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Conserved domains on  [gi|1242548464|gb|ATA69274|]
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Crp/Fnr family transcriptional regulator [Capnocytophaga cynodegmi]

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 ...
 2-196 6.90e-49

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


:

Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 158.61  E-value: 6.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   2 LRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPVN 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  82 LSAVALTDMKVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGtdeqGYIN 161
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLD----GRID 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1242548464 162 IQLSREEIGNMIGSATESLIRMLSEFSKNEWIETR 196
Cdd:COG0664   157 LPLTQEEIASYLGLTRETVSRILKKLEKEGLIELE 191
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 2-196 6.90e-49

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 158.61  E-value: 6.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   2 LRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPVN 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  82 LSAVALTDMKVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGtdeqGYIN 161
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLD----GRID 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1242548464 162 IQLSREEIGNMIGSATESLIRMLSEFSKNEWIETR 196
Cdd:COG0664   157 LPLTQEEIASYLGLTRETVSRILKKLEKEGLIELE 191
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-114 4.42e-21

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: 84.30  E-value: 4.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   1 MLRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPV 80
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1242548464  81 NLSAVALTDMKVCFIPKEEVLNFFATNAGFSVEV 114
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 21-107 9.38e-21

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 82.66  E-value: 9.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  21 NIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPVNLSAVALTDMKVCFIPKEEV 100
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDF 82


                  ....*..
gi 1242548464 101 LNFFATN 107
Cdd:pfam00027  83 LELLERD 89
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
4-194 7.27e-14

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 67.82  E-value: 7.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   4 TLSEGEL----RVISECKTasnIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDP 79
Cdd:PRK11161   23 TLNEHELdqldNIIERKKP---IQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGQH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  80 VNLSAVALTDMkVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGtdEQGY 159
Cdd:PRK11161  100 PSFAQALETSM-VCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLSRRFA--QRGF 176

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242548464 160 ----INIQLSREEIGNMIGSATESLIRMLSEFSKNEWIE 194
Cdd:PRK11161  177 spreFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLA 215
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 1-117 2.70e-13

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: 63.96  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464    1 MLRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACD-- 78
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSrr 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1242548464   79 PVNLSAVALTDMKVCFIPKEEVLNFFATNAGFSVEVFRN 117
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 5-150 3.97e-03

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: 37.57  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   5 LSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSkLSSNGKSQIVRFVGKGDILGQRSVIACDPVNLSA 84
Cdd:TIGR03896 149 LHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLS-ISPDGPGREVGSSRRGEILGETPFLNGSLPGTAT 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242548464  85 V-ALTDMKVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLED 150
Cdd:TIGR03896 228 VkAIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLLSQRSRDQVSSRGYARRVYLREGLEYDEE 294
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 2-196 6.90e-49

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


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 158.61  E-value: 6.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   2 LRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPVN 81
Cdd:COG0664     1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGELSLLGGEPSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  82 LSAVALTDMKVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGtdeqGYIN 161
Cdd:COG0664    81 ATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLD----GRID 156

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1242548464 162 IQLSREEIGNMIGSATESLIRMLSEFSKNEWIETR 196
Cdd:COG0664   157 LPLTQEEIASYLGLTRETVSRILKKLEKEGLIELE 191
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 1-114 4.42e-21

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: 84.30  E-value: 4.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   1 MLRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPV 80
Cdd:cd00038     1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGELALLGNGPR 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1242548464  81 NLSAVALTDMKVCFIPKEEVLNFFATNAGFSVEV 114
Cdd:cd00038    81 SATVRALTDSELLVLPRSDFRRLLQEYPELARRL 114
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 21-107 9.38e-21

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


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 82.66  E-value: 9.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  21 NIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDPVNLSAVALTDMKVCFIPKEEV 100
Cdd:pfam00027   3 SYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPREDF 82


                  ....*..
gi 1242548464 101 LNFFATN 107
Cdd:pfam00027  83 LELLERD 89
PRK11161 PRK11161
fumarate/nitrate reduction transcriptional regulator Fnr;
4-194 7.27e-14

fumarate/nitrate reduction transcriptional regulator Fnr;


Pssm-ID: 183004 [Multi-domain]  Cd Length: 235  Bit Score: 67.82  E-value: 7.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   4 TLSEGEL----RVISECKTasnIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACDP 79
Cdd:PRK11161   23 TLNEHELdqldNIIERKKP---IQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGQH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  80 VNLSAVALTDMkVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGtdEQGY 159
Cdd:PRK11161  100 PSFAQALETSM-VCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLSRRFA--QRGF 176

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1242548464 160 ----INIQLSREEIGNMIGSATESLIRMLSEFSKNEWIE 194
Cdd:PRK11161  177 spreFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLA 215
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 1-117 2.70e-13

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: 63.96  E-value: 2.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464    1 MLRTLSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSVIACD-- 78
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSrr 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1242548464   79 PVNLSAVALTDMKVCFIPKEEVLNFFATNAGFSVEVFRN 117
Cdd:smart00100  81 AASAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLE 119
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 139-196 2.92e-11

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: 57.08  E-value: 2.92e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1242548464 139 QRLADTLIFLEDnfgTDEQGYINIQLSREEIGNMIGSATESLIRMLSEFSKNEWIETR 196
Cdd:pfam13545   1 QRLARFLLELAA---RDGGGRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIERG 55
fixK PRK09391
transcriptional regulator FixK; Provisional
 23-187 1.19e-08

transcriptional regulator FixK; Provisional


Pssm-ID: 236494 [Multi-domain]  Cd Length: 230  Bit Score: 53.50  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  23 KKGKTIFEEGNVLAGVYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRSviacDPVN-LSAVALTDMKVCFIPKEEVL 101
Cdd:PRK09391   44 KKGEEIYGEGEPADYVYQVESGAVRTYRLLSDGRRQIGAFHLPGDVFGLES----GSTHrFTAEAIVDTTVRLIKRRSLE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464 102 NFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLEDNFGTDEQgyINIQLSREEIGNMIGSATESLI 181
Cdd:PRK09391  120 QAAATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEMDERLGGAGM--MALPMSRRDIADYLGLTIETVS 197


                  ....*.
gi 1242548464 182 RMLSEF 187
Cdd:PRK09391  198 RALSQL 203
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 38-195 1.73e-05

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 44.04  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464  38 VYCIKEGICKLSKLSSNGKSQIVRFVGKGDILGQRsVIACDPVNLSAVALTDMKVcfipkeEVLNFFATNAGFSVEVFRN 117
Cdd:PRK13918   29 LYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGEE-ALAGAERAYFAEAVTDSRI------DVLNPALMSAEDNLVLTQH 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464 118 VCDELKKADNAIVDLAQKTVKQRLADTLIFLEDN--FGTDEQGYINIQLSREEIGNMIGSATESLIRMLSEFSKNEWIET 195
Cdd:PRK13918  102 LVRTLARAYESIYRLVGQRLKNRIAAALLELSDTplATQEDSGETMIYATHDELAAAVGSVRETVTKVIGELSREGYIRS 181
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
160-196 8.38e-04

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 36.26  E-value: 8.38e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1242548464  160 INIQLSREEIGNMIGSATESLIRMLSEFSKNEWIETR 196
Cdd:smart00419   5 VRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISRE 41
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 137-187 1.58e-03

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: 35.72  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1242548464 137 VKQRLADTLIFLEDNFGTDEQgyINIQLSREEIGNMIGSATESLIRMLSEF 187
Cdd:cd00092     1 AKERLASFLLNLSLRYGAGDL--VQLPLTRQEIADYLGLTRETVSRTLKEL 49
cyc_nuc_ocin TIGR03896
bacteriocin-type transport-associated protein; Members of this protein family are ...
 5-150 3.97e-03

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: 37.57  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242548464   5 LSEGELRVISECKTASNIKKGKTIFEEGNVLAGVYCIKEGICKLSkLSSNGKSQIVRFVGKGDILGQRSVIACDPVNLSA 84
Cdd:TIGR03896 149 LHESDVAWMMASGTPQKLPAGTILIHEGGTVDALYILLYGEASLS-ISPDGPGREVGSSRRGEILGETPFLNGSLPGTAT 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1242548464  85 V-ALTDMKVCFIPKEEVLNFFATNAGFSVEVFRNVCDELKKADNAIVDLAQKTVKQRLADTLIFLED 150
Cdd:TIGR03896 228 VkAIENSVLLAIDKQQLAAKLQQDVGFASRFYRVIASLLSQRSRDQVSSRGYARRVYLREGLEYDEE 294
 
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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