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Conserved domains on  [gi|1622835147|ref|XP_002802206|]
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period circadian protein homolog 3 isoform X4 [Macaca mulatta]

Protein Classification

GGDEF and EAL domain-containing protein; PAS domain-containing sensor histidine kinase; GGDEF domain-containing protein; GGDEF domain-containing protein; bifunctional diguanylate cyclase/phosphodiesterase; GGDEF domain-containing protein; phosphodiesterase; bifunctional diguanylate cyclase/phosphodiesterase; sensor domain-containing phosphodiesterase; sensor domain-containing diguanylate cyclase; GGDEF domain-containing protein; sensor domain-containing diguanylate cyclase; PAS domain-containing hybrid sensor histidine kinase/response regulator; PAS domain-containing protein; PAS domain-containing sensor histidine kinase; PAS domain-containing sensor histidine kinase; PAS domain-containing sensor histidine kinase; hybrid sensor histidine kinase/response regulator; PAS domain-containing protein( domain architecture ID 13752267)

GGDEF and EAL domain-containing protein with PAS sensor domain(s); may function as diguanylate cyclase and/or diguanylate phosphodiesterase; two-component sensor histidine kinase with a PAS ligand binding domain, similar to Brucella cell-division control histidine kinase PdhS and Streptococcus mutans CovS; two-component sensor histidine kinase with a PAS sensor and-or ligand binding domain, similar to Escherichia coli nitrogen regulator II, Azorhizobium caulinodans FixL and Streptococcus mutans CovS, having a variety of functions; two-component sensor histidine kinase with a PAS sensor domain, similar to Pseudomonas aeruginosa PilS, which may function as a membrane-associated protein kinase that phosphorylates PilR in response to environmental signals to regulate the expression of type 4 fimbriae; GGDEF domain-containing protein having an EAL domain and one or more PAS sensor or ligand binding domains, similar to E. coli DosP, an oxygen sensor and response regulator.; GGDEF domain-containing protein having an EAL domain and one or more PAS sensor or ligand binding domains, similar to E. coli DosP, an oxygen sensor and response regulator.; bifunctional diguanylate cyclase/phosphodiesterase (GGDEF/EAL) with PAS sensor domain(s); similar to MorA, a regulator affecting flagellar development, biofilm formation and virulence-associated protease secretion in diverse Pseudomonas species; GGDEF domain-containing protein having an EAL domain and one or more PAS sensor or ligand binding domains, similar to E. coli DosP, an oxygen sensor and response regulator.; phosphodiesterase with GGDEF domain and PAS sensor domains; GGDEF domain-containing protein with an EAL domain and PAS sensor domain(s), may have diguanylate cyclase and/or phosphodiesterase activities; similar to Shewanella oneidensis MR-1 cyclic-guanylate-specific phosphodiesterase PdeB; GGDEF domain-containing protein with an EAL domain, a GAF sensor domain and PAS sensor domain(s), may have diguanylate cyclase and/or phosphodiesterase activities; similar to Komagataeibacter xylinus PDEA1 cyclic-guanylate-specific phosphodiesterase; bifunctional diguanylate cyclase/phosphodiesterase (GGDEF/EAL) similar to Pseudomonas aeruginosa MorA.; sensor domain-containing phosphodiesterase (EAL) having a GGDEF domain and one or more PAS sensor domains, may have diguanylate cyclase and/or phosphodiesterase activities; similar to the global regulator Pseudomonas aeruginosa PAO1 MorA; sensor domain-containing phosphodiesterase with PAS sensor domain(s), may have diguanylate cyclase activity and/or phosphodiesterase activity; sensor domain-containing diguanylate cyclase with one or more PAS sensor domains; GGDEF domain-containing protein with PAS sensor domain(s), may have diguanylate cyclase activity; similar to Azospirillum brasilense diguanylate cyclase A, CdgA; GGDEF domain-containing protein with an EAL domain and PAS sensor domain(s), may have diguanylate cyclase and/or phosphodiesterase activities; similar to Shewanella oneidensis MR-1 cyclic-guanylate-specific phosphodiesterase PdeB; sensor domain-containing diguanylate cyclase (GGDEF) with EAL domain, MASE1 sensor domain and PAS sensor domain(s); PAS domain-containing protein; PAS domain-containing protein binds ligand(s) and may act as sensors for light and oxygen in signal transduction; PAS domain-containing protein similar to human HERG voltage-dependent K+ channel that plays a role in cardiac electrical excitability; hybrid sensor histidine kinase/response regulator having PAS sensor and/or ligand binding domains, receives the signal from the sensor partner in a two-component systems through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals; two-component hybrid sensor histidine kinase/response regulator with one or more PAS sensor and/or ligand binding domains; two-component hybrid sensor histidine kinase/response regulator having PAS sensor and/or ligand binding domains, similar to Aspergillus nidulans tcsA and Rhizobium leguminosarum FixL; two-component sensor histidine kinase with a PAS sensor and-or ligand binding domain, similar to Escherichia coli nitrogen regulator II, Azorhizobium caulinodans FixL and Streptococcus mutans CovS, having a variety of functions; two-component sensor histidine kinase with a PAS sensor and-or ligand binding domain functions as a protein kinase that phosphorylates a target protein in response to various signals; two-component hybrid sensor histidine kinase/response regulator with one or more PAS sensor and/or ligand binding domains; two-component sensor histidine kinase with a PAS sensor and-or ligand binding domain functions as a protein kinase that phosphorylates a target protein in response to various signals; PAS domain-containing protein binds ligand(s) and may act as sensors for light and oxygen in signal transduction; PAS domain-containing protein may bind ligands and/or act as sensors for light and oxygen in signal transduction; similar to human circadian clock protein PASD1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Period_C pfam12114
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
 1006-1154 1.85e-29

Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.


:

Pssm-ID: 463464  Cd Length: 171  Bit Score: 115.58  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1006 SMGSPPSRTPSHPTASVLSTGSPPCeSLSGTGSAASGSSDSSIYFTSSVYSKISQNGRQSQDVQKKETFPNDA-EESIWR 1084
Cdd:pfam12114   23 GTGSALSGSGSSATSGSLGSGSNGC-DTSGSGTGSSDTSHSSKYFGSIDSSENNHKAKKTAEVGEEEHFIKCVlQDPIWL 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1085 MIRQTPECVLMTYQVPERVKEVVLKEDLEKLESMRQQQPQFSHGQKEELAKVYNWIQSQTVPQEINIQAC 1154
Cdd:pfam12114  102 LMANTDDSVMMTYQIPSRDLETVLKEDREKLKAMQKMQPRFTEDQKGELAEVHPWIQKGGLPAALDLSEC 171
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 292-380 8.72e-13

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: 65.05  E-value: 8.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  292 FLEVDERAVPLLGYLPQDLIGT--SILSYLHPEDRSLMVAIHQKVLKYAGhpPFEHsPIRFCTQNGDYIILDSSWSSFVN 369
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                           90
                   ....*....|.
gi 1622835147  370 pWSRKVSFIIG 380
Cdd:pfam08447   78 -ENGKPVRVIG 87
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 758-1029 8.68e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  758 LPEPPDSNSSNAGSgphrgARQNAQPCCPSTASSLHTLGPTFPPAAMVPSQAPylvPAFPLPAATCPGREYAVPGTVPEG 837
Cdd:pfam03154  148 IPSPQDNESDSDSS-----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA---TAGPTPSAPSVPPQGSPATSQPPN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  838 LHGPPLSKD--LQPYPAFPSPYLDTfmtvflPDPPVCPLLSPsffpCPflgatassaispsmSSAMTPTLDPPASVTNQr 915
Cdd:pfam03154  220 QTQSTAAPHtlIQQTPTLHPQRLPS------PHPPLQPMTQP----PP--------------PSQVSPQPLPQPSLHGQ- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  916 reeekweAQSEGHPFITSRSSSPLQLNllqeemPRRSESPDQMRRNTCPQAEYQCVAGNSSSES-SPATTGALSMGSPPR 994
Cdd:pfam03154  275 -------MPPMPHSLQTGPSHMQHPVP------PQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIhTPPSQSQLQSQQPPR 341

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622835147  995 ENPSHPTASTLSMGSPPSRTPSHPTASVLSTGSPP 1029
Cdd:pfam03154  342 EQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPP 376
 
Name Accession Description Interval E-value
Period_C pfam12114
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
 1006-1154 1.85e-29

Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.


Pssm-ID: 463464  Cd Length: 171  Bit Score: 115.58  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1006 SMGSPPSRTPSHPTASVLSTGSPPCeSLSGTGSAASGSSDSSIYFTSSVYSKISQNGRQSQDVQKKETFPNDA-EESIWR 1084
Cdd:pfam12114   23 GTGSALSGSGSSATSGSLGSGSNGC-DTSGSGTGSSDTSHSSKYFGSIDSSENNHKAKKTAEVGEEEHFIKCVlQDPIWL 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1085 MIRQTPECVLMTYQVPERVKEVVLKEDLEKLESMRQQQPQFSHGQKEELAKVYNWIQSQTVPQEINIQAC 1154
Cdd:pfam12114  102 LMANTDDSVMMTYQIPSRDLETVLKEDREKLKAMQKMQPRFTEDQKGELAEVHPWIQKGGLPAALDLSEC 171
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 292-380 8.72e-13

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: 65.05  E-value: 8.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  292 FLEVDERAVPLLGYLPQDLIGT--SILSYLHPEDRSLMVAIHQKVLKYAGhpPFEHsPIRFCTQNGDYIILDSSWSSFVN 369
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                           90
                   ....*....|.
gi 1622835147  370 pWSRKVSFIIG 380
Cdd:pfam08447   78 -ENGKPVRVIG 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 292-384 1.62e-12

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: 64.96  E-value: 1.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  292 FLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKYAGHPPFEhspIRFCTQNGDYIILDSSWSSFVNPW 371
Cdd:cd00130     14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLE---VRLRRKDGSVIWVLVSLTPIRDEG 90

                           90
                   ....*....|...
gi 1622835147  372 SRKVSFIIGRHKV 384
Cdd:cd00130     91 GEVIGLLGVVRDI 103
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 292-336 9.99e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.09  E-value: 9.99e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1622835147   292 FLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLK 336
Cdd:smart00091   23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 758-1029 8.68e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  758 LPEPPDSNSSNAGSgphrgARQNAQPCCPSTASSLHTLGPTFPPAAMVPSQAPylvPAFPLPAATCPGREYAVPGTVPEG 837
Cdd:pfam03154  148 IPSPQDNESDSDSS-----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA---TAGPTPSAPSVPPQGSPATSQPPN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  838 LHGPPLSKD--LQPYPAFPSPYLDTfmtvflPDPPVCPLLSPsffpCPflgatassaispsmSSAMTPTLDPPASVTNQr 915
Cdd:pfam03154  220 QTQSTAAPHtlIQQTPTLHPQRLPS------PHPPLQPMTQP----PP--------------PSQVSPQPLPQPSLHGQ- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  916 reeekweAQSEGHPFITSRSSSPLQLNllqeemPRRSESPDQMRRNTCPQAEYQCVAGNSSSES-SPATTGALSMGSPPR 994
Cdd:pfam03154  275 -------MPPMPHSLQTGPSHMQHPVP------PQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIhTPPSQSQLQSQQPPR 341

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622835147  995 ENPSHPTASTLSMGSPPSRTPSHPTASVLSTGSPP 1029
Cdd:pfam03154  342 EQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPP 376
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 759-880 6.17e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  759 PEPPDSNS------SNAGSGPHRGARQNAQPCCPSTASSLHTLGPTfPPAAMVPSQAPYLVPAFPLPAATCPGREYAV-P 831
Cdd:PHA02682    40 PCPPDADVdpldkySVKEAGRYYQSRLKANSACMQRPSGQSPLAPS-PACAAPAPACPACAPAAPAPAVTCPAPAPACpP 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622835147  832 GTVPEGLHGPPLSKDLQPYPAFPSPYLDTFMTVFLPDPPVCPLLSPSFF 880
Cdd:PHA02682   119 ATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPTPKPAPAAKPIFL 167
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 281-381 7.37e-03

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 40.49  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  281 IFTTTHTPGcVFLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKYAGHPPFEHSPIrfcTQNGDYIIL 360
Cdd:COG5805    169 LICVIDTDG-RILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREII---TKDGRIRYF 244

                           90       100
                   ....*....|....*....|..
gi 1622835147  361 DSSWSSFVNP-WSRKVSFIIGR 381
Cdd:COG5805    245 EAVIVPLIDTdGSVKGILVILR 266
 
Name Accession Description Interval E-value
Period_C pfam12114
Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is ...
 1006-1154 1.85e-29

Period protein 2/3C-terminal region; This domain is found in eukaryotes. This domain is typically between 164 to 200 amino acids in length. This domain is found associated with pfam08447.


Pssm-ID: 463464  Cd Length: 171  Bit Score: 115.58  E-value: 1.85e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1006 SMGSPPSRTPSHPTASVLSTGSPPCeSLSGTGSAASGSSDSSIYFTSSVYSKISQNGRQSQDVQKKETFPNDA-EESIWR 1084
Cdd:pfam12114   23 GTGSALSGSGSSATSGSLGSGSNGC-DTSGSGTGSSDTSHSSKYFGSIDSSENNHKAKKTAEVGEEEHFIKCVlQDPIWL 101

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147 1085 MIRQTPECVLMTYQVPERVKEVVLKEDLEKLESMRQQQPQFSHGQKEELAKVYNWIQSQTVPQEINIQAC 1154
Cdd:pfam12114  102 LMANTDDSVMMTYQIPSRDLETVLKEDREKLKAMQKMQPRFTEDQKGELAEVHPWIQKGGLPAALDLSEC 171
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 292-380 8.72e-13

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: 65.05  E-value: 8.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  292 FLEVDERAVPLLGYLPQDLIGT--SILSYLHPEDRSLMVAIHQKVLKYAGhpPFEHsPIRFCTQNGDYIILDSSWSSFVN 369
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE--PYSG-EYRIRRKDGEYRWVEARARPIRD 77

                           90
                   ....*....|.
gi 1622835147  370 pWSRKVSFIIG 380
Cdd:pfam08447   78 -ENGKPVRVIG 87
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 292-384 1.62e-12

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: 64.96  E-value: 1.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  292 FLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKYAGHPPFEhspIRFCTQNGDYIILDSSWSSFVNPW 371
Cdd:cd00130     14 ILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLE---VRLRRKDGSVIWVLVSLTPIRDEG 90

                           90
                   ....*....|...
gi 1622835147  372 SRKVSFIIGRHKV 384
Cdd:cd00130     91 GEVIGLLGVVRDI 103
PAS_11 pfam14598
PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), ...
 282-384 2.16e-10

PAS domain; This family includes the PAS-B domain of NCOA1 (Nuclear receptor coactivator 1), which binds to an LXXLL motif in the C-terminal region of STAT6 (Signal transducer and activator of transcription 6).


Pssm-ID: 464214 [Multi-domain]  Cd Length: 110  Bit Score: 58.85  E-value: 2.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  282 FTTTHTPGCVFLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKYAGHppfEHSPI-RFCTQNGDYIIL 360
Cdd:pfam14598    4 FTTRHDIDGKIISCDTRAPFSLGYEKDELVGRSIYDLVHPQDLRTAKSHLREIIQTRGR---ATSPSyRLRLRDGDFLSV 80

                           90       100
                   ....*....|....*....|....
gi 1622835147  361 DSSWSSFVNPWSRKVSFIIGRHKV 384
Cdd:pfam14598   81 HTKSKLFLNQNSNQQPFIMCTHTI 104
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 279-378 1.73e-08

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 53.58  E-value: 1.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  279 KRIFTTTHTPGCV------FLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKyAGHPPFEHSpIRFCT 352
Cdd:pfam00989    4 RAILESLPDGIFVvdedgrILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALL-QGEESRGFE-VSFRV 81

                           90       100
                   ....*....|....*....|....*.
gi 1622835147  353 QNGDYIILDSSWSSFVNPWSRKVSFI 378
Cdd:pfam00989   82 PDGRPRHVEVRASPVRDAGGEILGFL 107
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 292-336 9.99e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 50.09  E-value: 9.99e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*
gi 1622835147   292 FLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLK 336
Cdd:smart00091   23 ILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 758-1029 8.68e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 47.07  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  758 LPEPPDSNSSNAGSgphrgARQNAQPCCPSTASSLHTLGPTFPPAAMVPSQAPylvPAFPLPAATCPGREYAVPGTVPEG 837
Cdd:pfam03154  148 IPSPQDNESDSDSS-----AQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAA---TAGPTPSAPSVPPQGSPATSQPPN 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  838 LHGPPLSKD--LQPYPAFPSPYLDTfmtvflPDPPVCPLLSPsffpCPflgatassaispsmSSAMTPTLDPPASVTNQr 915
Cdd:pfam03154  220 QTQSTAAPHtlIQQTPTLHPQRLPS------PHPPLQPMTQP----PP--------------PSQVSPQPLPQPSLHGQ- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  916 reeekweAQSEGHPFITSRSSSPLQLNllqeemPRRSESPDQMRRNTCPQAEYQCVAGNSSSES-SPATTGALSMGSPPR 994
Cdd:pfam03154  275 -------MPPMPHSLQTGPSHMQHPVP------PQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIhTPPSQSQLQSQQPPR 341

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1622835147  995 ENPSHPTASTLSMGSPPSRTPSHPTASVLSTGSPP 1029
Cdd:pfam03154  342 EQPLPPAPLSMPHIKPPPTTPIPQLPNPQSHKHPP 376
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 773-1030 2.63e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 45.53  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  773 PHRGARQNAQPCCPSTAS-------SLHTLGPTFP-PAAMVPSQAPYLVPAFPLPAATC-------PGREYAVPGTVPEG 837
Cdd:pfam03154  245 PHPPLQPMTQPPPPSQVSpqplpqpSLHGQMPPMPhSLQTGPSHMQHPVPPQPFPLTPQssqsqvpPGPSPAAPGQSQQR 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  838 LHGPPLSKDL---QPYPAFPSPYLDTFMTVFLPDP--PVCPLLSPSFFPCPflgatasSAISPSMSSAMTPTLDPPASVt 912
Cdd:pfam03154  325 IHTPPSQSQLqsqQPPREQPLPPAPLSMPHIKPPPttPIPQLPNPQSHKHP-------PHLSGPSPFQMNSNLPPPPAL- 396

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  913 nqrreeEKWEAQSEGHPfiTSRSSSPLQLNLLQEEMPrrsESPDQmrrntcPQAEYQCVAGNSSSESSPATTGALSMGSp 992
Cdd:pfam03154  397 ------KPLSSLSTHHP--PSAHPPPLQLMPQSQQLP---PPPAQ------PPVLTQSQSLPPPAASHPPTSGLHQVPS- 458

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1622835147  993 preNPSHPTASTLSMGSPPSRTPSHPTASV---LSTGSPPC 1030
Cdd:pfam03154  459 ---QSPFPQHPFVPGGPPPITPPSGPPTSTssaMPGIQPPS 496
PHA02682 PHA02682
ORF080 virion core protein; Provisional
 759-880 6.17e-04

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 43.31  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  759 PEPPDSNS------SNAGSGPHRGARQNAQPCCPSTASSLHTLGPTfPPAAMVPSQAPYLVPAFPLPAATCPGREYAV-P 831
Cdd:PHA02682    40 PCPPDADVdpldkySVKEAGRYYQSRLKANSACMQRPSGQSPLAPS-PACAAPAPACPACAPAAPAPAVTCPAPAPACpP 118

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1622835147  832 GTVPEGLHGPPLSKDLQPYPAFPSPYLDTFMTVFLPDPPVCPLLSPSFF 880
Cdd:PHA02682   119 ATAPTCPPPAVCPAPARPAPACPPSTRQCPPAPPLPTPKPAPAAKPIFL 167
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 759-1029 1.08e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  759 PEPPDSNSSNAGSGPHRGARQNAQPCCPSTASSlhTLGPTFPPAAMVPSQAPYLVPAFPLPAATCPGREYAVPGTVPEGL 838
Cdd:PHA03307   123 PASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA--GASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPA 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  839 HGPPLSKDLQPYPAFPSPYLDtfmtvflPDPPVCPLLSPSFfpCPFLGATASSAISPSMSSAMTPtLDPPASVTNQRREE 918
Cdd:PHA03307   201 AASPRPPRRSSPISASASSPA-------PAPGRSAADDAGA--SSSDSSSSESSGCGWGPENECP-LPRPAPITLPTRIW 270

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  919 EKWEAQSEGHPFITSRSSSPLQlnllqEEMPRRSES-PDQMRRNTCPQAEYQCVAGNSSSESSPATTGALSMGSPPRENP 997
Cdd:PHA03307   271 EASGWNGPSSRPGPASSSSSPR-----ERSPSPSPSsPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGP 345

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1622835147  998 SHPTASTLSMGSPPSRTPSHPTASVLSTGSPP 1029
Cdd:PHA03307   346 SPSRSPSPSRPPPPADPSSPRKRPRPSRAPSS 377
PHA03247 PHA03247
large tegument protein UL36; Provisional
 761-1027 3.98e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  761 PPDSNSSNAGSGPHRGARQNAQPCCPSTASSLHTLGPTfPPAAMVPSQAPYLVPAFPLPAATCPGreyavPGTVPEGLHG 840
Cdd:PHA03247  2742 PAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP-PRRLTRPAVASLSESRESLPSPWDPA-----DPPAAVLAPA 2815

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  841 PPLSKDLQPYPAFPSPYLDTFMTVFLPDPPVCPLLSPSFFPCPflgatassaisPSMSSAMTPTLDPPASVTNQRREEEK 920
Cdd:PHA03247  2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP-----------GGDVRRRPPSRSPAAKPAAPARPPVR 2884

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  921 WEAQSEghpfiTSRSSSPLQLNLLQEEMPRRSESPDQMRRNTCPQAEYQ---------------------CVAGNSSSES 979
Cdd:PHA03247  2885 RLARPA-----VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQpqppppppprpqpplapttdpAGAGEPSGAV 2959

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1622835147  980 SPATTGALSMG--SPPRENPSHPTASTLSMGSPPSRTPSHPTASVLSTGS 1027
Cdd:PHA03247  2960 PQPWLGALVPGrvAVPRFRVPQPAPSREAPASSTPPLTGHSLSRVSSWAS 3009
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 759-1029 6.03e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.92  E-value: 6.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  759 PEPPDSNSSNAGSGPHRGARQNAQP-----CCPSTASSLHTLGPTFPPAAMVPSQAPYLVPAFPLPAATCPGREYAVPGT 833
Cdd:PHA03307    76 GTEAPANESRSTPTWSLSTLAPASParegsPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAA 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  834 ------VPEGLHGPPLSKDLQPYPAFPSPYLDTfmtvflpdPPVCPLLSPSFFPCPflgATASSAISPSMSSAMTPTLDP 907
Cdd:PHA03307   156 gaspaaVASDAASSRQAALPLSSPEETARAPSS--------PPAEPPPSTPPAAAS---PRPPRRSSPISASASSPAPAP 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  908 PASvTNQRREEEKWEAqseghpfitSRSSSPLQLNLLQEEMPRRSESPdqmrrNTCPQAEYQCVAGNS----SSESSPAT 983
Cdd:PHA03307   225 GRS-AADDAGASSSDS---------SSSESSGCGWGPENECPLPRPAP-----ITLPTRIWEASGWNGpssrPGPASSSS 289

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622835147  984 TGALSMGSPPRENPSHP-------------------TASTLSMGSPPSRTPSHPTASVLSTGSPP 1029
Cdd:PHA03307   290 SPRERSPSPSPSSPGSGpapssprasssssssressSSSTSSSSESSRGAAVSPGPSPSRSPSPS 354
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 281-381 7.37e-03

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 40.49  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622835147  281 IFTTTHTPGcVFLEVDERAVPLLGYLPQDLIGTSILSYLHPEDRSLMVAIHQKVLKYAGHPPFEHSPIrfcTQNGDYIIL 360
Cdd:COG5805    169 LICVIDTDG-RILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREII---TKDGRIRYF 244

                           90       100
                   ....*....|....*....|..
gi 1622835147  361 DSSWSSFVNP-WSRKVSFIIGR 381
Cdd:COG5805    245 EAVIVPLIDTdGSVKGILVILR 266
 
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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