|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
143-517 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 525.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 143 PHQLlegMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVF 221
Cdd:pfam00282 1 PGYL---KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPAC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 222 VLMEQITLKKMREIIGWSN----KDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEHSHYS 292
Cdd:pfam00282 78 TELENVVMNWLGEMLGLPAeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 293 IKKAGAALGFGtdnVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVD 372
Cdd:pfam00282 158 IEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 373 AAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAI 452
Cdd:pfam00282 235 AAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259121451 453 QCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 517
Cdd:pfam00282 311 PLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
186-589 |
6.15e-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: 458.21 E-value: 6.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 186 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYK 265
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 266 YFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAG 345
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 346 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 425
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 426 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 505
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 506 EPEHTNVCFWYIPQSlrgvpdsperreKLHRVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 585
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 259121451 586 IERL 589
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
151-592 |
3.46e-131 |
|
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: 3.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 151 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 229
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 230 KKMREIIGWSnKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVI 308
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 309 LIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 388
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 389 LSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 468
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 469 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPqslrgvPDSPERREKLHRVApkikALMMES 548
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKP------AGLDEEDALNYALR----DRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 259121451 549 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 592
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
159-518 |
2.53e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 145.62 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 159 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 237
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 238 W-----SNKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKC 312
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 313 NERGK--IIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 390
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 391 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 470
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 259121451 471 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 518
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
143-517 |
0e+00 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 525.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 143 PHQLlegMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVF 221
Cdd:pfam00282 1 PGYL---KPLLPLAAPIIPEPELQIDGDIRRNLMPGVTTWHsPHFHAYMPTGNSYPSLLGDMLTDAINCNGFTWESSPAC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 222 VLMEQITLKKMREIIGWSN----KDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVP-----KLVLFTSEHSHYS 292
Cdd:pfam00282 78 TELENVVMNWLGEMLGLPAeflgQEGGGVLQPGSSESNLLALLAARTKWIKRMKAAGKPADSsgilaKLVAYTSDQAHSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 293 IKKAGAALGFGtdnVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVD 372
Cdd:pfam00282 158 IEKAALYGGVK---LREIPSDDNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 373 AAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKqydvSYDTGDKAI 452
Cdd:pfam00282 235 AAYGGSAFICPEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDS----AYDTGHKQI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259121451 453 QCGRHVDIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEMVFngEPEHTNVCFWYI 517
Cdd:pfam00282 311 PLSRRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICA--EVGLGLVCFRLK 373
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
186-589 |
6.15e-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: 458.21 E-value: 6.15e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 186 FFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYK 265
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFTWDESPAATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 266 YFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGfgtDNVILIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAG 345
Cdd:cd06450 81 ARKRLKAGGGRGIDKLVIVCSDQAHVSVEKAAAYLD---VKVRLVPVDEDGRMDPEALEAAIDEDKAEGLNPIMVVATAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 346 TTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKekgilqg 425
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 426 cnqmcagylfqpdkqydvsydtgdkaiqcgrhvdIFKFWLMWKAKGTVGFENQINKCLELAEYLYAKIKNREEFEmvFNG 505
Cdd:cd06450 231 ----------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFE--LLG 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 506 EPEHTNVCFWYIPQSlrgvpdsperreKLHRVAPKIKALMMESGTTMVGYQPQGDKaNFFRMVISNPAATQSDIDFLIEE 585
Cdd:cd06450 275 EPNLSLVCFRLKPSV------------KLDELNYDLSDRLNERGGWHVPATTLGGP-NVLRFVVTNPLTTRDDADALLED 341
|
....
gi 259121451 586 IERL 589
Cdd:cd06450 342 IERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
151-592 |
3.46e-131 |
|
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: 3.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 151 EGFNLELSDHPESLEQILVDCRDT-LKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITL 229
Cdd:COG0076 34 AALDEPLPEEGLPPEEALAELEDLvLPGSVDWNHPRFLAFVTGGTTPAALAADLLASALNQNMGDWDTSPAATELEREVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 230 KKMREIIGWSnKDGDGIFSPGGAISNMYSIMAARYKYFPE-VKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVI 308
Cdd:COG0076 114 RWLADLLGLP-EGAGGVFTSGGTEANLLALLAARDRALARrVRAEGLPGAPRPRIVVSEEAHSSVDKAARLLGLGRDALR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 309 LIKCNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHK 388
Cdd:COG0076 193 KVPVDEDGRMDPDALEAAIDEDRAAGLNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPELRHL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 389 LSGIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDkqyDVSYDTGDKAIQCGRHVDIFKFWLMWK 468
Cdd:COG0076 273 LDGIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASYLGPAD---DGVPNLGDYTLELSRRFRALKLWATLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 469 AKGTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIPqslrgvPDSPERREKLHRVApkikALMMES 548
Cdd:COG0076 350 ALGREGYRELIERCIDLARYLAEGIAALPGFELL--APPELNIVCFRYKP------AGLDEEDALNYALR----DRLRAR 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 259121451 549 GTTMVGYQPQGDKANfFRMVISNPAATQSDIDFLIEEIERLGQD 592
Cdd:COG0076 418 GRAFLSPTKLDGRVV-LRLVVLNPRTTEDDVDALLDDLREAAAE 460
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
159-518 |
2.53e-37 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 145.62 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 159 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 237
Cdd:PLN02590 105 ERPESLKELLDDVSKKIMPGITHWQsPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 238 W-----SNKDGDGIFSPGGAISNMYSIMAARYKYFPEVktkGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKC 312
Cdd:PLN02590 185 LpdhflSTGNGGGVIQGTGCEAVLVVVLAARDRILKKV---GKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKT 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 313 NERGK--IIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 390
Cdd:PLN02590 262 DSSTNygMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFID 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 391 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 470
Cdd:PLN02590 342 GIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLY 421
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 259121451 471 GTVGFENQINKCLELAEYLYAKIKNREEFEMVFNgePEHTNVCFWYIP 518
Cdd:PLN02590 422 GSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTT--RYFSLVCFRLAP 467
|
|
| PLN02880 |
PLN02880 |
tyrosine decarboxylase |
159-518 |
3.38e-36 |
|
tyrosine decarboxylase
Pssm-ID: 215475 [Multi-domain] Cd Length: 490 Bit Score: 141.58 E-value: 3.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 159 DHPESLEQILVDCRDTLKYGVRTGH-PRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIG 237
Cdd:PLN02880 57 NQPETLDQVLDDVQAKILPGVTHWQsPNYFAYYPSNSSVAGFLGEMLSAGLNIVGFSWITSPAATELEMIVLDWLAKLLN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 238 -----WSNKDGDGIFSPGGAISNMYSIMAARYKYfpeVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIK- 311
Cdd:PLN02880 137 lpeqfLSTGNGGGVIQGTASEAVLVVLLAARDRV---LRKVGKNALEKLVVYASDQTHSALQKACQIAGIHPENCRLLKt 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 312 -CNERGKIIPADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHRHKLS 390
Cdd:PLN02880 214 dSSTNYALAPELLSEAISTDLSSGLIPFFLCATVGTTSSTAVDPLLELGKIAKSNGMWFHVDAAYAGSACICPEYRHYID 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 391 GIERANSVTWNPHKMMGVLLQCSAILVKEKGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAK 470
Cdd:PLN02880 294 GVEEADSFNMNAHKWFLTNFDCSLLWVKDRNALIQSLSTNPEFLKNKASQANSVVDYKDWQIPLGRRFRSLKLWMVLRLY 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 259121451 471 GTVGFENQINKCLELAEYLYAKIKNREEFEMVfnGEPEHTNVCFWYIP 518
Cdd:PLN02880 374 GVENLQSYIRNHIKLAKEFEQLVAQDSRFEVV--TPRIFSLVCFRLVP 419
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
245-497 |
1.36e-23 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 102.81 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 245 GIFSPGGAISNMYSIMAARyKYFPEVktkgmaavpklVLFTSEHSHYSIKKAGAALGFgTDNVILIKCNerGKIIPADLE 324
Cdd:PRK02769 87 GYITNGGTEGNLYGCYLAR-ELFPDG-----------TLYYSKDTHYSVSKIARLLRI-KSRVITSLPN--GEIDYDDLI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 325 AKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEIADICEKYNL---WLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWN 401
Cdd:PRK02769 152 SKIKENKNQ---PPIIFANIGTTMTGAIDNIKEIQEILKKIGIddyYIHADAALSGMILPFVNNPPPFSFADGIDSIAIS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 402 PHKMMGVLLQCSAILVKEKGIlqgcnqmcagylfqpDKQY-DVSY-DTGDKAIQCGR--HVDIfkfwLMWKA---KGTVG 474
Cdd:PRK02769 229 GHKFIGSPMPCGIVLAKKKYV---------------ERISvDVDYiGSRDQTISGSRngHTAL----LLWAAirsLGSKG 289
|
250 260
....*....|....*....|...
gi 259121451 475 FENQINKCLELAEYLYAKIKNRE 497
Cdd:PRK02769 290 LRQRVQHCLDMAQYAVDRLQANG 312
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
245-494 |
5.35e-12 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 67.54 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 245 GIFSPGGAISNMYSIMAARYKYfpevktkgmaavPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIkcnERGKIIPADLE 324
Cdd:PLN03032 88 GYITTCGTEGNLHGILVGREVF------------PDGILYASRESHYSVFKAARMYRMEAVKVPTL---PSGEIDYDDLE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 325 AKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEIADICEKYN-----LWLHVDAAWGGGLLMSRKHRHKLSGIERANSVT 399
Cdd:PLN03032 153 RALAKNRDK---PAILNVNIGTTVKGAVDDLDRILRILKELGytedrFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 400 WNPHKMMGVLLQCSAILVKEKGILQgcnqmcagylFQPDKQYDVSYDTGDKAIQCGrHVDIFkFWLMWKAKGTVGFENQI 479
Cdd:PLN03032 230 VSGHKFLGCPMPCGVALTRKKHVKA----------LSQNVEYLNSRDATIMGSRNG-HAPLY-LWYTLRRKGYRGIKRDV 297
|
250
....*....|....*
gi 259121451 480 NKCLELAEYLYAKIK 494
Cdd:PLN03032 298 QHCMRNAHYLKDRLT 312
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
279-495 |
9.90e-12 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 67.53 E-value: 9.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 279 PKLVLFTSEHSHYSIKKAGAALGFGtdnVILIKCNERGKIIPADLEAKILDAKQKgfvPLYVNATAGTTVYGAFDPIQEI 358
Cdd:PLN02263 177 PDGILYASRESHYSVFKAARMYRME---CVKVDTLVSGEIDCADFKAKLLANKDK---PAIINVNIGTTVKGAVDDLDLV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 359 ADICEKY-----NLWLHVDAAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVLLQCSAILVKEKGIlqgcNQMCAgy 433
Cdd:PLN02263 251 IKTLEECgfsqdRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRMEHI----NVLSS-- 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 259121451 434 lfqpdkqyDVSY-DTGDKAIQCGR--HVDIFkFWLMWKAKGTVGFENQINKCLELAEYLYAKIKN 495
Cdd:PLN02263 325 --------NVEYlASRDATIMGSRngHAPIF-LWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLRE 380
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
240-418 |
8.05e-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: 55.08 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 240 NKDGDGIFSPGGAISNMYSIMAARykyfpevktkgmaaVPKLVLFTSEHSHYSIKKAGAALGFGtdNVILIKCNERGKii 319
Cdd:cd01494 15 PGNDKAVFVPSGTGANEAALLALL--------------GPGDEVIVDANGHGSRYWVAAELAGA--KPVPVPVDDAGY-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 320 pADLEAKILDAKQKGFVPLYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMSRKHrhkLSGIERANSVT 399
Cdd:cd01494 77 -GGLDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGV---LIPEGGADVVT 152
|
170
....*....|....*....
gi 259121451 400 WNPHKMMGVlLQCSAILVK 418
Cdd:cd01494 153 FSLHKNLGG-EGGGVVIVK 170
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
223-513 |
8.59e-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: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 223 LMEQiTLKKMREIIGWSNKDgDGIFSPGGAisnmYSIMAARYKYFPEVKTKGmaavpKLVLFTSEHsHYSIKKAGAALGF 302
Cdd:pfam00266 44 AYEE-AREKVAEFINAPSND-EIIFTSGTT----EAINLVALSLGRSLKPGD-----EIVITEMEH-HANLVPWQELAKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 303 GTDNVILIKCNERGKIIPADLEAKIlDAKQKgfvplYVNATAGTTVYGAFDPIQEIADICEKYNLWLHVDAAWGgglLMS 382
Cdd:pfam00266 112 TGARVRVLPLDEDGLLDLDELEKLI-TPKTK-----LVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQA---IGH 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 383 RKHRHKLSGIERANSVTwnpHKMM-----GVLLQCSAILVKEKGILQGcnqmcAGYLFQPDKQYDVSYDTGDK------- 450
Cdd:pfam00266 183 RPIDVQKLGVDFLAFSG---HKLYgptgiGVLYGRRDLLEKMPPLLGG-----GGMIETVSLQESTFADAPWKfeagtpn 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259121451 451 ---AIQCGRHVDifkfWLMwkakgTVGFENQINKCLELAEYLYAKIKNREEFEmvFNGEPEHTNVC 513
Cdd:pfam00266 255 iagIIGLGAALE----YLS-----EIGLEAIEKHEHELAQYLYERLLSLPGIR--LYGPERRASII 309
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
347-419 |
6.82e-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: 6.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 259121451 347 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGGLLMS---RKHRHKLSGIERANSVtwnpHKMMGVLLQCSAILVKE 419
Cdd:cd00615 164 TYYGICYNLRKIVEEAHHRGLPVLVDEAHGAHFRFHpilPSSAAMAGADIVVQST----HKTLPALTQGSMIHVKG 235
|
|
| TA_like |
cd06502 |
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ... |
233-374 |
1.82e-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: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 233 REIIGwsnkDGDGIFSPGGAISNMYSIMAarykyfpevktkgMAAVPKLVLfTSEHSHYSIKKAGAALGFGTDNVILIKc 312
Cdd:cd06502 42 AELFG----KEAALFVPSGTAANQLALAA-------------HTQPGGSVI-CHETAHIYTDEAGAPEFLSGVKLLPVP- 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 259121451 313 NERGKIIPADLEAKILDAKQKGFVPLYV----NATAGTTVYgafdPIQEIADICE---KYNLWLHVDAA 374
Cdd:cd06502 103 GENGKLTPEDLEAAIRPRDDIHFPPPSLvsleNTTEGGTVY----PLDELKAISAlakENGLPLHLDGA 167
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
283-374 |
2.54e-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: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 283 LFTS--EHShySIKKAGAAL---GFgtdNVILIKCNERGKIIPADLEAKIldAKQKGFVPL-YVNATAGTtVYgafdPIQ 356
Cdd:COG1104 93 IITSaiEHP--AVLETARFLekeGF---EVTYLPVDEDGRVDLEALEAAL--RPDTALVSVmHANNETGT-IQ----PIA 160
|
90
....*....|....*...
gi 259121451 357 EIADICEKYNLWLHVDAA 374
Cdd:COG1104 161 EIAEIAKEHGVLFHTDAV 178
|
|
| LdcC |
COG1982 |
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism]; |
347-422 |
4.31e-04 |
|
Arginine/lysine/ornithine decarboxylase [Amino acid transport and metabolism];
Pssm-ID: 441585 [Multi-domain] Cd Length: 486 Bit Score: 43.18 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 347 TVYGAFDPIQEIADICEKYNLWLHVDAAWGGgllmsrkHRH-----KLSGIER-----ANSVtwnpHKMMGVLLQCSAIL 416
Cdd:COG1982 171 TYYGVCYDLKAIAELAHEHGIPVLVDEAHGA-------HFGfhpdlPRSAMEAgadlvVQST----HKTLGALTQSSMLH 239
|
....*.
gi 259121451 417 VKEKGI 422
Cdd:COG1982 240 VKGGRV 245
|
|
| Beta_elim_lyase |
pfam01212 |
Beta-eliminating lyase; |
231-374 |
1.91e-03 |
|
Beta-eliminating lyase;
Pssm-ID: 426128 [Multi-domain] Cd Length: 288 Bit Score: 40.66 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 231 KMREIIGwsnKDGdGIFSPGGAISNMYSIMAArykyfpevktkgmaAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILI 310
Cdd:pfam01212 40 RVAELFG---KEA-ALFVPSGTAANQLALMAH--------------CQRGDEVICGEPAHIHFDETGGHAELGGVQPRPL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 311 KCNERGKIIPADLEAKILDAKQKGFVPLYV------NATAGTTVYgAFDPIQEIADICEKYNLWLHVDAA 374
Cdd:pfam01212 102 DGDEAGNMDLEDLEAAIREVGADIFPPTGLislentHNSAGGQVV-SLENLREIAALAREHGIPVHLDGA 170
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
320-380 |
2.54e-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: 2.54e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 259121451 320 PADLEAKILDAKQKgFVPLYVnATAGttVY---GAFDPIQEIADICEKYNLWLHVDAAWGGGLL 380
Cdd:cd06454 117 MEDLEKLLREARRP-YGKKLI-VTEG--VYsmdGDIAPLPELVDLAKKYGAILFVDEAHSVGVY 176
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
246-374 |
4.32e-03 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 39.64 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 246 IFSPGGAISNMYSIMAArYKYFPEVKtkgmaavPKLVLFTSEHShySIKKAGAALGFGTDNVILIKCNERGKIIPADLEA 325
Cdd:PLN02651 64 IFTSGATESNNLAIKGV-MHFYKDKK-------KHVITTQTEHK--CVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAA 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 259121451 326 KILDAkqkgfvplyvnaTAGTTV------YGAFDPIQEIADICEKYNLWLHVDAA 374
Cdd:PLN02651 134 AIRPD------------TALVSVmavnneIGVIQPVEEIGELCREKKVLFHTDAA 176
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
282-374 |
8.71e-03 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 38.58 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259121451 282 VLFTSEHSHYS--------IKKAGAalgfgtdNVILIKCNERGKIIPADLEAKIlDAKQKgfvplYVNATAGTTVYGAFD 353
Cdd:COG0520 105 EILITEMEHHSnivpwqelAERTGA-------EVRVIPLDEDGELDLEALEALL-TPRTK-----LVAVTHVSNVTGTVN 171
|
90 100
....*....|....*....|.
gi 259121451 354 PIQEIADICEKYNLWLHVDAA 374
Cdd:COG0520 172 PVKEIAALAHAHGALVLVDGA 192
|
|
| |
