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Conserved domains on  [gi|1195426320|gb|OUI67361|]
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fumarate and nitrate reduction regulatory protein [Serratia marcescens]

Protein Classification

FNR family transcription factor( domain architecture ID 11485234)

FNR family transcription factor similar to Escherichia coli fumarate and nitrate reduction regulatory protein FNR that controls the expression of over 100 target genes in response to anoxia

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
11-245 0e+00

fumarate/nitrate reduction transcriptional regulator Fnr;


:

Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 538.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  11 IQSGGCAIHCQDCSISQLCIPFTLNAHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 90
Cdd:PRK11161    1 IQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  91 GFHLAGDLVGFDAIGGLKHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERL 170
Cdd:PRK11161   81 GFHLAGDLVGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195426320 171 AAFVYNLSRRFAERGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITIENADALSVLAGT 245
Cdd:PRK11161  161 AAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAGH 235
 
Name Accession Description Interval E-value
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
11-245 0e+00

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 538.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  11 IQSGGCAIHCQDCSISQLCIPFTLNAHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 90
Cdd:PRK11161    1 IQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  91 GFHLAGDLVGFDAIGGLKHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERL 170
Cdd:PRK11161   81 GFHLAGDLVGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195426320 171 AAFVYNLSRRFAERGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITIENADALSVLAGT 245
Cdd:PRK11161  161 AAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAGH 235
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
34-243 7.36e-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: 7.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  34 LNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDA-IGGLKHPSF 112
Cdd:COG0664     4 LSDEELEALLAHLELRT-LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSlLGGEPSPAT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320 113 AQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFVYNLSRRFAERgfspreFR 192
Cdd:COG0664    83 AEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGR------ID 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1195426320 193 LTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITIENADALSVLA 243
Cdd:COG0664   157 LPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
34-144 2.07e-22

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: 88.54  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  34 LNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI-GGLKHPSF 112
Cdd:cd00038     5 LDDEELEELADALEERR-FPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALlGNGPRSAT 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1195426320 113 AQALETSMVCEIPFETLDDLSGKMPNLRQQIM 144
Cdd:cd00038    84 VRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
30-147 8.48e-19

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: 79.37  E-value: 8.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320   30 IPFTLNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGGLKH 109
Cdd:smart00100   1 LFKNLDAEELRELADALEPVR-YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSR 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1195426320  110 PSFAQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLM 147
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
49-132 1.35e-17

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: 75.34  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  49 KKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI-GGLKHPSFAQALETSMVCEIPFE 127
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALlGGEPRSATVVALTDSELLVIPRE 80

                  ....*
gi 1195426320 128 TLDDL 132
Cdd:pfam00027  81 DFLEL 85
 
Name Accession Description Interval E-value
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
11-245 0e+00

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 538.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  11 IQSGGCAIHCQDCSISQLCIPFTLNAHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 90
Cdd:PRK11161    1 IQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  91 GFHLAGDLVGFDAIGGLKHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERL 170
Cdd:PRK11161   81 GFHLAGDLVGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1195426320 171 AAFVYNLSRRFAERGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITIENADALSVLAGT 245
Cdd:PRK11161  161 AAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAGH 235
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
34-243 7.36e-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: 7.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  34 LNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDA-IGGLKHPSF 112
Cdd:COG0664     4 LSDEELEALLAHLELRT-LKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSlLGGEPSPAT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320 113 AQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFVYNLSRRFAERgfspreFR 192
Cdd:COG0664    83 AEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGR------ID 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1195426320 193 LTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITIENADALSVLA 243
Cdd:COG0664   157 LPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
fixK PRK09391
transcriptional regulator FixK; Provisional
54-242 1.19e-34

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 124.00  E-value: 1.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  54 KGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAigGLKHPSFAQALETSMVCEIPFETLDDLS 133
Cdd:PRK09391   45 KGEEIYGEGEPADYVYQVESGAVRTYRLLSDGRRQIGAFHLPGDVFGLES--GSTHRFTAEAIVDTTVRLIKRRSLEQAA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320 134 GKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFVYNLSRRFAergfSPREFRLTMTRGDIGNYLGLTVETISR 213
Cdd:PRK09391  123 ATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEMDERLG----GAGMMALPMSRRDIADYLGLTIETVSR 198
                         170       180       190
                  ....*....|....*....|....*....|
gi 1195426320 214 LLGRFQKSEILSVKG-KYITIENADALSVL 242
Cdd:PRK09391  199 ALSQLQDRGLIGLSGaRQIELRNRQALRNL 228
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
34-144 2.07e-22

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: 88.54  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  34 LNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI-GGLKHPSF 112
Cdd:cd00038     5 LDDEELEELADALEERR-FPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALlGNGPRSAT 83
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1195426320 113 AQALETSMVCEIPFETLDDLSGKMPNLRQQIM 144
Cdd:cd00038    84 VRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
30-147 8.48e-19

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: 79.37  E-value: 8.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320   30 IPFTLNAHELDQLDNIIERKKpIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGGLKH 109
Cdd:smart00100   1 LFKNLDAEELRELADALEPVR-YPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSR 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1195426320  110 PSFAQALETSMVCEIPFETLDDLSGKMPNLRQQIMRLM 147
Cdd:smart00100  80 RAASAAAVALELATLLRIDFRDFLQLLPELPQLLLELL 117
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
49-132 1.35e-17

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: 75.34  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  49 KKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAI-GGLKHPSFAQALETSMVCEIPFE 127
Cdd:pfam00027   1 LRSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALlGGEPRSATVVALTDSELLVIPRE 80

                  ....*
gi 1195426320 128 TLDDL 132
Cdd:pfam00027  81 DFLEL 85
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
166-233 3.74e-13

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: 62.68  E-value: 3.74e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1195426320 166 AEERLAAFVYNLSRRFAErgfsPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKG-KYITI 233
Cdd:cd00092     1 AKERLASFLLNLSLRYGA----GDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGrGKYRV 65
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
168-239 7.46e-12

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: 59.01  E-value: 7.46e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1195426320 168 ERLAAFVYNLSRRFAERgfsprEFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGkyITIENADAL 239
Cdd:pfam13545   1 QRLARFLLELAARDGGG-----RIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIERGR--ITILDPEAL 65
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
187-233 7.17e-11

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 55.91  E-value: 7.17e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1195426320  187 SPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSEILSVKGKYITI 233
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVI 47
Crp pfam00325
Bacterial regulatory proteins, crp family;
193-224 1.02e-07

Bacterial regulatory proteins, crp family;


Pssm-ID: 425608  Cd Length: 32  Bit Score: 46.91  E-value: 1.02e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1195426320 193 LTMTRGDIGNYLGLTVETISRLLGRFQKSEIL 224
Cdd:pfam00325   1 LRMSRQDIANYLGLTRETVSRVLGKLQEKGLI 32
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
57-233 3.03e-06

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 46.51  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  57 TLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVG----FDAigGLKHPSFAQALETSMVCEIPFETLDDL 132
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGelglFEE--GQERSAWVRAKTACEVAEISYKKFRQL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320 133 SGKMPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFVYNLSRRfAERGFSPREFRLTMTRGDIGNYLGLTVETIS 212
Cdd:PRK11753  108 IQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQ-PDAMTHPDGMQIKITRQEIGRIVGCSREMVG 186
                         170       180
                  ....*....|....*....|.
gi 1195426320 213 RLLGRFQKSEILSVKGKYITI 233
Cdd:PRK11753  187 RVLKMLEDQGLISAHGKTIVV 207
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
55-243 3.47e-03

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 37.49  E-value: 3.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320  55 GQTLFKAGDELKS--LYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGGLKHPSFAQALETSMVCEIPFETLDdl 132
Cdd:PRK13918   14 GAVILYPGVPGPSdmLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEEALAGAERAYFAEAVTDSRIDVLNPALMS-- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1195426320 133 sgkmPNLRQQIMRLMSGEIKGDQDMILLLSKKNAEERLAAFVYNLSRRFAERGFSPREFRLTMTRGDIGNYLGLTVETIS 212
Cdd:PRK13918   92 ----AEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGETMIYATHDELAAAVGSVRETVT 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1195426320 213 RLLGRFQKSEILSVKGKYITIENADALSVLA 243
Cdd:PRK13918  168 KVIGELSREGYIRSGYGKIQLLDLKGLEELA 198
 
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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