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Conserved domains on  [gi|492124630|ref|WP_005755118|]
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MULTISPECIES: 4-hydroxyphenylacetate catabolism regulatory protein HpaA [Pasteurella]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HpaA TIGR02297
4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional ...
 7-292 2.53e-175

4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway.


:

Pssm-ID: 131350 [Multi-domain]  Cd Length: 287  Bit Score: 485.85  E-value: 2.53e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630    7 ETQNINIEKTYGGQESSSIIHYETFDNLALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPH 86
Cdd:TIGR02297   1 EIPNIDIGKVYDGRYADSDVHYETFDNLALFFGRNMPVHFHDRYYQLHYLTEGSIALQLDEHEYSEYAPCFFLTPPSVPH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   87 GFYTDLDTHGHVLTIPQEFVWQLLESLKRDIN-YFYPMCIELSPQEEAQQIFKFEYLFNLLAGEYRQHTDEKQTALRLSA 165
Cdd:TIGR02297  81 GFVTDLDADGHVLTVRQELVWQLLESLKGDIGdAFYPMCIELSPQEEAEQIAKLEYLFELLASEYRQHTDGRQTALQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  166 KLILLEIYRLSKSNEKKYSPRNNELYLFNQFNFLIEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQI 245
Cdd:TIGR02297 161 QLILIELLRLSKSNEKSTSPRNNELYLFNRFNFLIEENYKQHLRLPEYADRLGISESRLNDICRRFSALSPKRLIIERVM 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 492124630  246 QEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:TIGR02297 241 QEARRLLLFTQHSINQIAYDLGYKDPAYFARFFQKETGLSPSAFRDR 287
 
Name Accession Description Interval E-value
HpaA TIGR02297
4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional ...
 7-292 2.53e-175

4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway.


Pssm-ID: 131350 [Multi-domain]  Cd Length: 287  Bit Score: 485.85  E-value: 2.53e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630    7 ETQNINIEKTYGGQESSSIIHYETFDNLALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPH 86
Cdd:TIGR02297   1 EIPNIDIGKVYDGRYADSDVHYETFDNLALFFGRNMPVHFHDRYYQLHYLTEGSIALQLDEHEYSEYAPCFFLTPPSVPH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   87 GFYTDLDTHGHVLTIPQEFVWQLLESLKRDIN-YFYPMCIELSPQEEAQQIFKFEYLFNLLAGEYRQHTDEKQTALRLSA 165
Cdd:TIGR02297  81 GFVTDLDADGHVLTVRQELVWQLLESLKGDIGdAFYPMCIELSPQEEAEQIAKLEYLFELLASEYRQHTDGRQTALQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  166 KLILLEIYRLSKSNEKKYSPRNNELYLFNQFNFLIEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQI 245
Cdd:TIGR02297 161 QLILIELLRLSKSNEKSTSPRNNELYLFNRFNFLIEENYKQHLRLPEYADRLGISESRLNDICRRFSALSPKRLIIERVM 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 492124630  246 QEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:TIGR02297 241 QEARRLLLFTQHSINQIAYDLGYKDPAYFARFFQKETGLSPSAFRDR 287
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 11-105 1.98e-25

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: 97.19  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  11 INIEKTYG---GQESSSIIHYETFDNLALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHG 87
Cdd:cd06999    1 IPTYALYGesaAAPTPDFLHCETIAARSRLHDWEIAPHRHADLFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHG 80

                         90
                 ....*....|....*...
gi 492124630  88 FYTDLDTHGHVLTIPQEF 105
Cdd:cd06999   81 FRFSPDTDGHVLTLADPL 98
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
207-290 1.14e-20

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.14  E-value: 1.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   207 NWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSP 286
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 492124630   287 KAFR 290
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
215-292 6.75e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.87  E-value: 6.75e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492124630  215 DRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLL-FTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
34-292 3.79e-19

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 84.83  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  34 LALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHGFYTDLDTHGHVLTIPQEFVWQLLESL 113
Cdd:COG2207    7 LLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 114 KRDINYFYPMCIELSPQEEAQQIFKFEYLFNLLAGEYRQHTDEKQTALRLSAKLILLEIYRLSKSNEKKYSPRNNELYLF 193
Cdd:COG2207   87 ALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 194 NQFNfliednfknnwrINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAY 273
Cdd:COG2207  167 LLLT------------LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSH 234

                        250
                 ....*....|....*....
gi 492124630 274 FSRFFQKETQLSPKAFRDQ 292
Cdd:COG2207  235 FSRAFKKRFGVTPSEYRKR 253
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
199-290 9.87e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 55.36  E-value: 9.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 199 LIEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFF 278
Cdd:PRK10572 191 YISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVF 270

                         90
                 ....*....|..
gi 492124630 279 QKETQLSPKAFR 290
Cdd:PRK10572 271 KKCTGASPSEFR 282
 
Name Accession Description Interval E-value
HpaA TIGR02297
4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional ...
 7-292 2.53e-175

4-hydroxyphenylacetate catabolism regulatory protein HpaA; This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway.


Pssm-ID: 131350 [Multi-domain]  Cd Length: 287  Bit Score: 485.85  E-value: 2.53e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630    7 ETQNINIEKTYGGQESSSIIHYETFDNLALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPH 86
Cdd:TIGR02297   1 EIPNIDIGKVYDGRYADSDVHYETFDNLALFFGRNMPVHFHDRYYQLHYLTEGSIALQLDEHEYSEYAPCFFLTPPSVPH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   87 GFYTDLDTHGHVLTIPQEFVWQLLESLKRDIN-YFYPMCIELSPQEEAQQIFKFEYLFNLLAGEYRQHTDEKQTALRLSA 165
Cdd:TIGR02297  81 GFVTDLDADGHVLTVRQELVWQLLESLKGDIGdAFYPMCIELSPQEEAEQIAKLEYLFELLASEYRQHTDGRQTALQALA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  166 KLILLEIYRLSKSNEKKYSPRNNELYLFNQFNFLIEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQI 245
Cdd:TIGR02297 161 QLILIELLRLSKSNEKSTSPRNNELYLFNRFNFLIEENYKQHLRLPEYADRLGISESRLNDICRRFSALSPKRLIIERVM 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 492124630  246 QEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:TIGR02297 241 QEARRLLLFTQHSINQIAYDLGYKDPAYFARFFQKETGLSPSAFRDR 287
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 11-105 1.98e-25

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: 97.19  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  11 INIEKTYG---GQESSSIIHYETFDNLALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHG 87
Cdd:cd06999    1 IPTYALYGesaAAPTPDFLHCETIAARSRLHDWEIAPHRHADLFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHG 80

                         90
                 ....*....|....*...
gi 492124630  88 FYTDLDTHGHVLTIPQEF 105
Cdd:cd06999   81 FRFSPDTDGHVLTLADPL 98
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
207-290 1.14e-20

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.14  E-value: 1.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   207 NWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSP 286
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 492124630   287 KAFR 290
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
215-292 6.75e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.87  E-value: 6.75e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492124630  215 DRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLL-FTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
34-292 3.79e-19

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 84.83  E-value: 3.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630  34 LALFYGRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHGFYTDLDTHGHVLTIPQEFVWQLLESL 113
Cdd:COG2207    7 LLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 114 KRDINYFYPMCIELSPQEEAQQIFKFEYLFNLLAGEYRQHTDEKQTALRLSAKLILLEIYRLSKSNEKKYSPRNNELYLF 193
Cdd:COG2207   87 ALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 194 NQFNfliednfknnwrINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAY 273
Cdd:COG2207  167 LLLT------------LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSH 234

                        250
                 ....*....|....*....
gi 492124630 274 FSRFFQKETQLSPKAFRDQ 292
Cdd:COG2207  235 FSRAFKKRFGVTPSEYRKR 253
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 199-290 1.00e-10

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: 61.33  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 199 LIEDNFKNNWRINDYLDRLCISESKLNaicQHFSA---TSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFS 275
Cdd:COG4977  218 WMEANLEEPLSVDELARRAGMSPRTLE---RRFRAatgTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFR 294

                         90
                 ....*....|....*
gi 492124630 276 RFFQKETQLSPKAFR 290
Cdd:COG4977  295 RAFRRRFGVSPSAYR 309
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 199-292 7.08e-09

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 56.22  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 199 LIEDNFKNNWRINDYLDRLCISESKLNAIC-QHFSATsPKRLIIERQIQEAkRKLLFTQHSIYQIAYDLGFKDPAYFSRF 277
Cdd:COG2169   92 LIEAGAEDRPSLEDLAARLGLSPRHLRRLFkAHTGVT-PKAYARARRLLRA-RQLLQTGLSVTDAAYAAGFGSLSRFYEA 169

                         90
                 ....*....|....*
gi 492124630 278 FQKETQLSPKAFRDQ 292
Cdd:COG2169  170 FKKLLGMTPSAYRRG 184
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
199-290 9.87e-09

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 55.36  E-value: 9.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 199 LIEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFF 278
Cdd:PRK10572 191 YISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVF 270

                         90
                 ....*....|..
gi 492124630 279 QKETQLSPKAFR 290
Cdd:PRK10572 271 KKCTGASPSEFR 282
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
1-101 1.31e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 48.69  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   1 MRDQSFETQNINIEKTYGGQESSSIIHYEtfdnlaLFYGRKSLVHFHDrFYQVHYLTEGSIALQLDAHEYRLYAPCFFIT 80
Cdd:COG1917    1 MRLAEIALTGVSVRVLADGEDELEVVRVT------FEPGARTPWHSHP-GEELIYVLEGEGEVEVGGEEYELKPGDVVFI 73

                         90       100
                 ....*....|....*....|.
gi 492124630  81 PPSIPHGFYTDLDTHGHVLTI 101
Cdd:COG1917   74 PPGVPHAFRNLGDEPAVLLVV 94
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 219-290 4.74e-07

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 50.45  E-value: 4.74e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492124630  219 ISESKLNAICQHFSATSPKRLIIERQIQEAKrKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFR 290
Cdd:TIGR04094 313 MSESKLRKLFKKEMGISIQEYISKRKIEEAK-YLLRSQIPVSEVSNELGFYDLSHFSRTFKKHTGVSPKQYQ 383
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
229-293 4.01e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 47.36  E-value: 4.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492124630 229 QHFSATsPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQD 293
Cdd:PRK13503 210 QQTGLT-PQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQGR 273
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 39-101 5.40e-06

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 43.40  E-value: 5.40e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492124630   39 GRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHGFYTDLDTHGHVLTI 101
Cdd:pfam07883   8 GESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 45-170 1.44e-05

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: 43.96  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   45 HFHDrFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPSIPHGFYTDLDT--HGHVLTIPQEFVWQLLeslkRDINYFYP 122
Cdd:pfam02311  19 HVHD-FYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDgwRYRWLYFEPELLERIL----ADISILAG 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 492124630  123 MCIELSPQEEAQQIfkFEYLFNLLAGeyrqhtDEKQTALRLSAKLILL 170
Cdd:pfam02311  94 GPLPLLRDPELAAL--LRALFRLLEE------AGRSDDLLAEALLYQL 133
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
200-292 2.28e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 45.28  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 200 IEDNFKNNWRINDYLDRLCISESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQ 279
Cdd:PRK13501 185 LQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFT 264

                         90
                 ....*....|...
gi 492124630 280 KETQLSPKAFRDQ 292
Cdd:PRK13501 265 REAGMTPRDYRQR 277
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 39-101 9.41e-05

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: 40.16  E-value: 9.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492124630  39 GRKSLVHFHDRFYQVHYLTEGSIALQLDA-HEYRLYAPCFFITPPSIPHGFYTDLDTHGHVLTI 101
Cdd:cd02208    9 GTSSPPHWHPEQDEIFYVLSGEGELTLDDgETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 220-290 1.03e-04

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 43.21  E-value: 1.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492124630 220 SESKLNAICQHFSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFR 290
Cdd:PRK10296 201 SQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYR 271
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 258-292 1.95e-04

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 42.33  E-value: 1.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 492124630 258 SIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:PRK09685 266 KITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYRRK 300
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
240-292 3.63e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 39.14  E-value: 3.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492124630 240 IIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSPKAFRDQ 292
Cdd:PRK10219  54 IRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFRRQFDRTPSDYRHR 106
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
9-101 1.24e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 37.81  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630   9 QNINIEKTYGGQESSSIIHYETFDNLALFY-----GRKSLVHFHDRFYQVHYLTEGSIALQLDAHEYRLYAPCFFITPPS 83
Cdd:COG0662    2 QDVNIEELKAIGWGSYEVLGEGGERLSVKRitvppGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAG 81

                         90
                 ....*....|....*...
gi 492124630  84 IPHGFYTDLDTHGHVLTI 101
Cdd:COG0662   82 VPHRLRNPGDEPLELLEV 99
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 208-298 3.83e-03

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 38.14  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 208 WRINDYLDRLCISESKLNAICQHfSATSPKRLIIERQIQEAKrKLLFTQHSIYQIAYDLGFKDPAYFSRFFQKETQLSP- 286
Cdd:PRK09940 151 WKLKDICDCLYISESLLKKKLKQ-EQTTFSQILLDARMQHAK-NLIRVEGSVNKIAEQCGYASTSYFIYAFRKHFGNSPk 228

                         90
                 ....*....|....*
gi 492124630 287 ---KAFRDQDHISSN 298
Cdd:PRK09940 229 rvsKEYRCQRHTGMN 243
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 258-290 5.36e-03

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: 34.05  E-value: 5.36e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 492124630  258 SIYQIAYDLGFkDPAYFSRFFQKETQLSPKAFR 290
Cdd:pfam00165  10 TIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 45-88 8.07e-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: 35.59  E-value: 8.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 492124630  45 HFHDRFYQVHYLTEGSIALQLDaHEYRLYAPCFFIT-PPSIPHGF 88
Cdd:cd02215   48 HYHKRHHETFYVLEGRLQLWLD-GESRLLTPGDFASvPPGTIHAY 91
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 194-289 8.92e-03

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 37.35  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492124630 194 NQFNFLIEDnFKNNWRINDYLDRLCISESKLNAICQHfSATSPKRLIIERQIQEAKRKLLFTQHSIYQIAYDLGFKDPAY 273
Cdd:PRK15186 185 NIYNIIISD-ISRKWALKDISDSLYMSCSTLKRKLKQ-ENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASY 262

                         90
                 ....*....|....*.
gi 492124630 274 FSRFFQKETQLSPKAF 289
Cdd:PRK15186 263 FTCVFKKHFKTTPSEF 278
 
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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