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Conserved domains on  [gi|15599122|ref|NP_252616|]
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transcriptional regulator [Pseudomonas aeruginosa PAO1]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 14398448)

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
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 11-105 2.39e-38

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly 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 in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


:

Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 129.61  E-value: 2.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  11 LAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQPETPTP 90
Cdd:cd06124   1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIDPEAAAGL 80

                        90
                ....*....|....*
gi 15599122  91 LSDCCVLAVTPLLRE 105
Cdd:cd06124  81 PAEPCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
175-250 2.15e-21

Helix-turn-helix domain;


:

Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.33  E-value: 2.15e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599122   175 RVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLL--AGDSVQVVARDLGYGSTRAFSSMFRRLLGETPRDYLGR 250
Cdd:pfam12833   4 ALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
 
Name Accession Description Interval E-value
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 11-105 2.39e-38

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly 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 in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 129.61  E-value: 2.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  11 LAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQPETPTP 90
Cdd:cd06124   1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIDPEAAAGL 80

                        90
                ....*....|....*
gi 15599122  91 LSDCCVLAVTPLLRE 105
Cdd:cd06124  81 PAEPCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
175-250 2.15e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.33  E-value: 2.15e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599122   175 RVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLL--AGDSVQVVARDLGYGSTRAFSSMFRRLLGETPRDYLGR 250
Cdd:pfam12833   4 ALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
166-248 3.39e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.53  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122    166 GLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLGYGSTRAFSSMFRRLLGETP 244
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 15599122    245 RDYL 248
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1-255 1.67e-18

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 82.14  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   1 MLIEHRPDGLLAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTL 80
Cdd:COG2207   6 LLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLAL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  81 FIEQPETPTPLSDCCVLAVTPLLREMILRAIHLESQPRLDDFCQRLQGLILSEIANLERMPLYLPMPRDRRLQAicqALL 160
Cdd:COG2207  86 LALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLL---LLL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122 161 KQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLGYGSTRAFSSMFRRL 239
Cdd:COG2207 163 LLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDlSISEIAYELGFSSQSHFSRAFKKR 242

                       250
                ....*....|....*.
gi 15599122 240 LGETPRDYLGRLEQLA 255
Cdd:COG2207 243 FGVTPSEYRKRLRARA 258
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 147-247 2.50e-17

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: 79.82  E-value: 2.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122 147 PRDRRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLG 225
Cdd:COG4977 207 HRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAAACG 286

                        90       100
                ....*....|....*....|..
gi 15599122 226 YGSTRAFSSMFRRLLGETPRDY 247
Cdd:COG4977 287 FGSASHFRRAFRRRFGVSPSAY 308
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
16-247 5.49e-08

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 52.67  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   16 LDFPDG--HHLGRHfhPQAQFLYaarglmrlatHHGAWVIPptRAVWIP----PRVEHEI----FMSGEV--HMRTLFIE 83
Cdd:PRK10572  77 LLFPPGeiHHYGRH--PDSDEWY----------HQWVYFRP--RAYWADwlnwPSIFAGVgrlrIPDEALqpEFSDLFGQ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   84 QPET---PTPLSDccVLAVTpLLREMILRAIHLEsqprlddfcqrlqglilseianlermPLYLPMPRDRRLQAICQALL 160
Cdd:PRK10572 143 IEQAgqsEGRYSE--LLAMN-LLERLLLRCMEAI--------------------------PESLHPPMDPRVREACQYIS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  161 KQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEAlpRLL---AGDSVQVVARDLGYGSTRAFSSMFR 237
Cdd:PRK10572 194 DHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRA--KLLlqtTRMPIATIGRNVGYDDQLYFSRVFK 271

                        250
                 ....*....|
gi 15599122  238 RLLGETPRDY 247
Cdd:PRK10572 272 KCTGASPSEF 281
ftrA PRK09393
transcriptional activator FtrA; Provisional
 145-247 4.97e-05

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 43.80  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  145 PMPRD--RRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLA-GDSVQVVA 221
Cdd:PRK09393 211 PVASResDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESsALSIDQIA 290

                         90       100
                 ....*....|....*....|....*.
gi 15599122  222 RDLGYGSTRAFSSMFRRLLGETPRDY 247
Cdd:PRK09393 291 ERAGFGSEESLRHHFRRRAATSPAAY 316
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 11-130 5.01e-03

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 36.26  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122    11 LAAISLDFPDgHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIfmsgevhmrtlfieQPETPTP 90
Cdd:pfam02311   4 LEGIEARYPG-HSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDY--------------EPESEDG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15599122    91 LSDCCVL----AVTPLLREMILRAIHLESQPRLDDFCQRLQGLI 130
Cdd:pfam02311  69 WRYRWLYfepeLLERILADISILAGGPLPLLRDPELAALLRALF 112
 
Name Accession Description Interval E-value
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 11-105 2.39e-38

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly 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 in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 129.61  E-value: 2.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  11 LAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQPETPTP 90
Cdd:cd06124   1 VLARAADYPAGHRTPWHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLGAVELRSLYIDPEAAAGL 80

                        90
                ....*....|....*
gi 15599122  91 LSDCCVLAVTPLLRE 105
Cdd:cd06124  81 PAEPCVLAVSPLLRE 95
HTH_18 pfam12833
Helix-turn-helix domain;
175-250 2.15e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.33  E-value: 2.15e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599122   175 RVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLL--AGDSVQVVARDLGYGSTRAFSSMFRRLLGETPRDYLGR 250
Cdd:pfam12833   4 ALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLedTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
166-248 3.39e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.53  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122    166 GLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLGYGSTRAFSSMFRRLLGETP 244
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDlSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 15599122    245 RDYL 248
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
1-255 1.67e-18

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 82.14  E-value: 1.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   1 MLIEHRPDGLLAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTL 80
Cdd:COG2207   6 LLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLAL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  81 FIEQPETPTPLSDCCVLAVTPLLREMILRAIHLESQPRLDDFCQRLQGLILSEIANLERMPLYLPMPRDRRLQAicqALL 160
Cdd:COG2207  86 LALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLL---LLL 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122 161 KQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLGYGSTRAFSSMFRRL 239
Cdd:COG2207 163 LLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDlSISEIAYELGFSSQSHFSRAFKKR 242

                       250
                ....*....|....*.
gi 15599122 240 LGETPRDYLGRLEQLA 255
Cdd:COG2207 243 FGVTPSEYRKRLRARA 258
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 147-247 2.50e-17

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: 79.82  E-value: 2.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122 147 PRDRRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLG 225
Cdd:COG4977 207 HRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAAACG 286

                        90       100
                ....*....|....*....|..
gi 15599122 226 YGSTRAFSSMFRRLLGETPRDY 247
Cdd:COG4977 287 FGSASHFRRAFRRRFGVSPSAY 308
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 147-260 1.44e-14

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: 72.39  E-value: 1.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122 147 PRDRRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGDSVQVVARDLGY 226
Cdd:COG2169  81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGF 160

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599122 227 GSTRAFSSMFRRLLGETPRDY--LGRLEQLARVRGR 260
Cdd:COG2169 161 GSLSRFYEAFKKLLGMTPSAYrrGGAGAAIRFAPTP 196
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
5-87 5.35e-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: 5.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   5 HRPDGLLAAISLDFPDGHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQ 84
Cdd:COG1917  17 ADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96


                ...
gi 15599122  85 PET 87
Cdd:COG1917  97 PGL 99
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
16-247 5.49e-08

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 52.67  E-value: 5.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   16 LDFPDG--HHLGRHfhPQAQFLYaarglmrlatHHGAWVIPptRAVWIP----PRVEHEI----FMSGEV--HMRTLFIE 83
Cdd:PRK10572  77 LLFPPGeiHHYGRH--PDSDEWY----------HQWVYFRP--RAYWADwlnwPSIFAGVgrlrIPDEALqpEFSDLFGQ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122   84 QPET---PTPLSDccVLAVTpLLREMILRAIHLEsqprlddfcqrlqglilseianlermPLYLPMPRDRRLQAICQALL 160
Cdd:PRK10572 143 IEQAgqsEGRYSE--LLAMN-LLERLLLRCMEAI--------------------------PESLHPPMDPRVREACQYIS 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  161 KQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEAlpRLL---AGDSVQVVARDLGYGSTRAFSSMFR 237
Cdd:PRK10572 194 DHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRA--KLLlqtTRMPIATIGRNVGYDDQLYFSRVFK 271

                        250
                 ....*....|
gi 15599122  238 RLLGETPRDY 247
Cdd:PRK10572 272 KCTGASPSEF 281
ftrA PRK09393
transcriptional activator FtrA; Provisional
 145-247 4.97e-05

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 43.80  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  145 PMPRD--RRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLA-GDSVQVVA 221
Cdd:PRK09393 211 PVASResDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESsALSIDQIA 290

                         90       100
                 ....*....|....*....|....*.
gi 15599122  222 RDLGYGSTRAFSSMFRRLLGETPRDY 247
Cdd:PRK09393 291 ERAGFGSEESLRHHFRRRAATSPAAY 316
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
146-247 1.53e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 40.29  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122  146 MPRDRRLQAICQALLKQPELGLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGDS-VQVVARDL 224
Cdd:PRK10219   1 MSHQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERpIFDIAMDL 80

                         90       100
                 ....*....|....*....|...
gi 15599122  225 GYGSTRAFSSMFRRLLGETPRDY 247
Cdd:PRK10219  81 GYVSQQTFSRVFRRQFDRTPSDY 103
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
179-254 9.46e-04

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 39.66  E-value: 9.46e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15599122  179 SSRTLARLFAQELQMSFHEWRQQLRLTEALPRLLAGD-SVQVVARDLGYGSTRAFSSMFRRLLGETPRDY-LGRLEQL 254
Cdd:PRK13503 200 SLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDaSVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIrQGRDGFL 277
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 21-90 1.13e-03

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 37.66  E-value: 1.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599122  21 GHHLGRHFHPQA-QFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQPETPTP 90
Cdd:cd06991  29 GERVSEHYHPYSeEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLVFHLSPLAPRP 99
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 27-82 2.72e-03

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 37.70  E-value: 2.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15599122   27 HFHPQ---AQFLYA--ARGLMRLATHHG-AWVIP--PTRAVWIPPRVEHEIFMSGEVHMRTLFI 82
Cdd:PRK04190  90 HFHAKadrAEIYYGlkGKGLMLLQDPEGeARWIEmePGTVVYVPPYWAHRSVNTGDEPLVFLAC 153
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 166-200 3.58e-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: 34.44  E-value: 3.58e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15599122   166 GLTLDDWGLRVGASSRTLARLFAQELQMSFHEWRQ 200
Cdd:pfam00165   8 NLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 11-130 5.01e-03

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 36.26  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599122    11 LAAISLDFPDgHHLGRHFHPQAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIfmsgevhmrtlfieQPETPTP 90
Cdd:pfam02311   4 LEGIEARYPG-HSFPPHVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDY--------------EPESEDG 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15599122    91 LSDCCVL----AVTPLLREMILRAIHLESQPRLDDFCQRLQGLI 130
Cdd:pfam02311  69 WRYRWLYfepeLLERILADISILAGGPLPLLRDPELAALLRALF 112
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 16-82 5.38e-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: 5.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599122  16 LDFPDGHHLGRHFHP-QAQFLYAARGLMRLATHHGAWV-IPPTRAVWIPPRVEHEIFMSGEVHMRTLFI 82
Cdd:cd02208   4 VTLPPGTSSPPHWHPeQDEIFYVLSGEGELTLDDGETVeLKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
18-87 6.63e-03

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 35.50  E-value: 6.63e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599122  18 FPDGHHLGRHFHP-QAQFLYAARGLMRLATHHGAWVIPPTRAVWIPPRVEHEIFMSGEVHMRTLFIEQPET 87
Cdd:COG0662  34 VPPGAELSLHVHPhRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQAPAY 104
 
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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