|
Name |
Accession |
Description |
Interval |
E-value |
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
14-324 |
4.32e-120 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 348.49 E-value: 4.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 14 PTVALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCG--PGPVR-VGPFTVEPDHGLERLVRADTVIVPACADVDE 90
Cdd:PRK09393 10 HLVVALAYDGLCTFEFGCAVEIFGLPRPELGVDWYRFAVAAvePGPLRaAGGITVVADGGLELLDRADTIVIPGWRGPDA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 91 PPPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAA 170
Cdd:PRK09393 90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 171 AVDLCLHLIHLDHGAAVANSIARRLVMAPHRPGGQAQFVATPVQVTGGDhQLAGLLAWAQQRLDRPLTVTDMARRASTSP 250
Cdd:PRK09393 170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1903802009 251 RHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRRAFRS 324
Cdd:PRK09393 249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
15-328 |
9.44e-120 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 347.14 E-value: 9.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 15 TVALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCGP--GPVRV-GPFTVEPDHGLERLVRADTVIVPACADVDEP 91
Cdd:COG4977 2 RVAFLLLPGFSLLDLAGPLEVFRLANRLAGRPLYRWRLVSLdgGPVRSsSGLTVAPDHGLADLAAADTLIVPGGLDPAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 92 PPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAAA 171
Cdd:COG4977 82 ADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 172 VDLCLHLIHLDHGAAVANSIARRLVMAPHRPGGQAQFVATPVQVTGGDHQLAGLLAWAQQRLDRPLTVTDMARRASTSPR 251
Cdd:COG4977 162 IDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1903802009 252 HLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRRAFRSANPT 328
Cdd:COG4977 242 TLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARAAA 318
|
|
| GATase1_AraC_1 |
cd03137 |
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
16-198 |
4.01e-62 |
|
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153231 [Multi-domain] Cd Length: 187 Bit Score: 195.80 E-value: 4.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 16 VALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCGPGPVRV---GPFTVEPDHGLERLVRADTVIVPACADVDE-P 91
Cdd:cd03137 1 VAVLVFPGVSLLDLSGPAEVFGEANRALGPPAYELRVCSPEGGPVrssSGLSLVADAGLDALAAADTVIVPGGPDVDGrP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 92 PPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAAA 171
Cdd:cd03137 81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160
|
170 180
....*....|....*....|....*..
gi 1903802009 172 VDLCLHLIHLDHGAAVANSIARRLVMA 198
Cdd:cd03137 161 IDLCLHLVREDLGAAVANRVARRLVVP 187
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
236-319 |
2.00e-23 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 91.85 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 236 PLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPP 315
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 1903802009 316 DTYR 319
Cdd:smart00342 81 SEYR 84
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
242-321 |
3.68e-22 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 88.42 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 242 MARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRA-QELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRR 320
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
.
gi 1903802009 321 A 321
Cdd:pfam12833 81 R 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
14-324 |
4.32e-120 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 348.49 E-value: 4.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 14 PTVALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCG--PGPVR-VGPFTVEPDHGLERLVRADTVIVPACADVDE 90
Cdd:PRK09393 10 HLVVALAYDGLCTFEFGCAVEIFGLPRPELGVDWYRFAVAAvePGPLRaAGGITVVADGGLELLDRADTIVIPGWRGPDA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 91 PPPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAA 170
Cdd:PRK09393 90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 171 AVDLCLHLIHLDHGAAVANSIARRLVMAPHRPGGQAQFVATPVQVTGGDhQLAGLLAWAQQRLDRPLTVTDMARRASTSP 250
Cdd:PRK09393 170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1903802009 251 RHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRRAFRS 324
Cdd:PRK09393 249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
15-328 |
9.44e-120 |
|
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];
Pssm-ID: 444002 [Multi-domain] Cd Length: 318 Bit Score: 347.14 E-value: 9.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 15 TVALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCGP--GPVRV-GPFTVEPDHGLERLVRADTVIVPACADVDEP 91
Cdd:COG4977 2 RVAFLLLPGFSLLDLAGPLEVFRLANRLAGRPLYRWRLVSLdgGPVRSsSGLTVAPDHGLADLAAADTLIVPGGLDPAAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 92 PPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAAA 171
Cdd:COG4977 82 ADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 172 VDLCLHLIHLDHGAAVANSIARRLVMAPHRPGGQAQFVATPVQVTGGDHQLAGLLAWAQQRLDRPLTVTDMARRASTSPR 251
Cdd:COG4977 162 IDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1903802009 252 HLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRRAFRSANPT 328
Cdd:COG4977 242 TLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARAAA 318
|
|
| GATase1_AraC_1 |
cd03137 |
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
16-198 |
4.01e-62 |
|
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153231 [Multi-domain] Cd Length: 187 Bit Score: 195.80 E-value: 4.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 16 VALAAAGRLLHFELAVAYEIFGNPPPDAPQGWYDVLLCGPGPVRV---GPFTVEPDHGLERLVRADTVIVPACADVDE-P 91
Cdd:cd03137 1 VAVLVFPGVSLLDLSGPAEVFGEANRALGPPAYELRVCSPEGGPVrssSGLSLVADAGLDALAAADTVIVPGGPDVDGrP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 92 PPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAAA 171
Cdd:cd03137 81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160
|
170 180
....*....|....*....|....*..
gi 1903802009 172 VDLCLHLIHLDHGAAVANSIARRLVMA 198
Cdd:cd03137 161 IDLCLHLVREDLGAAVANRVARRLVVP 187
|
|
| GATase1_PfpI_2 |
cd03139 |
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ... |
33-195 |
7.83e-26 |
|
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153233 [Multi-domain] Cd Length: 183 Bit Score: 101.47 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 33 YEIFGNPPPDAPQgwYDVLLCG--PGPVRV-GPFTVEPDHGLERLVRADTVIVPACADVD-EPPPPELVDAVRAAHAAGA 108
Cdd:cd03139 18 YEVFGRAPRLAAP--FEVFLVSetGGPVSSrSGLTVLPDTSFADPPDLDVLLVPGGGGTRaLVNDPALLDFIRRQAARAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 109 RVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPlaEVDPDVLYTDNGSVLTAAGKAAAVDLCLHLIHLDHGAAVA 188
Cdd:cd03139 96 YVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGA--IVVVDARWVVDGNIWTSGGVSAGIDMALALVARLFGEELA 173
|
....*..
gi 1903802009 189 NSIARRL 195
Cdd:cd03139 174 QAVALLI 180
|
|
| GATase1_AraC_ArgR_like |
cd03136 |
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ... |
64-196 |
1.91e-25 |
|
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153230 [Multi-domain] Cd Length: 185 Bit Score: 100.35 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 64 TVEPDHGLERLVRADTVIVPACADVDEPPPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSA 143
Cdd:cd03136 52 RVAPDAALEDAPPLDYLFVVGGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAE 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1903802009 144 RHPLAEVDPDvLYTDNGSVLTAAGKAAAVDLCLHLIHLDHGAAVANSIARRLV 196
Cdd:cd03136 132 AFPRVQVTRD-LFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFL 183
|
|
| GATase1_AraC_2 |
cd03138 |
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ... |
64-197 |
1.01e-23 |
|
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.
Pssm-ID: 153232 [Multi-domain] Cd Length: 195 Bit Score: 96.18 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 64 TVEPDHGLERLVRADTVIVPACADVDEPPP----PELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAA 139
Cdd:cd03138 57 LILPDATLADVPAPDLVIVPGLGGDPDELLladnPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAP 136
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1903802009 140 ELSARHPLAEVDPDVLYTDNGSVLTAAGKAAAVDLCLHLIHLDHGAAVANSIARRLVM 197
Cdd:cd03138 137 QFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
236-319 |
2.00e-23 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 91.85 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 236 PLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPP 315
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 1903802009 316 DTYR 319
Cdd:smart00342 81 SEYR 84
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
91-326 |
6.96e-23 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 95.62 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 91 PPPPELVDAVRAAHAAGARVASLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVLYTDNGSVLTAAGKAA 170
Cdd:COG2207 19 LLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 171 AVDLCLHLIHLDHGAAVANSIARRLVMAPHRPGGQAQFVATPVQVTGGDHQLAG----LLAWAQQRLDRPLTVTDMARRA 246
Cdd:COG2207 99 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLllllLLLLLLLLLLLLLTLEELAREL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 247 STSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRRAFRSAN 326
Cdd:COG2207 179 GLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
242-321 |
3.68e-22 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 88.42 E-value: 3.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 242 MARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRA-QELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRR 320
Cdd:pfam12833 1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
|
.
gi 1903802009 321 A 321
Cdd:pfam12833 81 R 81
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
219-321 |
1.06e-14 |
|
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];
Pssm-ID: 441772 [Multi-domain] Cd Length: 358 Bit Score: 73.93 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 219 DHQLAGLLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEaTDETIEAVAVATGMG 298
Cdd:COG2169 83 ADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAGFG 161
|
90 100
....*....|....*....|...
gi 1903802009 299 TATTLRRQFKRVVGVPPDTYRRA 321
Cdd:COG2169 162 SLSRFYEAFKKLLGMTPSAYRRG 184
|
|
| PRK10219 |
PRK10219 |
superoxide response transcriptional regulator SoxS; |
225-321 |
9.37e-12 |
|
superoxide response transcriptional regulator SoxS;
Pssm-ID: 182314 [Multi-domain] Cd Length: 107 Bit Score: 61.09 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 225 LLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLR 304
Cdd:PRK10219 10 LIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFS 89
|
90
....*....|....*..
gi 1903802009 305 RQFKRVVGVPPDTYRRA 321
Cdd:PRK10219 90 RVFRRQFDRTPSDYRHR 106
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
225-319 |
2.03e-11 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 60.50 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 225 LLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLR 304
Cdd:PRK11511 14 ILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLT 93
|
90
....*....|....*
gi 1903802009 305 RQFKRVVGVPPDTYR 319
Cdd:PRK11511 94 RTFKNYFDVPPHKYR 108
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
237-326 |
2.80e-10 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 60.37 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 237 LTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPD 316
Cdd:PRK10572 200 FDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPS 279
|
90
....*....|
gi 1903802009 317 TYRRAFRSAN 326
Cdd:PRK10572 280 EFRARCEEKN 289
|
|
| PRK15435 |
PRK15435 |
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada; |
234-320 |
5.31e-09 |
|
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
Pssm-ID: 185333 [Multi-domain] Cd Length: 353 Bit Score: 56.73 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 234 DRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLeATDETIEAVAVATGMGTATTLRRQFKRVVGV 313
Cdd:PRK15435 97 ETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREAL-AKGESVTTSILNAGFPDSSSYYRKADETLGM 175
|
....*..
gi 1903802009 314 PPDTYRR 320
Cdd:PRK15435 176 TAKQFRH 182
|
|
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
234-324 |
8.18e-09 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 55.98 E-value: 8.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 234 DRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGV 313
Cdd:PRK10371 205 DQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGM 284
|
90
....*....|.
gi 1903802009 314 PPDTYRRAFRS 324
Cdd:PRK10371 285 SPQQYRKLSQQ 295
|
|
| PRK15121 |
PRK15121 |
MDR efflux pump AcrAB transcriptional activator RobA; |
225-321 |
3.27e-07 |
|
MDR efflux pump AcrAB transcriptional activator RobA;
Pssm-ID: 185076 [Multi-domain] Cd Length: 289 Bit Score: 50.78 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 225 LLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLR 304
Cdd:PRK15121 10 LLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFT 89
|
90
....*....|....*..
gi 1903802009 305 RQFKRVVGVPPDTYRRA 321
Cdd:PRK15121 90 RAFKKQFAQTPALYRRS 106
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
230-269 |
3.28e-07 |
|
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.
Pssm-ID: 425497 [Multi-domain] Cd Length: 42 Bit Score: 45.99 E-value: 3.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1903802009 230 QQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWL 269
Cdd:pfam00165 2 RENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
|
|
| DJ-1_PfpI |
pfam01965 |
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ... |
112-179 |
6.99e-07 |
|
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.
Pssm-ID: 396514 [Multi-domain] Cd Length: 165 Bit Score: 48.41 E-value: 6.99e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1903802009 112 SLCTGAFVLGAAGLLDGRRATTHWAHAAELSARHPLAEVDPDVlytDNGSVLTAAGKAAAVDLCLHLI 179
Cdd:pfam01965 99 AICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVV---VDGNLVTSRGPGDAPEFALEIL 163
|
|
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
182-319 |
7.40e-07 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 49.67 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 182 DHGAAVANSIAR----RLVMAPHRpggqAQFVATPVQVTGGDHQLAGLLAWAQQRLDRPLTVTDMARRASTSPRHLGRQF 257
Cdd:PRK13502 138 NGRDPLANEMAEllfgQLVMTLKR----HRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQF 213
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1903802009 258 RAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYR 319
Cdd:PRK13502 214 RAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
216-319 |
1.36e-06 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 48.90 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 216 TGGDHQLAGLLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVAT 295
Cdd:PRK13503 167 ENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRC 246
|
90 100
....*....|....*....|....
gi 1903802009 296 GMGTATTLRRQFKRVVGVPPDTYR 319
Cdd:PRK13503 247 GFGDSNHFSTLFRREFSWSPRDIR 270
|
|
| PRK13501 |
PRK13501 |
HTH-type transcriptional activator RhaR; |
221-322 |
4.03e-06 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184092 [Multi-domain] Cd Length: 290 Bit Score: 47.59 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 221 QLAGLLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTA 300
Cdd:PRK13501 177 QLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDS 256
|
90 100
....*....|....*....|..
gi 1903802009 301 TTLRRQFKRVVGVPPDTYRRAF 322
Cdd:PRK13501 257 NYFSAVFTREAGMTPRDYRQRF 278
|
|
| PRK13500 |
PRK13500 |
HTH-type transcriptional activator RhaR; |
180-319 |
3.08e-05 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184091 [Multi-domain] Cd Length: 312 Bit Score: 45.09 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 180 HLDHGAAVANSIARRLVMAPHRpggqAQFVATPVQVTGGDHQLAGLLAWAQQRLDRPLTVTDMARRASTSPRHLGRQFRA 259
Cdd:PRK13500 170 HVPFANEMAELLFGQLVMLLNR----HRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQ 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 260 VTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYR 319
Cdd:PRK13500 246 QTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWR 305
|
|
| PRK10296 |
PRK10296 |
DNA-binding transcriptional regulator ChbR; Provisional |
241-326 |
7.82e-04 |
|
DNA-binding transcriptional regulator ChbR; Provisional
Pssm-ID: 182362 [Multi-domain] Cd Length: 278 Bit Score: 40.51 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1903802009 241 DMARRASTSPRHLGRQFRAVTGQTPLQWLLTQRVRRAQELLEATDETIEAVAVATGMGTATTLRRQFKRVVGVPPDTYRR 320
Cdd:PRK10296 193 NMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRK 272
|
....*.
gi 1903802009 321 AFRSAN 326
Cdd:PRK10296 273 KLTEFN 278
|
|
| |
