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Conserved domains on  [gi|1162406014|gb|OPX20717|]
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MAG: transcriptional regulator [Desulfobacca sp. 4484_104]

Protein Classification

Crp/Fnr family transcriptional regulator( domain architecture ID 11429533)

Crp/Fnr family transcriptional regulator containing a DNA-binding Crp-like helix-turn-helix (HTH) domain, may bind cyclic nucleotides

CATH:  2.60.120.10|1.10.10.10
Gene Ontology:  GO:0003677|GO:0030552
PubMed:  11407111|14638413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 13-221 2.86e-66

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: 203.29  E-value: 2.86e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  13 FEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFP 92
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  93 ANAEALEDCRVFFFPRAAFVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQAGsdEVELD 172
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--RIDLP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1162406014 173 IPKNLLASLLGTIPETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:COG0664   159 LTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 13-221 2.86e-66

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: 203.29  E-value: 2.86e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  13 FEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFP 92
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  93 ANAEALEDCRVFFFPRAAFVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQAGsdEVELD 172
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--RIDLP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1162406014 173 IPKNLLASLLGTIPETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:COG0664   159 LTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 12-126 2.42e-31

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: 111.26  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  12 LFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRF 91
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1162406014  92 PANAEALEDCRVFFFPRAAFVELIKRNPSLALNML 126
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 31-118 4.89e-29

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: 104.23  E-value: 4.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  31 KVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFPANAEALEDCRVFFFPRAA 110
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                  ....*...
gi 1162406014 111 FVELIKRN 118
Cdd:pfam00027  82 FLELLERD 89
ftrB PRK09392
transcriptional activator FtrB; Provisional
 7-221 2.51e-26

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 101.64  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014   7 LAAIPLFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKlSREGKEQILHIFGAGEPFGEVPVF 86
Cdd:PRK09392    9 LRNLPLFADMADATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVELSA-SSQDRETTLAILRPVSTFILAAVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  87 AGQRFPANAEALEDCRVFFFPRAAFVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQAGS 166
Cdd:PRK09392   88 LDAPYLMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVFELAGCYRGLVKSLKNQKLRSSAERLANYLLKQSLRQGGA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1162406014 167 DEVELDIPKNLLASLLGTIPETLSRILARMIRQGlIEAEGPRIKIVDRQGLQALA 221
Cdd:PRK09392  168 DVVTLPYEKRVLASYLGMTPENLSRAFAALASHG-VHVDGSAVTITDPAGLARFA 221
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 12-127 2.21e-21

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: 85.53  E-value: 2.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014   12 LFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRF 91
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1162406014   92 PAN--AEALEDCRVFFFPRAAFVELIKRNPSLALNMLA 127
Cdd:smart00100  81 AASaaAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 13-221 2.86e-66

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: 203.29  E-value: 2.86e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  13 FEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFP 92
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  93 ANAEALEDCRVFFFPRAAFVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQAGsdEVELD 172
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--RIDLP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1162406014 173 IPKNLLASLLGTIPETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:COG0664   159 LTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 12-126 2.42e-31

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: 111.26  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  12 LFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRF 91
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1162406014  92 PANAEALEDCRVFFFPRAAFVELIKRNPSLALNML 126
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 31-118 4.89e-29

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: 104.23  E-value: 4.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  31 KVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFPANAEALEDCRVFFFPRAA 110
Cdd:pfam00027   2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRED 81


                  ....*...
gi 1162406014 111 FVELIKRN 118
Cdd:pfam00027  82 FLELLERD 89
ftrB PRK09392
transcriptional activator FtrB; Provisional
 7-221 2.51e-26

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 101.64  E-value: 2.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014   7 LAAIPLFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKlSREGKEQILHIFGAGEPFGEVPVF 86
Cdd:PRK09392    9 LRNLPLFADMADATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVELSA-SSQDRETTLAILRPVSTFILAAVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  87 AGQRFPANAEALEDCRVFFFPRAAFVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQAGS 166
Cdd:PRK09392   88 LDAPYLMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVFELAGCYRGLVKSLKNQKLRSSAERLANYLLKQSLRQGGA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1162406014 167 DEVELDIPKNLLASLLGTIPETLSRILARMIRQGlIEAEGPRIKIVDRQGLQALA 221
Cdd:PRK09392  168 DVVTLPYEKRVLASYLGMTPENLSRAFAALASHG-VHVDGSAVTITDPAGLARFA 221
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 12-127 2.21e-21

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: 85.53  E-value: 2.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014   12 LFEGLSEENYADLAAIVLDKVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRF 91
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRR 80

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1162406014   92 PAN--AEALEDCRVFFFPRAAFVELIKRNPSLALNMLA 127
Cdd:smart00100  81 AASaaAVALELATLLRIDFRDFLQLLPELPQLLLELLL 118
fixK PRK09391
transcriptional regulator FixK; Provisional
 33-220 5.61e-21

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 87.40  E-value: 5.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  33 FHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGevpVFAGQRFPANAEALEDCRVFFFPRAAFV 112
Cdd:PRK09391   43 YKKGEEIYGEGEPADYVYQVESGAVRTYRLLSDGRRQIGAFHLPGDVFG---LESGSTHRFTAEAIVDTTVRLIKRRSLE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014 113 ELIKRNPSLALNMLAVLS---RRLRQFTLLIEDLSLKEvpgRLAAYLLYLSHQQAGSDEVELDIPKNLLASLLGTIPETL 189
Cdd:PRK09391  120 QAAATDVDVARALLSLTAgglRHAQDHMLLLGRKTAME---RVAAFLLEMDERLGGAGMMALPMSRRDIADYLGLTIETV 196

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1162406014 190 SRILARMIRQGLIEAEGPR-IKIVDRQGLQAL 220
Cdd:PRK09391  197 SRALSQLQDRGLIGLSGARqIELRNRQALRNL 228
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
31-221 1.97e-19

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 83.22  E-value: 1.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  31 KVFHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGeVPVFAGQRFPANAEALEDCRVFFFPRAA 110
Cdd:PRK11161   40 KPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVG-FDAIGSGQHPSFAQALETSMVCEIPFET 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014 111 FVELIKRNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQQA----GSDEVELDIPKNLLASLLGTIP 186
Cdd:PRK11161  119 LDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLSRRFAqrgfSPREFRLTMTRGDIGNYLGLTV 198

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1162406014 187 ETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:PRK11161  199 ETISRLLGRFQKSGMLAVKGKYITIENNDALAQLA 233
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
38-209 4.86e-18

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 79.26  E-value: 4.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  38 TIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFA-GQRFPANAEALEDCRVFFFPRAAFVELIK 116
Cdd:PRK11753   30 TLIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEeGQERSAWVRAKTACEVAEISYKKFRQLIQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014 117 RNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQ-QAGS--DEVELDIPKNLLASLLGTIPETLSRIL 193
Cdd:PRK11753  110 VNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQpDAMThpDGMQIKITRQEIGRIVGCSREMVGRVL 189

                         170
                  ....*....|....*.
gi 1162406014 194 ARMIRQGLIEAEGPRI 209
Cdd:PRK11753  190 KMLEDQGLISAHGKTI 205
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 150-220 9.00e-16

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: 69.41  E-value: 9.00e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162406014 150 GRLAAYLLYLSHQQAGsDEVELDIPKNLLASLLGTIPETLSRILARMIRQGLIEAEgpRIKIVDRQGLQAL 220
Cdd:pfam13545   1 QRLARFLLELAARDGG-GRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIERG--RITILDPEALEAL 68
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
165-211 1.03e-09

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 52.44  E-value: 1.03e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1162406014  165 GSDEVELDIPKNLLASLLGTIPETLSRILARMIRQGLIEAEGPRIKI 211
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVI 47
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 28-221 6.25e-09

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 54.06  E-value: 6.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  28 VLDKV-FHKGQTIFSEGEEG--NGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEvPVFAGQRFPANAEALEDCRVF 104
Cdd:PRK13918    5 VVDTVtYRPGAVILYPGVPGpsDMLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGE-EALAGAERAYFAEAVTDSRID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014 105 FFPRAAFvelikrNPSLALNMLAVLSRRLRQFTLLIEDLSLKEVPGRLAAYLLYLSHQ----QAGSDEVELDIPKNLLAS 180
Cdd:PRK13918   84 VLNPALM------SAEDNLVLTQHLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTplatQEDSGETMIYATHDELAA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1162406014 181 LLGTIPETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:PRK13918  158 AVGSVRETVTKVIGELSREGYIRSGYGKIQLLDLKGLEELA 198
PRK10402 PRK10402
DNA-binding transcriptional activator YeiL; Provisional
 33-221 4.88e-08

DNA-binding transcriptional activator YeiL; Provisional


Pssm-ID: 236682 [Multi-domain]  Cd Length: 226  Bit Score: 51.65  E-value: 4.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014  33 FHKGQTIFSEGEEGNGFYVVVAGRLKIFKLSREGKEQILHIFGAGEPFGEVPVFAGQRFPANAEALEDCRVFFFPraafv 112
Cdd:PRK10402   36 FLAREYIVQEGQQPSYLFYLTRGRAKLYATLANGKVSLIDFFAAPCFIGEIELIDKDHETKAVQAIEECWCLALP----- 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406014 113 elIKRNPSLALNMlAVLSRRLRQF-----TLLIEDLSLKE---VPGRLAAYLLYlshqqagSDEVELDIPKNLLAS-LLG 183
Cdd:PRK10402  111 --MKDCRPLLLND-ALFLRKLCKFlshknYRNIVSLTQNQsfpLENRLAAFILL-------TQEGDLYHEKHTQAAeYLG 180

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1162406014 184 TIPETLSRILARMIRQGLIEAEGPRIKIVDRQGLQALA 221
Cdd:PRK10402  181 VSYRHLLYVLAQFIQDGYLKKSKRGYLIKNRKQLSGLA 218
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 150-208 1.79e-07

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: 46.89  E-value: 1.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1162406014 150 GRLAAYLLYLSHQQAGSDEVELDIPKNLLASLLGTIPETLSRILARMIRQGLIEAEGPR 208
Cdd:cd00092     3 ERLASFLLNLSLRYGAGDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGRG 61
 
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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