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Conserved domains on  [gi|674751981|gb|AIL28227|]
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tryptophan synthase subunit B, partial [Burkholderia cenocepacia]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 1-100 4.78e-74

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


The actual alignment was detected with superfamily member PRK04346:

Pssm-ID: 444852  Cd Length: 397  Bit Score: 223.79  E-value: 4.78e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PRK04346 191 IGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKH 270

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PRK04346 271 AATLTKGRPGVLHGAKTYLL 290
 
Name Accession Description Interval E-value
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 1-100 4.78e-74

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 223.79  E-value: 4.78e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PRK04346 191 IGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKH 270

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PRK04346 271 AATLTKGRPGVLHGAKTYLL 290
TrpB COG0133
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ...
 1-100 2.44e-73

Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439903  Cd Length: 400  Bit Score: 222.22  E-value: 2.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:COG0133  194 IGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLETGEH 273

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:COG0133  274 AATLTKGRPGVLHGARTYLL 293
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 1-100 5.41e-60

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 186.97  E-value: 5.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:cd06446  167 LGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETGGH 246

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:cd06446  247 AAYLFGGTAGVLHGLKMYTL 266
trpB TIGR00263
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ...
 1-100 3.84e-56

tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 272987  Cd Length: 385  Bit Score: 177.55  E-value: 3.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981    1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:TIGR00263 183 LGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFIDDPSVQLIGVEAGGLGIDTHKH 262

                          90       100
                  ....*....|....*....|
gi 674751981   81 AASLIAGSPGVLHGNRTYLL 100
Cdd:TIGR00263 263 AATLSKGSPGVLHGMKTYLL 282
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 18-72 4.61e-04

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 37.29  E-value: 4.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 674751981   18 QRVIGDECKVQMpelaGRQPDAVIACVGGGSNAMGIFYPYID-DTSVQLIGVEAAG 72
Cdd:pfam00291 143 YGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLKElGPDVRVIGVEPEG 194
 
Name Accession Description Interval E-value
PRK04346 PRK04346
tryptophan synthase subunit beta; Validated
 1-100 4.78e-74

tryptophan synthase subunit beta; Validated


Pssm-ID: 235288  Cd Length: 397  Bit Score: 223.79  E-value: 4.78e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PRK04346 191 IGSVAGPHPYPTMVRDFQSVIGEEAKAQILEKEGRLPDAVVACVGGGSNAIGIFHPFIDDESVRLIGVEAAGKGLETGKH 270

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PRK04346 271 AATLTKGRPGVLHGAKTYLL 290
TrpB COG0133
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ...
 1-100 2.44e-73

Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439903  Cd Length: 400  Bit Score: 222.22  E-value: 2.44e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:COG0133  194 IGSVVGPHPYPMMVRDFQSVIGREAREQILEKEGRLPDAVVACVGGGSNAIGIFYPFLDDESVRLIGVEAGGKGLETGEH 273

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:COG0133  274 AATLTKGRPGVLHGARTYLL 293
Trp-synth_B cd06446
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ...
 1-100 5.41e-60

Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.


Pssm-ID: 107207  Cd Length: 365  Bit Score: 186.97  E-value: 5.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:cd06446  167 LGSVVGPHPYPNMVRDFQSVIGEEAKKQILEKEGELPDVVIACVGGGSNAAGLFYPFINDKDVKLIGVEAGGCGLETGGH 246

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:cd06446  247 AAYLFGGTAGVLHGLKMYTL 266
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 1-100 2.33e-56

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 183.09  E-value: 2.33e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PRK13803 403 IGSAVGPHPYPEMVAYFQSVIGEEAKEQLKEQTGKLPDAIIACVGGGSNAIGIFYHFLDDPSVKLIGVEAGGKGVNTGEH 482

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PRK13803 483 AATIKKGRKGVLHGSMTYLM 502
trpB TIGR00263
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ...
 1-100 3.84e-56

tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 272987  Cd Length: 385  Bit Score: 177.55  E-value: 3.84e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981    1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:TIGR00263 183 LGSAVGPHPFPTMVRDFQSVIGEEAKEQILEQEGRLPDAVIACVGGGSNAIGIFYAFIDDPSVQLIGVEAGGLGIDTHKH 262

                          90       100
                  ....*....|....*....|
gi 674751981   81 AASLIAGSPGVLHGNRTYLL 100
Cdd:TIGR00263 263 AATLSKGSPGVLHGMKTYLL 282
PRK13028 PRK13028
tryptophan synthase subunit beta; Provisional
 1-100 7.02e-56

tryptophan synthase subunit beta; Provisional


Pssm-ID: 183851  Cd Length: 402  Bit Score: 177.37  E-value: 7.02e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PRK13028 195 IGSVVGPHPFPMMVRDFQSVIGEEAREQFLEMTGRLPDAVVACVGGGSNAIGLFSAFLDDESVRLVGVEPAGRGLDLGEH 274

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PRK13028 275 AATLTLGKPGVIHGFKSYVL 294
PLN02618 PLN02618
tryptophan synthase, beta chain
 1-100 2.35e-50

tryptophan synthase, beta chain


Pssm-ID: 215333  Cd Length: 410  Bit Score: 163.39  E-value: 2.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAGRQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGHH 80
Cdd:PLN02618 204 LGSVAGPHPYPMMVRDFHSVIGKETRRQAMEKWGGKPDVLVACVGGGSNAMGLFHEFIDDEDVRLIGVEAAGFGLDSGKH 283

                         90       100
                 ....*....|....*....|
gi 674751981  81 AASLIAGSPGVLHGNRTYLL 100
Cdd:PLN02618 284 AATLTKGEVGVLHGAMSYLL 303
PRK13802 PRK13802
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
 1-100 4.84e-34

bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 184335 [Multi-domain]  Cd Length: 695  Bit Score: 122.83  E-value: 4.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981   1 IGTVAGPHPYPMMVRDFQRVIGDECKVQMPELAG-RQPDAVIACVGGGSNAMGIFYPYIDDTSVQLIGVEAAGDGLDTGH 79
Cdd:PRK13802 464 LGTVAGPHPFPAMVRDFQKIIGEEAKQQLQDWYGiDHPDAICACVGGGSNAIGVMNAFLDDERVNLYGYEAGGNGPESGK 543

                         90       100
                 ....*....|....*....|...
gi 674751981  80 HAASLIAGSP--GVLHGNRTYLL 100
Cdd:PRK13802 544 HAIRFAPGTGelGMFQGAKSYLL 566
PRK12391 PRK12391
TrpB-like pyridoxal phosphate-dependent enzyme;
17-71 1.15e-14

TrpB-like pyridoxal phosphate-dependent enzyme;


Pssm-ID: 237087  Cd Length: 427  Bit Score: 67.51  E-value: 1.15e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 674751981  17 FQRVIGDECKVQMpELAGRQPDAVIACVGGGSNAMGIFYPYIDD-----TSVQLIGVEAA 71
Cdd:PRK12391 235 HQTVIGLEAKKQL-ELAGEYPDVVIGCVGGGSNFAGLAFPFLGDklegkKDTRFIAVEPA 293
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 7-70 3.81e-12

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 59.84  E-value: 3.81e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674751981   7 PHPY-PMMVRDFQRVIGDECKVQMPelaGRQPDAVIACVGGGSNAMGIFYPYIDDT-SVQLIGVEA 70
Cdd:cd00640  126 VNQFdNPANIAGQGTIGLEILEQLG---GQKPDAVVVPVGGGGNIAGIARALKELLpNVKVIGVEP 188
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 18-72 4.61e-04

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 37.29  E-value: 4.61e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 674751981   18 QRVIGDECKVQMpelaGRQPDAVIACVGGGSNAMGIFYPYID-DTSVQLIGVEAAG 72
Cdd:pfam00291 143 YGTIGLEILEQL----GGDPDAVVVPVGGGGLIAGIARGLKElGPDVRVIGVEPEG 194
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 28-89 3.51e-03

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 34.77  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674751981  28 QMPELagrqpDAVIACVGGGSNAMGI------FYPyiddtSVQLIGVEAAG-DGLdtghhAASLIAGSP 89
Cdd:cd01562  162 QVPDL-----DAVFVPVGGGGLIAGIatavkaLSP-----NTKVIGVEPEGaPAM-----AQSLAAGKP 215
 
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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