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Conserved domains on  [gi|1468633876|ref|WP_117509585|]
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MULTISPECIES: AraC family transcriptional regulator [Lachnospiraceae]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 15196608)

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

CATH:  1.10.10.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0003677
PubMed:  8831795|2644244|10473770|15808743|9409145|33837749|11282467
SCOP:  4000332

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
200-283 3.87e-18

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 77.21  E-value: 3.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  200 PITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTP 279
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1468633876  280 LQLR 283
Cdd:smart00342  81 SEYR 84
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
1-92 1.33e-12

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


:

Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 62.56  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876   1 MPRKDHLPRQTRQEHITLQPNRSIEFRVTDDFGSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHT 80
Cdd:COG1917     1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80

                          90
                  ....*....|..
gi 1468633876  81 ARCPSTGNRSIL 92
Cdd:COG1917    81 FRNLGDEPAVLL 92
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
200-283 3.87e-18

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 77.21  E-value: 3.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  200 PITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTP 279
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1468633876  280 LQLR 283
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
201-290 7.72e-14

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 69.81  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 201 ITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPL 280
Cdd:COG2207   169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                          90
                  ....*....|
gi 1468633876 281 QLRKAAREKG 290
Cdd:COG2207   249 EYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
207-285 1.21e-12

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 62.22  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 207 ADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLI-ATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPLQLRKA 285
Cdd:pfam12833   2 AAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
1-92 1.33e-12

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 62.56  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876   1 MPRKDHLPRQTRQEHITLQPNRSIEFRVTDDFGSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHT 80
Cdd:COG1917     1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80

                          90
                  ....*....|..
gi 1468633876  81 ARCPSTGNRSIL 92
Cdd:COG1917    81 FRNLGDEPAVLL 92
ftrA PRK09393
transcriptional activator FtrA; Provisional
 177-284 2.74e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 59.98  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 177 PMSSRTQTRLDTILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIyRDLIATD-LPVGTL 255
Cdd:PRK09393  211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARA-RDLLESSaLSIDQI 289

                          90       100
                  ....*....|....*....|....*....
gi 1468633876 256 AEKHGFTNDKLFHRLFRERFHTTPLQLRK 284
Cdd:PRK09393  290 AERAGFGSEESLRHHFRRRAATSPAAYRK 318
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 37-136 1.38e-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: 52.44  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  37 PPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGNRSILMQIPDAFLANYLPDPSQLWFSIDY 116
Cdd:pfam02311  17 PPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPELLERILADISILAGGPL 96

                          90       100
                  ....*....|....*....|.
gi 1468633876 117 DST-NPEVQKNISQLRRLLLS 136
Cdd:pfam02311  97 PLLrDPELAALLRALFRLLEE 117
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 33-85 2.21e-07

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: 47.48  E-value: 2.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468633876  33 GSFSPPHWHDAL-EIIYILEGSSIVTLSDRTKTVL-PGQFLLINSGRIHTARCPS 85
Cdd:cd02208     9 GTSSPPHWHPEQdEIFYVLSGEGELTLDDGETVELkAGDIVLIPPGVPHSFVNTS 63
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 33-102 2.27e-03

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: 37.65  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876   33 GSFSPPHWH-DALEIIYILEGSSIVTLSD------RTKTVLPGQFLLINSGRIHT--------------------ARCPS 85
Cdd:smart00835  40 GGMLPPHYHpRATELLYVVRGEGRVGVVDpngnkvYDARLREGDVFVVPQGHPHFqvnsgdenlefvafntndpnRRFFL 119

                           90
                   ....*....|....*..
gi 1468633876   86 TGNRSILMQIPDAFLAN 102
Cdd:smart00835 120 AGRNSVLRGLPPEVLAA 136
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
200-283 3.87e-18

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 77.21  E-value: 3.87e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  200 PITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTP 279
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1468633876  280 LQLR 283
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
201-290 7.72e-14

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 69.81  E-value: 7.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 201 ITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPL 280
Cdd:COG2207   169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                          90
                  ....*....|
gi 1468633876 281 QLRKAAREKG 290
Cdd:COG2207   249 EYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
207-285 1.21e-12

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 62.22  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 207 ADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLI-ATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPLQLRKA 285
Cdd:pfam12833   2 AAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
1-92 1.33e-12

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 62.56  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876   1 MPRKDHLPRQTRQEHITLQPNRSIEFRVTDDFGSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHT 80
Cdd:COG1917     1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80

                          90
                  ....*....|..
gi 1468633876  81 ARCPSTGNRSIL 92
Cdd:COG1917    81 FRNLGDEPAVLL 92
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 172-287 1.86e-12

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: 66.33  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 172 PLAHHPMSSRTQTRLDTILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLP 251
Cdd:COG4977   198 FSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLS 277

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1468633876 252 VGTLAEKHGFTNDKLFHRLFRERFHTTPLQLRKAAR 287
Cdd:COG4977   278 IEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFR 313
ftrA PRK09393
transcriptional activator FtrA; Provisional
 177-284 2.74e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 59.98  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 177 PMSSRTQTRLDTILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIyRDLIATD-LPVGTL 255
Cdd:PRK09393  211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARA-RDLLESSaLSIDQI 289

                          90       100
                  ....*....|....*....|....*....
gi 1468633876 256 AEKHGFTNDKLFHRLFRERFHTTPLQLRK 284
Cdd:PRK09393  290 AERAGFGSEESLRHHFRRRAATSPAAYRK 318
PRK10371 PRK10371
transcriptional regulator MelR;
139-289 3.25e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 56.75  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 139 QLHDEMPDGYLLTFQR-ELFTFLDLLYTKFSEKSPLAhhpMSSRTQTRLDTILTYTQENYQRPITLKEAADVVSLQPEYF 217
Cdd:PRK10371  148 QIRQLAIDEIGLMLKRfSLSGWEPILVNKTSRTHKNS---VSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYA 224

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468633876 218 CRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPLQLRKAAREK 289
Cdd:PRK10371  225 MGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRKLSQQR 296
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 37-136 1.38e-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: 52.44  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  37 PPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGNRSILMQIPDAFLANYLPDPSQLWFSIDY 116
Cdd:pfam02311  17 PPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPELLERILADISILAGGPL 96

                          90       100
                  ....*....|....*....|.
gi 1468633876 117 DST-NPEVQKNISQLRRLLLS 136
Cdd:pfam02311  97 PLLrDPELAALLRALFRLLEE 117
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 33-93 2.41e-08

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: 49.95  E-value: 2.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1468633876  33 GSFSPPHWH-DALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGNRSILM 93
Cdd:pfam07883   8 GESSPPHRHpGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
37-283 4.39e-08

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 53.14  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  37 PPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARcpSTGN---RSILMQIPDAFlaNYLPDPSQLwFS 113
Cdd:PRK13503   29 PEHHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHLYE--HTDNlclTNVLYRSPDAF--RFLAGLNQL-LP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 114 IDYDSTNPE----VQKNISQLRRLLLSMMQLHDEMpDGYLLTFQRELFTFLDLLYTKFSEKSPLAHhpmssrTQTRLDTI 189
Cdd:PRK13503  104 QEQDGQYPShwrvNQSVLQQVRQLVAQMEQQEESN-DLEAIASREILFMQLLVLLRKSSLQENGEN------SDARLNQL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 190 LTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLFHR 269
Cdd:PRK13503  177 LAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFST 256

                         250
                  ....*....|....
gi 1468633876 270 LFRERFHTTPLQLR 283
Cdd:PRK13503  257 LFRREFSWSPRDIR 270
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 33-85 2.21e-07

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: 47.48  E-value: 2.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468633876  33 GSFSPPHWHDAL-EIIYILEGSSIVTLSDRTKTVL-PGQFLLINSGRIHTARCPS 85
Cdd:cd02208     9 GTSSPPHWHPEQdEIFYVLSGEGELTLDDGETVELkAGDIVLIPPGVPHSFVNTS 63
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
15-99 4.43e-07

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 47.83  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  15 HITLQPNRSIefrvtddfgsfsPPHWHDAL-EIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGN-RSIL 92
Cdd:COG0662    31 RITVPPGAEL------------SLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPlELLE 98


                  ....*..
gi 1468633876  93 MQIPDAF 99
Cdd:COG0662    99 VQAPAYL 105
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
186-283 6.06e-07

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 47.79  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 186 LDTILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDK 265
Cdd:PRK11511   11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                          90
                  ....*....|....*...
gi 1468633876 266 LFHRLFRERFHTTPLQLR 283
Cdd:PRK11511   91 TLTRTFKNYFDVPPHKYR 108
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
39-289 3.52e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 47.79  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  39 HWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTarcpstgnrsiLMQIPDAFLANYLPDPSQLWFSIDYDS 118
Cdd:PRK13500   64 HTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHS-----------YASVNDLVLQNIIYCPERLKLNLDWQG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 119 TNPEVQKNISQLRRLLLSMMQLHDEMPDGYL-------LTFQRE----LFTFLDLLYTKFSEKSPlAHHPMSSrtQTRLD 187
Cdd:PRK13500  133 AIPGFSASAGQPHWRLGSVGMAQARQVIGQLehessqhVPFANEmaelLFGQLVMLLNRHRYTSD-SLPPTSS--ETLLD 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 188 TILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKLF 267
Cdd:PRK13500  210 KLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYF 289

                         250       260
                  ....*....|....*....|..
gi 1468633876 268 HRLFRERFHTTPLQLRKAAREK 289
Cdd:PRK13500  290 SVVFTRETGMTPSQWRHLNSQK 311
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 33-92 4.15e-06

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 44.49  E-value: 4.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1468633876  33 GSFSPPHWHDALEIIYILEGSSIVTLSDR-TKTVLPGQFLLINSGRIHTARCPSTGNRSIL 92
Cdd:cd02235    29 GAVAGRHTHPGEESGYVLEGSLELEVDGQpPVTLKAGDSFFIPAGTVHNAKNVGSGPAKLL 89
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 25-79 1.03e-05

Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is a manganese-containing polyketide cyclase present in bacteria that is involved in the biosynthesis of resistomycin, the aromatic pentacyclic metabolite in Streptomyces resistomycificus. Structure of this enzyme shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold that forms a homodimer. It contains an unusual octahedral zinc-binding site in a large hydrophobic pocket that may represent the active site. The zinc ion, coordinated to four histidine side chains and two water molecules, could act as a Lewis acid in the aldol condensation reaction catalyzed by RemF, reminiscent of class II aldolases.


Pssm-ID: 380384 [Multi-domain]  Cd Length: 93  Bit Score: 43.22  E-value: 1.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1468633876  25 EFRVTDDFGSfSPPHWHDALE-IIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIH 79
Cdd:cd06979    21 EFEVSPNAGM-PPPHYHEDWEeTIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVH 75
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
15-86 2.45e-05

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 42.70  E-value: 2.45e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1468633876  15 HITLQPNrsiefrvtddfGSFSPPHWHDAL-EIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPST 86
Cdd:COG3837    32 LITLPPG-----------ASSSPYHAHSAEeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGD 93
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
39-289 6.97e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 43.50  E-value: 6.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  39 HWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTarcpstgnrsiLMQIPDAFLANYLPDPSQLWFSIDYDS 118
Cdd:PRK13502   34 HTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHS-----------YTSVNDLVLQNIIYCPERLKLNVNWQA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 119 TNPEVQK------------NISQLRRLLlsmMQLHDEMPDGYLLTFQRELFTFLDLLYTKFSEKSPLAHHPMSSRtQTRL 186
Cdd:PRK13502  103 MIPGFQGaqwhphwrlgsmGMNQARQVI---NQLEHESNGRDPLANEMAELLFGQLVMTLKRHRYATDDLPATSR-ETLL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 187 DTILTYTQENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRIYRDLIATDLPVGTLAEKHGFTNDKL 266
Cdd:PRK13502  179 DKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNY 258

                         250       260
                  ....*....|....*....|...
gi 1468633876 267 FHRLFRERFHTTPLQLRKAAREK 289
Cdd:PRK13502  259 FSVVFTRETGMTPSQWRHLSNQS 281
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 33-79 9.72e-05

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 40.51  E-value: 9.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1468633876  33 GSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIH 79
Cdd:cd02222    27 GGHTPLHTHPWEHEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH 73
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 33-88 1.81e-04

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1468633876  33 GSFSPPHWH-DALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARcpSTGN 88
Cdd:cd02214    29 GESTLPHRLkGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIE--NTGE 83
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 33-83 2.26e-04

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: 39.76  E-value: 2.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1468633876  33 GSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARC 83
Cdd:cd02238    37 GAVVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEA 87
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
162-291 2.88e-04

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 41.50  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876 162 LLYTKFSEKSPLAHHPMSSRTQTRLDTILTYTQENyqrpITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLNSYRLSRI 241
Cdd:PRK10572  165 LLLRCMEAIPESLHPPMDPRVREACQYISDHLASE----FDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRA 240

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1468633876 242 YRDLIATDLPVGTLAEKHGFTNDKLFHRLFRERFHTTPLQLRKAAREKGS 291
Cdd:PRK10572  241 KLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEKNN 290
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 33-79 3.61e-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: 395138  Cd Length: 151  Bit Score: 40.01  E-value: 3.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468633876  33 GSFSPPHWH-DALEIIYILEGSSIVTL-------SDRTKTVLPGQFLLINSGRIH 79
Cdd:pfam00190  43 GGMNPPHWHpNATEILYVLQGRGRVGFvvpgngnRVFHKVLREGDVFVVPQGLPH 97
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 194-234 5.23e-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: 5.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1468633876 194 QENYQRPITLKEAADVVSLQPEYFCRFFRQNMETTYLEYLN 234
Cdd:pfam00165   2 RENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 33-102 2.27e-03

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: 37.65  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876   33 GSFSPPHWH-DALEIIYILEGSSIVTLSD------RTKTVLPGQFLLINSGRIHT--------------------ARCPS 85
Cdd:smart00835  40 GGMLPPHYHpRATELLYVVRGEGRVGVVDpngnkvYDARLREGDVFVVPQGHPHFqvnsgdenlefvafntndpnRRFFL 119

                           90
                   ....*....|....*..
gi 1468633876   86 TGNRSILMQIPDAFLAN 102
Cdd:smart00835 120 AGRNSVLRGLPPEVLAA 136
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 33-99 3.11e-03

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: 36.75  E-value: 3.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1468633876  33 GSFSPPHWH-DALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGNRSILMQIPDAF 99
Cdd:cd02215    42 GDAIPPHYHkRHHETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYRMLSPDTRFLGVITPGGF 109
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 33-106 4.01e-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: 37.58  E-value: 4.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1468633876  33 GSFSPPHWH-DALEIIYILEGS----SIVTLSDR--TKTVLPGQFLLINSGRIHTARCPSTGNRSIL----------MQI 95
Cdd:cd02241    80 CGVNPPHTHpRATELLYVVEGTlyvgFVDENGNRlfTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVaafnsedpgtQQI 159

                          90
                  ....*....|.
gi 1468633876  96 PDAFLANYLPD 106
Cdd:cd02241   160 AQALFGLPPPD 170
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 38-79 4.21e-03

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 36.80  E-value: 4.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1468633876  38 PHWHD-ALEIIYILEGSSIVTLSDRTK-----TVLPGQFLLINSGRIH 79
Cdd:cd20306    49 PHWHPnANELGYVISGEARVSILDPTGsldtfTVKPGQVVFIPQGWLH 96
cupin_DAD_ChrR cd02237
2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; ...
 33-87 5.03e-03

2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; cupin domain; This family includes the proteins 2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR. DAD catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. The enzyme is a homotetramer containing one iron per molecule of enzyme. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the Rsp extra cytoplasmic function (ECF) sigma factor E (sigmaE). Some ChrR members contain tandem repeats of two distinct homologous functional domains. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380365 [Multi-domain]  Cd Length: 82  Bit Score: 35.45  E-value: 5.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1468633876  33 GSFSPPHWHDALEIIYILEGSsivtLSDRTKTVLPGQFLLINSGRIHTARCPSTG 87
Cdd:cd02237    24 GARLPDHEHVGGEEFYVLDGA----LTDEDGTAGAGDFVREPPGSRHSAVAPREG 74
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 20-93 6.83e-03

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: 35.18  E-value: 6.83e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1468633876  20 PNRSIE-FRVT-DDFGSFSPPHWHDALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHTARCPSTGNRSILM 93
Cdd:cd02209    12 PGRKMEpFLVTlPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVLW 87
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 33-93 7.30e-03

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 35.11  E-value: 7.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1468633876  33 GSFsppHWH---DALEIIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHtarCPSTGNRSILM 93
Cdd:cd02226    33 GEF---VWHkhdDEDELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEH---RPVAEEETVVL 90
cupin_MmsR-like_N cd06986
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This ...
 46-80 8.99e-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: 8.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1468633876  46 IIYILEGSSIVTLSDRTKTVLPGQFLLINSGRIHT 80
Cdd:cd06986    31 LHYVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHS 65
 
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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