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Conserved domains on  [gi|1340240333|gb|POV80591|]
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HTH-type transcriptional activator RhaR [Enterobacter cloacae complex sp. ECNIH9]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13502 super family cl32883
HTH-type transcriptional activator RhaR;
1-281 9.47e-165

HTH-type transcriptional activator RhaR;


The actual alignment was detected with superfamily member PRK13502:

Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 457.98  E-value: 9.47e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   1 MAAPLILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVN 80
Cdd:PRK13502    1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  81 DLVLQNVIYCPDRLSLNVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLK 160
Cdd:PRK13502   81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 161 RHRYETDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHT 240
Cdd:PRK13502  161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1340240333 241 EFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRA 281
Cdd:PRK13502  241 PLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQS 281
 
Name Accession Description Interval E-value
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1-281 9.47e-165

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 457.98  E-value: 9.47e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   1 MAAPLILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVN 80
Cdd:PRK13502    1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  81 DLVLQNVIYCPDRLSLNVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLK 160
Cdd:PRK13502   81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 161 RHRYETDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHT 240
Cdd:PRK13502  161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1340240333 241 EFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRA 281
Cdd:PRK13502  241 PLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQS 281
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 17-163 8.91e-61

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: 189.40  E-value: 8.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  17 EQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVNDLVLQNVIYCPDRLSL 96
Cdd:cd06977     1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340240333  97 NVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLKRHR 163
Cdd:cd06977    81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
195-275 4.92e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 95.31  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  195 LEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQW 274
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 1340240333  275 R 275
Cdd:smart00342  84 R 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 177-282 1.97e-20

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: 89.06  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 177 LLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDS 256
Cdd:COG4977   211 RLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSA 290

                          90       100
                  ....*....|....*....|....*.
gi 1340240333 257 NYFSVVFNREVGMTPVQWRHHSRRAA 282
Cdd:COG4977   291 SHFRRAFRRRFGVSPSAYRRRFRARA 316
HTH_18 pfam12833
Helix-turn-helix domain;
204-275 3.08e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.94  E-value: 3.08e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340240333 204 CSERALRQQFRTQTGMTVNHYLRQLRICHA-QYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWR 275
Cdd:pfam12833   7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
 
Name Accession Description Interval E-value
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1-281 9.47e-165

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 457.98  E-value: 9.47e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   1 MAAPLILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVN 80
Cdd:PRK13502    1 MANQLILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  81 DLVLQNVIYCPDRLSLNVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLK 160
Cdd:PRK13502   81 DLVLQNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 161 RHRYETDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHT 240
Cdd:PRK13502  161 RHRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1340240333 241 EFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRA 281
Cdd:PRK13502  241 PLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQS 281
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
1-276 2.96e-149

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 420.28  E-value: 2.96e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   1 MAAPLILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVN 80
Cdd:PRK13500   31 VAHQLKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  81 DLVLQNVIYCPDRLSLNVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLK 160
Cdd:PRK13500  111 DLVLQNIIYCPERLKLNLDWQGAIPGFSASAGQPHWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLN 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 161 RHRYETDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHT 240
Cdd:PRK13500  191 RHRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHS 270

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1340240333 241 EFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRH 276
Cdd:PRK13500  271 RLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRH 306
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1-282 1.50e-125

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 359.22  E-value: 1.50e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   1 MAAPLILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVN 80
Cdd:PRK13501    1 MRAPLLLESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  81 DLVLQNVIYCPDRLSLNVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLK 160
Cdd:PRK13501   81 DLVLDNIIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKTDSWSIQLTEVLLLQLAIVLK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 161 RHRYETDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHT 240
Cdd:PRK13501  161 RHRYRAEQAHLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGS 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1340240333 241 EFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRAA 282
Cdd:PRK13501  241 EHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSP 282
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
6-276 5.62e-68

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 212.23  E-value: 5.62e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333   6 ILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVNDLVLQ 85
Cdd:PRK13503    3 VLHSVDFFPSGNAPVAIEPRLPQAAFPEHHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHLYEHTDNLCLT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  86 NVIY-CPDRLSLNVDWAACIP-GFNGAKGSpHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLKRHR 163
Cdd:PRK13503   83 NVLYrSPDAFRFLAGLNQLLPqEQDGQYPS-HWRVNQSVLQQVRQLVAQMEQQEESNDLEAIASREILFMQLLVLLRKSS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 164 YETdnpSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFM 243
Cdd:PRK13503  162 LQE---NGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDAS 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1340240333 244 VSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRH 276
Cdd:PRK13503  239 VTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQ 271
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 17-163 8.91e-61

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: 189.40  E-value: 8.91e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  17 EQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVNDLVLQNVIYCPDRLSL 96
Cdd:cd06977     1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340240333  97 NVDWAACIPGFNGAKGSPHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLKRHR 163
Cdd:cd06977    81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
195-275 4.92e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 95.31  E-value: 4.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  195 LEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQW 274
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 1340240333  275 R 275
Cdd:smart00342  84 R 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 177-282 1.97e-20

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: 89.06  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 177 LLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDS 256
Cdd:COG4977   211 RLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSA 290

                          90       100
                  ....*....|....*....|....*.
gi 1340240333 257 NYFSVVFNREVGMTPVQWRHHSRRAA 282
Cdd:COG4977   291 SHFRRAFRRRFGVSPSAYRRRFRARA 316
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
114-282 2.58e-20

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 87.53  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 114 PHWRLSSSGMTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLKRHRYETDNPSATQQETLLDKLIATLAASLNksf 193
Cdd:COG2207    94 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLT--- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 194 vLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQ 273
Cdd:COG2207   171 -LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                  ....*....
gi 1340240333 274 WRHHSRRAA 282
Cdd:COG2207   250 YRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
204-275 3.08e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.94  E-value: 3.08e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340240333 204 CSERALRQQFRTQTGMTVNHYLRQLRICHA-QYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWR 275
Cdd:pfam12833   7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 20-156 4.22e-16

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: 73.24  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  20 VAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASV--NDLVLQNVIYCPDRLSLN 97
Cdd:pfam02311   5 EGIEARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPEseDGWRYRWLYFEPELLERI 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340240333  98 VDWAACIPGFNgakgsPHWRLSSSGMTAIRQAISLLEQesykTDPLANPMAEILFAQLV 156
Cdd:pfam02311  85 LADISILAGGP-----LPLLRDPELAALLRALFRLLEE----AGRSDDLLAEALLYQLL 134
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 166-282 1.94e-11

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: 63.53  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 166 TDNPSATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQhTEFMVS 245
Cdd:COG2169    74 DLAPGSPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVT 152

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1340240333 246 DVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRAA 282
Cdd:COG2169   153 DAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRGGAGAA 189
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
174-276 6.47e-10

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 55.32  E-value: 6.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 174 QETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGF 253
Cdd:PRK10219    3 HQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGY 82

                          90       100
                  ....*....|....*....|...
gi 1340240333 254 EDSNYFSVVFNREVGMTPVQWRH 276
Cdd:PRK10219   83 VSQQTFSRVFRRQFDRTPSDYRH 105
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
6-81 2.93e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 2.93e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1340240333   6 ILRKDDFFASAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYASVND 81
Cdd:COG1917    11 VSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGD 86
ftrA PRK09393
transcriptional activator FtrA; Provisional
 178-280 3.45e-09

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 56.51  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 178 LDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSN 257
Cdd:PRK09393  220 LGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEE 299

                          90       100
                  ....*....|....*....|...
gi 1340240333 258 YFSVVFNREVGMTPVQWRHHSRR 280
Cdd:PRK09393  300 SLRHHFRRRAATSPAAYRKRFGR 322
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
134-281 6.31e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 55.75  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 134 EQESYKTDPLANPMAEILFAQLVMmlkrHRYETDNPSatQQETLLDKLIAT---LAASLNKSFVLEKFCEQEQCSERALR 210
Cdd:PRK10572  144 EQAGQSEGRYSELLAMNLLERLLL----RCMEAIPES--LHPPMDPRVREAcqyISDHLASEFDIESVAQHVCLSPSRLA 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1340240333 211 QQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSRRA 281
Cdd:PRK10572  218 HLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEK 288
PRK10371 PRK10371
transcriptional regulator MelR;
15-279 9.88e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 55.21  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  15 SAEQAVAVADRYPQNVFAEHTHEFYELVLVWRGNGLHILNDRPYRITRG--DLFY-------IRAEDKHAYASVNDLVLQ 85
Cdd:PRK10371   23 SEYQRLEIEFRPPHIMPTSHWHGQVEVNVPFDGDVEYLINNEKVQINQGhiTLFWactphqlTDPGNCRSMAIFNLPMHL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333  86 NVIYCPDRLSLN-VDWAACIPGFNGAKGSPHwrlsssgmtairqAISLLEQESYKTDPlanPMAEILFAQLVMMLKR--- 161
Cdd:PRK10371  103 FLSWPLDKDLINhVTHGMVIKSLATQQLSPF-------------EVRRWQQELNSPNE---QIRQLAIDEIGLMLKRfsl 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 162 ---HRYETDNPSATQQETL-------LDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRIC 231
Cdd:PRK10371  167 sgwEPILVNKTSRTHKNSVsrhaqfyVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRIN 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1340240333 232 HAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHSR 279
Cdd:PRK10371  247 HVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQ 294
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 239-276 9.63e-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: 44.45  E-value: 9.63e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1340240333 239 HTEFMVSDVAMRCGFeDSNYFSVVFNREVGMTPVQWRH 276
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 117-275 3.12e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 44.64  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 117 RLSSSgmTAIRQAISLLEQESYKTDPLANPMAEILFAQLVMMLKR--HRYETDNPSATQQ----ETLLDKLI-------A 183
Cdd:PRK09685  141 RLSAS--LPMVQLSHRLLQQSMNGPALSETESEALLEALIALLRPalHQRESVQPRRERQfqkvVALIDQSIqeeilrpE 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 184 TLAASLNksfvlekfceqeqCSERALRQQFRTQtGMTVNHYLRQLRI--CHAQYLLQHTEFMVSDVAMRCGFEDSNYFSV 261
Cdd:PRK09685  219 WIAGELG-------------ISVRSLYRLFAEQ-GLVVAQYIRNRRLdrCADDLRPAADDEKITSIAYKWGFSDSSHFST 284

                         170
                  ....*....|....
gi 1340240333 262 VFNREVGMTPVQWR 275
Cdd:PRK09685  285 AFKQRFGVSPGEYR 298
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 174-274 9.54e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.13  E-value: 9.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 174 QETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQlRICHAQYLLQHTEFMVSDVAMRCGF 253
Cdd:PRK15186  179 QNTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGY 257

                          90       100
                  ....*....|....*....|.
gi 1340240333 254 EDSNYFSVVFNREVGMTPVQW 274
Cdd:PRK15186  258 DSASYFTCVFKKHFKTTPSEF 278
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 27-81 1.33e-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: 1.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340240333  27 PQNVFAEHTHEF-YELVLVWRGNGLHILND-RPYRITRGDLFYIRAEDKHAYASVND 81
Cdd:cd02208     8 PGTSSPPHWHPEqDEIFYVLSGEGELTLDDgETVELKAGDIVLIPPGVPHSFVNTSD 64
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 32-75 4.97e-04

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 37.99  E-value: 4.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1340240333  32 AEHTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHA 75
Cdd:cd06988    16 TPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHY 59
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 34-76 7.45e-04

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: 37.81  E-value: 7.45e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1340240333  34 HTHEFYELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAY 76
Cdd:cd02222    33 HTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQF 75
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 205-278 1.43e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 39.52  E-value: 1.43e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340240333 205 SERALRQQFRTQtGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRHHS 278
Cdd:PRK09978  171 SPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERS 243
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 27-77 2.59e-03

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: 35.70  E-value: 2.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1340240333  27 PQNVFAEHTHEF-YELVLVWRGNGLHILNDRPYRITRGDLFYIRAEDKHAYA 77
Cdd:pfam07883   7 PGESSPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFR 58
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
168-275 3.31e-03

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 37.00  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 168 NPSATQQETLLDKLIATLAASLNksfvLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYLLQHTEFMVSDV 247
Cdd:PRK11511    5 NTDAITIHSILDWIEDNLESPLS----LEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYL 80

                          90       100
                  ....*....|....*....|....*...
gi 1340240333 248 AMRCGFEDSNYFSVVFNREVGMTPVQWR 275
Cdd:PRK11511   81 AERYGFESQQTLTRTFKNYFDVPPHKYR 108
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
160-276 4.48e-03

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 38.24  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 160 KRHRYETDNPsatqQETLLDKLiaTLAASL---NKSFVLEKFCEQEQCSERALRQQFRTQTGMTVNHYLRQLRICHAQYL 236
Cdd:PRK15435   70 KRCQPDKANP----QQHRLDKI--THACRLleqETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREA 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1340240333 237 LQHTEfMVSDVAMRCGFEDSNYFSVVFNREVGMTPVQWRH 276
Cdd:PRK15435  144 LAKGE-SVTTSILNAGFPDSSSYYRKADETLGMTAKQFRH 182
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 195-271 6.94e-03

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 37.37  E-value: 6.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340240333 195 LEKFCEQEQCSERALRQQFRtQTGMTVNHYLRQLRICHAQYLLQhTEFMVSDVAMRCGFEDSNYFSVVFNREVGMTP 271
Cdd:PRK09940  153 LKDICDCLYISESLLKKKLK-QEQTTFSQILLDARMQHAKNLIR-VEGSVNKIAEQCGYASTSYFIYAFRKHFGNSP 227
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 170-271 8.39e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 37.28  E-value: 8.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340240333 170 SATQQETLLDKLIATLAASLNKSFVLEKFCEQEQCSERALRQQFRTQtGMTVNHYLRQLRICHAQYLLQHTEFMVSDVAM 249
Cdd:PRK15185  200 LSSAQITLKERVYNIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVAL 278

                          90       100
                  ....*....|....*....|..
gi 1340240333 250 RCGFEDSNYFSVVFNREVGMTP 271
Cdd:PRK15185  279 KCGYDSTSYFIQCFKKYFKTTP 300
 
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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