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Conserved domains on  [gi|1622939069|ref|XP_028704207|]
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O-phosphoseryl-tRNA(Sec) selenium transferase isoform X2 [Macaca mulatta]

Protein Classification

O-phosphoseryl-tRNA(Sec) selenium transferase( domain architecture ID 10022574)

O-phosphoseryl-tRNA(Sec) selenium transferase converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
selenium_SpcS TIGR03531
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ...
1-398 0e+00

O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation]


:

Pssm-ID: 211833  Cd Length: 444  Bit Score: 738.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069   1 MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV 80
Cdd:TIGR03531  50 MDTNNFPNNVGVGEREGRVFSKLVARRHYRFCHGIGRSGDLVAPQPKAAGSSLLYKLTNKLVKDFLKLLGLRSIKSAFVV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069  81 PMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDYILCI 160
Cdd:TIGR03531 130 PLATGMSLSLCLSALRHKRPKAKYVIWPRIDQKSCIKAISTAGFEPRVIETVLDGDELTTDVEDIERAIEEIGPDNILCV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 161 HSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND 240
Cdd:TIGR03531 210 LSTTSCFAPRSPDDIEEIAKICANYDIPHIVNNAYGLQSNKYMELINKAIKVGRVDAVVSSTDKNFMVPVGGAIIYSFDE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 241 SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL 320
Cdd:TIGR03531 290 NFIQEISKSYPGRASASPSLDVLITLLSLGSKGYLELLKERKEMYKYLKELLQKLAERHGERLLDTPENPISSAMTLSTL 369
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622939069 321 DEHhdeAVTQLGSMLFTRQVSGARVVPLGSVQTVSGYTFRGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDKCL 398
Cdd:TIGR03531 370 KGK---DPTMLGSMLYSRRVTGPRVVTNGDSKTVGGCEFKGYGSHTSNYPCPYITAAAAIGMTKEDVDTFVSRLEKSL 444
 
Name Accession Description Interval E-value
selenium_SpcS TIGR03531
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ...
1-398 0e+00

O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 211833  Cd Length: 444  Bit Score: 738.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069   1 MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV 80
Cdd:TIGR03531  50 MDTNNFPNNVGVGEREGRVFSKLVARRHYRFCHGIGRSGDLVAPQPKAAGSSLLYKLTNKLVKDFLKLLGLRSIKSAFVV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069  81 PMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDYILCI 160
Cdd:TIGR03531 130 PLATGMSLSLCLSALRHKRPKAKYVIWPRIDQKSCIKAISTAGFEPRVIETVLDGDELTTDVEDIERAIEEIGPDNILCV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 161 HSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND 240
Cdd:TIGR03531 210 LSTTSCFAPRSPDDIEEIAKICANYDIPHIVNNAYGLQSNKYMELINKAIKVGRVDAVVSSTDKNFMVPVGGAIIYSFDE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 241 SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL 320
Cdd:TIGR03531 290 NFIQEISKSYPGRASASPSLDVLITLLSLGSKGYLELLKERKEMYKYLKELLQKLAERHGERLLDTPENPISSAMTLSTL 369
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622939069 321 DEHhdeAVTQLGSMLFTRQVSGARVVPLGSVQTVSGYTFRGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDKCL 398
Cdd:TIGR03531 370 KGK---DPTMLGSMLYSRRVTGPRVVTNGDSKTVGGCEFKGYGSHTSNYPCPYITAAAAIGMTKEDVDTFVSRLEKSL 444
SepSecS pfam05889
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ...
1-399 0e+00

O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes.


Pssm-ID: 399111  Cd Length: 389  Bit Score: 619.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069   1 MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV 80
Cdd:pfam05889   1 MDTNNDPDTVGIGEREGRVLTELVTRPHFDFIHGIGRSGNLLDPQPKALGSSVLAKLTNELVKDFLKLLGLREVKNCFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069  81 PMATGMSLTLCFLTLRhKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDYILCI 160
Cdd:pfam05889  81 PLATGMSLALCLSALR-KRPKAKYVIWPRIDQKSSIKAAERAGFEPRLVETVLDGDYLITDVNDVETIIEEKGEEVILAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 161 HSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND 240
Cdd:pfam05889 160 LSTTSCFAPRSPDNVKEIAKICAEYDVPHLVNGAYGIQSEEYIRKIAAAHKCGRVDAVVQSLDKNFIVPVGGAIIAAFDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 241 SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL 320
Cdd:pfam05889 240 SFIQEISEEYPGRASARPSKDKLISLLSLGCKAYLALMKEQKEMFPLLRELLKDLAEEVGEQLLDVPHNPISSAMTLETL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 321 DEHHDEAVTQLGSMLFTRQVSGARVV-PLGSVQTvsgytfrgfmSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDKCLK 399
Cdd:pfam05889 320 DEISKKGRTDLGSELFSRRVTGARGVrSSDPFGT----------SHTTEYHGRYLNIASAIGMKDEDVDYVIERLDEILE 389
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
122-235 4.55e-04

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 40.83  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 122 AGFEPVVIeNVLEGDELRTDLKAVEAKvqeLGPDYILCIHSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAY-GVQSS 200
Cdd:cd01494    62 AGAKPVPV-PVDDAGYGGLDVAILEEL---KAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASaGGASP 137
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622939069 201 KCMHLIqqgaRVGRIDAFVQSLDKNFMVPVGGAII 235
Cdd:cd01494   138 APGVLI----PEGGADVVTFSLHKNLGGEGGGVVI 168
 
Name Accession Description Interval E-value
selenium_SpcS TIGR03531
O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion ...
1-398 0e+00

O-phosphoseryl-tRNA(Sec) selenium transferase; In the archaea and eukaryotes, the conversion of the mischarged serine to selenocysteine (Sec) on its tRNA is accomplished in two steps. This enzyme, O-phosphoseryl-tRNA(Sec) selenium transferase, acts second, after a phosphophorylation step catalyzed by a homolog of the bacterial SelA protein. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 211833  Cd Length: 444  Bit Score: 738.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069   1 MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV 80
Cdd:TIGR03531  50 MDTNNFPNNVGVGEREGRVFSKLVARRHYRFCHGIGRSGDLVAPQPKAAGSSLLYKLTNKLVKDFLKLLGLRSIKSAFVV 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069  81 PMATGMSLTLCFLTLRHKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDYILCI 160
Cdd:TIGR03531 130 PLATGMSLSLCLSALRHKRPKAKYVIWPRIDQKSCIKAISTAGFEPRVIETVLDGDELTTDVEDIERAIEEIGPDNILCV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 161 HSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND 240
Cdd:TIGR03531 210 LSTTSCFAPRSPDDIEEIAKICANYDIPHIVNNAYGLQSNKYMELINKAIKVGRVDAVVSSTDKNFMVPVGGAIIYSFDE 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 241 SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL 320
Cdd:TIGR03531 290 NFIQEISKSYPGRASASPSLDVLITLLSLGSKGYLELLKERKEMYKYLKELLQKLAERHGERLLDTPENPISSAMTLSTL 369
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622939069 321 DEHhdeAVTQLGSMLFTRQVSGARVVPLGSVQTVSGYTFRGFMSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDKCL 398
Cdd:TIGR03531 370 KGK---DPTMLGSMLYSRRVTGPRVVTNGDSKTVGGCEFKGYGSHTSNYPCPYITAAAAIGMTKEDVDTFVSRLEKSL 444
SepSecS pfam05889
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ...
1-399 0e+00

O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes.


Pssm-ID: 399111  Cd Length: 389  Bit Score: 619.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069   1 MDSNNFLGNCGVGEREGRVASALVARRHYRFIHGIGRSGDISAVQPKAAGSSLLNKITNSLVLDIIKLAGVHTVANCFVV 80
Cdd:pfam05889   1 MDTNNDPDTVGIGEREGRVLTELVTRPHFDFIHGIGRSGNLLDPQPKALGSSVLAKLTNELVKDFLKLLGLREVKNCFVV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069  81 PMATGMSLTLCFLTLRhKRPKAKYIIWPRIDQKSCFKSMITAGFEPVVIENVLEGDELRTDLKAVEAKVQELGPDYILCI 160
Cdd:pfam05889  81 PLATGMSLALCLSALR-KRPKAKYVIWPRIDQKSSIKAAERAGFEPRLVETVLDGDYLITDVNDVETIIEEKGEEVILAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 161 HSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAYGVQSSKCMHLIQQGARVGRIDAFVQSLDKNFMVPVGGAIIAGFND 240
Cdd:pfam05889 160 LSTTSCFAPRSPDNVKEIAKICAEYDVPHLVNGAYGIQSEEYIRKIAAAHKCGRVDAVVQSLDKNFIVPVGGAIIAAFDE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 241 SFIQEISKMYPGRASASPSLDVLITLLSLGSNGYKKLLKERKEMFSYLSNQIKKLSEAYNERLLHTPHNPISLAMTLKTL 320
Cdd:pfam05889 240 SFIQEISEEYPGRASARPSKDKLISLLSLGCKAYLALMKEQKEMFPLLRELLKDLAEEVGEQLLDVPHNPISSAMTLETL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 321 DEHHDEAVTQLGSMLFTRQVSGARVV-PLGSVQTvsgytfrgfmSHTNNYPCAYLNAASAIGMKMQDVDLFIKRLDKCLK 399
Cdd:pfam05889 320 DEISKKGRTDLGSELFSRRVTGARGVrSSDPFGT----------SHTTEYHGRYLNIASAIGMKDEDVDYVIERLDEILE 389
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
122-235 4.55e-04

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 40.83  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 122 AGFEPVVIeNVLEGDELRTDLKAVEAKvqeLGPDYILCIHSTTSCFAPRVPDRLEELAVICANYGIPHIVNNAY-GVQSS 200
Cdd:cd01494    62 AGAKPVPV-PVDDAGYGGLDVAILEEL---KAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASaGGASP 137
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622939069 201 KCMHLIqqgaRVGRIDAFVQSLDKNFMVPVGGAII 235
Cdd:cd01494   138 APGVLI----PEGGADVVTFSLHKNLGGEGGGVVI 168
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
114-295 1.42e-03

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 40.79  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 114 SCFKSMIT-AGFEPVVIEnVLEGDELRTDLKAVEAKVQElGPDYILCI--HSTTSCFAPRvpDRLEELAVICANYGIPHI 190
Cdd:cd00609    94 PGYEAAARlAGAEVVPVP-LDEEGGFLLDLELLEAAKTP-KTKLLYLNnpNNPTGAVLSE--EELEELAELAKKHGILII 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939069 191 VNNAYG--VQSSKCMHLIQQGARVGRIdAFVQSLDKNFMVP---VGGAIIAgfNDSFIQEISKMYPGRASASPSLD--VL 263
Cdd:cd00609   170 SDEAYAelVYDGEPPPALALLDAYERV-IVLRSFSKTFGLPglrIGYLIAP--PEELLERLKKLLPYTTSGPSTLSqaAA 246
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622939069 264 ITLLSLGSNGYKKLLKERKEMFSYLSNQIKKL 295
Cdd:cd00609   247 AAALDDGEEHLEELRERYRRRRDALLEALKEL 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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