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Conserved domains on  [gi|491563488|ref|WP_005421074|]
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MULTISPECIES: cAMP-activated global transcriptional regulator CRP [Aliivibrio]

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 4.02e-167

cAMP-activated global transcriptional regulator CRP;


:

Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 457.91  E-value: 4.02e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   1 MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753   2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  81 QERSAWVRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753  82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491563488 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR 210
Cdd:PRK11753 162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
1-210 4.02e-167

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 457.91  E-value: 4.02e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   1 MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753   2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  81 QERSAWVRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753  82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491563488 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR 210
Cdd:PRK11753 162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
8-206 5.03e-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: 174.02  E-value: 5.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWV 87
Cdd:COG0664    5 SDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLL-GGEPSPATA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  88 RAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAmthpdGMQIK 167
Cdd:COG0664   84 EALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG-----RIDLP 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491563488 168 ITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVV 206
Cdd:COG0664  159 LTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITI 197
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
8-117 9.93e-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: 116.66  E-value: 9.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWV 87
Cdd:cd00038    6 DDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALL-GNGPRSATV 84
                         90       100       110
                 ....*....|....*....|....*....|
gi 491563488  88 RAKSPCEVAEISFKKFRQLIQVNPDILMRL 117
Cdd:cd00038   85 RALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
8-121 1.37e-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: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488     8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFE-EGQERSAW 86
Cdd:smart00100   6 DAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTnSRRAASAA 85
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 491563488    87 VRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQM 121
Cdd:smart00100  86 AVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
21-110 2.11e-24

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: 91.90  E-value: 2.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   21 IHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKSPCEVAEISF 100
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALL-GGEPRSATVVALTDSELLVIPR 79
                          90
                  ....*....|
gi 491563488  101 KKFRQLIQVN 110
Cdd:pfam00027  80 EDFLELLERD 89
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
9-130 3.77e-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: 40.65  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488    9 DPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSyLNQGDFIGELGLFEEGQERSAWVR 88
Cdd:TIGR03896 151 ESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDGPGREVGS-SRRGEILGETPFLNGSLPGTATVK 229
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 491563488   89 AKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQ 130
Cdd:TIGR03896 230 AIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLLSQRSR 271
 
Name Accession Description Interval E-value
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
1-210 4.02e-167

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 457.91  E-value: 4.02e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   1 MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 80
Cdd:PRK11753   2 MVLGKPQTDPTLEWFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  81 QERSAWVRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTH 160
Cdd:PRK11753  82 QERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMTH 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 491563488 161 PDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVYGTR 210
Cdd:PRK11753 162 PDGMQIKITRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVVYGTR 211
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
8-206 5.03e-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: 174.02  E-value: 5.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWV 87
Cdd:COG0664    5 SDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLL-GGEPSPATA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  88 RAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAmthpdGMQIK 167
Cdd:COG0664   84 EALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG-----RIDLP 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491563488 168 ITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVV 206
Cdd:COG0664  159 LTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITI 197
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
8-117 9.93e-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: 116.66  E-value: 9.93e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWV 87
Cdd:cd00038    6 DDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALL-GNGPRSATV 84
                         90       100       110
                 ....*....|....*....|....*....|
gi 491563488  88 RAKSPCEVAEISFKKFRQLIQVNPDILMRL 117
Cdd:cd00038   85 RALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
8-121 1.37e-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: 1.37e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488     8 TDPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFE-EGQERSAW 86
Cdd:smart00100   6 DAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTnSRRAASAA 85
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 491563488    87 VRAKSPCEVAEISFKKFRQLIQVNPDILMRLSAQM 121
Cdd:smart00100  86 AVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
21-110 2.11e-24

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: 91.90  E-value: 2.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   21 IHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeEGQERSAWVRAKSPCEVAEISF 100
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALL-GGEPRSATVVALTDSELLVIPR 79
                          90
                  ....*....|
gi 491563488  101 KKFRQLIQVN 110
Cdd:pfam00027  80 EDFLELLERD 89
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
140-207 1.53e-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: 68.08  E-value: 1.53e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491563488 140 VTGRIAQTLLNLAKQPDAmthPDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHG-KTIVVY 207
Cdd:cd00092    1 AKERLASFLLNLSLRYGA---GDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGrGKYRVN 66
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
160-207 1.02e-14

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 65.54  E-value: 1.02e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 491563488   160 HPDGMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKTIVVY 207
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVIL 48
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
36-202 4.11e-13

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 65.23  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  36 KAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFeeGQERSAWVRAKSPCEVAEISFKkfrqliQVNPDILM 115
Cdd:PRK13918  25 PSDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALA--GAERAYFAEAVTDSRIDVLNPA------LMSAEDNL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488 116 RLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQPDAMTHPDG-MQIKITRQEIGQIVGCSRETVGRILKMLEEQ 194
Cdd:PRK13918  97 VLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGeTMIYATHDELAAAVGSVRETVTKVIGELSRE 176

                 ....*....
gi 491563488 195 NLISA-HGK 202
Cdd:PRK13918 177 GYIRSgYGK 185
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
142-198 4.55e-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: 53.61  E-value: 4.55e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 491563488  142 GRIAQTLLNLAKQPDAMThpdgMQIKITRQEIGQIVGCSRETVGRILKMLEEQNLIS 198
Cdd:pfam13545   1 QRLARFLLELAARDGGGR----IDLPLTQEDLADLLGTTRETVSRVLSELRREGLIE 53
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
29-206 9.61e-07

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 47.78  E-value: 9.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  29 TLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLfeEGQERSAWVRAKSPCEVAEISFkkfrqliq 108
Cdd:PRK11161  47 TLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI--GSGQHPSFAQALETSMVCEIPF-------- 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488 109 vnpDILMRLSAQMAT-RLQI----TSQKVGD------LAFLDVTGRIAQTLLNLAKQPDAMT-HPDGMQIKITRQEIGQI 176
Cdd:PRK11161 117 ---ETLDDLSGKMPKlRQQImrlmSGEIKGDqemillLSKKNAEERLAAFIYNLSRRFAQRGfSPREFRLTMTRGDIGNY 193
                        170       180       190
                 ....*....|....*....|....*....|
gi 491563488 177 VGCSRETVGRILKMLEEQNLISAHGKTIVV 206
Cdd:PRK11161 194 LGLTVETISRLLGRFQKSGMLAVKGKYITI 223
fixK PRK09391
transcriptional regulator FixK; Provisional
34-205 9.79e-07

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 47.73  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  34 GEKAETLYYIVKGSVAV--LIKDeeGKEMILSYLNQGDFIGelglFEEGQERSAWVRAKSPCEVAEISFKKFRQLIQVNP 111
Cdd:PRK09391  53 GEPADYVYQVESGAVRTyrLLSD--GRRQIGAFHLPGDVFG----LESGSTHRFTAEAIVDTTVRLIKRRSLEQAAATDV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488 112 DILMRLSAQMATRLQITSQKVGDLAFLDVTGRIAQTLLNLAKQpdaMTHPDGMQIKITRQEIGQIVGCSRETVGRILKML 191
Cdd:PRK09391 127 DVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEMDER---LGGAGMMALPMSRRDIADYLGLTIETVSRALSQL 203
                        170
                 ....*....|....*
gi 491563488 192 EEQNLISAHG-KTIV 205
Cdd:PRK09391 204 QDRGLIGLSGaRQIE 218
Crp pfam00325
Bacterial regulatory proteins, crp family;
166-197 7.81e-06

Bacterial regulatory proteins, crp family;


Pssm-ID: 425608  Cd Length: 32  Bit Score: 41.51  E-value: 7.81e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 491563488  166 IKITRQEIGQIVGCSRETVGRILKMLEEQNLI 197
Cdd:pfam00325   1 LRMSRQDIANYLGLTRETVSRVLGKLQEKGLI 32
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
21-117 3.80e-05

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 43.18  E-value: 3.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488  21 IHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAwVRAKSPCEVAEISF 100
Cdd:PRK10402  33 LFHFLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKA-VQAIEECWCLALPM 111
                         90
                 ....*....|....*..
gi 491563488 101 KKFRQLIQVNPDILMRL 117
Cdd:PRK10402 112 KDCRPLLLNDALFLRKL 128
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
9-130 3.77e-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: 40.65  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488    9 DPTLEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSyLNQGDFIGELGLFEEGQERSAWVR 88
Cdd:TIGR03896 151 ESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLSISPDGPGREVGS-SRRGEILGETPFLNGSLPGTATVK 229
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 491563488   89 AKSPCEVAEISFKKFRQLIQVNPDILMRLSAQMATRLQITSQ 130
Cdd:TIGR03896 230 AIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLLSQRSR 271
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
12-88 5.98e-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: 39.88  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491563488   12 LEWFLSHCHIHKYPSKSTLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMI----LSYLNQGDFIGELGLFEE-------- 79
Cdd:TIGR03896   1 IDWMVAIGHQREIAAGTTLIEEGKAADFLFILLDGTFTVTTPQPEDNPLTrafeLARLSRGEIVGEMSLLETrppvatik 80

                  ....*....
gi 491563488   80 GQERSAWVR 88
Cdd:TIGR03896  81 AVPKSRVMS 89
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
169-203 2.02e-03

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 37.95  E-value: 2.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 491563488 169 TRQEIGQIVGCSRETVGRILKMLEEQNLISAHGKT 203
Cdd:COG4742   31 TRSELAESLDVSRSTILRQLKELEERGLIERDDGE 65
 
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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