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Conserved domains on  [gi|1709669569|gb|TTN83631|]
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AraC family transcriptional regulator [Klebsiella quasivariicola]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 13722860)

AraC family transcriptional regulator contains a helix-turn-helix DNA-binding motif and controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

Gene Ontology:  GO:0003700|GO:0006355|GO:0043565

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AraC_N pfam06719
AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of ...
 26-174 7.81e-49

AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of bacterial ARAC-type transcriptional regulators. In E. coli, these regulate the L-arabinose operon through sensing the presence of arabinose, and when the sugar is present, transmitting this information from the arabinose-binding domains to the protein's DNA-binding domains. This family might represent the N-terminal arm of the protein, which binds to the C-terminal DNA binding domains to hold them in a state where the protein prefers to loop and remain non-activating. All family members contain the pfam00165 domain.


:

Pssm-ID: 461994  Cd Length: 152  Bit Score: 159.20  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  26 PVPGITLVRALHPGDLQAAIARPLVAMLLQGRKQVTTGLTSFDYGPGEAMVIAADVPTTSQITEASQRFPYYALVLELDM 105
Cdd:pfam06719   1 AIPGLTLFRTSEPTEPTPVVYEPSLCIVAQGAKRVHLGDETYEYDPGEYLVVSVDLPVTGEVTEASPEEPYLGLALDLDP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709669569 106 AILREL--QEAGPSGPDEAPR-VGIEPMNADVTDAAYRLARLFDQPGALAVLGEGLRRELHYWLLQSVHGPA 174
Cdd:pfam06719  81 ALLAELllEAPPPGPPPRAGRgLAVSPLDEELLDAVLRLLRLLDTPEDIPVLAPLILREILYRLLTGPQGAR 152
GlxA super family cl34854
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 175-287 1.25e-24

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


The actual alignment was detected with superfamily member COG4977:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 100.62  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 175 IRALGAVDSHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSI 254
Cdd:COG4977   199 SPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSI 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709669569 255 AQAAGEVGYISVSQFTREYARLYGAPPGRDRRR 287
Cdd:COG4977   279 EEIAAACGFGSASHFRRAFRRRFGVSPSAYRRR 311
 
Name Accession Description Interval E-value
AraC_N pfam06719
AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of ...
 26-174 7.81e-49

AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of bacterial ARAC-type transcriptional regulators. In E. coli, these regulate the L-arabinose operon through sensing the presence of arabinose, and when the sugar is present, transmitting this information from the arabinose-binding domains to the protein's DNA-binding domains. This family might represent the N-terminal arm of the protein, which binds to the C-terminal DNA binding domains to hold them in a state where the protein prefers to loop and remain non-activating. All family members contain the pfam00165 domain.


Pssm-ID: 461994  Cd Length: 152  Bit Score: 159.20  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  26 PVPGITLVRALHPGDLQAAIARPLVAMLLQGRKQVTTGLTSFDYGPGEAMVIAADVPTTSQITEASQRFPYYALVLELDM 105
Cdd:pfam06719   1 AIPGLTLFRTSEPTEPTPVVYEPSLCIVAQGAKRVHLGDETYEYDPGEYLVVSVDLPVTGEVTEASPEEPYLGLALDLDP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709669569 106 AILREL--QEAGPSGPDEAPR-VGIEPMNADVTDAAYRLARLFDQPGALAVLGEGLRRELHYWLLQSVHGPA 174
Cdd:pfam06719  81 ALLAELllEAPPPGPPPRAGRgLAVSPLDEELLDAVLRLLRLLDTPEDIPVLAPLILREILYRLLTGPQGAR 152
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 175-287 1.25e-24

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: 100.62  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 175 IRALGAVDSHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSI 254
Cdd:COG4977   199 SPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSI 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709669569 255 AQAAGEVGYISVSQFTREYARLYGAPPGRDRRR 287
Cdd:COG4977   279 EEIAAACGFGSASHFRRAFRRRFGVSPSAYRRR 311
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
202-285 8.96e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.14  E-value: 8.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  202 PVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVGYISVSQFTREYARLYGAPP 281
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1709669569  282 GRDR 285
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
208-287 4.58e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.56  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 208 LADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAE-GMSIAQAAGEVGYISVSQFTREYARLYGAPPGRDRR 286
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 1709669569 287 R 287
Cdd:pfam12833  81 R 81
ftrA PRK09393
transcriptional activator FtrA; Provisional
 185-287 4.33e-13

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 68.45  E-value: 4.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 185 SARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVGYI 264
Cdd:PRK09393  217 SDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFG 296

                          90       100
                  ....*....|....*....|...
gi 1709669569 265 SVSQFTREYARLYGAPPGRDRRR 287
Cdd:PRK09393  297 SEESLRHHFRRRAATSPAAYRKR 319
 
Name Accession Description Interval E-value
AraC_N pfam06719
AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of ...
 26-174 7.81e-49

AraC-type transcriptional regulator N-terminus; This family represents the N-terminus of bacterial ARAC-type transcriptional regulators. In E. coli, these regulate the L-arabinose operon through sensing the presence of arabinose, and when the sugar is present, transmitting this information from the arabinose-binding domains to the protein's DNA-binding domains. This family might represent the N-terminal arm of the protein, which binds to the C-terminal DNA binding domains to hold them in a state where the protein prefers to loop and remain non-activating. All family members contain the pfam00165 domain.


Pssm-ID: 461994  Cd Length: 152  Bit Score: 159.20  E-value: 7.81e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  26 PVPGITLVRALHPGDLQAAIARPLVAMLLQGRKQVTTGLTSFDYGPGEAMVIAADVPTTSQITEASQRFPYYALVLELDM 105
Cdd:pfam06719   1 AIPGLTLFRTSEPTEPTPVVYEPSLCIVAQGAKRVHLGDETYEYDPGEYLVVSVDLPVTGEVTEASPEEPYLGLALDLDP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709669569 106 AILREL--QEAGPSGPDEAPR-VGIEPMNADVTDAAYRLARLFDQPGALAVLGEGLRRELHYWLLQSVHGPA 174
Cdd:pfam06719  81 ALLAELllEAPPPGPPPRAGRgLAVSPLDEELLDAVLRLLRLLDTPEDIPVLAPLILREILYRLLTGPQGAR 152
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 175-287 1.25e-24

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: 100.62  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 175 IRALGAVDSHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSI 254
Cdd:COG4977   199 SPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSI 278

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1709669569 255 AQAAGEVGYISVSQFTREYARLYGAPPGRDRRR 287
Cdd:COG4977   279 EEIAAACGFGSASHFRRAFRRRFGVSPSAYRRR 311
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
202-285 8.96e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.14  E-value: 8.96e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  202 PVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVGYISVSQFTREYARLYGAPP 281
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1709669569  282 GRDR 285
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
93-292 3.13e-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: 3.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569  93 RFPYYALVLELDMAILRELQEAGPSGPDEAPRVGIEPMNADVTDAAYRLARLFDQPGALAVLGEGLRRELHYWLLQSVHG 172
Cdd:COG2207    60 LLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 173 PAIRALGAVDSHSARIRRAVAMLRRDFMQpVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGM 252
Cdd:COG2207   140 LLLLLLLLLLLLLLLLLLLLLLLLLLLLL-LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDL 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1709669569 253 SIAQAAGEVGYISVSQFTREYARLYGAPPGRDRRREKMSA 292
Cdd:COG2207   219 SISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
208-287 4.58e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.56  E-value: 4.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 208 LADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAE-GMSIAQAAGEVGYISVSQFTREYARLYGAPPGRDRR 286
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 1709669569 287 R 287
Cdd:pfam12833  81 R 81
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 184-287 2.24e-17

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: 80.87  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 184 HSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLmLAEGMSIAQAAGEVGY 263
Cdd:COG2169    82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQL-LQTGLSVTDAAYAAGF 160

                          90       100
                  ....*....|....*....|....
gi 1709669569 264 ISVSQFTREYARLYGAPPGRDRRR 287
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAYRRG 184
ftrA PRK09393
transcriptional activator FtrA; Provisional
 185-287 4.33e-13

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 68.45  E-value: 4.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 185 SARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVGYI 264
Cdd:PRK09393  217 SDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFG 296

                          90       100
                  ....*....|....*....|...
gi 1709669569 265 SVSQFTREYARLYGAPPGRDRRR 287
Cdd:PRK09393  297 SEESLRHHFRRRAATSPAAYRKR 319
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
186-286 7.82e-09

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 55.95  E-value: 7.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 186 ARIRRAVAMLRRDfmQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRlihARRL--MLAEGMSIAQAAGEVGY 263
Cdd:PRK15435   85 DKITHACRLLEQE--TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWR---ARRLreALAKGESVTTSILNAGF 159

                          90       100
                  ....*....|....*....|...
gi 1709669569 264 ISVSQFTREYARLYGAPPGRDRR 286
Cdd:PRK15435  160 PDSSSYYRKADETLGMTAKQFRH 182
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
182-286 4.20e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 50.06  E-value: 4.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 182 DSHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEV 261
Cdd:PRK13503  167 ENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRC 246

                          90       100
                  ....*....|....*....|....*
gi 1709669569 262 GYISVSQFTREYARLYGAPPgRDRR 286
Cdd:PRK13503  247 GFGDSNHFSTLFRREFSWSP-RDIR 270
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
183-285 5.18e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 43.94  E-value: 5.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 183 SHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVG 262
Cdd:PRK13500  203 SSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECG 282

                          90       100
                  ....*....|....*....|...
gi 1709669569 263 YISVSQFTREYARLYGAPPGRDR 285
Cdd:PRK13500  283 FEDSNYFSVVFTRETGMTPSQWR 305
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 195-236 8.59e-05

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: 39.06  E-value: 8.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1709669569 195 LRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQK 236
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
181-285 8.72e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 43.12  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 181 VDSHSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGE 260
Cdd:PRK13502  171 ATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQ 250

                          90       100
                  ....*....|....*....|....*
gi 1709669569 261 VGYISVSQFTREYARLYGAPPGRDR 285
Cdd:PRK13502  251 CGFEDSNYFSVVFTRETGMTPSQWR 275
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
184-288 2.42e-04

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 41.88  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709669569 184 HSARIRRAVAMLRRDFMQPVSVDALADAAGMSVSVFHRHFRAMTTLSPLQFQKQLRLIHARRLMLAEGMSIAQAAGEVGY 263
Cdd:PRK10572  181 MDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGY 260

                          90       100
                  ....*....|....*....|....*
gi 1709669569 264 ISVSQFTREYARLYGAPPGRDRRRE 288
Cdd:PRK10572  261 DDQLYFSRVFKKCTGASPSEFRARC 285
 
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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