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Conserved domains on  [gi|27734721|ref|NP_002596|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A isoform 1 [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;
555-806 1.31e-106

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 327.20  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   555 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 634
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   635 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 714
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   715 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 793
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 27734721   794 DAFV-DLPDLMQHL 806
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
219-324 8.49e-15

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 75.06  E-value: 8.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 298
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                        90       100
                ....*....|....*....|....*.
gi 27734721 299 NIQQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:COG2202  95 LFWVELSISPVRDEDGEITGFVGIAR 120
RpfG super family cl34613
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 73-169 5.67e-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: 5.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721  73 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 150
Cdd:COG3437   1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                        90
                ....*....|....*....
gi 27734721 151 KLSENTVIVGVVRRVDREE 169
Cdd:COG3437  76 PSTRDIPVIFLTALADPED 94
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
555-806 1.31e-106

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 327.20  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   555 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 634
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   635 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 714
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   715 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 793
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 27734721   794 DAFV-DLPDLMQHL 806
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
219-324 8.49e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 75.06  E-value: 8.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 298
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                        90       100
                ....*....|....*....|....*.
gi 27734721 299 NIQQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:COG2202  95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 219-324 2.59e-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: 58.20  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYA-KKKNG 297
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfRVPDG 84

                          90       100
                  ....*....|....*....|....*..
gi 27734721   298 DNIQQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:pfam00989  85 RPRHVEVRASPVRDAGGEILGFLGVLR 111
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 555-749 4.63e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 4.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 555 YHNSTHSADVLHATAYFLSKErikeTLDPIDEVAALIAATIHDVDHPGRTNSFlcnagselailYNDTAVLESHHAALAF 634
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEEL----GLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 635 QLTtgddkcnifknmERNDYRTLRQGIIDMVLATEMtKHFEHVNKFvnsinkplatleengetdknqeviNTMLRTPENR 714
Cdd:cd00077  66 EIL------------RELLLEEVIKLIDELILAVDA-SHHERLDGL------------------------GYPDGLKGEE 108

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27734721 715 TLIKRMLIKCADVSNPCRPL--QYCIEWAARISEEYF 749
Cdd:cd00077 109 ITLEARIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 230-324 8.35e-08

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: 51.09  E-value: 8.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 230 ITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPV 309
Cdd:cd00130   7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                        90
                ....*....|....*
gi 27734721 310 IGQGGKIRHYVSIIR 324
Cdd:cd00130  87 RDEGGEVIGLLGVVR 101
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 553-655 1.00e-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: 51.53  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721    553 NPYHNSTHSADVLHATAYflskerIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNagselailyndTAVLESHHAAL 632
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63

                           90       100
                   ....*....|....*....|...
gi 27734721    633 AFQLtTGDDKCNIFKNMERNDYR 655
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 ...
 219-324 4.37e-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: 49.60  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKK-KNG 297
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRrKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 27734721   298 DNIQQNVKIIPVIGQGGkIRHYVSIIR 324
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 73-169 5.67e-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: 5.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721  73 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 150
Cdd:COG3437   1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                        90
                ....*....|....*....
gi 27734721 151 KLSENTVIVGVVRRVDREE 169
Cdd:COG3437  76 PSTRDIPVIFLTALADPED 94
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 219-281 1.68e-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: 37.76  E-value: 1.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27734721    219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIR 281
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
555-806 1.31e-106

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 327.20  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   555 YHNSTHSADVLHATAYFLSKERIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNAGSELAILYNDTAVLESHHAALAF 634
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   635 QLTTgDDKCNIFKNMERNDYRTLRQGIIDMVLATEMTKHFEHVNKFVNSINKPLATLEENGETDKnqevintmlrtpenR 714
Cdd:pfam00233  81 QILQ-DEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEEDR--------------R 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   715 TLIKRMLIKCADVSNPCRPLQYCIEWAARISEEYFSQTDEEKQQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW 793
Cdd:pfam00233 146 LLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEAL 224

                         250
                  ....*....|....
gi 27734721   794 DAFV-DLPDLMQHL 806
Cdd:pfam00233 225 AKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
219-324 8.49e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 75.06  E-value: 8.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGD 298
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94

                        90       100
                ....*....|....*....|....*.
gi 27734721 299 NIQQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:COG2202  95 LFWVELSISPVRDEDGEITGFVGIAR 120
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 219-324 2.59e-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: 58.20  E-value: 2.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYA-KKKNG 297
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSfRVPDG 84

                          90       100
                  ....*....|....*....|....*..
gi 27734721   298 DNIQQNVKIIPVIGQGGKIRHYVSIIR 324
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 ...
 237-324 2.43e-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: 2.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   237 IQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTInsCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPVIGQGGKI 316
Cdd:pfam13426   4 IIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGEL 81


                  ....*...
gi 27734721   317 RHYVSIIR 324
Cdd:pfam13426  82 VGIIAILR 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 555-749 4.63e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 55.81  E-value: 4.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 555 YHNSTHSADVLHATAYFLSKErikeTLDPIDEVAALIAATIHDVDHPGRTNSFlcnagselailYNDTAVLESHHAALAF 634
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEEL----GLSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 635 QLTtgddkcnifknmERNDYRTLRQGIIDMVLATEMtKHFEHVNKFvnsinkplatleengetdknqeviNTMLRTPENR 714
Cdd:cd00077  66 EIL------------RELLLEEVIKLIDELILAVDA-SHHERLDGL------------------------GYPDGLKGEE 108

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 27734721 715 TLIKRMLIKCADVSNPCRPL--QYCIEWAARISEEYF 749
Cdd:cd00077 109 ITLEARIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 230-324 8.35e-08

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: 51.09  E-value: 8.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 230 ITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPV 309
Cdd:cd00130   7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86

                        90
                ....*....|....*
gi 27734721 310 IGQGGKIRHYVSIIR 324
Cdd:cd00130  87 RDEGGEVIGLLGVVR 101
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 553-655 1.00e-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: 51.53  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721    553 NPYHNSTHSADVLHATAYflskerIKETLDPIDEVAALIAATIHDVDHPGRTNSFLCNagselailyndTAVLESHHAAL 632
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63

                           90       100
                   ....*....|....*....|...
gi 27734721    633 AFQLtTGDDKCNIFKNMERNDYR 655
Cdd:smart00471  64 AEIL-LEEEEPRILEEILRTAIL 85
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
219-324 2.01e-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: 2.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPinEKKADLLDTINSCIRIGKE-WQGIYYAKKKNG 297
Cdd:COG3852  11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELF--PEDSPLRELLERALAEGQPvTEREVTLRRKDG 88

                        90       100
                ....*....|....*....|....*..
gi 27734721 298 DNIQQNVKIIPVIGQGGKIrHYVSIIR 324
Cdd:COG3852  89 EERPVDVSVSPLRDAEGEG-GVLLVLR 114
PAS COG2202
PAS domain [Signal transduction mechanisms];
206-324 4.12e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 52.33  E-value: 4.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 206 RSQLKLRAcnsvftALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKE 285
Cdd:COG2202 134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE 207

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 27734721 286 -WQGIYYAKKKNGDNIQQNVKIIPVIGqGGKIRHYVSIIR 324
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 ...
 219-324 4.37e-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: 49.60  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721   219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKK-KNG 297
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERRVRrKDG 86

                          90       100
                  ....*....|....*....|....*..
gi 27734721   298 DNIQQNVKIIPVIGQGGkIRHYVSIIR 324
Cdd:TIGR00229  87 SEIWVEVSVSPIRTNGG-ELGVVGIVR 112
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 219-324 5.11e-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: 5.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEkkadlldTINSCIRIGKEWQGIYYakKKNGD 298
Cdd:COG3829  15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS-------PLLEVLKTGKPVTGVIQ--KTGGK 85

                        90       100
                ....*....|....*....|....*.
gi 27734721 299 NIQQNVKIIPVIgQGGKIRHYVSIIR 324
Cdd:COG3829  86 GKTVIVTAIPIF-EDGEVIGAVETFR 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 175-324 4.46e-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: 49.97  E-value: 4.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 175 FISAGFTRRYVENPNIMACY------NELLQLEfGEVR-SQLKLRacnsvfTALENSEDAIEITSEDRFIQYANPAFETT 247
Cdd:COG5809 101 EFSSKLSPIFDQNGDIEGMLaisrdiTERKRME-EALReSEEKFR------LIFNHSPDGIIVTDLDGRIIYANPAACKL 173

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27734721 248 MGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNIQQNVKIIPvIGQGGKIRHYVSIIR 324
Cdd:COG5809 174 LGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAP-IKKNGEVDGIVIIFR 249
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 218-322 6.91e-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: 49.34  E-value: 6.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 218 FTALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVpINEKKADLLDTINSCIRIGKEWQGIYYAKKKNG 297
Cdd:COG5805  37 ETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDF-LEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDG 115

                        90       100
                ....*....|....*....|....*
gi 27734721 298 DNIQQNVKIIPVIGQGGKIRHYVSI 322
Cdd:COG5805 116 ELIYVEVKLFPIYNQNGQAAILALR 140
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 221-324 2.03e-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: 47.80  E-value: 2.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 221 LENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIRIGKEWQGIYYAKKKNGDNI 300
Cdd:COG5805 163 IENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIR 242

                        90       100
                ....*....|....*....|....
gi 27734721 301 QQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:COG5805 243 YFEAVIVPLIDTDGSVKGILVILR 266
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 206-324 2.44e-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: 44.58  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721 206 RSQLKLRACNSVFTAL-ENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEV--PINEKKADLLDTINSCIRI 282
Cdd:COG5809   5 KMELQLRKSEQRFRSLfENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFlhPDDEKELREILKLLKEGES 84

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 27734721 283 GKEWqgIYYAKKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIR 324
Cdd:COG5809  85 RDEL--EFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISR 124
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 73-169 5.67e-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: 5.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721  73 MRFHQdQLQVLLVftkEDNQCN--GFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 150
Cdd:COG3437   1 MRTGQ-APTVLIV---DDDPENleLLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75

                        90
                ....*....|....*....
gi 27734721 151 KLSENTVIVGVVRRVDREE 169
Cdd:COG3437  76 PSTRDIPVIFLTALADPED 94
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 219-281 1.68e-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: 37.76  E-value: 1.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27734721    219 TALENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADLLDTINSCIR 281
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
 82-181 3.05e-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: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721  82 VLLVftkEDNQ--CNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSSKLSENTVIV 159
Cdd:COG0784   8 ILVV---DDNPdnRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPG-MDGLELLRRIRALPRLPDIPII 83

                        90       100
                ....*....|....*....|....*
gi 27734721 160 ---GVVRRVDREElsvmpFISAGFT 181
Cdd:COG0784  84 altAYADEEDRER-----ALEAGAD 103
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 221-272 3.39e-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: 3.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 27734721   221 LENSEDAIEITSEDRFIQYANPAFETTMGYQSGELIGKELGEVPINEKKADL 272
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARL 52
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 82-161 6.32e-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: 38.35  E-value: 6.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27734721  82 VLLVftkEDNQCNG--FCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPrQLDAEALCRSIRSSKLSENTVIV 159
Cdd:COG3706   4 ILVV---DDDPTNRklLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79


                ..
gi 27734721 160 GV 161
Cdd:COG3706  80 FL 81
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
 79-150 6.54e-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: 6.54e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27734721  79 QLQVLLVftkEDNQ--CNGFCRACEKAGFKCTVTKEAQAVLACFLDKHHDIIIIDHRNPRqLDAEALCRSIRSS 150
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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