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Conserved domains on  [gi|488141035|ref|WP_002212243|]
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MULTISPECIES: transcriptional regulator ChbR [Yersinia pseudotuberculosis complex]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 11484648)

AraC family transcriptional regulator controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 1-271 0e+00

DNA-binding transcriptional regulator ChbR; Provisional


:

Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 499.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   1 MDVRLVRERDFFNGKEFHLFIYNKTESATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQSFYEFGA 80
Cdd:PRK10296   8 MEIATVREQQLFNGKNFHVFIYNKTESVSGLHQHDYYEFTLVLTGRYYQEINGKRVLLERGDFVFIPLGSHHQSFYEFGA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  81 TRILNVGISKAFFEEHYFHLLSRPIVASQAYRLRGDFLSYIESAISAPHYRENEQTELLELLTFYVTNRISHYKESEVND 160
Cdd:PRK10296  88 TRILNVGISKRFFEQHYLPLLPYCFVASQVYRTNNAFLTYIETVISSLNFRETGLDEFVELVTFYVINRLRHYREEQVID 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 161 DIPSWLKATIDKMHDNAMFSEKALVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEA 240
Cdd:PRK10296 168 DIPQWLKATVEKMHDKEQFSESALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEA 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488141035 241 GYSDTTLFIKNFKKLTSFTPGNYRKNFYSAR 271
Cdd:PRK10296 248 GYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN 278
 
Name Accession Description Interval E-value
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 1-271 0e+00

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 499.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   1 MDVRLVRERDFFNGKEFHLFIYNKTESATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQSFYEFGA 80
Cdd:PRK10296   8 MEIATVREQQLFNGKNFHVFIYNKTESVSGLHQHDYYEFTLVLTGRYYQEINGKRVLLERGDFVFIPLGSHHQSFYEFGA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  81 TRILNVGISKAFFEEHYFHLLSRPIVASQAYRLRGDFLSYIESAISAPHYRENEQTELLELLTFYVTNRISHYKESEVND 160
Cdd:PRK10296  88 TRILNVGISKRFFEQHYLPLLPYCFVASQVYRTNNAFLTYIETVISSLNFRETGLDEFVELVTFYVINRLRHYREEQVID 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 161 DIPSWLKATIDKMHDNAMFSEKALVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEA 240
Cdd:PRK10296 168 DIPQWLKATVEKMHDKEQFSESALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEA 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488141035 241 GYSDTTLFIKNFKKLTSFTPGNYRKNFYSAR 271
Cdd:PRK10296 248 GYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN 278
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
184-264 1.75e-17

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 75.28  E-value: 1.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   184 LVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNY 263
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 488141035   264 R 264
Cdd:smart00342  84 R 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
28-271 1.02e-14

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 72.12  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  28 ATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQSFYEFGATRILNVGISKAFFEEHYFHLLSRPIVA 107
Cdd:COG2207   15 ALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 108 SQAYRLRGDFLSYIESAISAPHYRENEQTELLELLTFYVTNRISHYKESEVNDDIPSWLKATIDKMHDNAMFSEKALVNM 187
Cdd:COG2207   95 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEEL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 188 VELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRKNF 267
Cdd:COG2207  175 ARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254


                 ....
gi 488141035 268 YSAR 271
Cdd:COG2207  255 RARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
197-266 3.77e-14

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 66.07  E-value: 3.77e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141035  197 YLTRATRRYYQKTPMQIINEIRINFAKTQL-EVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRKN 266
Cdd:pfam12833  11 TLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 11-73 3.65e-06

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: 44.10  E-value: 3.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488141035  11 FFNGKEFHLFIYNKTeSATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQ 73
Cdd:cd06996    9 FFKNKDIYIRKHNRF-ADYPLHTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTHS 70
 
Name Accession Description Interval E-value
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 1-271 0e+00

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 499.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   1 MDVRLVRERDFFNGKEFHLFIYNKTESATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQSFYEFGA 80
Cdd:PRK10296   8 MEIATVREQQLFNGKNFHVFIYNKTESVSGLHQHDYYEFTLVLTGRYYQEINGKRVLLERGDFVFIPLGSHHQSFYEFGA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  81 TRILNVGISKAFFEEHYFHLLSRPIVASQAYRLRGDFLSYIESAISAPHYRENEQTELLELLTFYVTNRISHYKESEVND 160
Cdd:PRK10296  88 TRILNVGISKRFFEQHYLPLLPYCFVASQVYRTNNAFLTYIETVISSLNFRETGLDEFVELVTFYVINRLRHYREEQVID 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 161 DIPSWLKATIDKMHDNAMFSEKALVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEA 240
Cdd:PRK10296 168 DIPQWLKATVEKMHDKEQFSESALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEA 247

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488141035 241 GYSDTTLFIKNFKKLTSFTPGNYRKNFYSAR 271
Cdd:PRK10296 248 GYSSPSLFIKTFKKLTSFTPGSYRKKLTEFN 278
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
184-264 1.75e-17

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 75.28  E-value: 1.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   184 LVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNY 263
Cdd:smart00342   4 LEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEY 83


                   .
gi 488141035   264 R 264
Cdd:smart00342  84 R 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
28-271 1.02e-14

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 72.12  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  28 ATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQSFYEFGATRILNVGISKAFFEEHYFHLLSRPIVA 107
Cdd:COG2207   15 ALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 108 SQAYRLRGDFLSYIESAISAPHYRENEQTELLELLTFYVTNRISHYKESEVNDDIPSWLKATIDKMHDNAMFSEKALVNM 187
Cdd:COG2207   95 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEEL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 188 VELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRKNF 267
Cdd:COG2207  175 ARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254


                 ....
gi 488141035 268 YSAR 271
Cdd:COG2207  255 RARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
197-266 3.77e-14

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 66.07  E-value: 3.77e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141035  197 YLTRATRRYYQKTPMQIINEIRINFAKTQL-EVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRKN 266
Cdd:pfam12833  11 TLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 166-271 1.58e-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: 1.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 166 LKATIDKMHDNamFSEK----ALVNMVELSGKTqeyLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAG 241
Cdd:COG4977  212 LARAQAWMEAN--LEEPlsvdELARRAGMSPRT---LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACG 286

                         90       100       110
                 ....*....|....*....|....*....|
gi 488141035 242 YSDTTLFIKNFKKLTSFTPGNYRKNFYSAR 271
Cdd:COG4977  287 FGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 180-265 1.43e-09

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: 57.76  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 180 SEKALVNMVELSgktQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEvTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFT 259
Cdd:COG2169  102 SLEDLAARLGLS---PRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAGFGSLSRFYEAFKKLLGMT 177


                 ....*.
gi 488141035 260 PGNYRK 265
Cdd:COG2169  178 PSAYRR 183
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
1-267 2.98e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 50.67  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035   1 MDVRLVReRDFFNGKEFHLFIYNKTESAT-GLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHH--QSFYE 77
Cdd:PRK13501   3 APLLLES-RDYLLSEQMPVAVTNRYPQETfVEHTHQFCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHsyESVHD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  78 FGATRI--------LNVGISK---AFFEEH---YFHL------LSRPIVaSQAYRlrgdflsyiESAISAPHYRENEQTE 137
Cdd:PRK13501  82 LVLDNIiycperlhLNAQWHKllpPLGPEQnqgYWRLttqgmaQARPII-QQLAQ---------ESRKTDSWSIQLTEVL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 138 LLEL-LTF----YVTNRISHYKESEVNDDIPSWLKATIDKMHDNAMFSEKAlvnmvELSGKTQEYLTRatrryyQKTPMQ 212
Cdd:PRK13501 152 LLQLaIVLkrhrYRAEQAHLLPDGEQLDLIMSALQQSLGAYFDMADFCHKN-----QLVERSLKQLFR------QQTGMS 220

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488141035 213 I---INEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRKNF 267
Cdd:PRK13501 221 IshyLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRF 278
PRK10371 PRK10371
transcriptional regulator MelR;
203-265 3.57e-07

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 50.59  E-value: 3.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488141035 203 RRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRK 265
Cdd:PRK10371 229 QRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
27-72 1.26e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.00  E-value: 1.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 488141035  27 SATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHH 72
Cdd:COG1917   34 ARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPH 79
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 11-73 3.65e-06

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: 44.10  E-value: 3.65e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488141035  11 FFNGKEFHLFIYNKTeSATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQ 73
Cdd:cd06996    9 FFKNKDIYIRKHNRF-ADYPLHTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTHS 70
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
27-87 4.48e-05

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 42.05  E-value: 4.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488141035  27 SATGLHQHDY-YEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHqsfyefgatRILNVG 87
Cdd:COG0662   38 AELSLHVHPHrDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPH---------RLRNPG 90
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
32-264 1.31e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 42.78  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  32 HQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHqSFYEFGATRILNV------------------GISKAFF 93
Cdd:PRK13500  64 HTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKH-SYASVNDLVLQNIiycperlklnldwqgaipGFSASAG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035  94 EEHYfHLLSrpIVASQAYRLRGDFLSyiESAISAPHyrENEQTELLELLTFYVTNRISHYKESEVNDDIPSWLKATIDKM 173
Cdd:PRK13500 143 QPHW-RLGS--VGMAQARQVIGQLEH--ESSQHVPF--ANEMAELLFGQLVMLLNRHRYTSDSLPPTSSETLLDKLITRL 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141035 174 HdNAMFSEKALVNMVELSGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFK 253
Cdd:PRK13500 216 A-ASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFT 294

                        250
                 ....*....|.
gi 488141035 254 KLTSFTPGNYR 264
Cdd:PRK13500 295 RETGMTPSQWR 305
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
191-264 3.12e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 39.52  E-value: 3.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488141035 191 SGKTQEYLTRATRRYYQKTPMQIINEIRINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYR 264
Cdd:PRK10219  31 SGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFRRQFDRTPSDYR 104
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 32-72 3.22e-04

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: 38.98  E-value: 3.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 488141035  32 HQHDYYEYTL-ILTGMCYQEINGKRVFLERGDFIFIPLGSHH 72
Cdd:cd06979   34 HYHEDWEETIyGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVH 75
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 27-73 5.14e-04

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


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 37.99  E-value: 5.14e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488141035  27 SATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQ 73
Cdd:cd06988   13 TTSTPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHY 59
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
218-265 1.23e-03

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 39.57  E-value: 1.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488141035 218 RINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRK 265
Cdd:PRK10572 236 RISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 218-265 4.88e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 37.67  E-value: 4.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 488141035 218 RINFAKTQLEVTNYLVSDIAFEAGYSDTTLFIKNFKKLTSFTPGNYRK 265
Cdd:PRK15185 258 RMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTFIK 305
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 32-72 5.67e-03

ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as E-2 and E-2') from Klebsiella pneumoniae share the same amino acid sequence, but bind different metal ions: ARD binds Ni2+, ARD' binds Fe2+. ARD and ARD' can be experimentally interconverted by removal of the bound metal ion and reconstitution with the appropriate metal ion. The two enzymes share the same substrate, 1,2-dihydroxy-3-keto-5-(methylthio)pentene, but yield different products. ARD' yields the alpha-keto precursor of methionine (and formate), thus forming part of the ubiquitous methionine salvage pathway that converts 5'-methylthioadenosine (MTA) to methionine. This pathway is responsible for the tight control of the concentration of MTA, which is a powerful inhibitor of polyamine biosynthesis and transmethylation reactions. ARD yields methylthiopropanoate, carbon monoxide and formate, and thus prevents the conversion of MTA to methionine. The role of the ARD catalyzed reaction is unclear: methylthiopropanoate is cytotoxic, and carbon monoxide can activate guanylyl cyclase, leading to increased intracellular cGMP levels. This family also contains other members, whose functions are not well characterized.


Pssm-ID: 281122  Cd Length: 157  Bit Score: 36.56  E-value: 5.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488141035   32 HQHDYYEYTLILTGMCYQEINGK-----RVFLERGDFIFIPLGSHH 72
Cdd:pfam03079  88 HLHTDEEIRYIVEGTGYFDVRDKddvwiRVFVEKGDLISLPAGIYH 133
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 29-73 6.44e-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: 34.54  E-value: 6.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488141035   29 TGLHQHDY-YEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHQ 73
Cdd:pfam07883  11 SPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHR 56
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 25-72 6.51e-03

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: 36.26  E-value: 6.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 488141035   25 TESATGLHQHDYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHH 72
Cdd:pfam02311  12 PGHSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPH 59
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 32-99 8.43e-03

monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small monomeric dehydratase Pac13 that mediates the formation of the 3'-deoxynucleotide of pacidamycins, which are uradyl peptide antibiotics (UPAs). Pac13 is involved in the formation of the unique 3'-deoxyuridine moiety found in these UPAs; it catalyzes the dehydration of uridine-5'-aldehyde. The similarity of the 3'-deoxy pacidamycin moiety with synthetic anti-retrovirals, offers a potential opportunity for the utilization of Pac13 in the biocatalytic generation of antiviral compounds. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380429 [Multi-domain]  Cd Length: 101  Bit Score: 34.89  E-value: 8.43e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488141035  32 HQH-DYYEYTLILTGMCYQEINGKRVFLERGDFIFIPLGSHHqsfYEFGATRILNVGISKafFEEHYFH 99
Cdd:cd20295   36 HYHkKSTEIYYVLEGEGIFELDGEAVPVKPGDLVLIPPGTRH---RAVGKMKILLIVIPA--FDPEDEW 99
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 29-73 9.24e-03

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: 34.38  E-value: 9.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 488141035  29 TGLHQHD-YYEYTLILTGMCYQEIN-GKRVFLERGDFIFIPLGSHHQ 73
Cdd:cd02208   12 SPPHWHPeQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHS 58
 
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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