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Conserved domains on  [gi|4557289|ref|NP_000021|]
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alanine--glyoxylate aminotransferase [Homo sapiens]

Protein Classification

alanine--glyoxylate aminotransferase family protein( domain architecture ID 10157834)

alanine--glyoxylate aminotransferase (AGAT) family protein such as AGAT, serine--glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 24-385 0e+00

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


:

Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 516.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   24 LLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG 103
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  104 ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVD 183
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  184 SVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYsRKTKPFSFYLDIKWLANFWGCDDqprMYHHT 263
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIK-KKTKPKGFYFDLLLLLKYWGEGY---SYPHT 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  264 IPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKdPALRLPTVTTVAVPAGYDWRDIVSYVIDHF 343
Cdd:cd06451 237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4557289  344 DIEIMGGLGPSTGKVLRIGLLGCnATRENVDRVTEALRAALQ 385
Cdd:cd06451 316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 24-385 0e+00

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 516.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   24 LLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG 103
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  104 ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVD 183
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  184 SVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYsRKTKPFSFYLDIKWLANFWGCDDqprMYHHT 263
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIK-KKTKPKGFYFDLLLLLKYWGEGY---SYPHT 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  264 IPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKdPALRLPTVTTVAVPAGYDWRDIVSYVIDHF 343
Cdd:cd06451 237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4557289  344 DIEIMGGLGPSTGKVLRIGLLGCnATRENVDRVTEALRAALQ 385
Cdd:cd06451 316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 24-385 1.55e-142

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 409.86  E-value: 1.55e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   24 LLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPlTLVISGSGHCALEAALVNVLEPGDSFLVG 103
Cdd:COG0075   2 LLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  104 ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPV-LLFLTHGESSTGVLQPLDGFGELCHRYKCLLLV 182
Cdd:COG0075  81 VNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIkAVAVVHNETSTGVLNPLEEIGALAKEHGALLIV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  183 DSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMysRKTKPFSFYLDIKWLANFWgcddQPRMYHH 262
Cdd:COG0075 161 DAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYW----EKGQTPY 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  263 TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDpALRLPTVTTVAVPAGYDWRDIVSYVIDH 342
Cdd:COG0075 235 TPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLKER 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4557289  343 FDIEIMGGLGPSTGKVLRIGLLGCNaTRENVDRVTEALRAALQ 385
Cdd:COG0075 314 YGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 21-368 8.23e-100

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 302.06  E-value: 8.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    21 PNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSF 100
Cdd:PLN02409   8 GRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   101 LVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQ---HKPVLLFLTHGESSTGVLQPLDGFGEL--CHR 175
Cdd:PLN02409  88 VSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCAQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   176 YKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF----YLDIKWLANFW 251
Cdd:PLN02409 168 HPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKLGTYW 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   252 GcddqprmyhHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYD 331
Cdd:PLN02409 248 P---------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGID 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 4557289   332 WRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNA 368
Cdd:PLN02409 319 SAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 25-376 1.49e-77

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 243.69  E-value: 1.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289     25 LLGPGPSNLPPRIMAAGGLQ----------MIGSMSKDMYQIMDEIKEGIQYVFQTR-NPLTLVISGSGHcALEAALVNV 93
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEYytdyngnvhrGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTE-AINLVALSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289     94 ---LEPGDSFLVGANGIWGQR--AVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAqHKPVLLFLTHGESSTGVLQPLDG 168
Cdd:pfam00266  82 grsLKPGDEIVITEMEHHANLvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    169 FGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKaLNAPPGTSLISFSDKAKKKMysRKTKPFSFYLDIKWLa 248
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    249 NFWGCDDQPRMYHH-TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPalRLPTVTTVAVP 327
Cdd:pfam00266 237 QESTFADAPWKFEAgTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557289    328 aGYDWRDIVSYVIDHfDIEIMGGL---GPS-----TGKVLRIGlLGCNATRENVDRV 376
Cdd:pfam00266 315 -GVHPHDVATLLDES-GIAVRSGHhcaQPLmvrlgLGGTVRAS-FYIYNTQEDVDRL 368
 
Name Accession Description Interval E-value
AGAT_like cd06451
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ...
 24-385 0e+00

Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.


Pssm-ID: 99744 [Multi-domain]  Cd Length: 356  Bit Score: 516.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   24 LLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSFLVG 103
Cdd:cd06451   1 LLLIPGPSNVPPRVLKAMNRPMLGHRSPEFLALMDEILEGLRYVFQTENGLTFLLSGSGTGAMEAALSNLLEPGDKVLVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  104 ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVD 183
Cdd:cd06451  81 VNGVFGDRWADMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDIKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  184 SVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYsRKTKPFSFYLDIKWLANFWGCDDqprMYHHT 263
Cdd:cd06451 161 AVSSLGGEPFRMDEWGVDVAYTGSQKALGAPPGLGPIAFSERALERIK-KKTKPKGFYFDLLLLLKYWGEGY---SYPHT 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  264 IPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKdPALRLPTVTTVAVPAGYDWRDIVSYVIDHF 343
Cdd:cd06451 237 PPVNLLYALREALDLILEEGLENRWARHRRLAKALREGLEALGLKLLAK-PELRSPTVTAVLVPEGVDGDEVVRRLMKRY 315

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 4557289  344 DIEIMGGLGPSTGKVLRIGLLGCnATRENVDRVTEALRAALQ 385
Cdd:cd06451 316 NIEIAGGLGPTAGKVFRIGHMGE-ATREDVLGVLSALEEALK 356
PucG COG0075
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ...
 24-385 1.55e-142

Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439845 [Multi-domain]  Cd Length: 376  Bit Score: 409.86  E-value: 1.55e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   24 LLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPlTLVISGSGHCALEAALVNVLEPGDSFLVG 103
Cdd:COG0075   2 LLLTPGPTPVPPRVLRAMARPMIGHRDPEFVELMDEVRELLKKVFGTEND-VVILTGSGTGAMEAALANLVSPGDKVLVL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  104 ANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPV-LLFLTHGESSTGVLQPLDGFGELCHRYKCLLLV 182
Cdd:COG0075  81 VNGAFGERWAEIAERYGAEVVVLEVPWGEAVDPEEVEEALAADPDIkAVAVVHNETSTGVLNPLEEIGALAKEHGALLIV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  183 DSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMysRKTKPFSFYLDIKWLANFWgcddQPRMYHH 262
Cdd:COG0075 161 DAVSSLGGVPLDMDEWGIDVVVSGSQKCLMLPPGLAFVAVSERALEAI--EARKLPSYYLDLKLWLKYW----EKGQTPY 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  263 TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDpALRLPTVTTVAVPAGYDWRDIVSYVIDH 342
Cdd:COG0075 235 TPPVSLLYALREALDLILEEGLENRFARHRRLAEALRAGLEALGLELFAEE-EYRSPTVTAVRVPEGVDAAALRKRLKER 313

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 4557289  343 FDIEIMGGLGPSTGKVLRIGLLGCNaTRENVDRVTEALRAALQ 385
Cdd:COG0075 314 YGIEIAGGLGPLKGKIFRIGHMGYV-NPEDVLRTLAALEEALR 355
PLN02409 PLN02409
serine--glyoxylate aminotransaminase
 21-368 8.23e-100

serine--glyoxylate aminotransaminase


Pssm-ID: 178031 [Multi-domain]  Cd Length: 401  Bit Score: 302.06  E-value: 8.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    21 PNQLLLGPGPSNLPPRIMAAGGLQMIGSMSKDMYQIMDEIKEGIQYVFQTRNPLTLVISGSGHCALEAALVNVLEPGDSF 100
Cdd:PLN02409   8 GRNHLFVPGPVNIPERVLRAMNRPNEDHRSPAFPALTKELLEDVKYIFKTKSGTPFIFPTTGTGAWESALTNTLSPGDKV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   101 LVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQ---HKPVLLFLTHGESSTGVLQPLDGFGEL--CHR 175
Cdd:PLN02409  88 VSFRIGQFSLLWIDQMQRLNFDVDVVESPWGQGADLDILKSKLRQdtnHKIKAVCVVHNETSTGVTNDLAGVRKLldCAQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   176 YKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGTSLISFSDKAKKKMYSRKTKPFSF----YLDIKWLANFW 251
Cdd:PLN02409 168 HPALLLVDGVSSIGALDFRMDEWGVDVALTGSQKALSLPTGLGIVCASPKALEASKTAKSPRVFFdwadYLKFYKLGTYW 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   252 GcddqprmyhHTIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPALRLPTVTTVAVPAGYD 331
Cdd:PLN02409 248 P---------YTPSIQLLYGLRAALDLIFEEGLENVIARHARLGEATRLAVEAWGLKLCTKKPEWRSDTVTAVVVPEGID 318

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 4557289   332 WRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCNA 368
Cdd:PLN02409 319 SAEIVKNAWKKYNLSLGLGLNKVAGKVFRIGHLGNVN 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 25-376 1.49e-77

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 243.69  E-value: 1.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289     25 LLGPGPSNLPPRIMAAGGLQ----------MIGSMSKDMYQIMDEIKEGIQYVFQTR-NPLTLVISGSGHcALEAALVNV 93
Cdd:pfam00266   3 LDSAATTQKPQEVLDAIQEYytdyngnvhrGVHTLGKEATQAYEEAREKVAEFINAPsNDEIIFTSGTTE-AINLVALSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289     94 ---LEPGDSFLVGANGIWGQR--AVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAqHKPVLLFLTHGESSTGVLQPLDG 168
Cdd:pfam00266  82 grsLKPGDEIVITEMEHHANLvpWQELAKRTGARVRVLPLDEDGLLDLDELEKLIT-PKTKLVAITHVSNVTGTIQPVPE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    169 FGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKaLNAPPGTSLISFSDKAKKKMysRKTKPFSFYLDIKWLa 248
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHK-LYGPTGIGVLYGRRDLLEKM--PPLLGGGGMIETVSL- 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    249 NFWGCDDQPRMYHH-TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVKDPalRLPTVTTVAVP 327
Cdd:pfam00266 237 QESTFADAPWKFEAgTPNIAGIIGLGAALEYLSEIGLEAIEKHEHELAQYLYERLLSLPGIRLYGPE--RRASIISFNFK 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 4557289    328 aGYDWRDIVSYVIDHfDIEIMGGL---GPS-----TGKVLRIGlLGCNATRENVDRV 376
Cdd:pfam00266 315 -GVHPHDVATLLDES-GIAVRSGHhcaQPLmvrlgLGGTVRAS-FYIYNTQEDVDRL 368
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 57-220 1.90e-38

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: 135.97  E-value: 1.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   57 MDEIKEGIQYVFQTRNPLTLVISgSGHCALEAALVNVLEPGDSFLVGANGIWGQRAVdIGERIGARVHPMTKDPGGHYTL 136
Cdd:cd01494   2 LEELEEKLARLLQPGNDKAVFVP-SGTGANEAALLALLGPGDEVIVDANGHGSRYWV-AAELAGAKPVPVPVDDAGYGGL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  137 --QEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTP---LYMDRQGIDILYSGSQKAL 211
Cdd:cd01494  80 dvAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPapgVLIPEGGADVVTFSLHKNL 159


                ....*....
gi 4557289  212 NAPPGTSLI 220
Cdd:cd01494 160 GGEGGGVVI 168
PRK13479 PRK13479
2-aminoethylphosphonate--pyruvate transaminase; Provisional
 24-334 4.52e-20

2-aminoethylphosphonate--pyruvate transaminase; Provisional


Pssm-ID: 184076 [Multi-domain]  Cd Length: 368  Bit Score: 90.74  E-value: 4.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    24 LLLGPGPSNLPPRIMAAgglqMI---GSMSKDMYQIMDEIKEGIQYVFQTRNPLTLV-ISGSGHCALEAALVNVLEPGDS 99
Cdd:PRK13479   7 LLLTPGPLTTSRTVREA----MLrdwGSWDDDFNALTASVRAKLVAIATGEEGYTCVpLQGSGTFSVEAAIGSLVPRDGK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   100 FLVGANGIWGQRAVDIGERIGARVHPMTKDPGGHYTLQEVEEGLAQHKPVL-LFLTHGESSTGVLQPLDGFGELCHRYKC 178
Cdd:PRK13479  83 VLVPDNGAYGARIAQIAEYLGIAHVVLDTGEDEPPDAAEVEAALAADPRIThVALVHCETTTGILNPLDEIAAVAKRHGK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   179 LLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAPPGtslISFSDKAKKKMYSRKTKPFSFYLDikwLANFWGCDDQPR 258
Cdd:PRK13479 163 RLIVDAMSSFGAIPIDIAELGIDALISSANKCIEGVPG---FGFVIARRSELEACKGNSRSLSLD---LYDQWAYMEKTG 236

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4557289   259 MYHHTIPVISLYSLRESLA-LIAEQGLENSWRQHREAAAYLHGRLQALGLQLFVkDPALRLPTVTTVAVPA--GYDWRD 334
Cdd:PRK13479 237 QWRFTPPTHVVAAFYQALLeLEEEGGVPARGARYANNQRTLVAGMRALGFEPLL-DAEIQSPIIVTFHAPAdpAYDFKE 314
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
88-386 1.01e-10

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 62.85  E-value: 1.01e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   88 AALVNVLEPGDSFLVG-----ANGI-WGQRAvdigERIGARVH--PMTKDpgGHYTLQEVEEGLaQHKPVLLFLTHGESS 159
Cdd:COG0520  94 AYGLGRLKPGDEILITemehhSNIVpWQELA----ERTGAEVRviPLDED--GELDLEALEALL-TPRTKLVAVTHVSNV 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  160 TGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALnAPPGTSLISFSDKAKKKMysrktKPFS 239
Cdd:COG0520 167 TGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLY-GPTGIGVLYGKRELLEAL-----PPFL 240

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  240 FYLD-IKWlanfwgCDDQPRMYHH--------TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQAL-GLQL 309
Cdd:COG0520 241 GGGGmIEW------VSFDGTTYADlprrfeagTPNIAGAIGLGAAIDYLEAIGMEAIEARERELTAYALEGLAAIpGVRI 314

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  310 F-VKDPALRLPTVT-TVavpAGYDWRDIVSYvIDHFDIEIMGGLGPSTGKVLRIGLLGC--------NaTRENVDRVTEA 379
Cdd:COG0520 315 LgPADPEDRSGIVSfNV---DGVHPHDVAAL-LDDEGIAVRAGHHCAQPLMRRLGVPGTvrasfhlyN-TEEEIDRLVEA 389


                ....*..
gi 4557289  380 LRAALQH 386
Cdd:COG0520 390 LKKLAEL 396
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 117-386 3.71e-10

Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];


Pssm-ID: 440721 [Multi-domain]  Cd Length: 381  Bit Score: 60.83  E-value: 3.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  117 ERIGARVHPMTKDPGGHYTLQEVEEGLAQhKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMD 196
Cdd:COG1104 111 EKEGFEVTYLPVDEDGRVDLEALEAALRP-DTALVSVMHANNETGTIQPIAEIAEIAKEHGVLFHTDAVQAVGKIPVDVK 189

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  197 RQGIDiLYSGS-QKaLNAPPGTSLisfsdkakkkMYSRKtkpfsfylDIKWlanfwgcddQPRMY--HH-------TIPV 266
Cdd:COG1104 190 ELGVD-LLSLSaHK-IYGPKGVGA----------LYVRK--------GVRL---------EPLIHggGQerglrsgTENV 240

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  267 ISLYSLRESLALIAEQgLENSWRQHREAAAYLHGRLQAL--GLQLFVkDPALRLPTVTTVAVPaGYDWRDIVSyvidHFD 344
Cdd:COG1104 241 PGIVGLGKAAELAAEE-LEEEAARLRALRDRLEEGLLAAipGVVING-DPENRLPNTLNFSFP-GVEGEALLL----ALD 313

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4557289  345 IE-IM---------GGLGPStgKVLR-IGL------------LGCNATRENVDRVTEALRAALQH 386
Cdd:COG1104 314 LAgIAvssgsacssGSLEPS--HVLLaMGLdeelahgsirfsLGRFTTEEEIDRAIEALKEIVAR 376
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 117-380 1.97e-06

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 49.39  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  117 ERIGARVHPMTKDPGGHYTLQEVEEGLAQhKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMD 196
Cdd:cd06453 110 ERTGAKLKVVPVDDDGQLDLEALEKLLTE-RTKLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAGHMPVDVQ 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  197 RQGID----------------ILYsGSQKALNAPP----GTSLISFSDKAkkkmysrKTKPfsfyldikwlanfwgcDDQ 256
Cdd:cd06453 189 DLGCDflafsghkmlgptgigVLY-GKEELLEEMPpyggGGEMIEEVSFE-------ETTY----------------ADL 244

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  257 PRMYHH-TIPVISLYSLRESLALIAEQGLENSWRQHREAAAYLHGRLQAL-GLQLFvKDPALRLPTVTTVAvpAGYDWRD 334
Cdd:cd06453 245 PHKFEAgTPNIAGAIGLGAAIDYLEKIGMEAIAAHEHELTAYALERLSEIpGVRVY-GDAEDRAGVVSFNL--EGIHPHD 321

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4557289  335 iVSYVIDHFDIEI----------MGGLGPsTGKVlRIGlLGCNATRENVDRVTEAL 380
Cdd:cd06453 322 -VATILDQYGIAVraghhcaqplMRRLGV-PGTV-RAS-FGLYNTEEEIDALVEAL 373
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
140-209 2.63e-05

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 45.88  E-value: 2.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4557289   140 EEGLAQH---KPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQK 209
Cdd:PRK02948 128 LVDLERAitpDTVLASIQHANSEIGTIQPIAEIGALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHK 200
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 137-386 2.30e-04

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 439846 [Multi-domain]  Cd Length: 460  Bit Score: 42.90  E-value: 2.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  137 QEVEEGLAQ-HKPVLLFLTHGESSTGVLQPLDGFGELCHRYKCLLLVDsvASLGG----TPLYMDR-QGID----ILYSG 206
Cdd:COG0076 209 AAIDEDRAAgLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVD--AAYGGfalpSPELRHLlDGIEradsITVDP 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  207 sQKALNAPPGTSLISFSDKAkkkmYSRKTkpFSFYldikwlANFWG--CDDQPRMYHHTI------PVISLYSlreSLAL 278
Cdd:COG0076 287 -HKWLYVPYGCGAVLVRDPE----LLREA--FSFH------ASYLGpaDDGVPNLGDYTLelsrrfRALKLWA---TLRA 350

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289  279 IAEQGLENSWRQHREAAAYLHGRLQAL-GLQLfVKDPalRLPTVTTVAVPAGYDWRDivsYVIDHFDIEIM--GGLGPST 355
Cdd:COG0076 351 LGREGYRELIERCIDLARYLAEGIAALpGFEL-LAPP--ELNIVCFRYKPAGLDEED---ALNYALRDRLRarGRAFLSP 424

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 4557289  356 GK-----VLRIGLLGCNATRENVDRVTEALRAALQH 386
Cdd:COG0076 425 TKldgrvVLRLVVLNPRTTEDDVDALLDDLREAAAE 460
SepCysS cd06452
Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent ...
 85-214 3.47e-04

Sep-tRNA:Cys-tRNA synthase. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Cys-tRNA(Cys) is produced by O-phosphoseryl-tRNA synthetase which ligates O-phosphoserine (Sep) to tRNA(Cys), and Sep-tRNA:Cys-tRNA synthase (SepCysS) converts Sep-tRNA(Cys) to Cys-tRNA(Cys), in methanogenic archaea. SepCysS forms a dimer, each monomer is composed of a large and small domain; the larger, a typical pyridoxal 5'-phosphate (PLP)-dependent-like enzyme fold. In the active site of each monomer, PLP is covalently bound to a conserved Lys residue near the dimer interface.


Pssm-ID: 99745  Cd Length: 361  Bit Score: 42.38  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289   85 ALEAALVNVLEPGDSFLVGANGIWGQR-AVdigERIGARVH--PMTKDPGGHYTLQEVEEGLAQHK------PVLLFLTH 155
Cdd:cd06452  71 GKFAVMHSLCEKGDWVVVDGLAHYTSYvAA---ERAGLNVRevPNTGHPEYHITPEGYAEVIEEVKdefgkpPALALLTH 147

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4557289  156 GESSTGVLQPLDGFGELCHRYKCLLLVDSVASLGGTPLYMDRQGIDILYSGSQKALNAP 214
Cdd:cd06452 148 VDGNYGNLHDAKKIAKVCHEYGVPLLLNGAYTVGRMPVSGKELGADFIVGSGHKSMAAS 206
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
66-380 9.81e-04

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 40.75  E-value: 9.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289     66 YVFQTRNPLTLVISGSGHcALEAALVNVLEPGDSFLVGANGiWGQRAVDI-GERIGARVHPMTKDPGGHYTLQEVEEGLA 144
Cdd:pfam00155  57 VLKLDREAAVVFGSGAGA-NIEALIFLLANPGDAILVPAPT-YASYIRIArLAGGEVVRYPLYDSNDFHLDFDALEAALK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    145 QhKPVLLFLTHGESSTGVLQPLDGF---GELCHRYKCLLLVD---SVASLGGTPLYMDRQGID------ILYSGSqKALN 212
Cdd:pfam00155 135 E-KPKVVLHTSPHNPTGTVATLEELeklLDLAKEHNILLLVDeayAGFVFGSPDAVATRALLAegpnllVVGSFS-KAFG 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    213 ApPGTSL--ISFSDKAKKKMysrktkpfsfyldIKWLANFWGCDdqprmyhHTiPVISLYSLRESLALIAEqgLENSWRQ 290
Cdd:pfam00155 213 L-AGWRVgyILGNAAVISQL-------------RKLARPFYSST-------HL-QAAAAAALSDPLLVASE--LEEMRQR 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557289    291 HREAAAYLHGRLQALGLQLFVKDPALRLptvttVAVPAGYDWRDIVSYVIDHFDIEIMGGLGPSTGKVLRIGLLGCnaTR 370
Cdd:pfam00155 269 IKERRDYLRDGLQAAGLSVLPSQAGFFL-----LTGLDPETAKELAQVLLEEVGVYVTPGSSPGVPGWLRITVAGG--TE 341

                         330
                  ....*....|
gi 4557289    371 ENVDRVTEAL 380
Cdd:pfam00155 342 EELEELLEAI 351
 
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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