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Conserved domains on  [gi|1559771174|ref|WP_128300313|]
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cAMP-activated global transcriptional regulator CRP [Escherichia coli]

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;
1-210 1.88e-168

cAMP-activated global transcriptional regulator CRP;


:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 461.37  E-value: 1.88e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   1 MVLGKPQKDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753    2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  81 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753   82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1559771174 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR 210
Cdd:PRK11753  162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
1-210 1.88e-168

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 461.37  E-value: 1.88e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   1 MVLGKPQKDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753    2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  81 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753   82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1559771174 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR 210
Cdd:PRK11753  162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 9-206 1.68e-55

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: 175.18  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVR 88
Cdd:COG0664     6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLL-GGEPSPATAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAmthpdGMQIKI 168
Cdd:COG0664    85 ALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG-----RIDLPL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1559771174 169 TRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVV 206
Cdd:COG0664   160 TQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITI 197
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 9-117 1.57e-34

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: 118.58  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVR 88
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALL-GNGPRSATVR 85

                          90       100
                  ....*....|....*....|....*....
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRL 117
Cdd:cd00038    86 ALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 21-110 1.33e-25

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: 94.98  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  21 IHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKTACEVAEISY 100
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALL-GGEPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1559771174 101 KKFRQLIQVN 110
Cdd:pfam00027  80 EDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 9-121 1.54e-24

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: 93.23  E-value: 1.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174    9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFE-EGQERSAWV 87
Cdd:smart00100   7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTnSRRAASAAA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1559771174   88 RAKTACEVAEISYKKFRQLIQVNPDILMRLSAQM 121
Cdd:smart00100  87 VALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 9-125 5.77e-06

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 46.04  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSyLNQGDFIGELGLFEEGQERSAWVR 88
Cdd:TIGR03896 151 ESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDGPGREVGS-SRRGEILGETPFLNGSLPGTATVK 229

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRL 125
Cdd:TIGR03896 230 AIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLL 266
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
1-210 1.88e-168

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 461.37  E-value: 1.88e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   1 MVLGKPQKDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753    2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  81 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753   82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1559771174 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVYGTR 210
Cdd:PRK11753  162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 9-206 1.68e-55

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: 175.18  E-value: 1.68e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVR 88
Cdd:COG0664     6 DEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLL-GGEPSPATAE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAmthpdGMQIKI 168
Cdd:COG0664    85 ALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG-----RIDLPL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1559771174 169 TRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVV 206
Cdd:COG0664   160 TQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITI 197
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 9-117 1.57e-34

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: 118.58  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVR 88
Cdd:cd00038     7 DEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALL-GNGPRSATVR 85

                          90       100
                  ....*....|....*....|....*....
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRL 117
Cdd:cd00038    86 ALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 21-110 1.33e-25

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: 94.98  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  21 IHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKTACEVAEISY 100
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALL-GGEPRSATVVALTDSELLVIPR 79

                          90
                  ....*....|
gi 1559771174 101 KKFRQLIQVN 110
Cdd:pfam00027  80 EDFLELLERD 89
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 9-121 1.54e-24

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: 93.23  E-value: 1.54e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174    9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFE-EGQERSAWV 87
Cdd:smart00100   7 AEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTnSRRAASAAA 86

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1559771174   88 RAKTACEVAEISYKKFRQLIQVNPDILMRLSAQM 121
Cdd:smart00100  87 VALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 140-207 4.26e-15

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: 66.92  E-value: 4.26e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1559771174 140 VTGRIAQTLLNLAKQPDAmthPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHG-KTIVVY 207
Cdd:cd00092     1 AKERLASFLLNLSLRYGA---GDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGrGKYRVN 66
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 36-202 6.18e-15

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 70.23  E-value: 6.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  36 KAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeeGQERSAWVRAKTACEVAEISYKkfrqliQVNPDILM 115
Cdd:PRK13918   25 PSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALA--GAERAYFAEAVTDSRIDVLNPA------LMSAEDNL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174 116 RLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDG-MQIKITRQEIGQIVGCSRETVGRILKMLEDQ 194
Cdd:PRK13918   97 VLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGeTMIYATHDELAAAVGSVRETVTKVIGELSRE 176


                  ....*....
gi 1559771174 195 NLISA-HGK 202
Cdd:PRK13918  177 GYIRSgYGK 185
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
160-207 9.68e-15

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 65.54  E-value: 9.68e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1559771174  160 HPDGMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKTIVVY 207
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVIL 48
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 142-198 6.61e-10

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: 53.23  E-value: 6.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1559771174 142 GRIAQTLLNLAKQPDAMThpdgMQIKITRQEIGQIVGCSRETVGRILKMLEDQNLIS 198
Cdd:pfam13545   1 QRLARFLLELAARDGGGR----IDLPLTQEDLADLLGTTRETVSRVLSELRREGLIE 53
fixK PRK09391
transcriptional regulator FixK; Provisional
 23-205 2.17e-07

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 49.65  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  23 KYPSKSTLIHQGEKAETLYYIVKGSVAV--LIKDeeGKEMILSYLNQGDFIGelglFEEGQERSAWVRAKTACEVAEISY 100
Cdd:PRK09391   42 SYKKGEEIYGEGEPADYVYQVESGAVRTyrLLSD--GRRQIGAFHLPGDVFG----LESGSTHRFTAEAIVDTTVRLIKR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174 101 KKFRQLIQVNPDILMRLSAQMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQpdaMTHPDGMQIKITRQEIGQIVGCS 180
Cdd:PRK09391  116 RSLEQAAATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEMDER---LGGAGMMALPMSRRDIADYLGLT 192

                         170       180
                  ....*....|....*....|....*.
gi 1559771174 181 RETVGRILKMLEDQNLISAHG-KTIV 205
Cdd:PRK09391  193 IETVSRALSQLQDRGLIGLSGaRQIE 218
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
29-206 1.89e-06

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 47.01  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  29 TLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLfeEGQERSAWVRAKTACEVAEISYK------- 101
Cdd:PRK11161   47 TLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI--GSGQHPSFAQALETSMVCEIPFEtlddlsg 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174 102 ---KFRQLIqvnpdilMRLsaqMARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMT-HPDGMQIKITRQEIGQIV 177
Cdd:PRK11161  125 kmpKLRQQI-------MRL---MSGEIKGDQEMILLLSKKNAEERLAAFIYNLSRRFAQRGfSPREFRLTMTRGDIGNYL 194

                         170       180
                  ....*....|....*....|....*....
gi 1559771174 178 GCSRETVGRILKMLEDQNLISAHGKTIVV 206
Cdd:PRK11161  195 GLTVETISRLLGRFQKSGMLAVKGKYITI 223
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 9-125 5.77e-06

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 46.04  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174   9 DPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSyLNQGDFIGELGLFEEGQERSAWVR 88
Cdd:TIGR03896 151 ESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDGPGREVGS-SRRGEILGETPFLNGSLPGTATVK 229

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1559771174  89 AKTACEVAEISYKKFRQLIQVNPDILMRLSAQMARRL 125
Cdd:TIGR03896 230 AIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLL 266
Crp pfam00325
Bacterial regulatory proteins, crp family;
166-197 3.67e-05

Bacterial regulatory proteins, crp family;


Pssm-ID: 425608  Cd Length: 32  Bit Score: 39.59  E-value: 3.67e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1559771174 166 IKITRQEIGQIVGCSRETVGRILKMLEDQNLI 197
Cdd:pfam00325   1 LRMSRQDIANYLGLTRETVSRVLGKLQEKGLI 32
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 21-117 7.77e-05

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 42.02  E-value: 7.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  21 IHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAwVRAKTACEVAEISY 100
Cdd:PRK10402   33 LFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKA-VQAIEECWCLALPM 111

                          90
                  ....*....|....*..
gi 1559771174 101 KKFRQLIQVNPDILMRL 117
Cdd:PRK10402  112 KDCRPLLLNDALFLRKL 128
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 12-204 1.29e-04

bacteriocin-type transport-associated protein; Members of this protein family are uncharacterized and contain two copies of the cyclic nucleotide-binding domain pfam00027. Members are restricted to select cyanobacteria but are found regularly in association with a transport operon that, in turn, is associated with the production of putative bacteriocins. The models describing the transport operon are TIGR03794, TIGR03796, and TIGR03797.


Pssm-ID: 274839 [Multi-domain]  Cd Length: 317  Bit Score: 41.80  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  12 LEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMI----LSYLNQGDFIGELGLFEE-------- 79
Cdd:TIGR03896   1 IDWMVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTrafeLARLSRGEIVGEMSLLETrppvatik 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1559771174  80 GQERSAWVR-------AKTACEVAeISYKKFRQLIQVNPDILMRLSAQMARRLQVTSE---KV----GNLAFLDV----- 140
Cdd:TIGR03896  81 AVPKSRVMSipvgelaAKLQSDVG-FAAHFYRAIAIKLALQIQNQNHQLHRRNGADSEplrKVlfifGELHESDVawmma 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1559771174 141 TGRIAQTLLN--LAKQPDAMthpDG--------MQIKITRQEIGQIVGCSR--ETVGRiLKMLEDQNLISAHGKTI 204
Cdd:TIGR03896 160 SGTPQKLPAGtiLIHEGGTV---DAlyillygeASLSISPDGPGREVGSSRrgEILGE-TPFLNGSLPGTATVKAI 231
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
169-203 2.30e-03

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 37.95  E-value: 2.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1559771174 169 TRQEIGQIVGCSRETVGRILKMLEDQNLISAHGKT 203
Cdd:COG4742    31 TRSELAESLDVSRSTILRQLKELEERGLIERDDGE 65
PLN02868 PLN02868
acyl-CoA thioesterase family protein
 29-95 4.19e-03

acyl-CoA thioesterase family protein


Pssm-ID: 178459 [Multi-domain]  Cd Length: 413  Bit Score: 37.39  E-value: 4.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1559771174  29 TLIHQGEKAETLYYIVKGSVAVLIKDEEGKEMILSyLNQGDFIGElGLFEEGQERSAWVRAKTACEV 95
Cdd:PLN02868   41 YVVREGEPGDGLYFIWKGEAEVSGPAEEESRPEFL-LKRYDYFGY-GLSGSVHSADVVAVSELTCLV 105
 
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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