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Conserved domains on  [gi|491053432|ref|WP_004915082|]
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MULTISPECIES: cAMP-activated global transcriptional regulator CRP [Acinetobacter]

Protein Classification

Crp/Fnr family transcriptional regulator( domain architecture ID 11485491)

Crp/Fnr family transcriptional regulator such as Escherichia coli cAMP-activated global transcriptional regulator CRP, which complexes with cyclic AMP (cAMP) to allosterically activate DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') and to directly regulate the transcription of about 300 genes in about 200 operons and indirectly regulate the expression of about half the genome

Gene Ontology:  GO:0003677|GO:0006355
PubMed:  29146813|24914983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
10-220 7.00e-134

cAMP-activated global transcriptional regulator CRP;


:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 375.09  E-value: 7.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  10 TDALSPGQLPESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEK 89
Cdd:PRK11753   1 MMVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  90 NPQRTAEVRTRDVCEIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMI 169
Cdd:PRK11753  81 GQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491053432 170 LPNGRQIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILIFDTS 220
Cdd:PRK11753 161 HPDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
10-220 7.00e-134

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 375.09  E-value: 7.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  10 TDALSPGQLPESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEK 89
Cdd:PRK11753   1 MMVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  90 NPQRTAEVRTRDVCEIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMI 169
Cdd:PRK11753  81 GQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491053432 170 LPNGRQIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILIFDTS 220
Cdd:PRK11753 161 HPDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 19-225 1.20e-49

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 161.31  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  19 PESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVR 98
Cdd:COG0664    6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEP-SPATAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  99 TRDVCEIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMIlpngrQIRI 178
Cdd:COG0664   85 ALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGRI-----DLPL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491053432 179 TRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILIFDTS-LEENA 225
Cdd:COG0664  160 TQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREaLERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 19-127 6.10e-26

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 97.40  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  19 PESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVR 98
Cdd:cd00038    7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGP-RSATVR 85

                         90       100
                 ....*....|....*....|....*....
gi 491053432  99 TRDVCEIAEISYDNFHELSKQYPDLSYAV 127
Cdd:cd00038   86 ALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 33-120 1.22e-21

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 85.35  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432   33 RYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVRTRDVCEIAEISYDN 112
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEP-RSATVVALTDSELLVIPRED 81


                  ....*...
gi 491053432  113 FHELSKQY 120
Cdd:pfam00027  82 FLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 12-131 1.34e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 78.60  E-value: 1.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432    12 ALSPGQLpESVKALLKRAHinrYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNP 91
Cdd:smart00100   4 NLDAEEL-RELADALEPVR---YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491053432    92 Q-RTAEVRTRDVCEIAEISYDNFHELSKQYPDLSYAVFAQL 131
Cdd:smart00100  80 RaASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
10-220 7.00e-134

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 375.09  E-value: 7.00e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  10 TDALSPGQLPESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEK 89
Cdd:PRK11753   1 MMVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  90 NPQRTAEVRTRDVCEIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMI 169
Cdd:PRK11753  81 GQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491053432 170 LPNGRQIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILIFDTS 220
Cdd:PRK11753 161 HPDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 19-225 1.20e-49

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 161.31  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  19 PESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVR 98
Cdd:COG0664    6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEP-SPATAE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  99 TRDVCEIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMIlpngrQIRI 178
Cdd:COG0664   85 ALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGRI-----DLPL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491053432 179 TRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILIFDTS-LEENA 225
Cdd:COG0664  160 TQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREaLERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 19-127 6.10e-26

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 97.40  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  19 PESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVR 98
Cdd:cd00038    7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGP-RSATVR 85

                         90       100
                 ....*....|....*....|....*....
gi 491053432  99 TRDVCEIAEISYDNFHELSKQYPDLSYAV 127
Cdd:cd00038   86 ALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 33-120 1.22e-21

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 85.35  E-value: 1.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432   33 RYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPqRTAEVRTRDVCEIAEISYDN 112
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEP-RSATVVALTDSELLVIPRED 81


                  ....*...
gi 491053432  113 FHELSKQY 120
Cdd:pfam00027  82 FLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 12-131 1.34e-18

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 78.60  E-value: 1.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432    12 ALSPGQLpESVKALLKRAHinrYPKRTTIVDAGTESKSLYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNP 91
Cdd:smart00100   4 NLDAEEL-RELADALEPVR---YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSR 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 491053432    92 Q-RTAEVRTRDVCEIAEISYDNFHELSKQYPDLSYAVFAQL 131
Cdd:smart00100  80 RaASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 40-225 2.08e-14

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 69.46  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  40 IVDAGTESKS--LYLILKGSVSIILREDDEREIVVAYLNPGDFFGEMGLFEKNPQRTAEVRTR---DVCEIAEISYDNFH 114
Cdd:PRK13918  17 ILYPGVPGPSdmLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAERAYFAEAVTDsriDVLNPALMSAEDNL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432 115 ELSKqypdlsyavfaQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMILPNGR-QIRITRQEIGRIVGCSREM 193
Cdd:PRK13918  97 VLTQ-----------HLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGEtMIYATHDELAAAVGSVRET 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 491053432 194 VGRVLKTLEDQGMIQTD-GKAILIFDTSLEENA 225
Cdd:PRK13918 166 VTKVIGELSREGYIRSGyGKIQLLDLKGLEELA 198
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
171-216 1.76e-10

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 54.75  E-value: 1.76e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 491053432   171 PNGRQIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGKAILI 216
Cdd:smart00419   2 GIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVI 47
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
36-218 3.69e-09

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 55.10  E-value: 3.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  36 KRTTIVDAGTESKSLYLILKGSV-SIILREDDEREIVVAYLnPGDFFGEMGLFEKNPQRTAE-VRTRDVCEIAeisYDNF 113
Cdd:PRK11161  44 KGQTLFKAGDELKSLYAIRSGTIkSYTITEQGDEQITGFHL-AGDLVGFDAIGSGQHPSFAQaLETSMVCEIP---FETL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432 114 HELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLSSQPEAMILpNGRQIRI--TRQEIGRIVGCSR 191
Cdd:PRK11161 120 DDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLSRRFAQRGF-SPREFRLtmTRGDIGNYLGLTV 198

                        170       180
                 ....*....|....*....|....*..
gi 491053432 192 EMVGRVLKTLEDQGMIQTDGKAILIFD 218
Cdd:PRK11161 199 ETISRLLGRFQKSGMLAVKGKYITIEN 225
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 152-218 4.28e-09

Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.


Pssm-ID: 463917 [Multi-domain]  Cd Length: 68  Bit Score: 51.30  E-value: 4.28e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491053432  152 GRIARCLIDLSSQPEAMILPngrqIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGkaILIFD 218
Cdd:pfam13545   1 QRLARFLLELAARDGGGRID----LPLTQEDLADLLGTTRETVSRVLSELRREGLIERGR--ITILD 61
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 152-212 3.83e-08

helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.


Pssm-ID: 238044 [Multi-domain]  Cd Length: 67  Bit Score: 48.82  E-value: 3.83e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491053432 152 GRIARCLIDLSSQPEAMILpngRQIRITRQEIGRIVGCSREMVGRVLKTLEDQGMIQTDGK 212
Cdd:cd00092    3 ERLASFLLNLSLRYGAGDL---VQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGR 60
ftrB PRK09392
transcriptional activator FtrB; Provisional
 19-218 9.79e-07

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 48.10  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  19 PESVKALLKRAHINRYPKRTTIVDAGTESKSLYLILKGSVSIILREDDeREIVVAYLNPGDFFGEMGLFEKNP----QRT 94
Cdd:PRK09392  20 DATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVELSASSQD-RETTLAILRPVSTFILAAVVLDAPylmsART 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  95 AEvRTRdvceIAEISYDNFHELSKQYPDLSYAVFAQLVRRLKNTTRKVTDLAFIDVSGRIARCLIDLS---SQPEAMILP 171
Cdd:PRK09392  99 LT-RSR----VLMIPAELVREAMSEDPGFMRAVVFELAGCYRGLVKSLKNQKLRSSAERLANYLLKQSlrqGGADVVTLP 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491053432 172 NGRQIritrqeIGRIVGCSREMVGRVLKTLEDQGmIQTDGKAILIFD 218
Cdd:PRK09392 174 YEKRV------LASYLGMTPENLSRAFAALASHG-VHVDGSAVTITD 213
Crp pfam00325
Bacterial regulatory proteins, crp family;
176-207 2.53e-06

Bacterial regulatory proteins, crp family;


Pssm-ID: 425608  Cd Length: 32  Bit Score: 43.05  E-value: 2.53e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 491053432  176 IRITRQEIGRIVGCSREMVGRVLKTLEDQGMI 207
Cdd:pfam00325   1 LRMSRQDIANYLGLTRETVSRVLGKLQEKGLI 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 35-147 3.46e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.31  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  35 PKRTTIVDAGTESKSLYLILKGSVSIILrEDDEREIVVAYLNPGDFFGEMGLFEKNPQrTAEVRTRDVCEIAEISYDNFH 114
Cdd:PLN03192 403 PPREDVIMQNEAPDDVYIVVSGEVEIID-SEGEKERVVGTLGCGDIFGEVGALCCRPQ-SFTFRTKTLSQLLRLKTSTLI 480

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491053432 115 ELSKQYPDLSYAV---FAQLVRRLKNTtrKVTDLAF 147
Cdd:PLN03192 481 EAMQTRQEDNVVIlknFLQHHKELHDL--NVGDLLG 514
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 17-108 3.77e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 37.78  E-value: 3.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491053432  17 QLPESvkALLKRAHI---NRYPKRTTIVDAGTESKSLYLILKGSVSiILREDDEREIVVAYLNPGDFFGEmGLFEknpqr 93
Cdd:PLN02868  18 RLPSS--SLKKIAEVvvpKRYGKGEYVVREGEPGDGLYFIWKGEAE-VSGPAEEESRPEFLLKRYDYFGY-GLSG----- 88

                         90
                 ....*....|....*
gi 491053432  94 taEVRTRDVCEIAEI 108
Cdd:PLN02868  89 --SVHSADVVAVSEL 101
 
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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