|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
64-427 |
1.17e-113 |
|
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: 338.79 E-value: 1.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 64 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 142
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 143 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 209
Cdd:cd06450 79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 210 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLYSdk 289
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 290 kyrnyqffvdtdwqggiyasptiagsrpggiSAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLS 369
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964186 370 VIALGSR-----DFDIYRLSNLMTAKG-WNLNQLQF--PPSIHFCITLLHARKRVAIQFLKDIRES 427
Cdd:cd06450 280 LVCFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
35-428 |
2.95e-89 |
|
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: 280.18 E-value: 2.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 35 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 110
Cdd:COG0076 39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 111 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 179
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 180 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 253
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 254 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 327
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 328 LMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLSNLMTAKGwnlnQLQFP 400
Cdd:COG0076 348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARG----RAFLS 423
|
410 420 430
....*....|....*....|....*....|....*
gi 767964186 401 PS-------IHFCITLLHARKRVAIQFLKDIRESV 428
Cdd:COG0076 424 PTkldgrvvLRLVVLNPRTTEDDVDALLDDLREAA 458
|
|
| tyr_de_CO2_Arch |
TIGR03812 |
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ... |
42-426 |
1.02e-82 |
|
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274796 Cd Length: 373 Bit Score: 260.36 E-value: 1.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 42 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 121
Cdd:TIGR03812 1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 122 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 201
Cdd:TIGR03812 77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 202 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 279
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 280 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKG 359
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGF 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964186 360 IFVFgNPQLSVIALGSRDFDiyRLSNLMTAKGWNLNQLQFPPSIHFcITLLHARKRVAIQFLKDIRE 426
Cdd:TIGR03812 310 EPVI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
121-373 |
4.26e-14 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 73.54 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 121 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 200
Cdd:PRK02769 84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 201 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 274
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 275 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSEL 354
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308
|
250
....*....|....*....
gi 767964186 355 ENIkGIFVFGNPQLSVIAL 373
Cdd:PRK02769 309 QAN-GIPAWRNPNSITVVF 326
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
127-372 |
1.17e-13 |
|
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: 72.28 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 202
Cdd:pfam00266 67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 203 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 281
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 282 SlVLY------------------SDKKYRNYQFFVDTDW--QGGiyaSPTIAGsrpggiSAACWAALMHFGENGYVEATK 341
Cdd:pfam00266 209 G-VLYgrrdllekmppllggggmIETVSLQESTFADAPWkfEAG---TPNIAG------IIGLGAALEYLSEIGLEAIEK 278
|
250 260 270
....*....|....*....|....*....|..
gi 767964186 342 QIIKTARFLKSELENIKGIFVFGNPQL-SVIA 372
Cdd:pfam00266 279 HEHELAQYLYERLLSLPGIRLYGPERRaSIIS 310
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
64-427 |
1.17e-113 |
|
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: 338.79 E-value: 1.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 64 RASGTVYSGEEKLTELLVKAYGDFAWSNPlhPDIFPGLRKIEAEIVRIACSLFNGGP-DSCGCVTSGGTESILMACKAYR 142
Cdd:cd06450 1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLPSeDADGVFTSGGSESNLLALLAAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 143 DLAFE-------KGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISR------NTAMLVCSTPQ 209
Cdd:cd06450 79 DRARKrlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATAGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 210 FPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYplehpfDFRVKGVTSISADTHKYGYAPKGSSLVLYSdk 289
Cdd:cd06450 159 TDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL------DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 290 kyrnyqffvdtdwqggiyasptiagsrpggiSAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLS 369
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767964186 370 VIALGSR-----DFDIYRLSNLMTAKG-WNLNQLQF--PPSIHFCITLLHARKRVAIQFLKDIRES 427
Cdd:cd06450 280 LVCFRLKpsvklDELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIERA 345
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
35-428 |
2.95e-89 |
|
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: 280.18 E-value: 2.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 35 ALPSQGLSSSAVLEKLKE-YSSMDAFWQEGRASGTVYSG---EEKLTELLVKAYGdfawSNPLHPDIFPGLRKIEAEIVR 110
Cdd:COG0076 39 PLPEEGLPPEEALAELEDlVLPGSVDWNHPRFLAFVTGGttpAALAADLLASALN----QNMGDWDTSPAATELEREVVR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 111 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEK--------GIKTPEIVAPQSAHAAFNKAASYFGMK---IVRV 179
Cdd:COG0076 115 WLADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglpGAPRPRIVVSEEAHSSVDKAARLLGLGrdaLRKV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 180 PLTKMMEVDVRAMRRAISR------NTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEkagypL 253
Cdd:COG0076 195 PVDEDGRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGFALPSPE-----L 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 254 EHPFDfRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVD-----TDWQGGI-YASPTIAGSRPGGIsAACWAA 327
Cdd:COG0076 270 RHLLD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHasylgPADDGVPnLGDYTLELSRRFRA-LKLWAT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 328 LMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIA-------LGSRDFDIYRLSNLMTAKGwnlnQLQFP 400
Cdd:COG0076 348 LRALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVCfrykpagLDEEDALNYALRDRLRARG----RAFLS 423
|
410 420 430
....*....|....*....|....*....|....*
gi 767964186 401 PS-------IHFCITLLHARKRVAIQFLKDIRESV 428
Cdd:COG0076 424 PTkldgrvvLRLVVLNPRTTEDDVDALLDDLREAA 458
|
|
| tyr_de_CO2_Arch |
TIGR03812 |
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of ... |
42-426 |
1.02e-82 |
|
tyrosine decarboxylase MnfA; Members of this protein family are the archaeal form, MnfA, of tyrosine decarboxylase, and are involved in methanofuran biosynthesis. Members show clear homology to the Enterococcus form, Tdc, that is involved in tyrosine decarboxylation for resistance to acidic conditions. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 274796 Cd Length: 373 Bit Score: 260.36 E-value: 1.02e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 42 SSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTellVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGgPD 121
Cdd:TIGR03812 1 SEEEVLEELKEYRSEDLKYSDGRILGSMCTNPHPIA---VKAYDMFIETNLGDPGLFPGTKKIEEEVVGSLGNLLHL-PD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 122 SCGCVTSGGTESILMACKAYRDLAFEKGiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTA 201
Cdd:TIGR03812 77 AYGYIVSGGTEANIQAVRAAKNLAREEK-RTPNIIVPESAHFSFEKAAEMLGLELRYAPLDEDYTVDVKDVEDLIDDNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 202 MLV--CSTPQFphGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLehPFDFRVKGVTSISADTHKYGYAPK 279
Cdd:TIGR03812 156 GIVgiAGTTEL--GQIDDIEELSKIALENGIYLHVDAAFGGFVIPFLKKGYNPP--PFDFSLPGVQSITIDPHKMGLSPI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 280 GSSLVLYSDKKYRNYqFFVDTDWQGGIYASpTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKG 359
Cdd:TIGR03812 232 PAGGILFRSKSYLKY-LSVDAPYLTVKKQA-TITGTRSGASAAATYAVIKYLGREGYRKIVAECMENTRYLVEELKKIGF 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767964186 360 IFVFgNPQLSVIALGSRDFDiyRLSNLMTAKGWNLNQLQFPPSIHFcITLLHARKRVAIQFLKDIRE 426
Cdd:TIGR03812 310 EPVI-EPVLNIVAFEVDDPE--EVRKKLRDRGWYVSVTRCPKALRI-VVMPHVTREHIEEFLEDLKE 372
|
|
| PRK02769 |
PRK02769 |
histidine decarboxylase; Provisional |
121-373 |
4.26e-14 |
|
histidine decarboxylase; Provisional
Pssm-ID: 235068 [Multi-domain] Cd Length: 380 Bit Score: 73.54 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 121 DSCGCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT 200
Cdd:PRK02769 84 ESWGYITNGGTEGNLYGCYLAREL-FPDGT----LYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 201 ---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP---LHVDACLGGFLIVFMEKagyplEHPFDFRvKGVTSISADTHKY 274
Cdd:PRK02769 159 nqpPIIFANIGTTMTGAIDNIKEIQEILKKIGIDdyyIHADAALSGMILPFVNN-----PPPFSFA-DGIDSIAISGHKF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 275 GYAPKGSSLVLySDKKYRNyQFFVDTDWQGGiyASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSEL 354
Cdd:PRK02769 233 IGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRL 308
|
250
....*....|....*....
gi 767964186 355 ENIkGIFVFGNPQLSVIAL 373
Cdd:PRK02769 309 QAN-GIPAWRNPNSITVVF 326
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
127-372 |
1.17e-13 |
|
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: 72.28 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTESILMACKAYRDlAFEKGiktPEIVAPQS-AHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAm 202
Cdd:pfam00266 67 TSGTTEAINLVALSLGR-SLKPG---DEIVITEMeHHANLVpwqELAKRTGARVRVLPLDEDGLLDLDELEKLITPKTK- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 203 LVCSTP-QFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmekAGYPlEHPFDFRVKGVTSISADTHKYgYAPKGS 281
Cdd:pfam00266 142 LVAITHvSNVTGTIQPVPEIGKLAHQYGALVLVDAA-----------QAIG-HRPIDVQKLGVDFLAFSGHKL-YGPTGI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 282 SlVLY------------------SDKKYRNYQFFVDTDW--QGGiyaSPTIAGsrpggiSAACWAALMHFGENGYVEATK 341
Cdd:pfam00266 209 G-VLYgrrdllekmppllggggmIETVSLQESTFADAPWkfEAG---TPNIAG------IIGLGAALEYLSEIGLEAIEK 278
|
250 260 270
....*....|....*....|....*....|..
gi 767964186 342 QIIKTARFLKSELENIKGIFVFGNPQL-SVIA 372
Cdd:pfam00266 279 HEHELAQYLYERLLSLPGIRLYGPERRaSIIS 310
|
|
| Pyridoxal_deC |
pfam00282 |
Pyridoxal-dependent decarboxylase conserved domain; |
111-356 |
1.12e-12 |
|
Pyridoxal-dependent decarboxylase conserved domain;
Pssm-ID: 395219 Cd Length: 373 Bit Score: 69.37 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 111 IACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAF----EKG--------IKTPEIVAPQSAHAAFNKAASYFGMKIVR 178
Cdd:pfam00282 92 LGLPAEFLGQEGGGVLQPGSSESNLLALLAARTKWIkrmkAAGkpadssgiLAKLVAYTSDQAHSSIEKAALYGGVKLRE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 179 VPLTKMMEVDVRAMRRAISRN-----TAMLVCSTPQFP-HGVIDPVPEVAKLAVKYKIPLHVDACLGGFLivFMEkagyP 252
Cdd:pfam00282 172 IPSDDNGKMRGMDLEKAIEEDkenglIPFFVVATLGTTgSGAFDDLQELGDICAKHNLWLHVDAAYGGSA--FIC----P 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 253 LEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASP-----TIAGSRPGGIsAACWAA 327
Cdd:pfam00282 246 EFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSRRFRI-LKLWFV 324
|
250 260
....*....|....*....|....*....
gi 767964186 328 LMHFGENGYVEATKQIIKTARFLKSELEN 356
Cdd:pfam00282 325 IRSLGVEGLQNQIRRHVELAQYLEALIRK 353
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
127-370 |
5.33e-12 |
|
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: 67.38 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTESILMACKAyrdLAFEKGIKTPEIVAPQSAHAAFNKAASYF---GMKIVRVPLTKMMEVDVRAMRRAISRNTA-- 201
Cdd:COG1104 68 TSGGTEANNLAIKG---AARAYRKKGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDGRVDLEALEAALRPDTAlv 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 202 --MLVCS-TpqfphGVIDPVPEVAKLAVKYKIPLHVDAC--LGgflivfmekagypleH-PFDFRVKGVTSISADTHKYg 275
Cdd:COG1104 145 svMHANNeT-----GTIQPIAEIAEIAKEHGVLFHTDAVqaVG---------------KiPVDVKELGVDLLSLSAHKI- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 276 YAPKGSSlVLYSDKkyrnyqffvdtdwqgGIYASPTIAGS------RPG--------GISAACWAALMHF-GENGYVEAT 340
Cdd:COG1104 204 YGPKGVG-ALYVRK---------------GVRLEPLIHGGgqerglRSGtenvpgivGLGKAAELAAEELeEEAARLRAL 267
|
250 260 270
....*....|....*....|....*....|
gi 767964186 341 KQiiktaRFLKSELENIKGIFVFGNPQLSV 370
Cdd:COG1104 268 RD-----RLEEGLLAAIPGVVINGDPENRL 292
|
|
| PLN03032 |
PLN03032 |
serine decarboxylase; Provisional |
102-355 |
2.31e-10 |
|
serine decarboxylase; Provisional
Pssm-ID: 166673 [Multi-domain] Cd Length: 374 Bit Score: 62.15 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 102 RKIEAEIVRIACSLFNGGPDS-CGCVTSGGTESILMACKAYRDlAFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVP 180
Cdd:PLN03032 65 RQFEVGVLDWFARLWELEKDEyWGYITTCGTEGNLHGILVGRE-VFPDGI----LYASRESHYSVFKAARMYRMEAVKVP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 181 LTKMMEVDVRAMRRAISRNT---AMLVCSTPQFPHGVIDPVPEVAKLAVKYKIP-----LHVDACLGGFLIVFMEKAgyP 252
Cdd:PLN03032 140 TLPSGEIDYDDLERALAKNRdkpAILNVNIGTTVKGAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA--P 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 253 LehpFDFRvKGVTSISADTHKYGYAPKGSSLVLySDKKY-----RNYQFFVDTDwqggiyasPTIAGSRPGGISAACWAA 327
Cdd:PLN03032 218 E---VTFR-KPIGSVSVSGHKFLGCPMPCGVAL-TRKKHvkalsQNVEYLNSRD--------ATIMGSRNGHAPLYLWYT 284
|
250 260
....*....|....*....|....*...
gi 767964186 328 LMHFGENGYVEATKQIIKTARFLKSELE 355
Cdd:PLN03032 285 LRRKGYRGIKRDVQHCMRNAHYLKDRLT 312
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
155-366 |
1.98e-08 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 56.09 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 155 IVAPQSAHAaFNKA-----ASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFpHGVI-DPVPEVAKLAVKY 228
Cdd:cd00613 111 VLVPDSAHP-TNPAvartrGEPLGIEVVEVPSDEGGTVDLEALKEEVSEEVAALMVQYPNT-LGVFeDLIKEIADIAHSA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 229 KIPLHVDA---CLGGflivfmekagypLEHPFDFrvkGVTSISADTHKYG------------------YAPK--GsSLVL 285
Cdd:cd00613 189 GALVYVDGdnlNLTG------------LKPPGEY---GADIVVGNLQKTGvphggggpgagffavkkeLVRFlpG-RLVG 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 286 YSDKKYRNYQFFVDtdwqggiYASPTIAGSRPGGISAACWA-----------ALMHfGENGYVEATKQIIKTARFLKSEL 354
Cdd:cd00613 253 VTKDAEGNRAFRLA-------LQTREQHIRREKATSNICTGqallalmaamyIVYL-GPEGLKEIAERAHLNANYLAKRL 324
|
250
....*....|..
gi 767964186 355 ENIKGIFVFGNP 366
Cdd:cd00613 325 KEVGGVLPFNGP 336
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
125-241 |
2.70e-08 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate 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. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 55.43 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 125 CVTSGGTESILMACKAYRDlafekgiKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK--MMEVDVRAMRRAISRNTAM 202
Cdd:cd00609 63 VVTNGAQEALSLLLRALLN-------PGDEVLVPDPTYPGYEAAARLAGAEVVPVPLDEegGFLLDLELLEAAKTPKTKL 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 767964186 203 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVDACLGGF 241
Cdd:cd00609 136 LYLNNPNNPTGAVLSEEEleeLAELAKKHGILIISDEAYAEL 177
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
127-280 |
5.53e-08 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 54.66 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTES----ILMACKAYRDlafekgiKTPEIVAPQSAHAAFN---KAASYFGMKIVRVPLTKMMEVDVRAMRRAISRN 199
Cdd:PLN02651 66 TSGATESnnlaIKGVMHFYKD-------KKKHVITTQTEHKCVLdscRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 200 TAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDAClggflivfmEKAGyplEHPFDFRVKGVTSISADTHKYgYAPK 279
Cdd:PLN02651 139 TALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDAA---------QAVG---KIPVDVDDLGVDLMSISGHKI-YGPK 205
|
.
gi 767964186 280 G 280
Cdd:PLN02651 206 G 206
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
105-259 |
1.97e-07 |
|
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: 50.84 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 105 EAEIVRIACSLFNGGpDSCGCVTSGGTESILMACKAYRdlafekGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVP--LT 182
Cdd:cd01494 2 LEELEEKLARLLQPG-NDKAVFVPSGTGANEAALLALL------GPGDEVIVDANGHGSRYWVAAELAGAKPVPVPvdDA 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767964186 183 KMMEVDVRAMR-RAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmeKAGYPLEHPFDF 259
Cdd:cd01494 75 GYGGLDVAILEeLKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPA--PGVLIPEGGADV 150
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
127-237 |
3.14e-07 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 52.45 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTESILMACKAYRDLafEKGiktPEIVAPQSAHAA----FNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAM 202
Cdd:COG0520 83 TRGTTEAINLVAYGLGRL--KPG---DEILITEMEHHSnivpWQELAERTGAEVRVIPLDEDGELDLEALEALLTPRTKL 157
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767964186 203 LVCStpqfpH-----GVIDPVPEVAKLAVKYKIPLHVDAC 237
Cdd:COG0520 158 VAVT-----HvsnvtGTVNPVKEIAALAHAHGALVLVDGA 192
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
125-235 |
4.28e-06 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 48.84 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 125 CVTSGGTESILMACKayrdLAFEKGiktPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKM--MEVDVRAMRRAISRNTAM 202
Cdd:pfam00155 67 VFGSGAGANIEALIF----LLANPG---DAILVPAPTYASYIRIARLAGGEVVRYPLYDSndFHLDFDALEAALKEKPKV 139
|
90 100 110
....*....|....*....|....*....|....*.
gi 767964186 203 LVCSTPQFPHGVIDPVPE---VAKLAVKYKIPLHVD 235
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVD 175
|
|
| PLN02590 |
PLN02590 |
probable tyrosine decarboxylase |
117-289 |
6.89e-06 |
|
probable tyrosine decarboxylase
Pssm-ID: 178200 [Multi-domain] Cd Length: 539 Bit Score: 48.55 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 117 NGGpdscGCVTSGGTESILMACKAYRDLAFEKGIKT--PEIVAPQS--AHAAFNKAASYFGM-----KIVRVPLTKMMEV 187
Cdd:PLN02590 194 NGG----GVIQGTGCEAVLVVVLAARDRILKKVGKTllPQLVVYGSdqTHSSFRKACLIGGIheeniRLLKTDSSTNYGM 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 188 DVRAMRRAISRNTA-----MLVCST-PQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFmekagyPLEHPFDFRV 261
Cdd:PLN02590 270 PPESLEEAISHDLAkgfipFFICATvGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIC------PEYRKFIDGI 343
|
170 180
....*....|....*....|....*...
gi 767964186 262 KGVTSISADTHKYGYAPKGSSLVLYSDK 289
Cdd:PLN02590 344 ENADSFNMNAHKWLFANQTCSPLWVKDR 371
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
127-327 |
1.12e-05 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 47.42 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 127 TSGGTESILMACKAYRDLAFEKG---IKTPeiVAPQSAHAAFNKAASYfGMKIVRVPLTKMMEVDVRAMRRAISRNTAML 203
Cdd:PRK02948 66 TSGGTESNYLAIQSLLNALPQNKkhiITTP--MEHASIHSYFQSLESQ-GYTVTEIPVDKSGLIRLVDLERAITPDTVLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 204 VCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDaCLGGFLIVfmekagyplehPFDFRVKGVTSISADTHKYgYAPKGSSL 283
Cdd:PRK02948 143 SIQHANSEIGTIQPIAEIGALLKKYNVLFHSD-CVQTFGKL-----------PIDVFEMGIDSLSVSAHKI-YGPKGVGA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767964186 284 VlYSDKKYRNYQFFVDTDWQGGIyasptiagsRPG-----GISAACWAA 327
Cdd:PRK02948 210 V-YINPQVRWKPVFPGTTHEKGF---------RPGtvnvpGIAAFLTAA 248
|
|
| SepSecS |
pfam05889 |
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ... |
126-239 |
2.81e-04 |
|
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, SepSecS, of several eukaryotic and archaeal proteins, was involved in antigen-antibodies responses in the liver and pancreas. Structural studies show that the family is O-phosphoseryl-tRNA(Sec) selenium transferase, an enzyme involved in the synthesis of the amino acid selenocysteine (Sec). Sec is the only amino acid whose biosynthesis occurs on its cognate transfer RNA (tRNA). SepSecS catalyzes the final step in the formation of the amino acid. The early observation that autoantibodies isolated from patients with type I autoimmune hepatitis targeted a ribonucleoprotein complex containing tRNASec led to the identification and characterization of the archaeal and the human SepSecS. SepSecS forms its own branch in the family of fold-type I pyridoxal phosphate (PLP) enzymes that goes back to the last universal common ancestor which explains why the archaeal sequences Swiss:Q8TXK0 and Swiss:Q8TYR3 are annotated as being pyridoxal phosphate-dependent enzymes.
Pssm-ID: 399111 Cd Length: 389 Bit Score: 42.96 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 126 VTSGGTESILMACKayrdLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTK---MMEVDVRAMRRAISR---N 199
Cdd:pfam05889 79 VVPLATGMSLALCL----SALRKRPKAKYVIWPRIDQKSSIKAAERAGFEPRLVETVLdgdYLITDVNDVETIIEEkgeE 154
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 767964186 200 TAMLVCSTPQ-FPHGVIDPVPEVAKLAVKYKIPLHVDACLG 239
Cdd:pfam05889 155 VILAVLSTTScFAPRSPDNVKEIAKICAEYDVPHLVNGAYG 195
|
|
| PRK00451 |
PRK00451 |
aminomethyl-transferring glycine dehydrogenase subunit GcvPA; |
129-225 |
4.10e-04 |
|
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
Pssm-ID: 234769 [Multi-domain] Cd Length: 447 Bit Score: 42.82 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 129 GGT---ESILMACKAYrdlafekgiKTPEIVAPQSAHA-AFNKAASYF---GMKIVRVPLTKMMeVDVRAMRRAISRNTA 201
Cdd:PRK00451 137 GATalaEAALMAVRIT---------KRKKVLVSGAVHPeYREVLKTYLkgqGIEVVEVPYEDGV-TDLEALEAAVDDDTA 206
|
90 100
....*....|....*....|....
gi 767964186 202 MLVCSTPQFpHGVIDPVPEVAKLA 225
Cdd:PRK00451 207 AVVVQYPNF-FGVIEDLEEIAEIA 229
|
|
| PLN02263 |
PLN02263 |
serine decarboxylase |
124-356 |
7.96e-04 |
|
serine decarboxylase
Pssm-ID: 177904 [Multi-domain] Cd Length: 470 Bit Score: 41.73 E-value: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 124 GCVTSGGTESILMACKAYRDLaFEKGIktpeIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNT--- 200
Cdd:PLN02263 155 GYITNCGTEGNLHGILVGREV-FPDGI----LYASRESHYSVFKAARMYRMECVKVDTLVSGEIDCADFKAKLLANKdkp 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 201 AMLVCSTPQFPHGVIDPVPEVAKLA-----VKYKIPLHVDACLGGFLIVFMEKAgyPLehpFDFRvKGVTSISADTHKYG 275
Cdd:PLN02263 230 AIINVNIGTTVKGAVDDLDLVIKTLeecgfSQDRFYIHCDGALFGLMMPFVKRA--PK---VTFK-KPIGSVSVSGHKFV 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 276 YAPKGSSLVL----YSDKKYRNYQFFVDTDwqggiyasPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLK 351
Cdd:PLN02263 304 GCPMPCGVQItrmeHINVLSSNVEYLASRD--------ATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLK 375
|
....*
gi 767964186 352 SELEN 356
Cdd:PLN02263 376 DRLRE 380
|
|
| PRK08361 |
PRK08361 |
aspartate aminotransferase; Provisional |
132-230 |
1.87e-03 |
|
aspartate aminotransferase; Provisional
Pssm-ID: 236248 [Multi-domain] Cd Length: 391 Bit Score: 40.63 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767964186 132 ESILMACKAYRD--LAFEKGIKT-PEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMME--VDVRAMRRAISRNTAMLVCS 206
Cdd:PRK08361 94 DNVIVTAGAYEAtyLAFESLLEEgDEVIIPDPAFVCYVEDAKIAEAKPIRIPLREENEfqPDPDELLELITKRTRMIVIN 173
|
90 100
....*....|....*....|....*..
gi 767964186 207 TPQFPHGVI---DPVPEVAKLAVKYKI 230
Cdd:PRK08361 174 YPNNPTGATldkEVAKAIADIAEDYNI 200
|
|
| PRK09105 |
PRK09105 |
pyridoxal phosphate-dependent aminotransferase; |
151-224 |
4.10e-03 |
|
pyridoxal phosphate-dependent aminotransferase;
Pssm-ID: 181651 Cd Length: 370 Bit Score: 39.26 E-value: 4.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767964186 151 KTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAiSRNTAMLVCSTPQFPHGVIDPVPEVAKL 224
Cdd:PRK09105 118 PTAGLVTADPTYEAGWRAADAQGAPVAKVPLRADGAHDVKAMLAA-DPNAGLIYICNPNNPTGTVTPRADIEWL 190
|
|
| |
