|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
1-282 |
0e+00 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 584.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
Cdd:PRK13502 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
Cdd:PRK13502 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
Cdd:PRK13502 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1090406580 241 PLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
Cdd:PRK13502 241 PLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
|
|
| cupin_RhaR_RhaS-like_N |
cd06977 |
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ... |
17-163 |
5.27e-62 |
|
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380382 [Multi-domain] Cd Length: 147 Bit Score: 192.48 E-value: 5.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 17 QQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVLQNIIYCPERLKL 96
Cdd:cd06977 1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090406580 97 NVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHR 163
Cdd:cd06977 81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
192-275 |
1.01e-27 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 102.25 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 192 PFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTP 271
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 1090406580 272 SQWR 275
Cdd:smart00342 81 SEYR 84
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
139-275 |
6.64e-25 |
|
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: 101.00 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 139 GRDpLANEMAEllfgQLVMTLKR----HRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFR 214
Cdd:COG4977 174 GAE-LANAVAR----RLVVDPRRpggqAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFR 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1090406580 215 AQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:COG4977 249 AATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYR 309
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
204-275 |
1.06e-21 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 86.49 E-value: 1.06e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090406580 204 CSERVLRQQFRAQTGMTINQYLRQVRICHA-QYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:pfam12833 7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13502 |
PRK13502 |
HTH-type transcriptional activator RhaR; |
1-282 |
0e+00 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184093 [Multi-domain] Cd Length: 282 Bit Score: 584.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
Cdd:PRK13502 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
Cdd:PRK13502 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
Cdd:PRK13502 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1090406580 241 PLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
Cdd:PRK13502 241 PLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
|
|
| PRK13500 |
PRK13500 |
HTH-type transcriptional activator RhaR; |
1-282 |
1.00e-169 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184091 [Multi-domain] Cd Length: 312 Bit Score: 471.89 E-value: 1.00e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
Cdd:PRK13500 31 VAHQLKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
Cdd:PRK13500 111 DLVLQNIIYCPERLKLNLDWQGAIPGFSASAGQPHWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
Cdd:PRK13500 191 RHRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHS 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1090406580 241 PLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
Cdd:PRK13500 271 RLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD 312
|
|
| PRK13501 |
PRK13501 |
HTH-type transcriptional activator RhaR; |
1-276 |
3.85e-125 |
|
HTH-type transcriptional activator RhaR;
Pssm-ID: 184092 [Multi-domain] Cd Length: 290 Bit Score: 358.06 E-value: 3.85e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80
Cdd:PRK13501 1 MRAPLLLESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160
Cdd:PRK13501 81 DLVLDNIIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKTDSWSIQLTEVLLLQLAIVLK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240
Cdd:PRK13501 161 RHRYRAEQAHLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGS 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1090406580 241 PLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRH 276
Cdd:PRK13501 241 EHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQ 276
|
|
| PRK13503 |
PRK13503 |
HTH-type transcriptional activator RhaS; |
6-276 |
3.57e-62 |
|
HTH-type transcriptional activator RhaS;
Pssm-ID: 184094 [Multi-domain] Cd Length: 278 Bit Score: 197.59 E-value: 3.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 6 ILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVLQ 85
Cdd:PRK13503 3 VLHSVDFFPSGNAPVAIEPRLPQAAFPEHHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHLYEHTDNLCLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 86 NIIY-CPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHRY 164
Cdd:PRK13503 83 NVLYrSPDAFRFLAGLNQLLPQEQDGQYPSHWRVNQSVLQQVRQLVAQMEQQEESNDLEAIASREILFMQLLVLLRKSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 165 ATddlPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMV 244
Cdd:PRK13503 163 QE---NGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASV 239
|
250 260 270
....*....|....*....|....*....|..
gi 1090406580 245 SEISMQCGFEDSNYFSVVFTRETGMTPSQWRH 276
Cdd:PRK13503 240 TDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQ 271
|
|
| cupin_RhaR_RhaS-like_N |
cd06977 |
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ... |
17-163 |
5.27e-62 |
|
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380382 [Multi-domain] Cd Length: 147 Bit Score: 192.48 E-value: 5.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 17 QQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVLQNIIYCPERLKL 96
Cdd:cd06977 1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090406580 97 NVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHR 163
Cdd:cd06977 81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
|
|
| HTH_ARAC |
smart00342 |
helix_turn_helix, arabinose operon control protein; |
192-275 |
1.01e-27 |
|
helix_turn_helix, arabinose operon control protein;
Pssm-ID: 197666 [Multi-domain] Cd Length: 84 Bit Score: 102.25 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 192 PFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTP 271
Cdd:smart00342 1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80
|
....
gi 1090406580 272 SQWR 275
Cdd:smart00342 81 SEYR 84
|
|
| GlxA |
COG4977 |
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ... |
139-275 |
6.64e-25 |
|
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: 101.00 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 139 GRDpLANEMAEllfgQLVMTLKR----HRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFR 214
Cdd:COG4977 174 GAE-LANAVAR----RLVVDPRRpggqAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFR 248
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1090406580 215 AQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:COG4977 249 AATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYR 309
|
|
| AraC |
COG2207 |
AraC-type DNA-binding domain and AraC-containing proteins [Transcription]; |
104-275 |
7.05e-23 |
|
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
Pssm-ID: 441809 [Multi-domain] Cd Length: 258 Bit Score: 94.85 E-value: 7.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 104 IPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHRYATDDLPATSRETLLDKLIT 183
Cdd:COG2207 91 LVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLT 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 184 alanslecpfaLDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVF 263
Cdd:COG2207 171 -----------LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAF 239
|
170
....*....|..
gi 1090406580 264 TRETGMTPSQWR 275
Cdd:COG2207 240 KKRFGVTPSEYR 251
|
|
| HTH_18 |
pfam12833 |
Helix-turn-helix domain; |
204-275 |
1.06e-21 |
|
Helix-turn-helix domain;
Pssm-ID: 432818 [Multi-domain] Cd Length: 81 Bit Score: 86.49 E-value: 1.06e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090406580 204 CSERVLRQQFRAQTGMTINQYLRQVRICHA-QYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:pfam12833 7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
|
|
| AraC_binding |
pfam02311 |
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ... |
23-151 |
5.47e-17 |
|
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.
Pssm-ID: 396749 [Multi-domain] Cd Length: 134 Bit Score: 75.55 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 23 ADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSV--NDLVLQNIIYCPERLKLNVNW 100
Cdd:pfam02311 8 EARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPEseDGWRYRWLYFEPELLERILAD 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1090406580 101 QAMIPGFQgaqwhPHWRLGSMGMNQARQVINQLEHESNGRDPLANE-MAELL 151
Cdd:pfam02311 88 ISILAGGP-----LPLLRDPELAALLRALFRLLEEAGRSDDLLAEAlLYQLL 134
|
|
| AdaA |
COG2169 |
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ... |
167-275 |
6.42e-15 |
|
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: 6.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 167 DDLPATS-RETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSpLMVS 245
Cdd:COG2169 74 DLAPGSPpRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTG-LSVT 152
|
90 100 110
....*....|....*....|....*....|
gi 1090406580 246 EISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:COG2169 153 DAAYAAGFGSLSRFYEAFKKLLGMTPSAYR 182
|
|
| PRK10572 |
PRK10572 |
arabinose operon transcriptional regulator AraC; |
132-275 |
1.14e-11 |
|
arabinose operon transcriptional regulator AraC;
Pssm-ID: 236717 [Multi-domain] Cd Length: 290 Bit Score: 63.84 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 132 QLEHESNGRDPLANEMAELLFGQLVmtLKRHRYAtddlPATSRETLLDKLITA---LANSLECPFALDAFCQQEQCSERV 208
Cdd:PRK10572 142 QIEQAGQSEGRYSELLAMNLLERLL--LRCMEAI----PESLHPPMDPRVREAcqyISDHLASEFDIESVAQHVCLSPSR 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1090406580 209 LRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:PRK10572 216 LAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFR 282
|
|
| ftrA |
PRK09393 |
transcriptional activator FtrA; Provisional |
144-275 |
2.35e-11 |
|
transcriptional activator FtrA; Provisional
Pssm-ID: 181818 [Multi-domain] Cd Length: 322 Bit Score: 63.06 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 144 ANEMAEllfgQLVMTLKRH----RYATDDLPATSRETLlDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGM 219
Cdd:PRK09393 187 ANRVAR----RLVVPPHRDggqaQFVPRPVASRESDRL-GPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGM 261
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1090406580 220 TINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:PRK09393 262 TPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYR 317
|
|
| QdoI |
COG1917 |
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
12-81 |
7.05e-10 |
|
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 55.24 E-value: 7.05e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 12 FFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVND 81
Cdd:COG1917 17 ADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGD 86
|
|
| PRK10219 |
PRK10219 |
superoxide response transcriptional regulator SoxS; |
173-276 |
1.26e-09 |
|
superoxide response transcriptional regulator SoxS;
Pssm-ID: 182314 [Multi-domain] Cd Length: 107 Bit Score: 54.55 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 173 SRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCG 252
Cdd:PRK10219 2 SHQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLG 81
|
90 100
....*....|....*....|....
gi 1090406580 253 FEDSNYFSVVFTRETGMTPSQWRH 276
Cdd:PRK10219 82 YVSQQTFSRVFRRQFDRTPSDYRH 105
|
|
| PRK10371 |
PRK10371 |
transcriptional regulator MelR; |
213-280 |
1.24e-08 |
|
transcriptional regulator MelR;
Pssm-ID: 182416 [Multi-domain] Cd Length: 302 Bit Score: 54.83 E-value: 1.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1090406580 213 FRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQ 280
Cdd:PRK10371 228 FQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQ 295
|
|
| HTH_AraC |
pfam00165 |
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ... |
239-276 |
1.07e-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: 47.15 E-value: 1.07e-07
10 20 30
....*....|....*....|....*....|....*...
gi 1090406580 239 HSPLMVSEISMQCGFeDSNYFSVVFTRETGMTPSQWRH 276
Cdd:pfam00165 6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
|
|
| cupin_TM1459-like |
cd02222 |
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ... |
34-76 |
4.76e-05 |
|
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.
Pssm-ID: 380351 [Multi-domain] Cd Length: 91 Bit Score: 41.28 E-value: 4.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1090406580 34 HTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSY 76
Cdd:cd02222 33 HTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQF 75
|
|
| PRK09685 |
PRK09685 |
DNA-binding transcriptional activator FeaR; Provisional |
210-275 |
1.51e-04 |
|
DNA-binding transcriptional activator FeaR; Provisional
Pssm-ID: 236612 [Multi-domain] Cd Length: 302 Bit Score: 42.33 E-value: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1090406580 210 RQQFR--AQTGMTINQYLRQVRI--ChAQYLlqHSPLM---VSEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
Cdd:PRK09685 229 RSLYRlfAEQGLVVAQYIRNRRLdrC-ADDL--RPAADdekITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298
|
|
| cupin_RmlC-like |
cd02208 |
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
27-88 |
1.68e-04 |
|
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.
Pssm-ID: 380338 [Multi-domain] Cd Length: 73 Bit Score: 39.39 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090406580 27 PQDVFAEHTHEF-CELVMVWRGNGLHVLN-ERPYRITRGDLFYIRAEDKHSY--TSVNDLVLQNII 88
Cdd:cd02208 8 PGTSSPPHWHPEqDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFvnTSDEPAVFLVVS 73
|
|
| PRK09978 |
PRK09978 |
DNA-binding transcriptional regulator GadX; Provisional |
205-280 |
3.81e-04 |
|
DNA-binding transcriptional regulator GadX; Provisional
Pssm-ID: 137624 [Multi-domain] Cd Length: 274 Bit Score: 41.06 E-value: 3.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1090406580 205 SERVLRQQFRAQtGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQ 280
Cdd:PRK09978 171 SPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQ 245
|
|
| PRK09940 |
PRK09940 |
transcriptional regulator YdeO; Provisional |
192-273 |
4.89e-04 |
|
transcriptional regulator YdeO; Provisional
Pssm-ID: 182157 [Multi-domain] Cd Length: 253 Bit Score: 40.84 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 192 PFALDAFCQQEQCSERVLRQQFRaQTGMTINQYLRQVRICHAQYLLQHSPlMVSEISMQCGFEDSNYFSVVFTRETGMTP 271
Cdd:PRK09940 150 PWKLKDICDCLYISESLLKKKLK-QEQTTFSQILLDARMQHAKNLIRVEG-SVNKIAEQCGYASTSYFIYAFRKHFGNSP 227
|
..
gi 1090406580 272 SQ 273
Cdd:PRK09940 228 KR 229
|
|
| PRK11511 |
PRK11511 |
MDR efflux pump AcrAB transcriptional activator MarA; |
181-275 |
8.87e-04 |
|
MDR efflux pump AcrAB transcriptional activator MarA;
Pssm-ID: 236920 [Multi-domain] Cd Length: 127 Bit Score: 38.54 E-value: 8.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 181 LITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFS 260
Cdd:PRK11511 14 ILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLT 93
|
90
....*....|....*
gi 1090406580 261 VVFTRETGMTPSQWR 275
Cdd:PRK11511 94 RTFKNYFDVPPHKYR 108
|
|
| Cupin_2 |
pfam07883 |
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ... |
27-76 |
9.49e-04 |
|
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).
Pssm-ID: 462300 [Multi-domain] Cd Length: 71 Bit Score: 36.85 E-value: 9.49e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1090406580 27 PQDVFAEHTHEF-CELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSY 76
Cdd:pfam07883 7 PGESSPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57
|
|
| PRK15186 |
PRK15186 |
AraC family transcriptional regulator; Provisional |
133-274 |
1.23e-03 |
|
AraC family transcriptional regulator; Provisional
Pssm-ID: 185108 [Multi-domain] Cd Length: 291 Bit Score: 39.66 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1090406580 133 LEHESNGRDPLANEMAELLFGQLVMTLKRHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQ 212
Cdd:PRK15186 138 LLHSSNKSQKLSQDKKEYLIRFLLSEFIYEPEAFALFRELSQNTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRK 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1090406580 213 FRaQTGMTINQYLRQVRICHAQYLLQHSPLMVSEISMQCGFEDSNYFSVVFTRETGMTPSQW 274
Cdd:PRK15186 218 LK-QENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
|
|
| |
