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Conserved domains on  [gi|409029277|gb|AFV07179|]
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glyceraldehyde 3 phosphate dehydrogenase, partial [Cortinarius aff. salmoneobasis 2 FS-2012]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1000016)

type I glyceraldehyde-3-phosphate dehydrogenase is responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02272 super family cl30355
glyceraldehyde-3-phosphate dehydrogenase
 1-156 1.87e-85

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 256.32  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSST 79
Cdd:PLN02272 215 VVGVNEKTYKPNMNIvSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSST 294

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PLN02272 295 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVG 371
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-156 1.87e-85

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 256.32  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSST 79
Cdd:PLN02272 215 VVGVNEKTYKPNMNIvSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSST 294

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PLN02272 295 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVG 371
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-156 4.42e-84

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 249.93  E-value: 4.42e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSST 79
Cdd:COG0057  132 VYGVNHDDYDADHRIiSNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTST 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:COG0057  211 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNG 287
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 20-156 9.73e-84

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 243.13  E-value: 9.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  20 CTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSnKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGL 99
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277 100 AFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVG 136
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-156 5.92e-79

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 236.79  E-value: 5.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277    1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSST 79
Cdd:TIGR01534 131 VYGVNHDEYDGEERIiSNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTST 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277   80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIG 286
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 25-156 3.27e-65

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 195.89  E-value: 3.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   25 LAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGLAFRVP 104
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 409029277  105 TLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIG 132
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-156 3.89e-46

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 152.78  E-value: 3.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQ--ISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSS 78
Cdd:NF033735 128 VYGVNDHLYDPARHriVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTT 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:NF033735 207 TGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVN 284
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-156 1.87e-85

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 256.32  E-value: 1.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSST 79
Cdd:PLN02272 215 VVGVNEKTYKPNMNIvSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSST 294

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PLN02272 295 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVG 371
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-156 4.42e-84

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 249.93  E-value: 4.42e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSST 79
Cdd:COG0057  132 VYGVNHDDYDADHRIiSNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTST 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:COG0057  211 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNG 287
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 20-156 9.73e-84

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 243.13  E-value: 9.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  20 CTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSnKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGL 99
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277 100 AFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVG 136
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-156 5.92e-79

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 236.79  E-value: 5.92e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277    1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSST 79
Cdd:TIGR01534 131 VYGVNHDEYDGEERIiSNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTST 209

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277   80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIG 286
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-155 9.13e-75

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 226.64  E-value: 9.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSN--KDWRGGRSVNNNIIPS 77
Cdd:PTZ00023 132 VMGVNHTQYDKSQRIvSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPA 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409029277  78 STGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFI 155
Cdd:PTZ00023 212 STGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFV 289
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-156 6.71e-70

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 213.83  E-value: 6.71e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSSTG 80
Cdd:PRK15425 131 VKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTG 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409029277  81 AAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PRK15425 211 AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNG 286
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-156 8.09e-69

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 211.50  E-value: 8.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSST 79
Cdd:PLN02358 136 VVGVNEHEYKSDLDIvSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSST 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PLN02358 216 GAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVG 292
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 25-156 3.27e-65

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 195.89  E-value: 3.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   25 LAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGLAFRVP 104
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 409029277  105 TLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIG 132
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 20-156 9.89e-61

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 185.13  E-value: 9.89e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  20 CTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGL 99
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277 100 AFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGeyKGIVDYTEDSVVSTDFIG 156
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRG 135
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-155 1.46e-59

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 188.34  E-value: 1.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPK--YQISNASCTTNCLAPLAKII-HDNFGIVEGLMTTVHATTATQKTVDGPSNKDWRGGRSVNNNIIPS 77
Cdd:PTZ00434 146 VMGVNQHEYSPTehHVVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPS 225

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409029277  78 STGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFI 155
Cdd:PTZ00434 226 TTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFI 303
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-154 1.95e-56

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 179.93  E-value: 1.95e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQ--ISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSS 78
Cdd:PRK07729 131 VVGVNEDQLDIEKHtiISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTT 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:PRK07729 210 TGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDF 285
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-157 1.47e-51

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 167.01  E-value: 1.47e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYD-PKYQ-ISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGpSNKDWRGGRSVNNNIIPSS 78
Cdd:PRK07403 133 VVGVNHHEYDhEDHNiISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTS 211

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIGH 157
Cdd:PRK07403 212 TGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGT 290
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-156 3.89e-46

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 152.78  E-value: 3.89e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQ--ISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSS 78
Cdd:NF033735 128 VYGVNDHLYDPARHriVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTT 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:NF033735 207 TGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVN 284
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-154 2.21e-42

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 144.69  E-value: 2.21e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGpSNKDWRGGRSVNNNIIPSST 79
Cdd:PLN03096 192 VVGVNADDYKHSDPIiSNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTST 270

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:PLN03096 271 GAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDF 345
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-154 4.37e-42

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 142.56  E-value: 4.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDP-KYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPsNKDWRGGRSVNNNIIPSS 78
Cdd:PRK08955 131 VMGVNDHLFDPaIHPIvTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTT 209

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:PRK08955 210 TGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDY 285
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-154 6.70e-42

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 144.66  E-value: 6.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQ--ISNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGpSNKDWRGGRSVNNNIIPSS 78
Cdd:PLN02237 208 VVGVNEDDYDHEVAniVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTS 286

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 409029277  79 TGAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPA-TYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:PLN02237 287 TGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDF 363
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-156 6.15e-36

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 129.27  E-value: 6.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDwRGGRSVNNNIIPSST 79
Cdd:PRK08289 269 VHGVNHSDITDEDKIvSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITET 347

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKAS-QGEYKGIVDYTEDS-VVSTDFIG 156
Cdd:PRK08289 348 GAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVG 426
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 20-156 8.20e-35

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 119.16  E-value: 8.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  20 CTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSNKDWrgGRSVNNNIIPSSTGAAKAVGKVIPSLN--GKLT 97
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 409029277  98 GLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVG 137
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-154 2.27e-33

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 119.78  E-value: 2.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277   1 VCGVNLDAYDPKYQI-SNASCTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGpSNKDWRGGRSVNNNIIPSST 79
Cdd:PRK13535 134 VYGVNHDQLRAEHRIvSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDT 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 409029277  80 GAAKAVGKVIPSLNGKLTGLAFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:PRK13535 213 KLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDF 287
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 20-154 5.13e-33

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 114.43  E-value: 5.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  20 CTTNCLAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGpSNKDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGL 99
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 409029277 100 AFRVPTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDF 154
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDF 134
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 25-156 3.02e-16

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 74.14  E-value: 3.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 409029277  25 LAPLAKIIHDNFGIVEGLMTTVHATTATQKTVDGPSN-KDWRGGRSVNNNIIPSSTGAAKAVGKVIPSLNGKLTGLAFRV 103
Cdd:PTZ00353 158 LAPVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKNsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQV 237

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 409029277 104 PTLDVSVVDLVVRTEKPATYQQIKDVVKKASQGEYKGIVDYTEDSVVSTDFIG 156
Cdd:PTZ00353 238 PVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIP 290
 
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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