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Conserved domains on  [gi|40538865|ref|NP_954889|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B [Rattus norvegicus]

Protein Classification

high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8 family protein( domain architecture ID 11452923)

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;
490-737 1.01e-97

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 302.16  E-value: 1.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   490 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 569
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   570 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKplaaESEGSDCEcnptgkNFPENQILIK 649
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLES----KKTLDFLE------NEEDRRLLLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   650 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 727
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                         250
                  ....*....|
gi 40538865   728 AHLPALMQHL 737
Cdd:pfam00233 229 PELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
149-252 1.17e-16

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.45  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 228
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                        90       100
                ....*....|....*....|....
gi 40538865 229 DSIQQHVKITPVIGQGGKIRHFVS 252
Cdd:COG2202  94 SLFWVELSISPVRDEDGEITGFVG 117
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 30-111 8.27e-04

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


The actual alignment was detected with superfamily member COG3706:

Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 41.05  E-value: 8.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865  30 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASvlplLHAG 109
Cdd:COG3706  23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                ..
gi 40538865 110 FN 111
Cdd:COG3706  98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
490-737 1.01e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 302.16  E-value: 1.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   490 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 569
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   570 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKplaaESEGSDCEcnptgkNFPENQILIK 649
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLES----KKTLDFLE------NEEDRRLLLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   650 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 727
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                         250
                  ....*....|
gi 40538865   728 AHLPALMQHL 737
Cdd:pfam00233 229 PELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
149-252 1.17e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.45  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 228
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                        90       100
                ....*....|....*....|....
gi 40538865 229 DSIQQHVKITPVIGQGGKIRHFVS 252
Cdd:COG2202  94 SLFWVELSISPVRDEDGEITGFVG 117
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 164-253 1.59e-11

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: 60.94  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   164 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 243
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|
gi 40538865   244 GGKIRHFVSL 253
Cdd:pfam13426  78 GGELVGIIAI 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 160-252 1.48e-09

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: 55.72  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 160 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 238
Cdd:cd00130   7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                        90
                ....*....|....
gi 40538865 239 PVIGQGGKIRHFVS 252
Cdd:cd00130  85 PIRDEGGEVIGLLG 98
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 149-252 2.92e-08

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: 52.68  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 227
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                          90       100
                  ....*....|....*....|....*
gi 40538865   228 GDSIQQHVKITPVIGQGGkIRHFVS 252
Cdd:TIGR00229  86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 490-680 4.67e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 46.95  E-value: 4.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 490 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 569
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 570 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkplaaesegsdcecnPTGKNFPENQILIK 649
Cdd:cd00077  66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                       170       180       190
                ....*....|....*....|....*....|...
gi 40538865 650 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 680
Cdd:cd00077 113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 149-193 1.30e-05

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: 43.54  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 40538865    149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 193
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 150-251 1.58e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865  150 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 226
Cdd:PRK13558 153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                         90       100
                 ....*....|....*....|....*
gi 40538865  227 SGDSIQQHVKITPVIGQGGKIRHFV 251
Cdd:PRK13558 232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 488-586 2.86e-04

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: 41.51  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865    488 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELavlyndtavlesHHTAL 567
Cdd:smart00471   1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLE------------DHHFI 62

                           90
                   ....*....|....*....
gi 40538865    568 AFQLTVKDTKCNIFKNIDR 586
Cdd:smart00471  63 GAEILLEEEEPRILEEILR 81
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 30-111 8.27e-04

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 41.05  E-value: 8.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865  30 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASvlplLHAG 109
Cdd:COG3706  23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                ..
gi 40538865 110 FN 111
Cdd:COG3706  98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
490-737 1.01e-97

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 302.16  E-value: 1.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   490 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 569
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   570 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKplaaESEGSDCEcnptgkNFPENQILIK 649
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLES----KKTLDFLE------NEEDRRLLLL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   650 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 727
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                         250
                  ....*....|
gi 40538865   728 AHLPALMQHL 737
Cdd:pfam00233 229 PELQPLLDQL 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
149-252 1.17e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.45  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 228
Cdd:COG2202  15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                        90       100
                ....*....|....*....|....
gi 40538865 229 DSIQQHVKITPVIGQGGKIRHFVS 252
Cdd:COG2202  94 SLFWVELSISPVRDEDGEITGFVG 117
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 164-253 1.59e-11

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: 60.94  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   164 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 243
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|
gi 40538865   244 GGKIRHFVSL 253
Cdd:pfam13426  78 GGELVGIIAI 87
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
149-248 1.87e-10

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 63.33  E-value: 1.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDknrADLLDTINTCIKKGKE-WQGVYYARRKS 227
Cdd:COG3852  11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPvTEREVTLRRKD 87

                        90       100
                ....*....|....*....|.
gi 40538865 228 GDSIQQHVKITPVIGQGGKIR 248
Cdd:COG3852  88 GEERPVDVSVSPLRDAEGEGG 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 160-252 1.48e-09

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: 55.72  E-value: 1.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 160 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 238
Cdd:cd00130   7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                        90
                ....*....|....
gi 40538865 239 PVIGQGGKIRHFVS 252
Cdd:cd00130  85 PIRDEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 149-251 2.87e-09

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 55.12  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKS 227
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLiPEED--DAEVAELLRQALLQGEESRGFEVSFRVP 82

                          90       100
                  ....*....|....*....|....*
gi 40538865   228 -GDSIQQHVKITPVIGQGGKIRHFV 251
Cdd:pfam00989  83 dGRPRHVEVRASPVRDAGGEILGFL 107
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 149-252 2.92e-08

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: 52.68  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 227
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                          90       100
                  ....*....|....*....|....*
gi 40538865   228 GDSIQQHVKITPVIGQGGkIRHFVS 252
Cdd:TIGR00229  86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 149-253 2.97e-08

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: 56.70  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSdknradllDTINTCIKKGKEWQGVYYarRKSG 228
Cdd:COG3829  15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPN--------SPLLEVLKTGKPVTGVIQ--KTGG 84

                        90       100
                ....*....|....*....|....*
gi 40538865 229 DSIQQHVKITPVIgQGGKIRHFVSL 253
Cdd:COG3829  85 KGKTVIVTAIPIF-EDGEVIGAVET 108
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 169-252 1.92e-07

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 49.26  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   169 YVNPAFERMMGYHKGELLGK--ELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGK 246
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPD-DRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81


                  ....*.
gi 40538865   247 IRHFVS 252
Cdd:pfam08447  82 PVRVIG 87
PAS COG2202
PAS domain [Signal transduction mechanisms];
136-253 1.06e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.79  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 136 RSQFKLRAcnsvftALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPkSDKNRADLLDTINTCIKKGK 215
Cdd:COG2202 134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLL-HPEDRERLLELLRRLLEGGR 206

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 40538865 216 EWQGVYYaRRKSGDSIQQHVKITPV-IGQGGKIRHFVSL 253
Cdd:COG2202 207 ESYELEL-RLKDGDGRWVWVEASAVpLRDGGEVIGVLGI 244
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 490-680 4.67e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 46.95  E-value: 4.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 490 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 569
Cdd:cd00077   1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 570 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkplaaesegsdcecnPTGKNFPENQILIK 649
Cdd:cd00077  66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                       170       180       190
                ....*....|....*....|....*....|...
gi 40538865 650 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 680
Cdd:cd00077 113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 149-193 1.30e-05

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: 43.54  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 40538865    149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 193
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 150-251 1.58e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865  150 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 226
Cdd:PRK13558 153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                         90       100
                 ....*....|....*....|....*
gi 40538865  227 SGDSIQQHVKITPVIGQGGKIRHFV 251
Cdd:PRK13558 232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 488-586 2.86e-04

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: 41.51  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865    488 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELavlyndtavlesHHTAL 567
Cdd:smart00471   1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLE------------DHHFI 62

                           90
                   ....*....|....*....
gi 40538865    568 AFQLTVKDTKCNIFKNIDR 586
Cdd:smart00471  63 GAEILLEEEEPRILEEILR 81
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 117-255 3.24e-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: 43.95  E-value: 3.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 117 NSSIIACYNELIQIEHGEvRSQFKLRACNSVFTALD-HCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpK 195
Cdd:COG5805 129 NQNGQAAILALRDITKKK-KIEEILQEQEERLQTLIeNSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLEL-L 206

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 196 SDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKK 255
Cdd:COG5805 207 HPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILR 266
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 30-111 8.27e-04

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


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 41.05  E-value: 8.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865  30 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTRNFDAEAVCRSIRATNPSEHTVILAVVSQASDDHEEASvlplLHAG 109
Cdd:COG3706  23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                ..
gi 40538865 110 FN 111
Cdd:COG3706  98 AD 99
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 149-208 1.36e-03

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 37.91  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 40538865   149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGY-HKGELLGKELADLPKSDKNRADLLDTIN 208
Cdd:pfam13188   5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYeLLGELLGELLDLLDPLLEDALELLRELR 65
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 151-247 1.62e-03

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: 41.88  E-value: 1.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 151 LDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRadLLDTINTCIKKGKEWQGVYYARR-KSGD 229
Cdd:COG5809  21 FENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK--ELREILKLLKEGESRDELEFELRhKNGK 98

                        90
                ....*....|....*...
gi 40538865 230 SIQQHVKITPVIGQGGKI 247
Cdd:COG5809  99 RLEFSSKLSPIFDQNGDI 116
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 1-100 2.06e-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: 40.53  E-value: 2.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865   1 MRLTQDPiQVLLIfakEDSQS--DGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRqTRNFDAEAVCRSIRAT 78
Cdd:COG3437   1 MRTGQAP-TVLIV---DDDPEnlELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVR-MPGMDGFELLRLLRAD 75

                        90       100
                ....*....|....*....|..
gi 40538865  79 NPSEHTVILAVVSQASDDHEEA 100
Cdd:COG3437  76 PSTRDIPVIFLTALADPEDRER 97
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 149-244 6.08e-03

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 39.95  E-value: 6.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40538865 149 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINtcikkgKEWQGVYyaRRKSG 228
Cdd:COG5000  94 TILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALE------RGWQEEI--ELTRD 165

                        90
                ....*....|....*.
gi 40538865 229 DSIQQHVKITPVIGQG 244
Cdd:COG5000 166 GRRTLLVRASPLRDDG 181
 
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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