|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
1-368 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 520.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 1 MEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQIT 79
Cdd:pfam00282 5 KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 80 LKKMREIIGWSN----KDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEHSHYSIKKAGAA 150
Cdd:pfam00282 85 MNWLGEMLGLPAeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 151 LGFGtdnVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGL 230
Cdd:pfam00282 165 GGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 231 LMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAIQCGRHVD 310
Cdd:pfam00282 242 FICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 193075653 311 IFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 368
Cdd:pfam00282 318 ILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-440 |
1.20e-159 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 454.35 E-value: 1.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 37 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYK 116
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 117 YFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAG 196
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 197 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 276
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 277 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 356
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 357 EPEHTNVCFWYIPQSlrgvpdsperreKLHRVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 436
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 193075653 437 IERL 440
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
2-443 |
2.42e-133 |
|
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: 391.89 E-value: 2.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 2 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 80
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 81 KKMREIIGWSnKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVI 159
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 160 LIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 239
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 240 LSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 319
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 320 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPqslrgvPDSPERREKLHRVApkikALMMES 399
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKP------AGLDEEDALNYALR----DRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 193075653 400 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 443
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
10-369 |
2.51e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 146.01 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 10 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 88
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 89 W-----SNKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKC 163
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 164 NERGK--IIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 241
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 242 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 321
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 193075653 322 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 369
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
1-368 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 520.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 1 MEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQIT 79
Cdd:pfam00282 5 KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 80 LKKMREIIGWSN----KDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEHSHYSIKKAGAA 150
Cdd:pfam00282 85 MNWLGEMLGLPAeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSSIEKAALY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 151 LGFGtdnVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGL 230
Cdd:pfam00282 165 GGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 231 LMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAIQCGRHVD 310
Cdd:pfam00282 242 FICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQIPLSRRFR 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 193075653 311 IFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 368
Cdd:pfam00282 318 ILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
37-440 |
1.20e-159 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 454.35 E-value: 1.20e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 37 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYK 116
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 117 YFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAG 196
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 197 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 276
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 277 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 356
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 357 EPEHTNVCFWYIPQSlrgvpdsperreKLHRVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 436
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 193075653 437 IERL 440
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
2-443 |
2.42e-133 |
|
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: 391.89 E-value: 2.42e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 2 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 80
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 81 KKMREIIGWSnKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVI 159
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 160 LIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 239
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 240 LSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 319
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 320 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPqslrgvPDSPERREKLHRVApkikALMMES 399
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKP------AGLDEEDALNYALR----DRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 193075653 400 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 443
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
10-369 |
2.51e-38 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 146.01 E-value: 2.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 10 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 88
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 89 W-----SNKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKC 163
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 164 NERGK--IIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 241
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 242 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 321
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 193075653 322 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 369
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
10-369 |
4.09e-37 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 141.58 E-value: 4.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 10 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 88
Cdd:PLN02880 57 NQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 89 -----WSNKDGDGIFSPGGAISNMYSIMAARYKYfpeVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIK- 162
Cdd:PLN02880 137 lpeqfLSTGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKt 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 163 -CNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 241
Cdd:PLN02880 214 dSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYID 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 242 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 321
Cdd:PLN02880 294 GVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLY 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 193075653 322 GTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIP 369
Cdd:PLN02880 374 GVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVP 419
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
96-348 |
1.12e-23 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 102.04 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 96 GIFSPGGAISNMYSIMAARyKYFPEVktkgmaavpklVLFTSEHSHYSIKKAGAALGFgTDNVILIKCNerGKIIPADLE 175
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRI-KSRVITSLPN--GEIDYDDLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 176 AKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEIADICEKYNL---WLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWN 252
Cdd:PRK02769 152 SKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 253 PHKMMGVLLQCSAILVKEKGIlqgcnqmcagylfqpDKQY-DVSY-DTGDKAIQCGR--HVDIfkfwLMWKA---KGTVG 325
Cdd:PRK02769 229 GHKFIGSPMPCGIVLAKKKYV---------------ERISvDVDYiGSRDQTISGSRngHTAL----LLWAAirsLGSKG 289
|
250 260
....*....|....*....|...
gi 193075653 326 FENQINKCLELAEYLYAKIKNRE 348
Cdd:PRK02769 290 LRQRVQHCLDMAQYAVDRLQANG 312
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
96-345 |
3.99e-12 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 67.54 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 96 GIFSPGGAISNMYSIMAARYKYfpevktkgmaavPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIkcnERGKIIPADLE 175
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 176 AKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEIADICEKYN-----LWLHVDAAWGGGLLMSRKHRHKLSGIERANSVT 250
Cdd:PLN03032 153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 251 WNPHKMMGVLLQCSAILVKEKGILQgcnqmcagylFQPDKQYDVSYDTGDKAIQCGrHVDIFkFWLMWKAKGTVGFENQI 330
Cdd:PLN03032 230 VSGHKFLGCPMPCGVALTRKKHVKA----------LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDV 297
|
250
....*....|....*
gi 193075653 331 NKCLELAEYLYAKIK 345
Cdd:PLN03032 298 QHCMRNAHYLKDRLT 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
130-346 |
5.56e-12 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 67.53 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 130 PKLVLFTSEHSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADLEAKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEI 209
Cdd:PLN02263 177 PDGILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 210 ADICEKY-----NLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGIlqgcNQMCAgy 284
Cdd:PLN02263 251 IKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHI----NVLSS-- 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193075653 285 lfqpdkqyDVSY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 346
Cdd:PLN02263 325 --------NVEYlASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
91-269 |
8.62e-09 |
|
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: 54.70 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 91 NKDGDGIFSPGGAISNMYSIMAARykyfpevktkgmaaVPKLVLFTSEHSHYSIKKAGAALGFGtdNVILIKCNERGKii 170
Cdd:cd01494 15 PGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAELAGA--KPVPVPVDDAGY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 171 pADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHrhkLSGIERANSVT 250
Cdd:cd01494 77 -GGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVVT 152
|
170
....*....|....*....
gi 193075653 251 WNPHKMMGVlLQCSAILVK 269
Cdd:cd01494 153 FSLHKNLGG-EGGGVVIVK 170
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
74-364 |
5.49e-07 |
|
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: 51.48 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 74 LMEQiTLKKMREIIGWSNKDgDGIFSPGGAisnmYSIMAARYKYFPEVKTKGmaavpKLVLFTSEHsHYSIKKAGAALGF 153
Cdd:pfam00266 44 AYEE-AREKVAEFINAPSND-EIIFTSGTT----EAINLVALSLGRSLKPGD-----EIVITEMEH-HANLVPWQELAKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 154 GTDNVILIKCNERGKIIPADLEAKIlDAKQKgfvplYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGgglLMS 233
Cdd:pfam00266 112 TGARVRVLPLDEDGLLDLDELEKLI-TPKTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 234 RKHRHKLSGIERANSVTwnpHKMM-----GVLLQCSAILVKEKGILQGcnqmcAGYLFQPDKQYDVSYDTGDK------- 301
Cdd:pfam00266 183 RPIDVQKLGVDFLAFSG---HKLYgptgiGVLYGRRDLLEKMPPLLGG-----GGMIETVSLQESTFADAPWKfeagtpn 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193075653 302 ---AIQCGRHVDifkfWLMwkakgTVGFENQINKCLELAEYLYAKIKNREEFEmvFNGEPEHTNVC 364
Cdd:pfam00266 255 iagIIGLGAALE----YLS-----EIGLEAIEKHEHELAQYLYERLLSLPGIR--LYGPERRASII 309
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
198-270 |
5.44e-06 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 48.01 E-value: 5.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193075653 198 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMS---RKHRHKLSGIERANSVtwnpHKMMGVLLQCSAILVKE 270
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
84-225 |
1.20e-05 |
|
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.
Pssm-ID: 99748 [Multi-domain] Cd Length: 338 Bit Score: 46.94 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 84 REIIGwsnkDGDGIFSPGGAISNMYSIMAarykyfpevktkgMAAVPKLVLfTSEHSHYSIKKAGAALGFGTDNVILIKc 163
Cdd:cd06502 42 AELFG----KEAALFVPSGTAANQLALAA-------------HTQPGGSVI-CHETAHIYTDEAGAPEFLSGVKLLPVP- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193075653 164 NERGKIIPADLEAKILDAKQKGFVPLYV----NATAGTTVYgafdPIQEIADICE---KYNLWLHVDAA 225
Cdd:cd06502 103 GENGKLTPEDLEAAIRPRDDIHFPPPSLvsleNTTEGGTVY----PLDELKAISAlakENGLPLHLDGA 167
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
134-225 |
1.68e-04 |
|
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: 43.50 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 134 LFTS--EHShySIKKAGAAL---GFgtdNVILIKCNERGKIIPADLEAKIldAKQKGFVPL-YVNATAGTtVYgafdPIQ 207
Cdd:COG1104 93 IITSaiEHP--AVLETARFLekeGF---EVTYLPVDEDGRVDLEALEAAL--RPDTALVSVmHANNETGT-IQ----PIA 160
|
90
....*....|....*...
gi 193075653 208 EIADICEKYNLWLHVDAA 225
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAV 178
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
198-273 |
2.84e-04 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 43.18 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 198 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGgllmsrkHRH-----KLSGIER-----ANSVtwnpHKMMGVLLQCSAIL 267
Cdd:COG1982 171 TYYGVCYDLKAIAELAHEHGIPVLVDEAHGA-------HFGfhpdlPRSAMEAgadlvVQST----HKTLGALTQSSMLH 239
|
....*.
gi 193075653 268 VKEKGI 273
Cdd:COG1982 240 VKGGRV 245
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
82-225 |
1.30e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 40.66 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 82 KMREIIGwsnKDGdGIFSPGGAISNMYSIMAArykyfpevktkgmaAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILI 161
Cdd:pfam01212 40 RVAELFG---KEA-ALFVPSGTAANQLALMAH--------------CQRGDEVICGEPAHIHFDETGGHAELGGVQPRPL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 162 KCNERGKIIPADLEAKILDAKQKGFVPLYV------NATAGTTVYgAFDPIQEIADICEKYNLWLHVDAA 225
Cdd:pfam01212 102 DGDEAGNMDLEDLEAAIREVGADIFPPTGLislentHNSAGGQVV-SLENLREIAALAREHGIPVHLDGA 170
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
171-231 |
1.71e-03 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 40.24 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193075653 171 PADLEAKILDAKQKgFVPLYVnATAGttVY---GAFDPIQEIADICEKYNLWLHVDAAWGGGLL 231
Cdd:cd06454 117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
97-225 |
2.91e-03 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 39.64 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 97 IFSPGGAISNMYSIMAArYKYFPEVKtkgmaavPKLVLFTSEHShySIKKAGAALGFGTDNVILIKCNERGKIIPADLEA 176
Cdd:PLN02651 64 IFTSGATESNNLAIKGV-MHFYKDKK-------KHVITTQTEHK--CVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAA 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 193075653 177 KILDAkqkgfvplyvnaTAGTTV------YGAFDPIQEIADICEKYNLWLHVDAA 225
Cdd:PLN02651 134 AIRPD------------TALVSVmavnneIGVIQPVEEIGELCREKKVLFHTDAA 176
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
133-225 |
5.87e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.58 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193075653 133 VLFTSEHSHYS--------IKKAGAalgfgtdNVILIKCNERGKIIPADLEAKIlDAKQKgfvplYVNATAGTTVYGAFD 204
Cdd:COG0520 105 EILITEMEHHSnivpwqelAERTGA-------EVRVIPLDEDGELDLEALEALL-TPRTK-----LVAVTHVSNVTGTVN 171
|
90 100
....*....|....*....|.
gi 193075653 205 PIQEIADICEKYNLWLHVDAA 225
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGA 192
|
|
| |
