NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1895617114|ref|WP_186328808|]
View 

AraC family transcriptional regulator [Bacillus sp. X1(2014)]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 12084213)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
75-288 2.15e-28

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 109.87  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  75 ILIYNAGIIHEEYSNPSNPLITYFCGISNLAIDQLKELCIIPFEFEPVIRENQYSDQIGSYFSHIFEESSLKGDGYEIIC 154
Cdd:COG2207    44 LLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 155 QGLLTSSIALIHRAIRLQNFKNDARDSNSLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLIN 234
Cdd:COG2207   124 LLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRE 203

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895617114 235 RRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKENHKKN 288
Cdd:COG2207   204 LRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 36-92 1.27e-10

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: 56.50  E-value: 1.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  36 PNWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:pfam07883   7 PGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPH-RFRNTGD 62
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
75-288 2.15e-28

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 109.87  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  75 ILIYNAGIIHEEYSNPSNPLITYFCGISNLAIDQLKELCIIPFEFEPVIRENQYSDQIGSYFSHIFEESSLKGDGYEIIC 154
Cdd:COG2207    44 LLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 155 QGLLTSSIALIHRAIRLQNFKNDARDSNSLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLIN 234
Cdd:COG2207   124 LLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRE 203

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895617114 235 RRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKENHKKN 288
Cdd:COG2207   204 LRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
199-282 9.94e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 102.63  E-value: 9.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  199 NLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETP 278
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1895617114  279 RQFK 282
Cdd:smart00342  81 SEYR 84
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
57-283 3.66e-23

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 96.20  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  57 GEGTFIINNKSYTAKKGDILIYNAGIIHEEYSNPSNP----LITYFCGISNLAiDQLKelciIPFEFEPVIR----ENQY 128
Cdd:PRK10572   58 GQGVIFNGGRAFVCRPGDLLLFPPGEIHHYGRHPDSDewyhQWVYFRPRAYWA-DWLN----WPSIFAGVGRlripDEAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 129 SDQIGSYFSHIFEESSLKGDGYEIICQGLLTSsiaLIHRAIRLQNfkndARDSNSLAHRIKE---YIDKNYKKNLKLEDI 205
Cdd:PRK10572  133 QPEFSDLFGQIEQAGQSEGRYSELLAMNLLER---LLLRCMEAIP----ESLHPPMDPRVREacqYISDHLASEFDIESV 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1895617114 206 ADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKE 283
Cdd:PRK10572  206 AQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
HTH_18 pfam12833
Helix-turn-helix domain;
205-284 2.62e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.72  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 205 IADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLV-STELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKE 283
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 1895617114 284 N 284
Cdd:pfam12833  81 R 81
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 36-92 1.27e-10

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: 56.50  E-value: 1.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  36 PNWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:pfam07883   7 PGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPH-RFRNTGD 62
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
36-92 7.20e-10

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 55.24  E-value: 7.20e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  36 PNWNFPSHKHDDlSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:COG1917    32 PGARTPWHSHPG-EELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPH-AFRNLGD 86
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 35-99 6.98e-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: 45.94  E-value: 6.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895617114  35 NPNWNFPSHKHDDLSEIIYICEGEGTFIIN-NKSYTAKKGDILIYNAGIIHEEYSNPSNPLITYFC 99
Cdd:cd02208     7 PPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 41-116 5.23e-03

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


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 35.50  E-value: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  41 PSHKHDdlSE-IIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSNplityfcgisnlaiDQLKELCIIP 116
Cdd:cd02222    31 PLHTHP--WEhEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH-QFRNTGD--------------EPLGFLCIVP 90
 
Name Accession Description Interval E-value
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
75-288 2.15e-28

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 109.87  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  75 ILIYNAGIIHEEYSNPSNPLITYFCGISNLAIDQLKELCIIPFEFEPVIRENQYSDQIGSYFSHIFEESSLKGDGYEIIC 154
Cdd:COG2207    44 LLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 155 QGLLTSSIALIHRAIRLQNFKNDARDSNSLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLIN 234
Cdd:COG2207   124 LLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRE 203

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895617114 235 RRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKENHKKN 288
Cdd:COG2207   204 LRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
199-282 9.94e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 102.63  E-value: 9.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  199 NLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETP 278
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1895617114  279 RQFK 282
Cdd:smart00342  81 SEYR 84
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
57-283 3.66e-23

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 96.20  E-value: 3.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  57 GEGTFIINNKSYTAKKGDILIYNAGIIHEEYSNPSNP----LITYFCGISNLAiDQLKelciIPFEFEPVIR----ENQY 128
Cdd:PRK10572   58 GQGVIFNGGRAFVCRPGDLLLFPPGEIHHYGRHPDSDewyhQWVYFRPRAYWA-DWLN----WPSIFAGVGRlripDEAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 129 SDQIGSYFSHIFEESSLKGDGYEIICQGLLTSsiaLIHRAIRLQNfkndARDSNSLAHRIKE---YIDKNYKKNLKLEDI 205
Cdd:PRK10572  133 QPEFSDLFGQIEQAGQSEGRYSELLAMNLLER---LLLRCMEAIP----ESLHPPMDPRVREacqYISDHLASEFDIESV 205

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1895617114 206 ADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKE 283
Cdd:PRK10572  206 AQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
HTH_18 pfam12833
Helix-turn-helix domain;
205-284 2.62e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.72  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 205 IADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLV-STELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKE 283
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 1895617114 284 N 284
Cdd:pfam12833  81 R 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 184-291 5.11e-20

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: 88.57  E-value: 5.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 184 LAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLvSTELKIGEIARIMGYDNT 263
Cdd:COG2169    85 LVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSL 163

                          90       100
                  ....*....|....*....|....*...
gi 1895617114 264 NYFTLLFKKMTGETPRQFKENHKKNLYY 291
Cdd:COG2169   164 SRFYEAFKKLLGMTPSAYRRGGAGAAIR 191
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
36-283 1.33e-14

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 72.63  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  36 PNWNFPSHKHDdLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHEeysnpsnplityFCGISNLAIDQL---KEL 112
Cdd:PRK13501   27 PQETFVEHTHQ-FCEIVIVWRGNGLHVLNDHPYRITCGDVFYIQAADHHS------------YESVHDLVLDNIiycPER 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 113 CIIPFEFEPVIRENQySDQIGSYFS-------------HIFEESSLKGDGYEIicqgLLTSSIaLIHRAIRLQNFKNDAR 179
Cdd:PRK13501   94 LHLNAQWHKLLPPLG-PEQNQGYWRlttqgmaqarpiiQQLAQESRKTDSWSI----QLTEVL-LLQLAIVLKRHRYRAE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 180 DSNSLAH-----RIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEI 254
Cdd:PRK13501  168 QAHLLPDgeqldLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDI 247

                         250       260
                  ....*....|....*....|....*....
gi 1895617114 255 ARIMGYDNTNYFTLLFKKMTGETPRQFKE 283
Cdd:PRK13501  248 AARCGFEDSNYFSAVFTREAGMTPRDYRQ 276
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 29-160 1.21e-13

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: 66.69  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  29 AGQVGGNPNWNFPSHKHDDLsEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSNPLITYFC-GISNLAID 107
Cdd:pfam02311   5 EGIEARYPGHSFPPHVHDFY-VIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPH-DYEPESEDGWRYRWlYFEPELLE 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1895617114 108 QLKELCIIPFEFEPVIRENQYSDQIgsyFSHIFEESSLKGDGYEIICQGLLTS 160
Cdd:pfam02311  83 RILADISILAGGPLPLLRDPELAAL---LRALFRLLEEAGRSDDLLAEALLYQ 132
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 186-285 5.65e-13

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: 67.88  E-value: 5.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 186 HRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNY 265
Cdd:COG4977   213 ARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292

                          90       100
                  ....*....|....*....|
gi 1895617114 266 FTLLFKKMTGETPRQFKENH 285
Cdd:COG4977   293 FRRAFRRRFGVSPSAYRRRF 312
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 36-92 1.27e-10

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: 56.50  E-value: 1.27e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  36 PNWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:pfam07883   7 PGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPH-RFRNTGD 62
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
36-92 7.20e-10

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 55.24  E-value: 7.20e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  36 PNWNFPSHKHDDlSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:COG1917    32 PGARTPWHSHPG-EELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPH-AFRNLGD 86
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
186-282 1.51e-09

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 54.55  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 186 HRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNY 265
Cdd:PRK10219    8 QTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQT 87

                          90
                  ....*....|....*..
gi 1895617114 266 FTLLFKKMTGETPRQFK 282
Cdd:PRK10219   88 FSRVFRRQFDRTPSDYR 104
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
36-288 1.63e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 57.80  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  36 PNWNFPSHKHDdLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHEEYSNPSNPLITYFCGISNLAIDQLKELCII 115
Cdd:PRK13500   57 PQDVFAEHTHD-FCELVIVWRGNGLHVLNDRPYRITRGDLFYIHADDKHSYASVNDLVLQNIIYCPERLKLNLDWQGAIP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 116 PFEF---EPVIRENQYS-DQIGSYFSHIFEESSLKGDGYEIICQGLLTSSIALIHRairlQNFKNDA---RDSNSLAHRI 188
Cdd:PRK13500  136 GFSAsagQPHWRLGSVGmAQARQVIGQLEHESSQHVPFANEMAELLFGQLVMLLNR----HRYTSDSlppTSSETLLDKL 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 189 KEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTL 268
Cdd:PRK13500  212 ITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSV 291

                         250       260
                  ....*....|....*....|.
gi 1895617114 269 LFKKMTGETPRQFKE-NHKKN 288
Cdd:PRK13500  292 VFTRETGMTPSQWRHlNSQKD 312
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 182-281 3.64e-09

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 56.61  E-value: 3.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 182 NSLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLiNRRIGEAKNLLVSTELKIGEIARIMGYD 261
Cdd:PRK15186  180 NTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENTSFSEVYL-NARMNKATKLLRNSEYNITRVAYMCGYD 258

                          90       100
                  ....*....|....*....|
gi 1895617114 262 NTNYFTLLFKKMTGETPRQF 281
Cdd:PRK15186  259 SASYFTCVFKKHFKTTPSEF 278
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
216-282 4.43e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 56.22  E-value: 4.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114 216 LSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFK 282
Cdd:PRK13502  209 LRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
35-92 6.67e-09

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 52.84  E-value: 6.67e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1895617114  35 NPNWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSN 92
Cdd:COG0662    35 PPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPH-RLRNPGD 91
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
36-285 7.99e-09

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 55.45  E-value: 7.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  36 PNWNFPSHKHDdLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHEeYSNPSNPLIT---Y-----FCGISNLAId 107
Cdd:PRK13503   24 PQAAFPEHHHD-FHEIVIVEHGTGIHVFNGQPYTLSGGTVCFVRDHDRHL-YEHTDNLCLTnvlYrspdaFRFLAGLNQ- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 108 qlkelcIIPFEFEPVIREN--------QYSDQIGSYFSHIFEESSLKGDG-YEIICQGLLTSsialihraIRLQNFKNDA 178
Cdd:PRK13503  101 ------LLPQEQDGQYPSHwrvnqsvlQQVRQLVAQMEQQEESNDLEAIAsREILFMQLLVL--------LRKSSLQENG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 179 RDSNSLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIM 258
Cdd:PRK13503  167 ENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRC 246

                         250       260
                  ....*....|....*....|....*..
gi 1895617114 259 GYDNTNYFTLLFKKMTGETPRQFKENH 285
Cdd:PRK13503  247 GFGDSNHFSTLFRREFSWSPRDIRQGR 273
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 192-232 2.43e-07

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: 46.38  E-value: 2.43e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1895617114 192 IDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYL 232
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 183-286 2.44e-07

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 50.85  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 183 SLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQmQMTPINYLINRRIGEAKNLlVSTELKIGEIARIMGYDN 262
Cdd:PRK09940  134 SVSGKVRNIVNMKLAHPWKLKDICDCLYISESLLKKKLKQE-QTTFSQILLDARMQHAKNL-IRVEGSVNKIAEQCGYAS 211

                          90       100
                  ....*....|....*....|....
gi 1895617114 263 TNYFTLLFKKMTGETPRQFKENHK 286
Cdd:PRK09940  212 TSYFIYAFRKHFGNSPKRVSKEYR 235
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 35-99 6.98e-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: 45.94  E-value: 6.98e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895617114  35 NPNWNFPSHKHDDLSEIIYICEGEGTFIIN-NKSYTAKKGDILIYNAGIIHEEYSNPSNPLITYFC 99
Cdd:cd02208     7 PPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
41-105 8.52e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 46.93  E-value: 8.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895617114  41 PSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSNPLITYFCGISNLA 105
Cdd:COG3837    43 PYHAHSAEEEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPH-RLRNRGDEPARYLVVGTRAP 106
cupin_MmsR-like_N cd06986
AraC/XylS family transcriptional regulators similar to MmsR, N-terminal cupin domain; This ...
 51-93 1.68e-06

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: 45.17  E-value: 1.68e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1895617114  51 IIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHEEYSNPSNP 93
Cdd:cd06986    31 LHYVLSGKGTFSVNGKTYHLKAGQGFLIPPGEPHSYGADEDDP 73
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 17-114 1.08e-05

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: 43.27  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114  17 PLKFKNPPV-LAYAG-QVGGNPNWnfpsHKHDDLSEIIYICEGEGTFIINNKSYTAKKGD-ILIyNAGIIHEeysnpsnp 93
Cdd:cd02214    11 PDNDGDPRYsLAHARvPPGESTLP----HRLKGSEEVYYILEGEGTMEIDGEPREVGPGDaVLI-PPGAVQR-------- 77

                          90       100
                  ....*....|....*....|.
gi 1895617114  94 lityfcgISNLAIDQLKELCI 114
Cdd:cd02214    78 -------IENTGEEDLVFLCI 91
cupin_Lmo2851-like_N cd06996
AraC/XylS family transcriptional regulators similar to Listeria monocytogenes Lmo2851 protein, ...
 39-85 1.80e-05

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: 42.56  E-value: 1.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1895617114  39 NFPSHKHDDLsEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHE 85
Cdd:cd06996    25 DYPLHTHNFL-EINYMYSGSCTQIVNGQEITLKEGDLLLLDQGSTHS 70
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 183-285 2.76e-05

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 44.99  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 183 SLAHRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQmQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDN 262
Cdd:PRK15185  206 TLKERVYNIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDS 284

                          90       100
                  ....*....|....*....|....*
gi 1895617114 263 TNYFTLLFKKMTGETPRQFKE--NH 285
Cdd:PRK15185  285 TSYFIQCFKKYFKTTPSTFIKmaNH 309
cupin_Pac13-like cd20295
monomeric dehydratase Pac13 and related proteins, cupin domain; This family includes a small ...
 42-77 1.35e-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: 40.28  E-value: 1.35e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1895617114  42 SHKHDDLSEIIYICEGEGTFIINNKSYTAKKGD-ILI 77
Cdd:cd20295    35 EHYHKKSTEIYYVLEGEGIFELDGEAVPVKPGDlVLI 71
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 246-281 2.69e-04

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 37.90  E-value: 2.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1895617114 246 STELKIGEIARIMGYDnTNYFTLLFKKMTGETPRQF 281
Cdd:pfam00165   6 STNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQY 40
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 43-77 3.66e-04

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 38.99  E-value: 3.66e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1895617114  43 HKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILI 77
Cdd:cd02221    35 HQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTF 69
cupin_RemF-like cd06979
Streptomyces resistomycificus RemF cyclase and related proteins, cupin domain; RemF cyclase is ...
 41-99 5.98e-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: 38.21  E-value: 5.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1895617114  41 PSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSNPLITYFC 99
Cdd:cd06979    32 PPHYHEDWEETIYGLEGSVTLTLPGKTVEVGPGDSIFIPRGEVH-GFVNRSGGPTCRLC 89
cupin_YbfI-like_N cd07001
AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal ...
 40-84 1.23e-03

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: 36.98  E-value: 1.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1895617114  40 FPSHKHDdLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd07001    15 FPNHFHD-FYVIGFIESGQRTLFCEGKEYTVEPGDLLLINPRDVH 58
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
186-282 1.45e-03

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 38.16  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 186 HRIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNY 265
Cdd:PRK11511   12 HSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQT 91

                          90
                  ....*....|....*..
gi 1895617114 266 FTLLFKKMTGETPRQFK 282
Cdd:PRK11511   92 LTRTFKNYFDVPPHKYR 108
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 155-285 1.57e-03

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 39.63  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 155 QGLLTSSIALIHRAirLQNFKNDARDSNSLAHRIKEYIDKNYKK-NLKLEDIADALFINKYYLSHVFKEQmQMTPINYLI 233
Cdd:PRK09685  171 EALLEALIALLRPA--LHQRESVQPRRERQFQKVVALIDQSIQEeILRPEWIAGELGISVRSLYRLFAEQ-GLVVAQYIR 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895617114 234 NRRIGEAKNLL--VSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKENH 285
Cdd:PRK09685  248 NRRLDRCADDLrpAADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 37-84 1.86e-03

AraC/XylS family transcriptional regulators similar to HpaA, 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, similar to Escherichia coli 4-hydroxyphenylacetate catabolism regulatory protein HpaA (also known as 4HPA). HpaA is encoded by the hpaA gene which is located upstream of hpaBC. It is activated by 4-HPA, 3-HPA and phenylacetate, and represents a member of the AraC/XylS family of regulators that recognizes aromatic effectors. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380403 [Multi-domain]  Cd Length: 98  Bit Score: 37.09  E-value: 1.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1895617114  37 NWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd06999    32 DWEIAPHRHADLFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVH 79
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 51-84 2.41e-03

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 36.33  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1895617114  51 IIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd02230    34 TVQVLEGEAEFTIGGETVTLKAGELIVMPANVPH 67
ftrA PRK09393
transcriptional activator FtrA; Provisional
 220-284 2.48e-03

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 38.79  E-value: 2.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1895617114 220 FKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPRQFKEN 284
Cdd:PRK09393  255 FEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKR 319
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 43-84 3.39e-03

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The 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).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 36.38  E-value: 3.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1895617114  43 HKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd06122    43 HAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPH 84
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 45-84 4.00e-03

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 35.98  E-value: 4.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1895617114  45 HDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd02223    29 HDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWH 68
EutQ COG4766
Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid ...
 50-98 4.45e-03

Ethanolamine utilization protein EutQ, cupin superfamily (function unknown) [Amino acid transport and metabolism];


Pssm-ID: 443798  Cd Length: 123  Bit Score: 36.50  E-value: 4.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1895617114  50 EIIYICEGEGTFIINNKSYTAKKGDILIYNAGI-IHeeYSNPSNPLITYF 98
Cdd:COG4766    69 EVDYVLEGTLTIEIDGETVTAGPGDVIYIPKGSsIT--FSTPEKARFFYV 116
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 187-289 4.45e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 37.98  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1895617114 187 RIKEYIDKNYKKNLKLEDIADALFINKYYLSHVFKEQmQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYF 266
Cdd:PRK09978  146 RVCTVINNNIAHEWTLARIASELLMSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYF 224

                          90       100
                  ....*....|....*....|...
gi 1895617114 267 TLLFKKMTGETPRQFKENHKKNL 289
Cdd:PRK09978  225 IYVFRNYYGMTPTEYQERSAQGL 247
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 25-96 4.97e-03

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 35.42  E-value: 4.97e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1895617114  25 VLAYAGQVGGnpnwnfPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHEEYSNPSNPLIT 96
Cdd:cd07006    16 VLAPGDTEGG------PDNRHRGSDQWLYVVSGSGEAIVEGERVALKPGSLLLIEAGETHEIRNTGDEPLKT 81
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 215-290 5.11e-03

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 37.81  E-value: 5.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895617114 215 YLSHVFKEQMQMTPINYLINRRIGEAKNLLVSTELKIGEIARIMGYDNTNYFTLLFKKMTGETPrqfkENHKKNLY 290
Cdd:PRK10296  204 YLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTP----GSYRKKLT 275
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 41-116 5.23e-03

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


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 35.50  E-value: 5.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1895617114  41 PSHKHDdlSE-IIYICEGEGTFIINNKSYTAKKGDILIYNAGIIHeEYSNPSNplityfcgisnlaiDQLKELCIIP 116
Cdd:cd02222    31 PLHTHP--WEhEVYVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPH-QFRNTGD--------------EPLGFLCIVP 90
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 50-76 5.39e-03

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 35.18  E-value: 5.39e-03
                          10        20
                  ....*....|....*....|....*..
gi 1895617114  50 EIIYICEGEGTFIINNKSYTAKKGDIL 76
Cdd:cd02228    35 EIKYVLEGELEITDDGQTVTAKPGDVL 61
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 35-103 5.73e-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: 395138  Cd Length: 151  Bit Score: 36.54  E-value: 5.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1895617114  35 NPNWNFPSHKHDDLSEIIYICEGEGTFII-----NNKSYTAK--KGDILIYNAGIIHEEYSNPSNPLITYFCGISN 103
Cdd:pfam00190  41 APGGMNPPHWHPNATEILYVLQGRGRVGFvvpgnGNRVFHKVlrEGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTN 116
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 31-84 6.33e-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: 35.97  E-value: 6.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1895617114  31 QVGGNPNWNFPSHKHDDLSEIIYICEGEGTFIINNKSYTAKKGDILIYNAGIIH 84
Cdd:cd02215    36 TTEGPKGDAIPPHYHKRHHETFYVLEGRLQLWLDGESRLLTPGDFASVPPGTIH 89
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 41-84 9.08e-03

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380411 [Multi-domain]  Cd Length: 101  Bit Score: 34.92  E-value: 9.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1895617114  41 PSHKHDDLSEIIYICEGEGTFIINN-KSYTAKKGDILIYNAGIIH 84
Cdd:cd07008    41 AAHIHPHGQDTWIVLSGEGEYLLGDgQTVPIKAGDIVIAPAGQVH 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH