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Conserved domains on  [gi|491051858|ref|WP_004913509|]
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MULTISPECIES: helix-turn-helix domain-containing protein [Morganellaceae]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13501 super family cl32882
HTH-type transcriptional activator RhaR;
8-284 5.90e-84

HTH-type transcriptional activator RhaR;


The actual alignment was detected with superfamily member PRK13501:

Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 253.67  E-value: 5.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   8 LNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVN 87
Cdd:PRK13501   7 LESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVHDLVLDN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  88 ILYKPNEFLIQQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRYQP 167
Cdd:PRK13501  87 IIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKTDSWSIQLTEVLLLQLAIVLKRHRYRA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 168 DQA-PISLLHQMDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISE 246
Cdd:PRK13501 167 EQAhLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISD 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491051858 247 IAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQKNKL 284
Cdd:PRK13501 247 IAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSPVL 284
 
Name Accession Description Interval E-value
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
8-284 5.90e-84

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 253.67  E-value: 5.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   8 LNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVN 87
Cdd:PRK13501   7 LESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVHDLVLDN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  88 ILYKPNEFLIQQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRYQP 167
Cdd:PRK13501  87 IIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKTDSWSIQLTEVLLLQLAIVLKRHRYRA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 168 DQA-PISLLHQMDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISE 246
Cdd:PRK13501 167 EQAhLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISD 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491051858 247 IAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQKNKL 284
Cdd:PRK13501 247 IAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSPVL 284
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 18-164 8.70e-46

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: 151.26  E-value: 8.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  18 ENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVNILYKPNEFLI 97
Cdd:cd06977    1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491051858  98 QQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLR 164
Cdd:cd06977   81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 189-276 1.69e-28

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: 111.02  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 189 INTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMN 268
Cdd:COG4977  223 LEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFG 302


                 ....*...
gi 491051858 269 MTASAYRR 276
Cdd:COG4977  303 VSPSAYRR 310
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
192-275 5.08e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 103.02  E-value: 5.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   192 PFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTA 271
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 491051858   272 SAYR 275
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
204-276 2.31e-25

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 96.12  E-value: 2.31e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491051858  204 LSARSLQRLFKSKTGMTVMEYLQQLRLCQA-TLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTASAYRR 276
Cdd:pfam12833   7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
 
Name Accession Description Interval E-value
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
8-284 5.90e-84

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 253.67  E-value: 5.90e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   8 LNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVN 87
Cdd:PRK13501   7 LESRDYLLSEQMPVAVTNRYPQETFVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYESVHDLVLDN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  88 ILYKPNEFLIQQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRYQP 167
Cdd:PRK13501  87 IIYCPERLHLNAQWHKLLPPLGPEQNQGYWRLTTQGMAQARPIIQQLAQESRKTDSWSIQLTEVLLLQLAIVLKRHRYRA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 168 DQA-PISLLHQMDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISE 246
Cdd:PRK13501 167 EQAhLLPDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISD 246

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491051858 247 IAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQKNKL 284
Cdd:PRK13501 247 IAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSPVL 284
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
6-281 2.26e-69

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 216.07  E-value: 2.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   6 ITLNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKL 85
Cdd:PRK13502   5 LILLKKDFFTDEQQAVTVADRYPQDVFAEHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHSYTSVNDLVL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  86 VNILYKPNEFLIQQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRY 165
Cdd:PRK13502  85 QNIIYCPERLKLNVNWQAMIPGFQGAQWHPHWRLGSMGMNQARQVINQLEHESNGRDPLANEMAELLFGQLVMTLKRHRY 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 166 QPDQAPISLLHQM-DQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSI 244
Cdd:PRK13502 165 ATDDLPATSRETLlDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMI 244

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491051858 245 SEIAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQK 281
Cdd:PRK13502 245 SEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQS 281
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
6-282 6.23e-61

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 195.71  E-value: 6.23e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   6 ITLNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKL 85
Cdd:PRK13500  35 LKLLKDDFFASDQQAVAVADRYPQDVFAEHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  86 VNILYKPNEFLIQQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRY 165
Cdd:PRK13500 115 QNIIYCPERLKLNLDWQGAIPGFSASAGQPHWRLGSVGMAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLNRHRY 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 166 QPDQ-APISLLHQMDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSI 244
Cdd:PRK13500 195 TSDSlPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLI 274

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491051858 245 SEIAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQKN 282
Cdd:PRK13500 275 SDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD 312
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
8-268 1.51e-51

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 170.24  E-value: 1.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   8 LNSSDYFIRTENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVN 87
Cdd:PRK13503   4 LHSVDFFPSGNAPVAIEPRLPQAAFPEHHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHLYEHTDNLCLTN 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  88 ILYK-PNEFLIQQSIEKYVPL---GHQPAisrHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRL 163
Cdd:PRK13503  84 VLYRsPDAFRFLAGLNQLLPQeqdGQYPS---HWRVNQSVLQQVRQLVAQMEQQEESNDLEAIASREILFMQLLVLLRKS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 164 RYQpDQAPISLLhQMDQLINCLNlsintpfslDNFAQE---------HQLSARSLQRLFKSKTGMTVMEYLQQLRLCQAT 234
Cdd:PRK13503 161 SLQ-ENGENSDA-RLNQLLAWLE---------DHFAEEvnwealadqFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKAR 229

                        250       260       270
                 ....*....|....*....|....*....|....
gi 491051858 235 LLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMN 268
Cdd:PRK13503 230 HLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFS 263
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 18-164 8.70e-46

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: 151.26  E-value: 8.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  18 ENTVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVNILYKPNEFLI 97
Cdd:cd06977    1 NQPVAVEPRAPQEPFPEHTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHSYESVDDLCLTNILFRPERLFL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491051858  98 QQSIEKYVPLGHQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLR 164
Cdd:cd06977   81 FLDWLDTLPGYLAHQFQSHWRLNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSRHR 147
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 189-276 1.69e-28

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: 111.02  E-value: 1.69e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 189 INTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMN 268
Cdd:COG4977  223 LEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFG 302


                 ....*...
gi 491051858 269 MTASAYRR 276
Cdd:COG4977  303 VSPSAYRR 310
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
192-275 5.08e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 103.02  E-value: 5.08e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   192 PFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTA 271
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 491051858   272 SAYR 275
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
29-276 6.18e-27

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 105.63  E-value: 6.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  29 QEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVNILYKPNEFLIQQSIEKYVPLG 108
Cdd:COG2207   13 LLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 109 HQPAISRHWKLPPSSLPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRYQPDQAPISLLHQMDQLINCLnls 188
Cdd:COG2207   93 GLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL--- 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 189 intpfSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMN 268
Cdd:COG2207  170 -----TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFG 244


                 ....*...
gi 491051858 269 MTASAYRR 276
Cdd:COG2207  245 VTPSEYRK 252
HTH_18 pfam12833
Helix-turn-helix domain;
204-276 2.31e-25

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 96.12  E-value: 2.31e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491051858  204 LSARSLQRLFKSKTGMTVMEYLQQLRLCQA-TLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTASAYRR 276
Cdd:pfam12833   7 MSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 161-276 2.49e-18

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: 83.56  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 161 YR--LRYQPDQAPISLLHQ--MDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLL 236
Cdd:COG2169   65 FRpcKRCRPDLAPGSPPRAdlVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQL 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 491051858 237 LRsTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTASAYRR 276
Cdd:COG2169  145 LQ-TGLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRR 183
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
171-282 3.49e-17

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 79.63  E-value: 3.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 171 PISLLHQMDQLIN--C--LNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISE 246
Cdd:PRK10572 174 PESLHPPMDPRVReaCqyISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIAT 253

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491051858 247 IAGQCGYEDSNYFSSVFHRKMNMTASAYRRCFLQKN 282
Cdd:PRK10572 254 IGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEKN 289
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
174-275 4.45e-14

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 66.87  E-value: 4.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 174 LLHQ--MDQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQC 251
Cdd:PRK10219   1 MSHQkiIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDL 80

                         90       100
                 ....*....|....*....|....
gi 491051858 252 GYEDSNYFSSVFHRKMNMTASAYR 275
Cdd:PRK10219  81 GYVSQQTFSRVFRRQFDRTPSDYR 104
ftrA PRK09393
transcriptional activator FtrA; Provisional
 192-278 5.02e-13

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 68.07  E-value: 5.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 192 PFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTA 271
Cdd:PRK09393 234 PHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSP 313


                 ....*..
gi 491051858 272 SAYRRCF 278
Cdd:PRK09393 314 AAYRKRF 320
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
178-276 1.00e-10

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 61.18  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 178 MDQ------LINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQC 251
Cdd:PRK15121   1 MDQagiirdLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQY 80

                         90       100
                 ....*....|....*....|....*
gi 491051858 252 GYEDSNYFSSVFHRKMNMTASAYRR 276
Cdd:PRK15121  81 RFDSQQTFTRAFKKQFAQTPALYRR 105
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 179-279 2.85e-10

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 59.66  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 179 DQLINCLNLsinTPfslDNFAQEHQLSARSLQRLFkSKTGMTVMEYLQQLRL--CQATLLLRSTSLSISEIAGQCGYEDS 256
Cdd:PRK09685 207 DQSIQEEIL---RP---EWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLdrCADDLRPAADDEKITSIAYKWGFSDS 279

                         90       100
                 ....*....|....*....|...
gi 491051858 257 NYFSSVFHRKMNMTASAYRRCFL 279
Cdd:PRK09685 280 SHFSTAFKQRFGVSPGEYRRKFR 302
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
35-88 1.50e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 51.39  E-value: 1.50e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491051858  35 HSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLVNI 88
Cdd:COG1917   39 HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLL 92
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 24-157 1.81e-07

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: 49.36  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   24 EKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVNNLKLV-NILYKPNEFLIQQSIE 102
Cdd:pfam02311   8 EARYPGHSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRyRWLYFEPELLERILAD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 491051858  103 KYVPLGHQPAISRHwklppsslPTLTPIIEKIASECQKPDIPSIHLCEGLFLQLA 157
Cdd:pfam02311  88 ISILAGGPLPLLRD--------PELAALLRALFRLLEEAGRSDDLLAEALLYQLL 134
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
164-276 1.13e-06

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 49.02  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 164 RYQPDQAPiSLLHQMDQLIN-CLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRStSL 242
Cdd:PRK15435  71 RCQPDKAN-PQQHRLDKITHaCRLLEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAK-GE 148

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491051858 243 SISEIAGQCGYEDsnyfSSVFHRKMN----MTASAYRR 276
Cdd:PRK15435 149 SVTTSILNAGFPD----SSSYYRKADetlgMTAKQFRH 182
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 239-276 1.63e-06

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: 44.07  E-value: 1.63e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 491051858  239 STSLSISEIAGQCGYeDSNYFSSVFHRKMNMTASAYRR 276
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 55-275 6.44e-06

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 46.46  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  55 NGDDYPITCGDLFYINAEDRHGYHSVNNLKLVNilykpnefliQQSIEKYVPLGHQPAISRHWKLPPSSLPTL-----TP 129
Cdd:PRK09978  23 NGEYRYFNGGDLVFADASQIRVDKCVENFVLVS----------RDTLSLFLPMLKEEALNLHAHKKVSSLLVHhcsrdIP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 130 IIEKIASECQKPDIPSIHLCEGLFLQLAIYIYRLRyqpDQAPISLLHQMDQ------LINCLNLSINTPFSLDNFAQEHQ 203
Cdd:PRK09978  93 VFQEVAQLSQNKNLRYAEMLRKRALIFALLSVFLE---DEHFIPLLLNVLQpnmrtrVCTVINNNIAHEWTLARIASELL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491051858 204 LSARSLQRLFKSKtGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTASAYR 275
Cdd:PRK09978 170 MSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQ 240
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 183-274 9.93e-06

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 46.14  E-value: 9.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 183 NCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKtGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSV 262
Cdd:PRK15185 213 NIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQC 291

                         90
                 ....*....|..
gi 491051858 263 FHRKMNMTASAY 274
Cdd:PRK15185 292 FKKYFKTTPSTF 303
PRK10371 PRK10371
transcriptional regulator MelR;
190-281 1.11e-05

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 45.97  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 190 NTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNM 269
Cdd:PRK10371 205 DQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGM 284

                         90
                 ....*....|..
gi 491051858 270 TASAYRRCFLQK 281
Cdd:PRK10371 285 SPQQYRKLSQQR 296
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
188-275 2.46e-05

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 43.17  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 188 SINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQLRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKM 267
Cdd:PRK11511  21 NLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTFKNYF 100


                 ....*...
gi 491051858 268 NMTASAYR 275
Cdd:PRK11511 101 DVPPHKYR 108
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 179-274 3.65e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 44.29  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858 179 DQLINCLNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQQlRLCQATLLLRSTSLSISEIAGQCGYEDSNY 258
Cdd:PRK15186 184 ENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGYDSASY 262

                         90
                 ....*....|....*.
gi 491051858 259 FSSVFHRKMNMTASAY 274
Cdd:PRK15186 263 FTCVFKKHFKTTPSEF 278
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 34-88 9.06e-05

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: 40.16  E-value: 9.06e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491051858  34 IHSHDF-NEFVIVFSGNGLHHWNGDD-YPITCGDLFYINAEDRHGYHSVNNLKLVNI 88
Cdd:cd02208   14 PHWHPEqDEIFYVLSGEGELTLDDGEtVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
cupin_YbfI-like_N cd07001
AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal ...
 25-75 1.44e-04

AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators, including YbfI, an uncharacterized Bacillus subtilis. In Pseudomonas putida, this protein is thought to regulate the expression of phenylserine aldolase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380405 [Multi-domain]  Cd Length: 76  Bit Score: 39.68  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491051858  25 KRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRH 75
Cdd:cd07001    8 KGIMQKSFPNHFHDFYVIGFIESGQRTLFCEGKEYTVEPGDLLLINPRDVH 58
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 185-226 4.69e-04

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: 37.13  E-value: 4.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 491051858  185 LNLSINTPFSLDNFAQEHQLSARSLQRLFKSKTGMTVMEYLQ 226
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 35-75 6.42e-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: 37.60  E-value: 6.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 491051858  35 HSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRH 75
Cdd:cd06988   18 HSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEH 58
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
35-78 8.65e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 38.46  E-value: 8.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 491051858  35 HSHDFN-EFVIVFSGNG-LHHwNGDDYPITCGDLFYINAEDRHGYH 78
Cdd:COG3837   45 HAHSAEeEFVYVLEGELtLRI-GGEEYVLEPGDSVGFPAGVPHRLR 89
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
 204-276 1.24e-03

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 39.63  E-value: 1.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491051858 204 LSARSLQRLFKSKTGMTVMEYLQQlRLCQATLLLRSTSLSISEIAGQCGYEDSNYFSSVFHRKMNMTASAYRR 276
Cdd:PRK15044 220 MSVSSLKRKLAAEEVSFSKIYLDA-RMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIFKRHFKITPLSFMR 291
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 30-78 1.93e-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: 36.08  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491051858   30 EDFIIHSHDFN-EFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYH 78
Cdd:pfam07883   9 ESSPPHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFR 58
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
2-88 2.52e-03

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 37.04  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858   2 IQKIITLNSSDYFIRTENT----VTVEKRNSQEDFIIHSH-DFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHG 76
Cdd:COG0662    6 IEELKAIGWGSYEVLGEGGerlsVKRITVPPGAELSLHVHpHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHR 85

                         90
                 ....*....|....
gi 491051858  77 YHSV--NNLKLVNI 88
Cdd:COG0662   86 LRNPgdEPLELLEV 99
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 10-92 4.64e-03

AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, N-terminal cupin domain; This family contains bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included is Listeria monocytogenes Lmo2851 protein, whose function is unknown. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380400 [Multi-domain]  Cd Length: 87  Bit Score: 35.63  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491051858  10 SSDYFIRTENtVTVEKRNSQEDFIIHSHDFNEFVIVFSGNGLHHWNGDDYPITCGDLFYINAEDRHGYHSVN-NLKLVNI 88
Cdd:cd06996    5 SNKYFFKNKD-IYIRKHNRFADYPLHTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTHSIKALGeDDILINI 83


                 ....
gi 491051858  89 LYKP 92
Cdd:cd06996   84 IFRN 87
 
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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