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Conserved domains on  [gi|1622945299|ref|XP_014995792|]
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high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B isoform X2 [Macaca mulatta]

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;
847-1094 2.50e-101

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 319.50  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  847 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 926
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  927 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 1006
Cdd:pfam00233   81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299 1007 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 1084
Cdd:pfam00233  150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                          250
                   ....*....|
gi 1622945299 1085 AHLPALMQHL 1094
Cdd:pfam00233  229 PELQPLLDQL 238
PDE8 super family cl07304
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
 235-281 1.54e-22

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: 91.40  E-value: 1.54e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622945299  235 MGCAPSIHVSQSGVIY--CRDSDESNSPRQT-TSVSQ--GPAAPLPGLFVQT 281
Cdd:pfam08629    1 MGCAPSIHISDSGVIYhsCKDSDDSSSPNQTnTSMSQqlGNAAPLPGLFIKS 52
PAS COG2202
PAS domain [Signal transduction mechanisms];
506-609 1.32e-16

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 1.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 585
Cdd:COG2202     15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                           90       100
                   ....*....|....*....|....
gi 1622945299  586 DSIQQHVKITPVIGQGGKIRHFVS 609
Cdd:COG2202     94 SLFWVELSISPVRDEDGEITGFVG 117
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 387-468 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  387 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 466
Cdd:COG3706     23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                   ..
gi 1622945299  467 FN 468
Cdd:COG3706     98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
847-1094 2.50e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 319.50  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  847 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 926
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  927 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 1006
Cdd:pfam00233   81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299 1007 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 1084
Cdd:pfam00233  150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                          250
                   ....*....|
gi 1622945299 1085 AHLPALMQHL 1094
Cdd:pfam00233  229 PELQPLLDQL 238
PDE8 pfam08629
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
 235-281 1.54e-22

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: 91.40  E-value: 1.54e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622945299  235 MGCAPSIHVSQSGVIY--CRDSDESNSPRQT-TSVSQ--GPAAPLPGLFVQT 281
Cdd:pfam08629    1 MGCAPSIHISDSGVIYhsCKDSDDSSSPNQTnTSMSQqlGNAAPLPGLFIKS 52
PAS COG2202
PAS domain [Signal transduction mechanisms];
506-609 1.32e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 1.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 585
Cdd:COG2202     15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                           90       100
                   ....*....|....*....|....
gi 1622945299  586 DSIQQHVKITPVIGQGGKIRHFVS 609
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 ...
 521-610 7.36e-12

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: 62.48  E-value: 7.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  521 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 600
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                           90
                   ....*....|
gi 1622945299  601 GGKIRHFVSL 610
Cdd:pfam13426   78 GGELVGIIAI 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 517-609 4.68e-10

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: 57.64  E-value: 4.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  517 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 595
Cdd:cd00130      7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                           90
                   ....*....|....
gi 1622945299  596 PVIGQGGKIRHFVS 609
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 ...
 506-609 3.90e-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: 53.06  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 584
Cdd:TIGR00229    7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                           90       100
                   ....*....|....*....|....*
gi 1622945299  585 GDSIQQHVKITPVIGQGGkIRHFVS 609
Cdd:TIGR00229   86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 847-1037 9.67e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 52.34  E-value: 9.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  847 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 926
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  927 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkpmaaeiegsdcecnPAGKNFPENQILIK 1006
Cdd:cd00077     66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622945299 1007 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 1037
Cdd:cd00077    113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 506-550 8.18e-06

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: 44.70  E-value: 8.18e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1622945299   506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 550
Cdd:smart00091    5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 845-943 4.75e-05

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: 44.21  E-value: 4.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299   845 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNagselavlyndTAVLESHHtAL 924
Cdd:smart00471    1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHH-FI 62

                            90
                    ....*....|....*....
gi 1622945299   925 AFQLTVKDTKCNIFKNIDR 943
Cdd:smart00471   63 GAEILLEEEEPRILEEILR 81
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 507-608 5.41e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 44.06  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  507 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 583
Cdd:PRK13558   153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                           90       100
                   ....*....|....*....|....*
gi 1622945299  584 SGDSIQQHVKITPVIGQGGKIRHFV 608
Cdd:PRK13558   232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 387-468 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  387 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 466
Cdd:COG3706     23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                   ..
gi 1622945299  467 FN 468
Cdd:COG3706     98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
847-1094 2.50e-101

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 319.50  E-value: 2.50e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  847 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 926
Cdd:pfam00233    1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  927 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 1006
Cdd:pfam00233   81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299 1007 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPvVMPVFDRN-TCSIPKSQISFIDYFITDMFDAW-DAF 1084
Cdd:pfam00233  150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQGDLEKELGLP-VSPLMDREkKTSLPKSQIGFIDFIVLPLFEALaKLF 228

                          250
                   ....*....|
gi 1622945299 1085 AHLPALMQHL 1094
Cdd:pfam00233  229 PELQPLLDQL 238
PDE8 pfam08629
PDE8 phosphodiesterase; This region is found in members of the PDE8 phosphodiesterase family. ...
 235-281 1.54e-22

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: 91.40  E-value: 1.54e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1622945299  235 MGCAPSIHVSQSGVIY--CRDSDESNSPRQT-TSVSQ--GPAAPLPGLFVQT 281
Cdd:pfam08629    1 MGCAPSIHISDSGVIYhsCKDSDDSSSPNQTnTSMSQqlGNAAPLPGLFIKS 52
PAS COG2202
PAS domain [Signal transduction mechanisms];
506-609 1.32e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 1.32e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 585
Cdd:COG2202     15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                           90       100
                   ....*....|....*....|....
gi 1622945299  586 DSIQQHVKITPVIGQGGKIRHFVS 609
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 ...
 521-610 7.36e-12

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: 62.48  E-value: 7.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  521 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 600
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                           90
                   ....*....|
gi 1622945299  601 GGKIRHFVSL 610
Cdd:pfam13426   78 GGELVGIIAI 87
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
506-605 2.06e-10

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 63.71  E-value: 2.06e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDknrADLLDTINTCIKKGKE-WQGVYYARRKS 584
Cdd:COG3852     11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPvTEREVTLRRKD 87

                           90       100
                   ....*....|....*....|.
gi 1622945299  585 GDSIQQHVKITPVIGQGGKIR 605
Cdd:COG3852     88 GEERPVDVSVSPLRDAEGEGG 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 517-609 4.68e-10

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: 57.64  E-value: 4.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  517 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 595
Cdd:cd00130      7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                           90
                   ....*....|....
gi 1622945299  596 PVIGQGGKIRHFVS 609
Cdd:cd00130     85 PIRDEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 506-608 1.93e-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: 56.27  E-value: 1.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKS 584
Cdd:pfam00989    5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLiPEED--DAEVAELLRQALLQGEESRGFEVSFRVP 82

                           90       100
                   ....*....|....*....|....*
gi 1622945299  585 -GDSIQQHVKITPVIGQGGKIRHFV 608
Cdd:pfam00989   83 dGRPRHVEVRASPVRDAGGEILGFL 107
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 506-641 1.90e-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: 58.24  E-value: 1.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSdknradllDTINTCIKKGKEWQGVYYarRKSG 585
Cdd:COG3829     15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPN--------SPLLEVLKTGKPVTGVIQ--KTGG 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622945299  586 DSIQQHVKITPVIGQGGKIRHFVSLKKLcctTDNNKQIHKIHRDSGDNSQTEPHSF 641
Cdd:COG3829     85 KGKTVIVTAIPIFEDGEVIGAVETFRDI---TELKRLERKLREEELERGLSAKYTF 137
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 506-609 3.90e-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: 53.06  E-value: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 584
Cdd:TIGR00229    7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                           90       100
                   ....*....|....*....|....*
gi 1622945299  585 GDSIQQHVKITPVIGQGGkIRHFVS 609
Cdd:TIGR00229   86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 847-1037 9.67e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 52.34  E-value: 9.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  847 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 926
Cdd:cd00077      1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  927 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkpmaaeiegsdcecnPAGKNFPENQILIK 1006
Cdd:cd00077     66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1622945299 1007 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 1037
Cdd:cd00077    113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 526-609 2.76e-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: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  526 YVNPAFERMMGYHKGELLGK--ELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGK 603
Cdd:pfam08447    3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPD-DRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81


                   ....*.
gi 1622945299  604 IRHFVS 609
Cdd:pfam08447   82 PVRVIG 87
PAS COG2202
PAS domain [Signal transduction mechanisms];
493-610 1.15e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.18  E-value: 1.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  493 RSQFKLRAcnsvftALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPkSDKNRADLLDTINTCIKKGK 572
Cdd:COG2202    134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLL-HPEDRERLLELLRRLLEGGR 206

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1622945299  573 EWQGVYYaRRKSGDSIQQHVKITPV-IGQGGKIRHFVSL 610
Cdd:COG2202    207 ESYELEL-RLKDGDGRWVWVEASAVpLRDGGEVIGVLGI 244
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 506-550 8.18e-06

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: 44.70  E-value: 8.18e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1622945299   506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 550
Cdd:smart00091    5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 845-943 4.75e-05

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: 44.21  E-value: 4.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299   845 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNagselavlyndTAVLESHHtAL 924
Cdd:smart00471    1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVK-----------TSVLEDHH-FI 62

                            90
                    ....*....|....*....
gi 1622945299   925 AFQLTVKDTKCNIFKNIDR 943
Cdd:smart00471   63 GAEILLEEEEPRILEEILR 81
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 474-612 2.93e-04

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 44.72  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  474 NSSIIACYNELIQIEHGEvRSQFKLRACNSVFTALD-HCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpK 552
Cdd:COG5805    129 NQNGQAAILALRDITKKK-KIEEILQEQEERLQTLIeNSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLEL-L 206

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  553 SDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKK 612
Cdd:COG5805    207 HPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILR 266
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 507-608 5.41e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 44.06  E-value: 5.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  507 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 583
Cdd:PRK13558   153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                           90       100
                   ....*....|....*....|....*
gi 1622945299  584 SGDSIQQHVKITPVIGQGGKIRHFV 608
Cdd:PRK13558   232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 506-565 8.96e-04

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: 38.68  E-value: 8.96e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGY-HKGELLGKELADLPKSDKNRADLLDTIN 565
Cdd:pfam13188    5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYeLLGELLGELLDLLDPLLEDALELLRELR 65
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 508-604 1.28e-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: 42.65  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  508 LDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRadLLDTINTCIKKGKEWQGVYYARR-KSGD 586
Cdd:COG5809     21 FENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK--ELREILKLLKEGESRDELEFELRhKNGK 98

                           90
                   ....*....|....*...
gi 1622945299  587 SIQQHVKITPVIGQGGKI 604
Cdd:COG5809     99 RLEFSSKLSPIFDQNGDI 116
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 387-468 2.63e-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: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  387 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 466
Cdd:COG3706     23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                   ..
gi 1622945299  467 FN 468
Cdd:COG3706     98 AD 99
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 358-457 5.26e-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: 39.76  E-value: 5.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  358 MRLTQDPiQVLLIfakEDSQS--DGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTqNFDAEAVCRSIRAT 435
Cdd:COG3437      1 MRTGQAP-TVLIV---DDDPEnlELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMP-GMDGFELLRLLRAD 75

                           90       100
                   ....*....|....*....|..
gi 1622945299  436 NPSEHTVILAVVSRVSDDHEEA 457
Cdd:COG3437     76 PSTRDIPVIFLTALADPEDRER 97
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 506-601 7.39e-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: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622945299  506 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINtcikkgKEWQGVYyaRRKSG 585
Cdd:COG5000     94 TILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALE------RGWQEEI--ELTRD 165

                           90
                   ....*....|....*.
gi 1622945299  586 DSIQQHVKITPVIGQG 601
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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