|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11161 |
PRK11161 |
fumarate/nitrate reduction transcriptional regulator Fnr; |
14-239 |
1.09e-115 |
|
fumarate/nitrate reduction transcriptional regulator Fnr;
Pssm-ID: 183004 [Multi-domain] Cd Length: 235 Bit Score: 330.52 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 14 HCKDCSLAPLCLPLSLTVEDMDSLDEIVKRGRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSEL 93
Cdd:PRK11161 9 HCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 94 VGLSGMDTETYPVSAQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLS 173
Cdd:PRK11161 89 VGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9947503 174 ARFRARGFSAQQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHILDSIELCALAG 239
Cdd:PRK11161 169 RRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAG 234
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
28-238 |
3.31e-57 |
|
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: 180.95 E-value: 3.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 28 SLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVG-LSGMDTETYPV 106
Cdd:COG0664 3 GLSDEELEALLAHLEL-RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGeLSLLGGEPSPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 107 SAQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRARgfsaqqF 186
Cdd:COG0664 82 TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGR------I 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9947503 187 RLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHILDSIELCALA 238
Cdd:COG0664 156 DLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
25-139 |
3.52e-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: 85.07 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 25 LPLSLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVG-LSGMDTET 103
Cdd:cd00038 1 LFSGLDDEELEELADALEE-RRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGeLALLGNGP 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 9947503 104 YPVSAQALETTSVCEIPFERLDELSEQLPQLRRQLM 139
Cdd:cd00038 80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
45-130 |
1.83e-18 |
|
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: 77.26 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 45 RPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSG-MDTETYPVSAQALETTSVCEIPFER 123
Cdd:pfam00027 2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELAlLGGEPRSATVVALTDSELLVIPRED 81
|
....*..
gi 9947503 124 LDELSEQ 130
Cdd:pfam00027 82 FLELLER 88
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
28-145 |
6.90e-16 |
|
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: 71.28 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 28 SLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSGMDTETYPVS 107
Cdd:smart00100 4 NLDAEELRELADALEP-VRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAA 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 9947503 108 AQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSRE 145
Cdd:smart00100 83 SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11161 |
PRK11161 |
fumarate/nitrate reduction transcriptional regulator Fnr; |
14-239 |
1.09e-115 |
|
fumarate/nitrate reduction transcriptional regulator Fnr;
Pssm-ID: 183004 [Multi-domain] Cd Length: 235 Bit Score: 330.52 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 14 HCKDCSLAPLCLPLSLTVEDMDSLDEIVKRGRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSEL 93
Cdd:PRK11161 9 HCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 94 VGLSGMDTETYPVSAQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLS 173
Cdd:PRK11161 89 VGFDAIGSGQHPSFAQALETSMVCEIPFETLDDLSGKMPKLRQQIMRLMSGEIKGDQEMILLLSKKNAEERLAAFIYNLS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9947503 174 ARFRARGFSAQQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHILDSIELCALAG 239
Cdd:PRK11161 169 RRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENNDALAQLAG 234
|
|
| Crp |
COG0664 |
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ... |
28-238 |
3.31e-57 |
|
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: 180.95 E-value: 3.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 28 SLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVG-LSGMDTETYPV 106
Cdd:COG0664 3 GLSDEELEALLAHLEL-RTLKKGEVLFREGDPADHLYFVLSGLVKLYRISEDGREQILGFLGPGDFFGeLSLLGGEPSPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 107 SAQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRARgfsaqqF 186
Cdd:COG0664 82 TAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDGR------I 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9947503 187 RLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHILDSIELCALA 238
Cdd:COG0664 156 DLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
|
|
| fixK |
PRK09391 |
transcriptional regulator FixK; Provisional |
48-219 |
5.13e-38 |
|
transcriptional regulator FixK; Provisional
Pssm-ID: 236494 [Multi-domain] Cd Length: 230 Bit Score: 132.47 E-value: 5.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 48 KKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGL-SGmdtETYPVSAQALETTSVCEIPFERLDE 126
Cdd:PRK09391 44 KKGEEIYGEGEPADYVYQVESGAVRTYRLLSDGRRQIGAFHLPGDVFGLeSG---STHRFTAEAIVDTTVRLIKRRSLEQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 127 LSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRArgfsAQQFRLAMSRNEIGNYLGLAVETV 206
Cdd:PRK09391 121 AAATDVDVARALLSLTAGGLRHAQDHMLLLGRKTAMERVAAFLLEMDERLGG----AGMMALPMSRRDIADYLGLTIETV 196
|
170
....*....|...
gi 9947503 207 SRVFTRFQQNGLI 219
Cdd:PRK09391 197 SRALSQLQDRGLI 209
|
|
| CAP_ED |
cd00038 |
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ... |
25-139 |
3.52e-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: 85.07 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 25 LPLSLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVG-LSGMDTET 103
Cdd:cd00038 1 LFSGLDDEELEELADALEE-RRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDGREQIVGFLGPGDLFGeLALLGNGP 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 9947503 104 YPVSAQALETTSVCEIPFERLDELSEQLPQLRRQLM 139
Cdd:cd00038 80 RSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
|
|
| cNMP_binding |
pfam00027 |
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ... |
45-130 |
1.83e-18 |
|
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: 77.26 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 45 RPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSG-MDTETYPVSAQALETTSVCEIPFER 123
Cdd:pfam00027 2 RSYKAGEVIFREGDPADSLYIVLSGKVKVYRTLEDGREQILAVLGPGDFFGELAlLGGEPRSATVVALTDSELLVIPRED 81
|
....*..
gi 9947503 124 LDELSEQ 130
Cdd:pfam00027 82 FLELLER 88
|
|
| HTH_CRP |
cd00092 |
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ... |
161-230 |
3.50e-16 |
|
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: 70.77 E-value: 3.50e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9947503 161 ADERIATFLVNLSARFRArgfsAQQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEG-KEVHILD 230
Cdd:cd00092 1 AKERLASFLLNLSLRYGA----GDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGrGKYRVNP 67
|
|
| cNMP |
smart00100 |
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ... |
28-145 |
6.90e-16 |
|
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: 71.28 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 28 SLTVEDMDSLDEIVKRgRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSGMDTETYPVS 107
Cdd:smart00100 4 NLDAEELRELADALEP-VRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDGEEQIVGTLGPGDFFGELALLTNSRRAA 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 9947503 108 AQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSRE 145
Cdd:smart00100 83 SAAAVALELATLLRIDFRDFLQLLPELPQLLLELLLEL 120
|
|
| PRK11753 |
PRK11753 |
cAMP-activated global transcriptional regulator CRP; |
53-226 |
3.37e-14 |
|
cAMP-activated global transcriptional regulator CRP;
Pssm-ID: 236969 [Multi-domain] Cd Length: 211 Bit Score: 69.24 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 53 LFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSGMDTETYPVSA--QALETTSVCEIPFERLDELSEQ 130
Cdd:PRK11753 31 LIHAGEKAETLYYIVKGSVAVLIKDEEGKEMILSYLNQGDFIGELGLFEEGQERSAwvRAKTACEVAEISYKKFRQLIQV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 131 LPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRARGfSAQQFRLAMSRNEIGNYLGLAVETVSRVF 210
Cdd:PRK11753 111 NPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQPDAMT-HPDGMQIKITRQEIGRIVGCSREMVGRVL 189
|
170
....*....|....*.
gi 9947503 211 TRFQQNGLISAEGKEV 226
Cdd:PRK11753 190 KMLEDQGLISAHGKTI 205
|
|
| HTH_CRP |
smart00419 |
helix_turn_helix, cAMP Regulatory protein; |
182-229 |
2.31e-12 |
|
helix_turn_helix, cAMP Regulatory protein;
Pssm-ID: 128696 [Multi-domain] Cd Length: 48 Bit Score: 59.76 E-value: 2.31e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 9947503 182 SAQQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHIL 229
Cdd:smart00419 1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVIL 48
|
|
| HTH_Crp_2 |
pfam13545 |
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ... |
163-230 |
1.68e-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: 58.24 E-value: 1.68e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9947503 163 ERIATFLVNLSARFRARgfsaqQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLIsaEGKEVHILD 230
Cdd:pfam13545 1 QRLARFLLELAARDGGG-----RIDLPLTQEDLADLLGTTRETVSRVLSELRREGLI--ERGRITILD 61
|
|
| Crp |
pfam00325 |
Bacterial regulatory proteins, crp family; |
188-219 |
2.00e-09 |
|
Bacterial regulatory proteins, crp family;
Pssm-ID: 425608 Cd Length: 32 Bit Score: 51.53 E-value: 2.00e-09
10 20 30
....*....|....*....|....*....|..
gi 9947503 188 LAMSRNEIGNYLGLAVETVSRVFTRFQQNGLI 219
Cdd:pfam00325 1 LRMSRQDIANYLGLTRETVSRVLGKLQEKGLI 32
|
|
| ftrB |
PRK09392 |
transcriptional activator FtrB; Provisional |
53-238 |
2.82e-05 |
|
transcriptional activator FtrB; Provisional
Pssm-ID: 181817 [Multi-domain] Cd Length: 236 Bit Score: 43.86 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 53 LFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSGMDTETYPVSAQALETTSVCEIPFERLDELSEQLP 132
Cdd:PRK09392 41 LITEGEPADFLFVVLDGLVELSASSQDRETTLAILRPVSTFILAAVVLDAPYLMSARTLTRSRVLMIPAELVREAMSEDP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 133 QLRR----QLMRLMSREIRDDQQMMLllskKTADERIATFLvnLSARFRARGfsAQQFRLAMSRNEIGNYLGLAVETVSR 208
Cdd:PRK09392 121 GFMRavvfELAGCYRGLVKSLKNQKL----RSSAERLANYL--LKQSLRQGG--ADVVTLPYEKRVLASYLGMTPENLSR 192
|
170 180 190
....*....|....*....|....*....|
gi 9947503 209 VFTRFQQNGlISAEGKEVHILDSIELCALA 238
Cdd:PRK09392 193 AFAALASHG-VHVDGSAVTITDPAGLARFA 221
|
|
| PRK13918 |
PRK13918 |
CRP/FNR family transcriptional regulator; Provisional |
48-241 |
9.86e-03 |
|
CRP/FNR family transcriptional regulator; Provisional
Pssm-ID: 237557 [Multi-domain] Cd Length: 202 Bit Score: 35.95 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 48 KKGEFLFRQGDPFGS--VFAVRSGALKTFSITDAGEEQITGFHLPSELVG---LSGMDTETYpvsAQALETTSVCEIPFE 122
Cdd:PRK13918 12 RPGAVILYPGVPGPSdmLYRVRSGLVRLHTVDDEGNALTLRYVRPGEYFGeeaLAGAERAYF---AEAVTDSRIDVLNPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9947503 123 RLDelSEQLPQLRRQLMRLMSREIRDDQQmmllLSKKTADERIATFLVNLSARFRARGFSAQQFRLAMSRNEIGNYLGLA 202
Cdd:PRK13918 89 LMS--AEDNLVLTQHLVRTLARAYESIYR----LVGQRLKNRIAAALLELSDTPLATQEDSGETMIYATHDELAAAVGSV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 9947503 203 VETVSRVFTRFQQNGLISAEGKEVHILDSIELCALAGGQ 241
Cdd:PRK13918 163 RETVTKVIGELSREGYIRSGYGKIQLLDLKGLEELAESA 201
|
|
| |
