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Conserved domains on  [gi|18410104|ref|NP_567004|]
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tryptophan synthase alpha chain [Arabidopsis thaliana]

Protein Classification

tryptophan synthase subunit alpha( domain architecture ID 10791415)

Tryptophan synthase (TRPS) alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P).

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 63-311 2.37e-168

tryptophan synthase


:

Pssm-ID: 178201  Cd Length: 250  Bit Score: 467.22  E-value: 2.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   63 KVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCP 142
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  143 ISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYL 222
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  223 VSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLGDAKSPTEGLKELEK 302
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 18410104  303 LTKSLKSAL 311
Cdd:PLN02591 241 LAKSLKAAL 249
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 63-311 2.37e-168

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 467.22  E-value: 2.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   63 KVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCP 142
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  143 ISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYL 222
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  223 VSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLGDAKSPTEGLKELEK 302
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 18410104  303 LTKSLKSAL 311
Cdd:PLN02591 241 LAKSLKAAL 249
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 51-311 5.63e-119

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


Pssm-ID: 439929  Cd Length: 262  Bit Score: 342.43  E-value: 5.63e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  51 LADTFTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILE 130
Cdd:COG0159   3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 131 MLDKVVPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMK 210
Cdd:COG0159  83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 211 LIVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWgADGVIVGSAMVKLLGDA 290
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                       250       260
                ....*....|....*....|.
gi 18410104 291 KsPTEGLKELEKLTKSLKSAL 311
Cdd:COG0159 242 G-DDEALEALAAFVRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 65-308 1.03e-108

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 315.96  E-value: 1.03e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  65 AFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCPIS 144
Cdd:cd04724   1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 145 LFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYLVS 224
Cdd:cd04724  81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 225 SIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWgADGVIVGSAMVKLLGDAKsPTEGLKELEKLT 304
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238


                ....
gi 18410104 305 KSLK 308
Cdd:cd04724 239 ESLK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
55-311 2.06e-106

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 310.78  E-value: 2.06e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104    55 FTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDK 134
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   135 V-VPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIV 213
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   214 DASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAgWGADGVIVGSAMVKLLGD-AKS 292
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEaADG 239

                         250
                  ....*....|....*....
gi 18410104   293 PTEGLKELEKLTKSLKSAL 311
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 55-308 3.90e-99

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 291.94  E-value: 3.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104    55 FTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDK 134
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   135 VVPQ-ISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIV 213
Cdd:TIGR00262  81 VRQKhPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   214 DASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLL-GDAKS 292
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIeENLNT 240

                         250
                  ....*....|....*.
gi 18410104   293 PTEGLKELEKLTKSLK 308
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
 
Name Accession Description Interval E-value
PLN02591 PLN02591
tryptophan synthase
 63-311 2.37e-168

tryptophan synthase


Pssm-ID: 178201  Cd Length: 250  Bit Score: 467.22  E-value: 2.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   63 KVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCP 142
Cdd:PLN02591   1 KVAFIPYITAGDPDLDTTAEALRLLDACGADVIELGVPYSDPLADGPVIQAAATRALEKGTTLDSVISMLKEVAPQLSCP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  143 ISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYL 222
Cdd:PLN02591  81 IVLFTYYNPILKRGIDKFMATIKEAGVHGLVVPDLPLEETEALRAEAAKNGIELVLLTTPTTPTERMKAIAEASEGFVYL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  223 VSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLGDAKSPTEGLKELEK 302
Cdd:PLN02591 161 VSSTGVTGARASVSGRVESLLQELKEVTDKPVAVGFGISKPEHAKQIAGWGADGVIVGSAMVKALGEAKSPEEGLKRLEK 240


                 ....*....
gi 18410104  303 LTKSLKSAL 311
Cdd:PLN02591 241 LAKSLKAAL 249
trpA PRK13111
tryptophan synthase subunit alpha; Provisional
 53-311 2.09e-120

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237285  Cd Length: 258  Bit Score: 345.94  E-value: 2.09e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   53 DTFTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEML 132
Cdd:PRK13111   1 ALFAALKAEGRKALIPYITAGDPDLETSLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASLRALAAGVTLADVFELV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  133 DKV-VPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKL 211
Cdd:PRK13111  81 REIrEKDPTIPIVLMTYYNPIFQYGVERFAADAAEAGVDGLIIPDLPPEEAEELRAAAKKHGLDLIFLVAPTTTDERLKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  212 IVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGwGADGVIVGSAMVKLLGDAK 291
Cdd:PRK13111 161 IASHASGFVYYVSRAGVTGARSADAADLAELVARLKAHTDLPVAVGFGISTPEQAAAIAA-VADGVIVGSALVKIIEENP 239

                        250       260
                 ....*....|....*....|
gi 18410104  292 sptEGLKELEKLTKSLKSAL 311
Cdd:PRK13111 240 ---EALEALAAFVKELKAAL 256
TrpA COG0159
Tryptophan synthase alpha chain [Amino acid transport and metabolism]; Tryptophan synthase ...
 51-311 5.63e-119

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


Pssm-ID: 439929  Cd Length: 262  Bit Score: 342.43  E-value: 5.63e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  51 LADTFTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILE 130
Cdd:COG0159   3 IDAAFAALKAEGRKALIPYLTAGDPDLETTLEIIKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLDDVFE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 131 MLDKVVPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMK 210
Cdd:COG0159  83 LVREFREDPDTPLVLMGYYNPVFRYGVERFAADAAEAGVDGLIVPDLPPEEAEELRAAADAHGLDLIFLVAPTTSDERIK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 211 LIVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWgADGVIVGSAMVKLLGDA 290
Cdd:COG0159 163 KIAAAASGFVYYVSVTGVTGARTAVSDDLAELVARIRAHTDLPVAVGFGISTPEQAAEVAAY-ADGVIVGSALVKLIEEG 241

                       250       260
                ....*....|....*....|.
gi 18410104 291 KsPTEGLKELEKLTKSLKSAL 311
Cdd:COG0159 242 G-DDEALEALAAFVRELKAAL 261
Tryptophan_synthase_alpha cd04724
Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 ...
 65-308 1.03e-108

Ttryptophan synthase (TRPS) alpha subunit (TSA). TPRS is a bifunctional tetrameric enzyme (2 alpha and 2 beta subunits) that catalyzes the last two steps of L-tryptophan biosynthesis. Alpha and beta subunit catalyze two distinct reactions which are both strongly stimulated by the formation of the complex. The alpha subunit catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Indole is then channeled to the active site of the beta subunit, a PLP-dependent enzyme that catalyzes a replacement reaction to convert L-serine into L-tryptophan.


Pssm-ID: 240075  Cd Length: 242  Bit Score: 315.96  E-value: 1.03e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  65 AFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDKVVPQISCPIS 144
Cdd:cd04724   1 ALIPYITAGDPDLETTLEILKALVEAGADIIELGIPFSDPVADGPVIQAASERALANGVTLKDVLELVKEIRKKNTIPIV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 145 LFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIYLVS 224
Cdd:cd04724  81 LMGYYNPILQYGLERFLRDAKEAGVDGLIIPDLPPEEAEEFREAAKEYGLDLIFLVAPTTPDERIKKIAELASGFIYYVS 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 225 SIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWgADGVIVGSAMVKLLGDAKsPTEGLKELEKLT 304
Cdd:cd04724 161 RTGVTGARTELPDDLKELIKRIRKYTDLPIAVGFGISTPEQAAEVAKY-ADGVIVGSALVKIIEEGG-EEEALEALKELA 238


                ....
gi 18410104 305 KSLK 308
Cdd:cd04724 239 ESLK 242
Trp_syntA pfam00290
Tryptophan synthase alpha chain;
55-311 2.06e-106

Tryptophan synthase alpha chain;


Pssm-ID: 395227  Cd Length: 258  Bit Score: 310.78  E-value: 2.06e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104    55 FTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDK 134
Cdd:pfam00290   1 FANLKAENRAAFVPYVTAGDPDLEQSLEILKTLEKAGADAIELGVPFSDPLADGPTIQRANLRALASGVTLQSTLEMVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   135 V-VPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIV 213
Cdd:pfam00290  81 VrSKGVEVPIVLMTYYNPVLNYGIERFYALAAEAGVDGLIVPDLPPEEADSLRQAAKDHGLELVFLVAPTTSDERLKTVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   214 DASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAgWGADGVIVGSAMVKLLGD-AKS 292
Cdd:pfam00290 161 EQAEGFVYLVSRAGVTGAENAVNAQVDELVERLKKYTAVPVAVGFGISTPEHVKQAA-AGADGVIVGSALVRIIEEaADG 239

                         250
                  ....*....|....*....
gi 18410104   293 PTEGLKELEKLTKSLKSAL 311
Cdd:pfam00290 240 PEQGLARLEELAGEMKAAA 258
trpA TIGR00262
tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the ...
 55-308 3.90e-99

tryptophan synthase, alpha subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. The alpha chain is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria and plants each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The signature pattern for trpA contains three conserved acidic residues. [LIVM]-E-[LIVM]-G-x(2)-[FYC]-[ST]-[DE]-[PA]-[LIVMY]-[AGLI]-[DE]-G and this is located between residues 43-58 of the model. The Sulfolobus solfataricus trpA is known to be quite divergent from other known trpA sequences. [Amino acid biosynthesis, Aromatic amino acid family]


Pssm-ID: 161792  Cd Length: 256  Bit Score: 291.94  E-value: 3.90e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104    55 FTQLKKQGKVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILEMLDK 134
Cdd:TIGR00262   1 FETLKQRGEGAFIPFVTAGDPTLETSLEIIKTLIEAGADALELGVPFSDPLADGPTIQAADLRALRAGMTPEKCFELLKK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   135 VVPQ-ISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMKLIV 213
Cdd:TIGR00262  81 VRQKhPNIPIGLLTYYNLIFRKGVEEFYAKCKEVGVDGVLVADLPLEESGDLVEAAKKHGVKPIFLVAPNADDERLKQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   214 DASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLL-GDAKS 292
Cdd:TIGR00262 161 EKSQGFVYLVSRAGVTGARNRAASALNELVKRLKAYSAKPVLVGFGISKPEQVKQAIDAGADGVIVGSAIVKIIeENLNT 240

                         250
                  ....*....|....*.
gi 18410104   293 PTEGLKELEKLTKSLK 308
Cdd:TIGR00262 241 PEKMLQALEEFVQNLK 256
trpA CHL00200
tryptophan synthase alpha subunit; Provisional
 51-311 5.49e-98

tryptophan synthase alpha subunit; Provisional


Pssm-ID: 214394  Cd Length: 263  Bit Score: 289.36  E-value: 5.49e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   51 LADTFTQLKKQgkVAFIPYITAGDPDLSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRSLERGTNLDSILE 130
Cdd:CHL00200   4 ISNVFEKLDKQ--CALIPFITAGDPDIVITKKALKILDKKGADIIELGIPYSDPLADGPIIQEASNRALKQGINLNKILS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  131 MLDKVVPQISCPISLFTYYNPILKRGLGKFMSSIRAVGVQGLVVPDVPLEETEMLRKEALNNDIELVLLTTPTTPTERMK 210
Cdd:CHL00200  82 ILSEVNGEIKAPIVIFTYYNPVLHYGINKFIKKISQAGVKGLIIPDLPYEESDYLISVCNLYNIELILLIAPTSSKSRIQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  211 LIVDASEGFIYLVSSIGVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVK-LLGD 289
Cdd:CHL00200 162 KIARAAPGCIYLVSTTGVTGLKTELDKKLKKLIETIKKMTNKPIILGFGISTSEQIKQIKGWNINGIVIGSACVQiLLGS 241

                        250       260
                 ....*....|....*....|..
gi 18410104  290 akSPTEGLKELEKLTKSLKSAL 311
Cdd:CHL00200 242 --SPEKGLDQLSEFCKVAKKSI 261
trpA PRK13125
tryptophan synthase subunit alpha; Provisional
 65-311 1.31e-22

tryptophan synthase subunit alpha; Provisional


Pssm-ID: 237286  Cd Length: 244  Bit Score: 93.95  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104   65 AFIPYITAGDPDLSTTAEALKVLDACgSDIIELGVPYSDPLADGPVIQAAatrslERGTNLDSILEMLDKVVPQISCPIS 144
Cdd:PRK13125   5 GLVVYLTAGYPNVESFKEFIIGLVEL-VDILELGIPPKYPKYDGPVIRKS-----HRKVKGLDIWPLLEEVRKDVSVPII 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  145 LFTYYNPILKRgLGKFMSSIRAVGVQGLVVPDVPL---EETEMLRKEALNNDIELVLLTTPTTPTERMKLIVDASEGFIY 221
Cdd:PRK13125  79 LMTYLEDYVDS-LDNFLNMARDVGADGVLFPDLLIdypDDLEKYVEIIKNKGLKPVFFTSPKFPDLLIHRLSKLSPLFIY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  222 LvssiGV---TGARSSVSgkVQSLLKDIKE-ATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKLLgdaksPTEGL 297
Cdd:PRK13125 158 Y----GLrpaTGVPLPVS--VERNIKRVRNlVGNKYLVVGFGLDSPEDARDALSAGADGVVVGTAFIEEL-----EKNGV 226

                        250
                 ....*....|....
gi 18410104  298 KELEKLTKSLKSAL 311
Cdd:PRK13125 227 ESALNLLKKIRGAL 240
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 66-281 1.70e-09

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 56.44  E-value: 1.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104  66 FIPYITAGDPDlSTTAEALKVLDACGSDIIELGVPYSDPLADGPVIQAAATRslergtnldsilemldkVVPQISCPISL 145
Cdd:cd04722   1 VILALLAGGPS-GDPVELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKE-----------------VAAETDLPLGV 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 146 FTYYNPILKR--GLGKFMSSIRAVGVQ-GLVVPDVPLEETEMLRK-EALNNDIELVLLTTPTTPTERMKLIVDAsEGFIY 221
Cdd:cd04722  63 QLAINDAAAAvdIAAAAARAAGADGVEiHGAVGYLAREDLELIRElREAVPDVKVVVKLSPTGELAAAAAEEAG-VDEVG 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410104 222 LVSSIGVTGARSsVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGS 281
Cdd:cd04722 142 LGNGGGGGGGRD-AVPIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
HisA_HisF cd04723
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) ...
 241-283 1.20e-05

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase (HisA) and the cyclase subunit of imidazoleglycerol phosphate synthase (HisF). The ProFAR isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene. The Imidazole glycerol phosphate synthase (IGPS) catalyzes the fifth step of histidine biosynthesis, the formation of the imidazole ring. IGPS converts N1-(5'-phosphoribulosyl)-formimino-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to imidazole glycerol phosphate (ImGP) and 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR). This conversion involves two tightly coupled reactions in distinct active sites of IGPS. The two catalytic domains can be fused, like in fungi and plants, or peformed by a heterodimer (HisH-glutaminase and HisF-cyclase), like in bacteria.


Pssm-ID: 240074 [Multi-domain]  Cd Length: 233  Bit Score: 45.72  E-value: 1.20e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 18410104 241 SLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAM 283
Cdd:cd04723 179 ELLERLAARADIPVIAAGGVRSVEDLELLKKLGASGALVASAL 221
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
 227-282 4.94e-05

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 43.72  E-value: 4.94e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18410104 227 GVTGARSSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSA 282
Cdd:cd04729 153 GYTEETAKTEDPDFELLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGSA 208
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 242-283 1.12e-04

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 42.85  E-value: 1.12e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 18410104   242 LLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAM 283
Cdd:pfam00977 181 LTRELAEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
 241-285 1.90e-04

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 42.08  E-value: 1.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 18410104   241 SLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVK 285
Cdd:pfam00977  63 DVVEEIAEEVFIPVQVGGGIRSLEDVERLLSAGADRVIIGTAAVK 107
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 242-282 2.40e-04

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 41.56  E-value: 2.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18410104 242 LLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSA 282
Cdd:COG0106 180 LYRELAAATGIPVIASGGVSSLDDLRALKELGVEGAIVGKA 220
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
227-282 2.54e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 41.67  E-value: 2.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18410104  227 GVTGARSSVSGKVQSLLKDIKEATDKPV-AVGfGISKPEHVKQIAGWGADGVIVGSA 282
Cdd:PRK01130 149 GYTEETKKPEEPDFALLKELLKAVGCPViAEG-RINTPEQAKKALELGAHAVVVGGA 204
IGPS cd00331
Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, ...
 259-300 5.38e-04

Indole-3-glycerol phosphate synthase (IGPS); an enzyme in the tryptophan biosynthetic pathway, catalyzing the ring closure reaction of 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP) to indole-3-glycerol phosphate (IGP), accompanied by the release of carbon dioxide and water. IGPS is active as a separate monomer in most organisms, but is also found fused to other enzymes as part of a bifunctional or multifunctional enzyme involved in tryptophan biosynthesis.


Pssm-ID: 238203  Cd Length: 217  Bit Score: 40.52  E-value: 5.38e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18410104 259 GISKPEHVKQIAGWGADGVIVGSAMVKllgdAKSPTEGLKEL 300
Cdd:cd00331 180 GISTPEDVKRLAEAGADAVLIGESLMR----APDPGAALREL 217
HisA cd04732
HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase ...
 241-282 8.67e-04

HisA. Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase catalyzes the fourth step in histidine biosynthesis, an isomerisation of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR (N-(5'-phospho-D-1'-ribulosylformimino)-5-amino-1-(5''-phospho-ribosyl)-4-imidazolecarboxamide). In bacteria and archaea, ProFAR isomerase is encoded by the HisA gene.


Pssm-ID: 240083  Cd Length: 234  Bit Score: 40.16  E-value: 8.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18410104 241 SLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSA 282
Cdd:cd04732 180 ELYKELAAATGIPVIASGGVSSLDDIKALKELGVAGVIVGKA 221
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 247-300 1.52e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 39.08  E-value: 1.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18410104  247 KEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVKllgdAKSPTEGLKEL 300
Cdd:PRK04302 169 KVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVK----AKDPEAALRDL 218
PRK14024 PRK14024
phosphoribosyl isomerase A; Provisional
 242-283 1.65e-03

phosphoribosyl isomerase A; Provisional


Pssm-ID: 237589  Cd Length: 241  Bit Score: 39.17  E-value: 1.65e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 18410104  242 LLKDIKEATDKPVAVGFGISKPEHVKQIAGW---GADGVIVGSAM 283
Cdd:PRK14024 181 LLREVCARTDAPVVASGGVSSLDDLRALAELvplGVEGAIVGKAL 225
trpC PRK00278
indole-3-glycerol phosphate synthase TrpC;
259-300 2.30e-03

indole-3-glycerol phosphate synthase TrpC;


Pssm-ID: 234710  Cd Length: 260  Bit Score: 38.98  E-value: 2.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 18410104  259 GISKPEHVKQIAGWGADGVIVGSAMVKllgdAKSPTEGLKEL 300
Cdd:PRK00278 219 GIFTPEDLKRLAKAGADAVLVGESLMR----ADDPGAALREL 256
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 242-300 3.10e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 37.95  E-value: 3.10e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18410104 242 LLKDIKEATDKPVAVGFGISkPEHVKQIAGWGADGVIVGSAMVKllgdAKSPTEGLKEL 300
Cdd:cd04726 149 DLKKVKKLLGVKVAVAGGIT-PDTLPEFKKAGADIVIVGRAITG----AADPAEAAREF 202
BtpA COG0434
Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];
228-283 6.65e-03

Membrane biogenesis protein, BtpA/SgcQ family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440203  Cd Length: 268  Bit Score: 37.46  E-value: 6.65e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18410104 228 VTGARSSVSGKvQSLLKDIKEAT-DKPVAVGFGIsKPEHVKQIAGWgADGVIVGSAM 283
Cdd:COG0434 189 VSGARTGEATD-LEDLKRVKEAApDVPVLVGSGV-TPENVAELLSV-ADGAIVGSSL 242
TIGR00007 TIGR00007
phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family ...
 217-282 7.52e-03

phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; This protein family consists of HisA, phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase, the enzyme catalyzing the fourth step in histidine biosynthesis. It is closely related to the enzyme HisF for the sixth step. Examples of this enzyme in Actinobacteria have been found to be bifunctional, also possessing phosphoribosylanthranilate isomerase activity; the trusted cutoff here has now been raised to 275.0 to exclude the bifunctional group, now represented by model TIGR01919. HisA from Lactococcus lactis was reported to be inactive (MEDLINE:93322317). [Amino acid biosynthesis, Histidine family]


Pssm-ID: 272850 [Multi-domain]  Cd Length: 230  Bit Score: 37.18  E-value: 7.52e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18410104   217 EGFIYlvSSIGVTGarsSVSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSA 282
Cdd:TIGR00007 160 EGIIY--TDISRDG---TLSGPNFELTKELVKAVNVPVIASGGVSSIDDLIALKKLGVYGVIVGKA 220
HisA COG0106
Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino ...
 230-285 7.74e-03

Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase [Amino acid transport and metabolism]; Phosphoribosylformimino-5-aminoimidazole carboxamide ribonucleotide (ProFAR) isomerase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439876  Cd Length: 236  Bit Score: 37.32  E-value: 7.74e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18410104 230 GARSSvSGKVQSLLKDIKEATDKPVAVGFGISKPEHVKQIAGWGADGVIVGSAMVK 285
Cdd:COG0106  53 GAFAG-KPVNLELIEEIAKATGLPVQVGGGIRSLEDIERLLDAGASRVILGTAAVK 107
 
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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