NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|496261957|ref|WP_008975342|]
View 

AraC family transcriptional regulator [Faecalimonas umbilicata]

Protein Classification

helix-turn-helix transcriptional regulator( domain architecture ID 11454547)

helix-turn-helix (HTH) transcriptional regulator containing an AraC family DNA-binding HTH domain controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

CATH:  1.10.10.1310
Gene Ontology:  GO:0003700|GO:0043565|GO:0006355
PubMed:  9409145|8831795|15808743|2644244
SCOP:  4000332

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
174-257 8.37e-25

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 94.16  E-value: 8.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957   174 ELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTP 253
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 496261957   254 SEYR 257
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
12-258 1.80e-24

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  12 FSMIRKKPHHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQVFSKGKNEVYQFYASLELSGPFM 91
Cdd:COG2207    6 LLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  92 ALLQKKCPENPVIASADLHREVKNALSCLIKDQKVSEVVGQAYLQIILYRCRETFRFIEKSSVGSNDLIYAAMTYLLSHF 171
Cdd:COG2207   86 LALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 172 QEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGR 251
Cdd:COG2207  166 LLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGV 245


                 ....*..
gi 496261957 252 TPSEYRK 258
Cdd:COG2207  246 TPSEYRK 252
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
174-257 8.37e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 94.16  E-value: 8.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957   174 ELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTP 253
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 496261957   254 SEYR 257
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
12-258 1.80e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  12 FSMIRKKPHHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQVFSKGKNEVYQFYASLELSGPFM 91
Cdd:COG2207    6 LLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  92 ALLQKKCPENPVIASADLHREVKNALSCLIKDQKVSEVVGQAYLQIILYRCRETFRFIEKSSVGSNDLIYAAMTYLLSHF 171
Cdd:COG2207   86 LALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 172 QEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGR 251
Cdd:COG2207  166 LLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGV 245


                 ....*..
gi 496261957 252 TPSEYRK 258
Cdd:COG2207  246 TPSEYRK 252
HTH_18 pfam12833
Helix-turn-helix domain;
180-258 9.32e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 86.10  E-value: 9.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  180 VASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYA-TSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 141-258 7.59e-19

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: 84.72  E-value: 7.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 141 RCR-ETFRfiekSSVGSNDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLL 219
Cdd:COG2169   70 RCRpDLAP----GSPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL 145

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496261957 220 EnTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:COG2169  146 Q-TGLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRR 183
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
157-257 3.43e-18

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 77.66  E-value: 3.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 157 NDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFE 236
Cdd:PRK10219   4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                         90       100
                 ....*....|....*....|.
gi 496261957 237 SQRTFNRVFRQKYGRTPSEYR 257
Cdd:PRK10219  84 SQQTFSRVFRRQFDRTPSDYR 104
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 20-141 1.81e-08

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: 52.05  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957   20 HHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQVfskGKNEVYQFYaSLELSGPFMALLQKkcp 99
Cdd:pfam02311  14 HSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEP---ESEDGWRYR-WLYFEPELLERILA--- 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 496261957  100 ENPVIASADL----HREVKNALSCLIKDQKVSEVVGQAYLQIILYR 141
Cdd:pfam02311  87 DISILAGGPLpllrDPELAALLRALFRLLEEAGRSDDLLAEALLYQ 132
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 22-69 1.26e-06

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 46.38  E-value: 1.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 496261957  22 VPPHLHNAI-ELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQV 69
Cdd:cd02215   45 IPPHYHKRHhETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYRM 93
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
23-258 1.50e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 48.36  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  23 PPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQ-VFSKGKNEVYQFYASLELSGPFMALLQKKCPEN 101
Cdd:PRK13501  32 VEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYEsVHDLVLDNIIYCPERLHLNAQWHKLLPPLGPEQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 102 ----------------PVIASadLHREVKNALSCLIKdqkVSEVVgqaYLQIIL------YRCRETFRFIEKSSVgsnDL 159
Cdd:PRK13501 112 nqgywrlttqgmaqarPIIQQ--LAQESRKTDSWSIQ---LTEVL---LLQLAIvlkrhrYRAEQAHLLPDGEQL---DL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 160 IYAAMT------YLLSHFQEELTLgkvasalgtNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEA 233
Cdd:PRK13501 181 IMSALQqslgayFDMADFCHKNQL---------VERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARC 251

                        250       260
                 ....*....|....*....|....*
gi 496261957 234 GFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:PRK13501 252 GFEDSNYFSAVFTREAGMTPRDYRQ 276
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 22-69 1.33e-04

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 41.11  E-value: 1.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 496261957    22 VPPHLH-NAIELVYVTKGEVELGI----GYELY--HMEKGDfAIVFPDLIHHYQV 69
Cdd:smart00835  43 LPPHYHpRATELLYVVRGEGRVGVvdpnGNKVYdaRLREGD-VFVVPQGHPHFQV 96
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
174-257 8.37e-25

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 94.16  E-value: 8.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957   174 ELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTP 253
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 496261957   254 SEYR 257
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
12-258 1.80e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.80e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  12 FSMIRKKPHHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQVFSKGKNEVYQFYASLELSGPFM 91
Cdd:COG2207    6 LLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  92 ALLQKKCPENPVIASADLHREVKNALSCLIKDQKVSEVVGQAYLQIILYRCRETFRFIEKSSVGSNDLIYAAMTYLLSHF 171
Cdd:COG2207   86 LALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 172 QEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGR 251
Cdd:COG2207  166 LLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGV 245


                 ....*..
gi 496261957 252 TPSEYRK 258
Cdd:COG2207  246 TPSEYRK 252
HTH_18 pfam12833
Helix-turn-helix domain;
180-258 9.32e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 86.10  E-value: 9.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  180 VASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYA-TSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 141-258 7.59e-19

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: 84.72  E-value: 7.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 141 RCR-ETFRfiekSSVGSNDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLL 219
Cdd:COG2169   70 RCRpDLAP----GSPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL 145

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 496261957 220 EnTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:COG2169  146 Q-TGLSVTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRR 183
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
157-257 3.43e-18

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 77.66  E-value: 3.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 157 NDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFE 236
Cdd:PRK10219   4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                         90       100
                 ....*....|....*....|.
gi 496261957 237 SQRTFNRVFRQKYGRTPSEYR 257
Cdd:PRK10219  84 SQQTFSRVFRRQFDRTPSDYR 104
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 157-258 2.12e-16

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: 77.12  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 157 NDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFE 236
Cdd:COG4977  209 DPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFG 288

                         90       100
                 ....*....|....*....|..
gi 496261957 237 SQRTFNRVFRQKYGRTPSEYRK 258
Cdd:COG4977  289 SASHFRRAFRRRFGVSPSAYRR 310
PRK10371 PRK10371
transcriptional regulator MelR;
164-259 1.23e-12

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 66.38  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 164 MTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNR 243
Cdd:PRK10371 197 LGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYS 276

                         90
                 ....*....|....*.
gi 496261957 244 VFRQKYGRTPSEYRKI 259
Cdd:PRK10371 277 TFGKYVGMSPQQYRKL 292
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
164-258 7.11e-11

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 61.18  E-value: 7.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 164 MTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNR 243
Cdd:PRK15121  11 LIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFTR 90

                         90
                 ....*....|....*
gi 496261957 244 VFRQKYGRTPSEYRK 258
Cdd:PRK15121  91 AFKKQFAQTPALYRR 105
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
135-259 1.55e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 54.34  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 135 LQIILYRCRETFRFIEKSSvgSNDLIYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNY 214
Cdd:PRK13500 185 LVMLLNRHRYTSDSLPPTS--SETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCH 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 496261957 215 ATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRKI 259
Cdd:PRK13500 263 AQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHL 307
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 20-141 1.81e-08

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: 52.05  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957   20 HHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQVfskGKNEVYQFYaSLELSGPFMALLQKkcp 99
Cdd:pfam02311  14 HSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEP---ESEDGWRYR-WLYFEPELLERILA--- 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 496261957  100 ENPVIASADL----HREVKNALSCLIKDQKVSEVVGQAYLQIILYR 141
Cdd:pfam02311  87 DISILAGGPLpllrDPELAALLRALFRLLEEAGRSDDLLAEALLYQ 132
ftrA PRK09393
transcriptional activator FtrA; Provisional
 207-258 4.20e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 53.04  E-value: 4.20e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496261957 207 LNEiRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:PRK09393 268 LRE-RLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRK 318
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
8-67 2.23e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 47.92  E-value: 2.23e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496261957   8 KKEKFSMIR---KKPHHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHY 67
Cdd:COG1917   19 GEDELEVVRvtfEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAF 81
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 205-258 2.68e-07

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 50.53  E-value: 2.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 496261957 205 QYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:PRK10296 219 QIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRK 272
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
155-257 6.11e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 49.29  E-value: 6.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 155 GSNDLIYAAMTYLLSHFQEELTLGKVAsalgtNKFALS--------KFFSGifHTNfNQYLNEIRLNYATSLLENTDRRI 226
Cdd:PRK13503 168 NSDARLNQLLAWLEDHFAEEVNWEALA-----DQFSLSlrtlhrqlKQQTG--LTP-QRYLNRLRLLKARHLLRHSDASV 239

                         90       100       110
                 ....*....|....*....|....*....|.
gi 496261957 227 TDIYLEAGFESQRTFNRVFRQKYGRTPSEYR 257
Cdd:PRK13503 240 TDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
204-259 6.68e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 49.28  E-value: 6.68e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496261957 204 NQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRKI 259
Cdd:PRK13502 222 NQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHL 277
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 22-69 1.26e-06

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 46.38  E-value: 1.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 496261957  22 VPPHLHNAI-ELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQV 69
Cdd:cd02215   45 IPPHYHKRHhETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYRM 93
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
23-258 1.50e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 48.36  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957  23 PPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQ-VFSKGKNEVYQFYASLELSGPFMALLQKKCPEN 101
Cdd:PRK13501  32 VEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHSYEsVHDLVLDNIIYCPERLHLNAQWHKLLPPLGPEQ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 102 ----------------PVIASadLHREVKNALSCLIKdqkVSEVVgqaYLQIIL------YRCRETFRFIEKSSVgsnDL 159
Cdd:PRK13501 112 nqgywrlttqgmaqarPIIQQ--LAQESRKTDSWSIQ---LTEVL---LLQLAIvlkrhrYRAEQAHLLPDGEQL---DL 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 160 IYAAMT------YLLSHFQEELTLgkvasalgtNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEA 233
Cdd:PRK13501 181 IMSALQqslgayFDMADFCHKNQL---------VERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARC 251

                        250       260
                 ....*....|....*....|....*
gi 496261957 234 GFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:PRK13501 252 GFEDSNYFSAVFTREAGMTPRDYRQ 276
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 222-258 1.55e-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: 1.55e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 496261957  222 TDRRITDIYLEAGFeSQRTFNRVFRQKYGRTPSEYRK 258
Cdd:pfam00165   7 TNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
23-67 1.90e-06

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 45.78  E-value: 1.90e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496261957  23 PPHLHNAI-ELVYVTKGEVELGIGYELYHMEKGDFaIVFP-DLIHHY 67
Cdd:COG3837   43 PYHAHSAEeEFVYVLEGELTLRIGGEEYVLEPGDS-VGFPaGVPHRL 88
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
160-257 2.29e-06

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 45.86  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 160 IYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQR 239
Cdd:PRK11511  11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                         90
                 ....*....|....*...
gi 496261957 240 TFNRVFRQKYGRTPSEYR 257
Cdd:PRK11511  91 TLTRTFKNYFDVPPHKYR 108
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
160-258 3.42e-06

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 47.28  E-value: 3.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 160 IYAAMTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIFHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQR 239
Cdd:PRK10572 185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264

                         90
                 ....*....|....*....
gi 496261957 240 TFNRVFRQKYGRTPSEYRK 258
Cdd:PRK10572 265 YFSRVFKKCTGASPSEFRA 283
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 23-67 4.90e-06

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: 43.40  E-value: 4.90e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 496261957   23 PPHLH-NAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHY 67
Cdd:pfam07883  12 PPHRHpGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRF 57
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 146-256 5.44e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.52  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 146 FRFIEKSSVGSNdlIYaamTYLLSHFQEELTLGKVASALGTNKFALSKFFSGIfHTNFNQ-YLNEiRLNYATSLLENTDR 224
Cdd:PRK15186 174 FRELSQNTLAEN--IY---NIIISDISRKWALKDISDSLYMSCSTLKRKLKQE-NTSFSEvYLNA-RMNKATKLLRNSEY 246

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496261957 225 RITDIYLEAGFESQRTFNRVFRQKYGRTPSEY 256
Cdd:PRK15186 247 NITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 120-258 5.46e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 43.48  E-value: 5.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 120 LIKDQKVSEVVGQAYLQIILYRCRETFRFIEKSSVGSNDLIYAAMTYLLSHFQEE-LTLGKVASALGTNKFALSKFFS-- 196
Cdd:PRK09685 159 SMNGPALSETESEALLEALIALLRPALHQRESVQPRRERQFQKVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLFAeq 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496261957 197 GIfhtNFNQYLNEIRLNYATSLLEN--TDRRITDIYLEAGFESQRTFNRVFRQKYGRTPSEYRK 258
Cdd:PRK09685 239 GL---VVAQYIRNRRLDRCADDLRPaaDDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRR 299
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 22-82 8.16e-05

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 41.94  E-value: 8.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496261957   22 VPPHLH-NAIELVYVTKGEVELGI-----GYELYH--MEKGDfAIVFPDLIHHYQvFSKGKNEVYQFYA 82
Cdd:pfam00190  46 NPPHWHpNATEILYVLQGRGRVGFvvpgnGNRVFHkvLREGD-VFVVPQGLPHFQ-YNIGDEPAVAFVA 112
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 27-67 8.71e-05

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 40.18  E-value: 8.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 496261957  27 HNAIELVYVTKGEVELGIGYELYHMEKGDfAIVFP-DLIHHY 67
Cdd:cd02209   35 HEGEEFGYVLEGELELTVGGETYVLEAGD-SIYFDsDVPHRY 75
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 169-257 9.83e-05

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 42.61  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496261957 169 SHFQEELTLGKVASALGTNKFALSKFFSGIfHTNFNQYLNEIRLNYATSLLENTDRRITDIYLEAGFESQRTFNRVFRQK 248
Cdd:PRK09978 153 NNIAHEWTLARIASELLMSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNY 231


                 ....*....
gi 496261957 249 YGRTPSEYR 257
Cdd:PRK09978 232 YGMTPTEYQ 240
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 22-69 1.33e-04

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 41.11  E-value: 1.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 496261957    22 VPPHLH-NAIELVYVTKGEVELGI----GYELY--HMEKGDfAIVFPDLIHHYQV 69
Cdd:smart00835  43 LPPHYHpRATELLYVVRGEGRVGVvdpnGNKVYdaRLREGD-VFVVPQGHPHFQV 96
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 12-81 4.22e-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: 37.85  E-value: 4.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496261957  12 FSMIRKKPHH-VPPHLH-NAIELVYVTKGEVELGIG-YELYHMEKGDFAIVFPDLIHHYQVFSKGKNEVYQFY 81
Cdd:cd02208    1 ISVVTLPPGTsSPPHWHpEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 22-84 1.36e-03

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 38.73  E-value: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496261957  22 VPPHLHN-AIELVYVTKGEVELGI----GYELYH--MEKGDfAIVFPD-LIhHYQvFSKGKNEVyQFYASL 84
Cdd:cd02241   83 NPPHTHPrATELLYVVEGTLYVGFvdenGNRLFTktLNPGD-VFVFPQgLI-HFQ-FNPGCEPA-VFVAAF 149
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 21-67 2.05e-03

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: 36.66  E-value: 2.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 496261957  21 HVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHY 67
Cdd:cd02222   29 HTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQF 75
cupin_MmsR-like_N cd06986
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This ...
 16-68 6.64e-03

AraC/XylS family transcriptional regulators similar to MmsR, 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 MmsR, a bacterial transcriptional regulator thought to positively regulate the expression of the mmsAB operon. The mmsAB operon contains two structural genes involved in valine metabolism: mmsA which encodes methylmalonate-semialdehyde dehydrogenase, and mmsB which encodes 3-hydroxyisobutyrate dehydrogenase. The cupin domain of members of this subfamily does not contain a metal binding site.


Pssm-ID: 380391 [Multi-domain]  Cd Length: 84  Bit Score: 34.77  E-value: 6.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496261957  16 RKKPHHVpphLHnaielvYVTKGEVELGIGYELYHMEKGDFAIVFPDLIHHYQ 68
Cdd:cd06986   24 AVRDYYI---LH------YVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYG 67
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 17-65 8.86e-03

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 35.14  E-value: 8.86e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 496261957  17 KKPHHVPPHLHNAIELVYVTKGEVELGIGYELYHMEKGDFAIVFPDLIH 65
Cdd:cd02238   35 EKGAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPH 83
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH