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Conserved domains on  [gi|1213887340|gb|ASH10212|]
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AraC family transcriptional regulator [Listeria monocytogenes serotype 1/2a str. 08-6056]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 12033754)

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

CATH:  2.60.120.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0043565
PubMed:  11282467|33837749|9409145|12270809|19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
136-276 1.32e-27

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 136 LILKAFVMQLIIHVLREATPEQLENNGVKLSTDEQQKQILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEET 215
Cdd:COG2207   114 LLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEET 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213887340 216 GESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWRKS 276
Cdd:COG2207   194 GTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE-YRKR 253
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 10-146 2.59e-23

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: 92.11  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  10 NPQILYIANCYTNEVRvgENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHYDITEPGMTNAQLHIGFRN 89
Cdd:pfam02311   1 NPGLEGIEARYPGHSF--PPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1213887340  90 FALEGYTRNTFPFKKAFLRKKEEEsAILSISKQIIEEKDAGKPGYDLILKAFVMQLI 146
Cdd:pfam02311  79 ELLERILADISILAGGPLPLLRDP-ELAALLRALFRLLEEAGRSDDLLAEALLYQLL 134
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
136-276 1.32e-27

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 136 LILKAFVMQLIIHVLREATPEQLENNGVKLSTDEQQKQILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEET 215
Cdd:COG2207   114 LLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEET 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213887340 216 GESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWRKS 276
Cdd:COG2207   194 GTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE-YRKR 253
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
190-271 1.52e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 99.16  E-value: 1.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  190 DVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPP 269
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ..
gi 1213887340  270 SE 271
Cdd:smart00342  81 SE 82
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 10-146 2.59e-23

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: 92.11  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  10 NPQILYIANCYTNEVRvgENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHYDITEPGMTNAQLHIGFRN 89
Cdd:pfam02311   1 NPGLEGIEARYPGHSF--PPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1213887340  90 FALEGYTRNTFPFKKAFLRKKEEEsAILSISKQIIEEKDAGKPGYDLILKAFVMQLI 146
Cdd:pfam02311  79 ELLERILADISILAGGPLPLLRDP-ELAALLRALFRLLEEAGRSDDLLAEALLYQLL 134
HTH_18 pfam12833
Helix-turn-helix domain;
196-276 1.85e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.02  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 196 LSQTMYISPAYISKVFKEETGESPINYLIKIRLTRA-EELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWR 274
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSE-YR 79


                  ..
gi 1213887340 275 KS 276
Cdd:pfam12833  80 RR 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
58-277 4.10e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 73.47  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  58 KGDMLIFNPGVSHY------------------------------DITEpgmtnaqlHIGFRNFALEGYTRNtfpFKKAFl 107
Cdd:PRK10572   73 PGDLLLFPPGEIHHygrhpdsdewyhqwvyfrpraywadwlnwpSIFA--------GVGRLRIPDEALQPE---FSDLF- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 108 rkkeeesailsisKQIIEEKDAGKPgydlilkaFVMQLIIHVLreatpEQLENNGVKLSTDEQQKQI--LVNEIIHYMEK 185
Cdd:PRK10572  141 -------------GQIEQAGQSEGR--------YSELLAMNLL-----ERLLLRCMEAIPESLHPPMdpRVREACQYISD 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 186 HHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYY 265
Cdd:PRK10572  195 HLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCT 274

                         250
                  ....*....|..
gi 1213887340 266 GFPPSEnWRKSS 277
Cdd:PRK10572  275 GASPSE-FRARC 285
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
30-71 2.25e-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: 2.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHY 71
Cdd:COG1917    39 HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 30-70 2.42e-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: 44.87  E-value: 2.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:cd06996    29 HTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTH 69
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
136-276 1.32e-27

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 136 LILKAFVMQLIIHVLREATPEQLENNGVKLSTDEQQKQILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEET 215
Cdd:COG2207   114 LLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEET 193

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213887340 216 GESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWRKS 276
Cdd:COG2207   194 GTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE-YRKR 253
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
190-271 1.52e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 99.16  E-value: 1.52e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  190 DVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPP 269
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ..
gi 1213887340  270 SE 271
Cdd:smart00342  81 SE 82
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 10-146 2.59e-23

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: 92.11  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  10 NPQILYIANCYTNEVRvgENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHYDITEPGMTNAQLHIGFRN 89
Cdd:pfam02311   1 NPGLEGIEARYPGHSF--PPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEP 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1213887340  90 FALEGYTRNTFPFKKAFLRKKEEEsAILSISKQIIEEKDAGKPGYDLILKAFVMQLI 146
Cdd:pfam02311  79 ELLERILADISILAGGPLPLLRDP-ELAALLRALFRLLEEAGRSDDLLAEALLYQLL 134
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 175-275 1.10e-21

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: 92.14  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 175 LVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDA 254
Cdd:COG4977   211 RLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSA 290

                          90       100
                  ....*....|....*....|.
gi 1213887340 255 YYFSKLFKKYYGFPPSEnWRK 275
Cdd:COG4977   291 SHFRRAFRRRFGVSPSA-YRR 310
HTH_18 pfam12833
Helix-turn-helix domain;
196-276 1.85e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 83.02  E-value: 1.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 196 LSQTMYISPAYISKVFKEETGESPINYLIKIRLTRA-EELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWR 274
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSE-YR 79


                  ..
gi 1213887340 275 KS 276
Cdd:pfam12833  80 RR 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 169-275 1.92e-16

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: 78.17  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 169 EQQKQILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKnKDVSVKQAANM 248
Cdd:COG2169    79 SPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYA 157

                          90       100
                  ....*....|....*....|....*..
gi 1213887340 249 VGYNDAYYFSKLFKKYYGFPPSEnWRK 275
Cdd:COG2169   158 AGFGSLSRFYEAFKKLLGMTPSA-YRR 183
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
58-277 4.10e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 73.47  E-value: 4.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  58 KGDMLIFNPGVSHY------------------------------DITEpgmtnaqlHIGFRNFALEGYTRNtfpFKKAFl 107
Cdd:PRK10572   73 PGDLLLFPPGEIHHygrhpdsdewyhqwvyfrpraywadwlnwpSIFA--------GVGRLRIPDEALQPE---FSDLF- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 108 rkkeeesailsisKQIIEEKDAGKPgydlilkaFVMQLIIHVLreatpEQLENNGVKLSTDEQQKQI--LVNEIIHYMEK 185
Cdd:PRK10572  141 -------------GQIEQAGQSEGR--------YSELLAMNLL-----ERLLLRCMEAIPESLHPPMdpRVREACQYISD 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 186 HHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYY 265
Cdd:PRK10572  195 HLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCT 274

                         250
                  ....*....|..
gi 1213887340 266 GFPPSEnWRKSS 277
Cdd:PRK10572  275 GASPSE-FRARC 285
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
30-271 3.21e-14

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 70.86  E-value: 3.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH-YDITEP-GMTNAqLHIGFRNFA-LEGYtrntfpfkKAF 106
Cdd:PRK13503   31 HHHDFHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHlYEHTDNlCLTNV-LYRSPDAFRfLAGL--------NQL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 107 LRKKEE---------ESAILSISKQIIEEKDAGKPGYDLILKA----FVMQLIIHVLREATPEQLENNgvklstDEQqkq 173
Cdd:PRK13503  102 LPQEQDgqypshwrvNQSVLQQVRQLVAQMEQQEESNDLEAIAsreiLFMQLLVLLRKSSLQENGENS------DAR--- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 174 ilVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYND 253
Cdd:PRK13503  173 --LNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGD 250

                         250
                  ....*....|....*...
gi 1213887340 254 AYYFSKLFKKYYGFPPSE 271
Cdd:PRK13503  251 SNHFSTLFRREFSWSPRD 268
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 190-277 1.37e-08

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 54.55  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 190 DVSLSTLSQTMYISPAYISKVFKEEtGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPP 269
Cdd:PRK09978  158 EWTLARIASELLMSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTP 236


                  ....*...
gi 1213887340 270 SENWRKSS 277
Cdd:PRK09978  237 TEYQERSA 244
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 192-271 2.23e-07

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 50.83  E-value: 2.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 192 SLSTLSQTMYISPAYISKVFKEETGESPINYLiKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSE 271
Cdd:PRK15186  199 ALKDISDSLYMSCSTLKRKLKQENTSFSEVYL-NARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSE 277
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
30-71 2.25e-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: 2.25e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHY 71
Cdd:COG1917    39 HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHA 80
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
1-277 9.33e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 48.90  E-value: 9.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340   1 MLKINTTTFNPQILYIANCYTNEVRVgeNHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH---------- 70
Cdd:PRK13502    7 LLKKDFFTDEQQAVTVADRYPQDVFA--EHTHEFCELVMVWRGNGLHVLNERPYRITRGDLFYIRAEDKHsytsvndlvl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  71 ---------------YDITEPGMTNAQLHIGFRNFALEgytrntfpfkkaflrkkeeesaiLSISKQIIEEKDAGKPGYD 135
Cdd:PRK13502   85 qniiycperlklnvnWQAMIPGFQGAQWHPHWRLGSMG-----------------------MNQARQVINQLEHESNGRD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 136 --------LILKAFVMQLIIHvlREATpeqlenNGVKLSTDEQqkqiLVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYI 207
Cdd:PRK13502  142 planemaeLLFGQLVMTLKRH--RYAT------DDLPATSRET----LLDKLITALANSLECPFALDAFCQQEQCSERVL 209

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 208 SKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWRKSS 277
Cdd:PRK13502  210 RQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQ-WRHLS 278
ftrA PRK09393
transcriptional activator FtrA; Provisional
 179-276 1.52e-06

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 48.42  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 179 IIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFS 258
Cdd:PRK09393  223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLR 302

                          90
                  ....*....|....*...
gi 1213887340 259 KLFKKYYGFPPSEnWRKS 276
Cdd:PRK09393  303 HHFRRRAATSPAA-YRKR 319
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
174-269 2.23e-06

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 45.86  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 174 ILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYND 253
Cdd:PRK11511    9 ITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFES 88

                          90
                  ....*....|....*.
gi 1213887340 254 AYYFSKLFKKYYGFPP 269
Cdd:PRK11511   89 QQTLTRTFKNYFDVPP 104
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 30-70 2.42e-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: 44.87  E-value: 2.42e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:cd06996    29 HTHNFLEINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTH 69
cupin_RhaR_RhaS-like_N cd06977
HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; ...
 30-151 2.73e-06

HTH-type transcriptional activator RhaR and RhaS and related proteins, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, including the HTH-type transcription activators RhaS and RhaR. RhaS and RhaR respond to the availability of L-rhamnose and activate transcription of the operons in the Escherichia coli L-rhamnose catabolic regulon. The E. coli RhaR protein activates expression of the rhaSR operon in the presence of its effector, L-rhamnose. The resulting RhaS protein (plus L-rhamnose) activates expression of the L-rhamnose catabolic operon rhaBAD as well as the transport operon rhaT. These proteins bind DNA as dimers, via their HTH motifs. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380382 [Multi-domain]  Cd Length: 147  Bit Score: 46.10  E-value: 2.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  30 HHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH-YDITEP-GMTNaqlhIGFRN----------FALEGYTR 97
Cdd:cd06977    18 HTHDFHEIVIVTKGSGIHVLNGHPYRITAGDVFYIRPDDRHsYESVDDlCLTN----ILFRPerlflfldwlDTLPGYLA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1213887340  98 NTFpfkKAFLR-KKEEESAILSISKQIIEEKDAGKPGYDLILKAFVMQLIIHVLR 151
Cdd:cd06977    94 HQF---QSHWRlNSSTLREIRQLIDQLESELEERDAGSELMAEALFLQLLVLLSR 145
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
1-274 7.77e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 46.25  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340   1 MLKINTTTFNPQILYIANCYTNEVRVgeNHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHYDITEPGMTN 80
Cdd:PRK13500   37 LLKDDFFASDQQAVAVADRYPQDVFA--EHTHDFCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340  81 AQLHIGFRNFALEGYTRNTFPFKKAFLRKKEEE--SAILSISKQII----EEKDAGKPGYDLILKAFVMQLIIHVLREAT 154
Cdd:PRK13500  115 QNIIYCPERLKLNLDWQGAIPGFSASAGQPHWRlgSVGMAQARQVIgqleHESSQHVPFANEMAELLFGQLVMLLNRHRY 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 155 PEQlenngvklSTDEQQKQILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEEL 234
Cdd:PRK13500  195 TSD--------SLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYL 266

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1213887340 235 LKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPSEnWR 274
Cdd:PRK13500  267 LQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQ-WR 305
ARD pfam03079
ARD/ARD' family; The two acireductone dioxygenase enzymes (ARD and ARD', previously known as ...
 28-76 8.17e-06

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: 45.04  E-value: 8.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1213887340  28 ENHHHDFLEISIICEGNVIYDIEGE-----RVKLGKGDMLIFNPGVSHYDITEP 76
Cdd:pfam03079  86 EEHLHTDEEIRYIVEGTGYFDVRDKddvwiRVFVEKGDLISLPAGIYHRFTTTP 139
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
25-70 8.35e-06

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 43.98  E-value: 8.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1213887340  25 RVGENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:COG0662    39 ELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPH 84
cupin_YbfI-like_N cd07001
AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal ...
 28-70 1.15e-05

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


Pssm-ID: 380405 [Multi-domain]  Cd Length: 76  Bit Score: 42.38  E-value: 1.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1213887340  28 ENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:cd07001    16 PNHFHDFYVIGFIESGQRTLFCEGKEYTVEPGDLLLINPRDVH 58
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 26-71 1.63e-05

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: 41.86  E-value: 1.63e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1213887340  26 VGENHHHDF-LEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHY 71
Cdd:pfam07883  10 SSPPHRHPGeDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHR 56
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 28-71 2.70e-05

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: 41.45  E-value: 2.70e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1213887340  28 ENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHY 71
Cdd:cd06988    16 TPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHY 59
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 239-275 1.15e-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: 38.67  E-value: 1.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1213887340 239 DVSVKQAANMVGYnDAYYFSKLFKKYYGFPPSEnWRK 275
Cdd:pfam00165   8 NLTIADIADELGF-SRSYFSRLFKKYTGVTPSQ-YRH 42
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
173-271 2.70e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 39.52  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213887340 173 QILVNEIIHYMEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYN 252
Cdd:PRK10219    4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                          90
                  ....*....|....*....
gi 1213887340 253 DAYYFSKLFKKYYGFPPSE 271
Cdd:PRK10219   84 SQQTFSRVFRRQFDRTPSD 102
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 26-70 2.93e-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: 39.37  E-value: 2.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1213887340  26 VGENHHHDFLEISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:cd02238    39 VVPLHSHPHEQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPH 83
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 23-71 6.41e-04

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: 38.35  E-value: 6.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1213887340  23 EVRVG-ENHHHDFL-EISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSHY 71
Cdd:cd20295    28 EVEEGhEEHYHKKStEIYYVLEGEGIFELDGEAVPVKPGDLVLIPPGTRHR 78
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 183-223 9.82e-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: 35.98  E-value: 9.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1213887340 183 MEKHHTEDVSLSTLSQTMYISPAYISKVFKEETGESPINYL 223
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
25-70 1.51e-03

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 37.69  E-value: 1.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1213887340  25 RVGENHHHDFL-EISIICEGNVIYDIEGERVKLGKGDMLIFNPGVSH 70
Cdd:COG3837    40 SSSPYHAHSAEeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPH 86
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 193-270 3.59e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 38.44  E-value: 3.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1213887340 193 LSTLSQTMYISPAYISKVFKEEtGESPINYLIKIRLTRAEELLKNKDVSVKQAANMVGYNDAYYFSKLFKKYYGFPPS 270
Cdd:PRK15185  225 LTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPS 301
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 30-71 5.84e-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: 34.77  E-value: 5.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1213887340  30 HHHDFLEISIIC-EGNVIYDIE-GERVKLGKGDMLIFNPGVSHY 71
Cdd:cd02208    15 HWHPEQDEIFYVlSGEGELTLDdGETVELKAGDIVLIPPGVPHS 58
cupin_PA3510-like cd02225
Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes ...
 30-70 6.06e-03

Pseudomonas aeruginosa PA3510 and related proteins, cupin domain; This family includes bacterial proteins homologous to PA3510, a Pseudomonas aeruginosa protein of unknown function with a beta-barrel fold that belongs to the cupin superfamily.


Pssm-ID: 380354  Cd Length: 150  Bit Score: 36.49  E-value: 6.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1213887340  30 HHHDFLEISIICEGN--VIYDIEGERVK--LGKGDMLIFNPGVSH 70
Cdd:cd02225    69 HTHEVEEVFFVLQGRltVFWEDEGEEHEreLGPRDMISVPAGVYR 113
 
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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