NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1774222155|ref|NP_001363001|]
View 

high affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8B isoform 20 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
513-705 2.00e-76

3'5'-cyclic nucleotide phosphodiesterase;


:

Pssm-ID: 459723  Cd Length: 238  Bit Score: 245.54  E-value: 2.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 513 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 592
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 593 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 672
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774222155 673 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQ 705
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQ 182
PAS COG2202
PAS domain [Signal transduction mechanisms];
172-275 8.26e-17

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 251
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                          90       100
                  ....*....|....*....|....
gi 1774222155 252 DSIQQHVKITPVIGQGGKIRHFVS 275
Cdd:COG2202    94 SLFWVELSISPVRDEDGEITGFVG 117
PleD super family cl34659
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 53-134 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  53 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 132
Cdd:COG3706    23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                  ..
gi 1774222155 133 FN 134
Cdd:COG3706    98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
513-705 2.00e-76

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 245.54  E-value: 2.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 513 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 592
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 593 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 672
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774222155 673 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQ 705
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQ 182
PAS COG2202
PAS domain [Signal transduction mechanisms];
172-275 8.26e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 251
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                          90       100
                  ....*....|....*....|....
gi 1774222155 252 DSIQQHVKITPVIGQGGKIRHFVS 275
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 ...
 187-276 1.61e-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: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 187 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 266
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|
gi 1774222155 267 GGKIRHFVSL 276
Cdd:pfam13426  78 GGELVGIIAI 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 183-275 1.33e-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: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 183 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 261
Cdd:cd00130     7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....
gi 1774222155 262 PVIGQGGKIRHFVS 275
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 ...
 172-275 2.49e-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: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 250
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                          90       100
                  ....*....|....*....|....*
gi 1774222155 251 GDSIQQHVKITPVIGQGGkIRHFVS 275
Cdd:TIGR00229  86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 513-703 1.54e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 513 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 592
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 593 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkpmaaeiegsdcecnPAGKNFPENQILIK 672
Cdd:cd00077    66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774222155 673 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 703
Cdd:cd00077   113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-216 1.12e-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: 1.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1774222155  172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 216
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 173-274 1.45e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 173 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 249
Cdd:PRK13558  153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                          90       100
                  ....*....|....*....|....*
gi 1774222155 250 SGDSIQQHVKITPVIGQGGKIRHFV 274
Cdd:PRK13558  232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 511-609 1.56e-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: 41.90  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  511 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELavlyndtavlesHHTAL 590
Cdd:smart00471   1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLE------------DHHFI 62

                           90
                   ....*....|....*....
gi 1774222155  591 AFQLTVKDTKCNIFKNIDR 609
Cdd:smart00471  63 GAEILLEEEEPRILEEILR 81
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 53-134 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  53 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 132
Cdd:COG3706    23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                  ..
gi 1774222155 133 FN 134
Cdd:COG3706    98 AD 99
 
Name Accession Description Interval E-value
PDEase_I pfam00233
3'5'-cyclic nucleotide phosphodiesterase;
513-705 2.00e-76

3'5'-cyclic nucleotide phosphodiesterase;


Pssm-ID: 459723  Cd Length: 238  Bit Score: 245.54  E-value: 2.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 513 YHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAF 592
Cdd:pfam00233   1 YHNWRHAFDVTQTMYYLLKTGKLKEVLTDLEILALLIAALCHDVDHPGTNNAFLIKTKSPLAILYNDSSVLENHHCATAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 593 QLtVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEgsdcecnpagKNFPENQILIK 672
Cdd:pfam00233  81 QI-LQDEECNIFSNLSDEEYKEVRKLIISLILATDMAKHFELLKKFKSLLESKKTLDFL----------ENEEDRRLLLL 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774222155 673 RMMIKCADVANPCRPLDLCIEWAGRISEEYFAQ 705
Cdd:pfam00233 150 SMLIKAADISNPTRPWEISKKWADLVAEEFFRQ 182
PAS COG2202
PAS domain [Signal transduction mechanisms];
172-275 8.26e-17

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 80.84  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSG 251
Cdd:COG2202    15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-LPPEDDDEFLELLRAALAGGGVWRGELRNRRKDG 93

                          90       100
                  ....*....|....*....|....
gi 1774222155 252 DSIQQHVKITPVIGQGGKIRHFVS 275
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 ...
 187-276 1.61e-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: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 187 DHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTcikKGKEWQGVYYARRKSGDSIQQHVKITPVIGQ 266
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77

                          90
                  ....*....|
gi 1774222155 267 GGKIRHFVSL 276
Cdd:pfam13426  78 GGELVGIIAI 87
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
172-271 1.75e-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: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDknrADLLDTINTCIKKGKE-WQGVYYARRKS 250
Cdd:COG3852    11 AILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED---SPLRELLERALAEGQPvTEREVTLRRKD 87

                          90       100
                  ....*....|....*....|.
gi 1774222155 251 GDSIQQHVKITPVIGQGGKIR 271
Cdd:COG3852    88 GEERPVDVSVSPLRDAEGEGG 108
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 183-275 1.33e-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: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 183 ITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKIT 261
Cdd:cd00130     7 VLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLiHPED--REELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLT 84

                          90
                  ....*....|....
gi 1774222155 262 PVIGQGGKIRHFVS 275
Cdd:cd00130    85 PIRDEGGEVIGLLG 98
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 172-274 2.72e-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: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL-PKSDknRADLLDTINTCIKKGKEWQGVYYARRKS 250
Cdd:pfam00989   5 AILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLiPEED--DAEVAELLRQALLQGEESRGFEVSFRVP 82

                          90       100
                  ....*....|....*....|....*
gi 1774222155 251 -GDSIQQHVKITPVIGQGGKIRHFV 274
Cdd:pfam00989  83 dGRPRHVEVRASPVRDAGGEILGFL 107
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 172-307 1.50e-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: 57.47  E-value: 1.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSdknradllDTINTCIKKGKEWQGVYYarRKSG 251
Cdd:COG3829    15 AILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPN--------SPLLEVLKTGKPVTGVIQ--KTGG 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222155 252 DSIQQHVKITPVIGQGGKIRHFVSLKKLcctTDNNKQIHKIHRDSGDNSQTEPHSF 307
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 ...
 172-275 2.49e-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: 2.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYA-RRKS 250
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE-DREEVRERIERRLEGEPEPVSEERRvRRKD 85

                          90       100
                  ....*....|....*....|....*
gi 1774222155 251 GDSIQQHVKITPVIGQGGkIRHFVS 275
Cdd:TIGR00229  86 GSEIWVEVSVSPIRTNGG-ELGVVG 109
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 192-275 1.52e-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: 49.64  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 192 YVNPAFERMMGYHKGELLGK--ELADLPKSDkNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGK 269
Cdd:pfam08447   3 YWSPRFEEILGYTPEELLGKgeSWLDLVHPD-DRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGK 81


                  ....*.
gi 1774222155 270 IRHFVS 275
Cdd:pfam08447  82 PVRVIG 87
PAS COG2202
PAS domain [Signal transduction mechanisms];
159-276 7.26e-07

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 51.18  E-value: 7.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 159 RSQFKLRAcnsvftALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPkSDKNRADLLDTINTCIKKGK 238
Cdd:COG2202   134 ESEERLRL------LVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLL-HPEDRERLLELLRRLLEGGR 206

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1774222155 239 EWQGVYYaRRKSGDSIQQHVKITPV-IGQGGKIRHFVSL 276
Cdd:COG2202   207 ESYELEL-RLKDGDGRWVWVEASAVpLRDGGEVIGVLGI 244
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
 513-703 1.54e-06

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 48.10  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 513 YHNSTHAADVLHATAFFLGKERvkgsLDQLDEVAALIAATVHDVDHPGRTNSFlcnagselavlYNDTAVLESHHTALAF 592
Cdd:cd00077     1 EHRFEHSLRVAQLARRLAEELG----LSEEDIELLRLAALLHDIGKPGTPDAI-----------TEEESELEKDHAIVGA 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 593 QLtvkdtkcnifknIDRNHYRTLRQAIIDMVLATEMtKHFEHVNKFvnsinkpmaaeiegsdcecnPAGKNFPENQILIK 672
Cdd:cd00077    66 EI------------LRELLLEEVIKLIDELILAVDA-SHHERLDGL--------------------GYPDGLKGEEITLE 112

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1774222155 673 RMMIKCADV--ANPCRPLDLCIEWAGRISEEYF 703
Cdd:cd00077   113 ARIVKLADRldALRRDSREKRRRIAEEDLEELL 145
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 172-216 1.12e-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: 1.12e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1774222155  172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 216
Cdd:smart00091   5 AILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLEL 49
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 173-274 1.45e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 173 ALDHCHEAIEI---TSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNrADLLDTINTCIKKGKEWQGVYYARRK 249
Cdd:PRK13558  153 ALDEAPVGITIadaTLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTN-EERVAELREAIDEERPTSVELRNYRK 231

                          90       100
                  ....*....|....*....|....*
gi 1774222155 250 SGDSIQQHVKITPVIGQGGKIRHFV 274
Cdd:PRK13558  232 DGSTFWNQVDIAPIRDEDGTVTHYV 256
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
 511-609 1.56e-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: 41.90  E-value: 1.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  511 NAYHNSTHAADVLHaTAFFLGKErvkgsLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELavlyndtavlesHHTAL 590
Cdd:smart00471   1 SDYHVFEHSLRVAQ-LAAALAEE-----LGLLDIELLLLAALLHDIGKPGTPDSFLVKTSVLE------------DHHFI 62

                           90
                   ....*....|....*....
gi 1774222155  591 AFQLTVKDTKCNIFKNIDR 609
Cdd:smart00471  63 GAEILLEEEEPRILEEILR 81
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 140-278 3.02e-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: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 140 NSSIIACYNELIQIEHGEvRSQFKLRACNSVFTALD-HCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLpK 218
Cdd:COG5805   129 NQNGQAAILALRDITKKK-KIEEILQEQEERLQTLIeNSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLEL-L 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 219 SDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKK 278
Cdd:COG5805   207 HPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILR 266
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 172-231 1.07e-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: 1.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGY-HKGELLGKELADLPKSDKNRADLLDTIN 231
Cdd:pfam13188   5 ALFESSPDGILVLDEGGRIIYVNPAALELLGYeLLGELLGELLDLLDPLLEDALELLRELR 65
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 174-270 1.49e-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: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 174 LDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRadLLDTINTCIKKGKEWQGVYYARR-KSGD 252
Cdd:COG5809    21 FENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK--ELREILKLLKEGESRDELEFELRhKNGK 98

                          90
                  ....*....|....*...
gi 1774222155 253 SIQQHVKITPVIGQGGKI 270
Cdd:COG5809    99 RLEFSSKLSPIFDQNGDI 116
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 53-134 1.74e-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: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  53 RAGYRCNIARTPESALECFLDKHHEIIVIDHrQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASvlplLHAG 132
Cdd:COG3706    23 AAGYEVVEAADGEEALELLQEHRPDLILLDL-EMPDMDGLELCRRLRADPRTADIPIIFLTALDDEEDRARA----LEAG 97


                  ..
gi 1774222155 133 FN 134
Cdd:COG3706    98 AD 99
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 172-267 5.60e-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: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155 172 TALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINtcikkgKEWQGVYyaRRKSG 251
Cdd:COG5000    94 TILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALE------RGWQEEI--ELTRD 165

                          90
                  ....*....|....*.
gi 1774222155 252 DSIQQHVKITPVIGQG 267
Cdd:COG5000   166 GRRTLLVRASPLRDDG 181
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
 24-123 5.81e-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: 38.99  E-value: 5.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222155  24 MRLTQDPiQVLLIfakEDSQS--DGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTqNFDAEAVCRSIRAT 101
Cdd:COG3437     1 MRTGQAP-TVLIV---DDDPEnlELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMP-GMDGFELLRLLRAD 75

                          90       100
                  ....*....|....*....|..
gi 1774222155 102 NPSEHTVILAVVSRVSDDHEEA 123
Cdd:COG3437    76 PSTRDIPVIFLTALADPEDRER 97
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 174-216 9.21e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 36.62  E-value: 9.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1774222155 174 LDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADL 216
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH