721
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 341823698  722 DAFV-DLPDLMQHL 734
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
147-252 1.38e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 226
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                         90       100
                 ....*....|....*....|....*.
gi 341823698 227 NIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:COG2202   95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 147-252 3.24e-10

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: 57.81  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYA-KKKNG 225
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfRVPDG 84

                          90       100
                  ....*....|....*....|....*..
gi 341823698  226 DNIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:pfam00989  85 RPRHVEVRASPVRDAGGEILGFLGVLR 111
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 483-677 1.19e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 54.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 483 YHNSTHSADVLHATAYFLSKErikeTLDPIDEVAALIAATIHDVDHPGRTNSFlcnagselailYNDTAVLESHHAALAF 562
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEEL----GLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 563 QLTtgddkcnifknmERNDYRTLRQGIIDMVLATEMtKHFEHVNKFvnsinkplatleengetdknqeviNTMLRTPENR 642
Cdd:cd00077   66 EIL------------RELLLEEVIKLIDELILAVDA-SHHERLDGL------------------------GYPDGLKGEE 108

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 341823698 643 TLIKRMLIKCADVSNPCRPL--QYCIEWAARISEEYF 677
Cdd:cd00077  109 ITLEARIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 158-252 1.31e-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: 50.32  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 158 ITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPV 237
Cdd:cd00130    7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                         90
                 ....*....|....*
gi 341823698 238 IGQGGKIRHYVSIIR 252
Cdd:cd00130   87 RDEGGEVIGLLGVVR 101
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 481-583 1.35e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 50.76  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698   481 NPYHNSTHSADVLHATAYflskerIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNagselailyndTAVLESHHAAL 560
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63

                           90       100
                   ....*....|....*....|...
gi 341823698   561 AFQLtTGDDKCNIFKNMERNDYR 583
Cdd:smart00471  64 AEIL-LEEEEPRILEEILRTAIL 85
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 147-252 5.14e-07

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: 49.21  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKK-KNG 225
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRrKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 341823698  226 DNIQQNVKIIPVIGQGGkIRHYVSIIR 252
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-97 5.43e-04

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: 42.07  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698   1 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 78
Cdd:COG3437    1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                         90
                 ....*....|....*....
gi 341823698  79 KLSENTVIVGVVRRVDREE 97
Cdd:COG3437   76 PSTRDIPVIFLTALADPED 94
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 147-209 2.11e-03

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: 37.38  E-value: 2.11e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341823698   147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIR 209
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
483-734 1.14e-105

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 322.96  E-value: 1.14e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  483 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 562
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  563 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 642
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  643 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 721
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 341823698  722 DAFV-DLPDLMQHL 734
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
147-252 1.38e-14

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 74.29  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 226
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                         90       100
                 ....*....|....*....|....*.
gi 341823698 227 NIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:COG2202   95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 147-252 3.24e-10

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: 57.81  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYA-KKKNG 225
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfRVPDG 84

                          90       100
                  ....*....|....*....|....*..
gi 341823698  226 DNIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:pfam00989  85 RPRHVEVRASPVRDAGGEILGFLGVLR 111
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 165-252 4.50e-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: 54.00  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  165 IQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTInsCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKI 244
Cdd:pfam13426   4 IIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGEL 81


                  ....*...
gi 341823698  245 RHYVSIIR 252
Cdd:pfam13426  82 VGIIAILR 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 483-677 1.19e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 54.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 483 YHNSTHSADVLHATAYFLSKErikeTLDPIDEVAALIAATIHDVDHPGRTNSFlcnagselailYNDTAVLESHHAALAF 562
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEEL----GLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 563 QLTtgddkcnifknmERNDYRTLRQGIIDMVLATEMtKHFEHVNKFvnsinkplatleengetdknqeviNTMLRTPENR 642
Cdd:cd00077   66 EIL------------RELLLEEVIKLIDELILAVDA-SHHERLDGL------------------------GYPDGLKGEE 108

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 341823698 643 TLIKRMLIKCADVSNPCRPL--QYCIEWAARISEEYF 677
Cdd:cd00077  109 ITLEARIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 158-252 1.31e-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: 50.32  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 158 ITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPV 237
Cdd:cd00130    7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                         90
                 ....*....|....*
gi 341823698 238 IGQGGKIRHYVSIIR 252
Cdd:cd00130   87 RDEGGEVIGLLGVVR 101
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 481-583 1.35e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 50.76  E-value: 1.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698   481 NPYHNSTHSADVLHATAYflskerIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNagselailyndTAVLESHHAAL 560
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63

                           90       100
                   ....*....|....*....|...
gi 341823698   561 AFQLtTGDDKCNIFKNMERNDYR 583
Cdd:smart00471  64 AEIL-LEEEEPRILEEILRTAIL 85
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
147-252 1.79e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 54.08  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPinEKKADLLDTINSCIRIGKE-WQGIYYAKKKNG 225
Cdd:COG3852   11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELF--PEDSPLRELLERALAEGQPvTEREVTLRRKDG 88

                         90       100
                 ....*....|....*....|....*..
gi 341823698 226 DNIQQNVKIIPVIGQGGKIrHYVSIIR 252
Cdd:COG3852   89 EERPVDVSVSPLRDAEGEG-GVLLVLR 114
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 147-252 5.14e-07

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: 49.21  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKK-KNG 225
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRrKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 341823698  226 DNIQQNVKIIPVIGQGGkIRHYVSIIR 252
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 147-252 5.68e-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: 52.85  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEkkadlldTINSCIRIGKEWQGIYYakKKNGD 226
Cdd:COG3829   15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS-------PLLEVLKTGKPVTGVIQ--KTGGK 85

                         90       100
                 ....*....|....*....|....*.
gi 341823698 227 NIQQNVKIIPVIgQGGKIRHYVSIIR 252
Cdd:COG3829   86 GKTVIVTAIPIF-EDGEVIGAVETFR 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
134-252 6.13e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.56  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 134 RSQLKLRAcnsvftALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKE 213
Cdd:COG2202  134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE 207

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 341823698 214 -WQGIYYAKKKNGDNIQQNVKIIPVIGqGGKIRHYVSIIR 252
Cdd:COG2202  208 sYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVR 246
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 103-252 6.83e-06

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: 49.20  E-value: 6.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 103 FISAGFTRRYVENPNIMACY------NELLQLEfGEVR-SQLKLRacnsvfTALENSEDAIEITSEDRFIQYANPAFETT 175
Cdd:COG5809  101 EFSSKLSPIFDQNGDIEGMLaisrdiTERKRME-EALReSEEKFR------LIFNHSPDGIIVTDLDGRIIYANPAACKL 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 341823698 176 MGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPvIGQGGKIRHYVSIIR 252
Cdd:COG5809  174 LGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAP-IKKNGEVDGIVIIFR 249
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 146-250 9.70e-06

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: 48.96  E-value: 9.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 146 FTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVpINEKKADLLDTINSCIRIGKEWQGIYYAKKKNG 225
Cdd:COG5805   37 ETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDF-LEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDG 115

                         90       100
                 ....*....|....*....|....*
gi 341823698 226 DNIQQNVKIIPVIGQGGKIRHYVSI 250
Cdd:COG5805  116 ELIYVEVKLFPIYNQNGQAAILALR 140
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 149-252 2.57e-05

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: 47.42  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 149 LENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI 228
Cdd:COG5805  163 IENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIR 242

                         90       100
                 ....*....|....*....|....
gi 341823698 229 QQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:COG5805  243 YFEAVIVPLIDTDGSVKGILVILR 266
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 134-252 3.58e-04

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: 43.81  E-value: 3.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698 134 RSQLKLRACNSVFTAL-ENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEV--PINEKKADLLDTINSCIRI 210
Cdd:COG5809    5 KMELQLRKSEQRFRSLfENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFlhPDDEKELREILKLLKEGES 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 341823698 211 GKEWqgIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIR 252
Cdd:COG5809   85 RDEL--EFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISR 124
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-97 5.43e-04

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: 42.07  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698   1 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 78
Cdd:COG3437    1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                         90
                 ....*....|....*....
gi 341823698  79 KLSENTVIVGVVRRVDREE 97
Cdd:COG3437   76 PSTRDIPVIFLTALADPED 94
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 147-209 2.11e-03

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: 37.38  E-value: 2.11e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341823698   147 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIR 209
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 10-109 2.71e-03

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 38.68  E-value: 2.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  10 VLLVftkEDNQ--CNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSSKLSENTVIV 87
Cdd:COG0784    8 ILVV---DDNPdnRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPG-MDGLELLRRIRALPRLPDIPII 83

                         90       100
                 ....*....|....*....|....*
gi 341823698  88 ---GVVRRVDREElsvmpFISAGFT 109
Cdd:COG0784   84 altAYADEEDRER-----ALEAGAD 103
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 149-200 2.96e-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: 38.16  E-value: 2.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 341823698  149 LENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADL 200
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARL 52
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 10-89 5.50e-03

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: 38.74  E-value: 5.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341823698  10 VLLVftkEDNQCNG--FCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPrQLDAEALCRSIRSSKLSENTVIV 87
Cdd:COG3706    4 ILVV---DDDPTNRklLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79


                 ..
gi 341823698  88 GV 89
Cdd:COG3706   80 FL 81
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 7-78 6.57e-03

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 38.78  E-value: 6.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 341823698   7 QLQVLLVftkEDNQ--CNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 78
Cdd:COG0745    1 MPRILVV---EDDPdiRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPG-MDGLEVCRRLRAR 70
 
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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