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Conserved domains on  [gi|564329086|ref|XP_006229500|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A isoform X2 [Rattus norvegicus]

Protein Classification

PAS and HDc domain-containing protein( domain architecture ID 11654464)

protein containing domains PDE8, PAS, and HDc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
548-800 1.80e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 313.72  E-value: 1.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  548 YHNSTHAADVLHATAYFLSRNKLKDTLDRLDEVAALIAATIHDVDHPGRTNSFLCNAGKELAVLYNDTAVLESHHAALAF 627
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  628 QLtLENDKCNIFKNTDRNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLKAQKNEVQEtgrslediramvrtpES 707
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEE---------------DR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  708 RTLIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDA 786
Cdd:pfam00233 145 RLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEA 223
                         250
                  ....*....|....*
gi 564329086  787 WDAFV-YLPNLMRHL 800
Cdd:pfam00233 224 LAKLFpELQPLLDQL 238
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
213-318 2.33e-12

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQKKNGD 292
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94
                         90       100
                 ....*....|....*....|....*.
gi 564329086 293 NIQQNVKIIPVIGQGGKIRHYVSIIR 318
Cdd:COG2202   95 LFWVELSISPVRDEDGEITGFVGIAR 120
PDE8 super family cl07304
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
1-24 2.26e-04

PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. It is found with pfam00233.


The actual alignment was detected with superfamily member pfam08629:

Pssm-ID: 400795  Cd Length: 52  Bit Score: 39.78  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....
gi 564329086    1 MGCAPSIHISDNRVSNPSDSDGED 24
Cdd:pfam08629   1 MGCAPSIHISDSGVIYHSCKDSDD 24
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
76-164 2.41e-03

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: 39.89  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  76 VLLVftkEDSQCNGFY--RACEKAGFKCTVTKEVQTVLACFQDKLHDIIIIDHRNPrQMDAEAMCRSIRSSKLSENTVIV 153
Cdd:COG3706    4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79
                         90
                 ....*....|.
gi 564329086 154 GVVRRVDKEEV 164
Cdd:COG3706   80 FLTALDDEEDR 90
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
548-800 1.80e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 313.72  E-value: 1.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  548 YHNSTHAADVLHATAYFLSRNKLKDTLDRLDEVAALIAATIHDVDHPGRTNSFLCNAGKELAVLYNDTAVLESHHAALAF 627
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  628 QLtLENDKCNIFKNTDRNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLKAQKNEVQEtgrslediramvrtpES 707
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEE---------------DR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  708 RTLIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDA 786
Cdd:pfam00233 145 RLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEA 223
                         250
                  ....*....|....*
gi 564329086  787 WDAFV-YLPNLMRHL 800
Cdd:pfam00233 224 LAKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
213-318 2.33e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQKKNGD 292
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94
                         90       100
                 ....*....|....*....|....*.
gi 564329086 293 NIQQNVKIIPVIGQGGKIRHYVSIIR 318
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 ...
228-318 6.22e-10

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: 56.70  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  228 DHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAInsCVTIDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQG 307
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                          90
                  ....*....|.
gi 564329086  308 GKIRHYVSIIR 318
Cdd:pfam13426  79 GELVGIIAILR 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
548-743 7.52e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.12  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 548 YHNSTHAADVLHATAYFLSRNKLKDtldrLDEVAALIAATIHDVDHPGRTNSFlcnagkelavlYNDTAVLESHHAALAF 627
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLSE----EDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 628 QLtlendkcnifknTDRNDYRTLRQSIIDMVLATEMtKHFEHVNKFINSINKPLKAQKNEVqetgrslediramvrtpes 707
Cdd:cd00077   66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGLGYPDGLKGEEITLEA------------------- 113
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564329086 708 rtlikrMMIKCADVSNPCRPL--EHCIEWAARISEEYF 743
Cdd:cd00077  114 ------RIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
546-648 2.62e-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: 49.99  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086   546 NPYHNSTHAADVLHATAYflsrnkLKDTLDRLDEVAALIAATIHDVDHPGRTNSFLCNagkelavlyndTAVLESHHAAL 625
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100
                   ....*....|....*....|...
gi 564329086   626 AFQLtLENDKCNIFKNTDRNDYR 648
Cdd:smart00471  64 AEIL-LEEEEPRILEEILRTAIL 85
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
224-318 3.64e-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: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 224 ITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQKKNGDNIQQNVKIIPV 303
Cdd:cd00130    7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86
                         90
                 ....*....|....*
gi 564329086 304 IGQGGKIRHYVSIIR 318
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 ...
213-318 5.62e-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: 46.13  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVpineKKGDLLDAINSCV--TIDKEWQGVYHT---Q 287
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLEL----IPEEDREEVRERIerRLEGEPEPVSEErrvR 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 564329086  288 KKNGDNIQQNVKIIPVIGQGGkIRHYVSIIR 318
Cdd:TIGR00229  83 RKDGSEIWVEVSVSPIRTNGG-ELGVVGIVR 112
PDE8 pfam08629
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
1-24 2.26e-04

PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. It is found with pfam00233.


Pssm-ID: 400795  Cd Length: 52  Bit Score: 39.78  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....
gi 564329086    1 MGCAPSIHISDNRVSNPSDSDGED 24
Cdd:pfam08629   1 MGCAPSIHISDSGVIYHSCKDSDD 24
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
213-257 1.63e-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: 1.63e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 564329086   213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQV 257
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
76-164 2.41e-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: 39.89  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  76 VLLVftkEDSQCNGFY--RACEKAGFKCTVTKEVQTVLACFQDKLHDIIIIDHRNPrQMDAEAMCRSIRSSKLSENTVIV 153
Cdd:COG3706    4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79
                         90
                 ....*....|.
gi 564329086 154 GVVRRVDKEEV 164
Cdd:COG3706   80 FLTALDDEEDR 90
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
548-800 1.80e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 313.72  E-value: 1.80e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  548 YHNSTHAADVLHATAYFLSRNKLKDTLDRLDEVAALIAATIHDVDHPGRTNSFLCNAGKELAVLYNDTAVLESHHAALAF 627
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  628 QLtLENDKCNIFKNTDRNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLKAQKNEVQEtgrslediramvrtpES 707
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFLENEE---------------DR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  708 RTLIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDA 786
Cdd:pfam00233 145 RLLLLSMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEA 223
                         250
                  ....*....|....*
gi 564329086  787 WDAFV-YLPNLMRHL 800
Cdd:pfam00233 224 LAKLFpELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
213-318 2.33e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 2.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQKKNGD 292
Cdd:COG2202   15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGS 94
                         90       100
                 ....*....|....*....|....*.
gi 564329086 293 NIQQNVKIIPVIGQGGKIRHYVSIIR 318
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 ...
228-318 6.22e-10

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: 56.70  E-value: 6.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  228 DHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAInsCVTIDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQG 307
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                          90
                  ....*....|.
gi 564329086  308 GKIRHYVSIIR 318
Cdd:pfam13426  79 GELVGIIAILR 89
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
548-743 7.52e-10

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 58.12  E-value: 7.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 548 YHNSTHAADVLHATAYFLSRNKLKDtldrLDEVAALIAATIHDVDHPGRTNSFlcnagkelavlYNDTAVLESHHAALAF 627
Cdd:cd00077    1 EHRFEHSLRVAQLARRLAEELGLSE----EDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 628 QLtlendkcnifknTDRNDYRTLRQSIIDMVLATEMtKHFEHVNKFINSINKPLKAQKNEVqetgrslediramvrtpes 707
Cdd:cd00077   66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGLGYPDGLKGEEITLEA------------------- 113
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564329086 708 rtlikrMMIKCADVSNPCRPL--EHCIEWAARISEEYF 743
Cdd:cd00077  114 ------RIVKLADRLDALRRDsrEKRRRIAEEDLEELL 145
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
213-318 3.68e-08

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: 52.42  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQK-KNG 291
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRvPDG 84
                          90       100
                  ....*....|....*....|....*..
gi 564329086  292 DNIQQNVKIIPVIGQGGKIRHYVSIIR 318
Cdd:pfam00989  85 RPRHVEVRASPVRDAGGEILGFLGVLR 111
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
546-648 2.62e-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: 49.99  E-value: 2.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086   546 NPYHNSTHAADVLHATAYflsrnkLKDTLDRLDEVAALIAATIHDVDHPGRTNSFLCNagkelavlyndTAVLESHHAAL 625
Cdd:smart00471   1 SDYHVFEHSLRVAQLAAA------LAEELGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHHFIG 63
                           90       100
                   ....*....|....*....|...
gi 564329086   626 AFQLtLENDKCNIFKNTDRNDYR 648
Cdd:smart00471  64 AEIL-LEEEEPRILEEILRTAIL 85
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
224-318 3.64e-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: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 224 ITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEWQGVYHTQKKNGDNIQQNVKIIPV 303
Cdd:cd00130    7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPI 86
                         90
                 ....*....|....*
gi 564329086 304 IGQGGKIRHYVSIIR 318
Cdd:cd00130   87 RDEGGEVIGLLGVVR 101
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
213-318 3.86e-07

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 52.93  E-value: 3.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKkgDLLDAINSCVTIDKE-WQGVYHTQKKNG 291
Cdd:COG3852   11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPvTEREVTLRRKDG 88
                         90       100
                 ....*....|....*....|....*..
gi 564329086 292 DNIQQNVKIIPVIGQGGKIrHYVSIIR 318
Cdd:COG3852   89 EERPVDVSVSPLRDAEGEG-GVLLVLR 114
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
213-318 5.06e-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: 5.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVpinEKKGDLLDAINSCVTIdkewqgVYHTQKKNGD 292
Cdd:COG3829   15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL---IPNSPLLEVLKTGKPV------TGVIQKTGGK 85
                         90       100
                 ....*....|....*....|....*.
gi 564329086 293 NIQQNVKIIPVIgQGGKIRHYVSIIR 318
Cdd:COG3829   86 GKTVIVTAIPIF-EDGEVIGAVETFR 110
PAS COG2202
PAS domain [Signal transduction mechanisms];
200-318 2.81e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 49.64  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 200 RSQLKLRAcnsvftALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCV-TIDK 278
Cdd:COG2202  134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLeGGRE 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564329086 279 EWQGVYHTQKKNGDNIQQNVKIIPVIGqGGKIRHYVSIIR 318
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 ...
213-318 5.62e-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: 46.13  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVpineKKGDLLDAINSCV--TIDKEWQGVYHT---Q 287
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLEL----IPEEDREEVRERIerRLEGEPEPVSEErrvR 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 564329086  288 KKNGDNIQQNVKIIPVIGQGGkIRHYVSIIR 318
Cdd:TIGR00229  83 RKDGSEIWVEVSVSPIRTNGG-ELGVVGIVR 112
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
201-318 5.68e-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: 46.51  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 201 SQLKLRacnsvfTALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTIDKEW 280
Cdd:COG5809  139 SEEKFR------LIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIA 212
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564329086 281 QGVYHTQKKNGDNIQQNVKIIPvIGQGGKIRHYVSIIR 318
Cdd:COG5809  213 QGEVRFWTKDGRWRLLEASGAP-IKKNGEVDGIVIIFR 249
PDE8 pfam08629
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
1-24 2.26e-04

PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. It is found with pfam00233.


Pssm-ID: 400795  Cd Length: 52  Bit Score: 39.78  E-value: 2.26e-04
                          10        20
                  ....*....|....*....|....
gi 564329086    1 MGCAPSIHISDNRVSNPSDSDGED 24
Cdd:pfam08629   1 MGCAPSIHISDSGVIYHSCKDSDD 24
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
215-318 4.95e-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: 43.57  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 215 LEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQVPINEKKGDLLDAINScvtIDKEWQ-GVYHTQK--KNG 291
Cdd:COG5805  163 IENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIES---ITEVWQeFIIEREIitKDG 239
                         90       100
                 ....*....|....*....|....*..
gi 564329086 292 DNIQQNVKIIPVIGQGGKIRHYVSIIR 318
Cdd:COG5805  240 RIRYFEAVIVPLIDTDGSVKGILVILR 266
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
212-316 1.46e-03

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: 42.03  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 212 FTALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGK--------ELAQVPINEKKGdlLDAINSCVTIDKEWqgv 283
Cdd:COG5805   37 ETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKtifdflekEYHYRVKTRIER--LQKGYDVVMIEQIY--- 111
                         90       100       110
                 ....*....|....*....|....*....|...
gi 564329086 284 yhtqKKNGDNIQQNVKIIPVIGQGGKIRHYVSI 316
Cdd:COG5805  112 ----CKDGELIYVEVKLFPIYNQNGQAAILALR 140
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
213-257 1.63e-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: 1.63e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 564329086   213 TALEKSQEAIEITSEDHIIQYANPAFETTMGYQSGELIGKELAQV 257
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
76-164 2.41e-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: 39.89  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  76 VLLVftkEDSQCNGFY--RACEKAGFKCTVTKEVQTVLACFQDKLHDIIIIDHRNPrQMDAEAMCRSIRSSKLSENTVIV 153
Cdd:COG3706    4 ILVV---DDDPTNRKLlrRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMP-DMDGLELCRRLRADPRTADIPII 79
                         90
                 ....*....|.
gi 564329086 154 GVVRRVDKEEV 164
Cdd:COG3706   80 FLTALDDEEDR 90
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
67-231 5.06e-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: 39.38  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086  67 MRFHQdQLQVLLVftkEDSQCNGFY--RACEKAGFKCTVTKEVQTVLACFQDKLHDIIIIDHRNPRqMDAEAMCRSIRSS 144
Cdd:COG3437    1 MRTGQ-APTVLIV---DDDPENLELlrQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPG-MDGFELLRLLRAD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564329086 145 KLSENTVIVGVVRRVDKEEVSLmpFLAAGFTrRYIENPNVMAcynELLQLafgeVRSQLKLRACNsvfTALEKSQEAIEI 224
Cdd:COG3437   76 PSTRDIPVIFLTALADPEDRER--ALEAGAD-DYLTKPFDPE---ELLAR----VRNALELRRLQ---RELDDLVLYLKL 142

                 ....*..
gi 564329086 225 TSEDHII 231
Cdd:COG3437  143 AAPLHDI 149
 
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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