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Conserved domains on  [gi|21355963|ref|NP_652032|]
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Sphingosine-1-phosphate lyase, isoform A [Drosophila melanogaster]

Protein Classification

aspartate aminotransferase family protein( domain architecture ID 10157828)

aspartate aminotransferase family protein is a pyridoxal phosphate (PLP)-dependent enzyme similar to cysteine sulfinic acid decarboxylase that catalyzes the decarboxylation of L-aspartate, 3-sulfino-L-alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine, and taurine, respectively

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 132-494 1.24e-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: 340.72  E-value: 1.24e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 132 RVSGAVYGYKPDLVELVTEVYGKASYTNPlhADLFPGVCKMEAEVVRMACNLFHG-NSASCGTMTTGGTESIVMAMKAYR 210
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLpSEDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 211 DFAREY------KGITRPNIVVPKTVHAAFDKGGQYFNIHVRSVDVDPETyEVDIKKFKRAINR------NTILLVGSAP 278
Cdd:cd06450  79 DRARKRlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDG-RMDPEALEAAIDEdkaeglNPIMVVATAG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 279 NFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFVVALVRNAGYklrpfDFEVKGVTSISADTHKYGFAPKGSSVILYSdk 358
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL-----DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 359 kykdhqftvttdwpggvygsptvngsraggiIAACWATMMSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATS 438
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355963 439 VIALGSNV-----FDIFRLSDSLCKLG-WNLNALQF--PSGIHLCVTDMHTQPGVADKFIADVR 494
Cdd:cd06450 280 LVCFRLKPsvkldELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIE 343
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 132-494 1.24e-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: 340.72  E-value: 1.24e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 132 RVSGAVYGYKPDLVELVTEVYGKASYTNPlhADLFPGVCKMEAEVVRMACNLFHG-NSASCGTMTTGGTESIVMAMKAYR 210
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLpSEDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 211 DFAREY------KGITRPNIVVPKTVHAAFDKGGQYFNIHVRSVDVDPETyEVDIKKFKRAINR------NTILLVGSAP 278
Cdd:cd06450  79 DRARKRlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDG-RMDPEALEAAIDEdkaeglNPIMVVATAG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 279 NFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFVVALVRNAGYklrpfDFEVKGVTSISADTHKYGFAPKGSSVILYSdk 358
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL-----DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 359 kykdhqftvttdwpggvygsptvngsraggiIAACWATMMSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATS 438
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355963 439 VIALGSNV-----FDIFRLSDSLCKLG-WNLNALQF--PSGIHLCVTDMHTQPGVADKFIADVR 494
Cdd:cd06450 280 LVCFRLKPsvkldELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIE 343
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 100-499 1.83e-90

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: 285.19  E-value: 1.83e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 100 SETLPEKGLSKEEILRLVDEHLKTGHYNWRDGRVSGAVYGYkPDLVELVTEVYGKASYTNPLHADLFPGVCKMEAEVVRM 179
Cdd:COG0076  37 DEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGG-TTPAALAADLLASALNQNMGDWDTSPAATELEREVVRW 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 180 ACNLFHGNSASCGTMTTGGTESIVMAMKAYRDFAREY-------KGITRPNIVVPKTVHAAFDKGGQYFNI---HVRSVD 249
Cdd:COG0076 116 LADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglPGAPRPRIVVSEEAHSSVDKAARLLGLgrdALRKVP 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 250 VDPEtYEVDIKKFKRAINR------NTILLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFvvALVRNAGYKL 323
Cdd:COG0076 196 VDED-GRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGF--ALPSPELRHL 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 324 rpFDfEVKGVTSISADTHKYGFAPKGSSVILYSDKKYKDHQFTVTTD-WPGGVYGSP-----TVNGSRAGGIIAAcWATM 397
Cdd:COG0076 273 --LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASyLGPADDGVPnlgdyTLELSRRFRALKL-WATL 348

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 398 MSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATSVIAlgsnvfdiFRL-SDSLCKLGWNLNALQ--------- 467
Cdd:COG0076 349 RALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVC--------FRYkPAGLDEEDALNYALRdrlrargra 420

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 21355963 468 FPSG--------IHLCVTDMHTQPGVADKFIADVRSCTAE 499
Cdd:COG0076 421 FLSPtkldgrvvLRLVVLNPRTTEDDVDALLDDLREAAAE 460
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
101-424 1.10e-17

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 84.78  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   101 ETLPEKGLSKEEILRLVDEHLKTGHYNWRDGRVSgAVYGYKPDLVELVTEVYGKASYTNPLHADLFPGVCKMEAEVVRMA 180
Cdd:pfam00282  10 LAAPIIPEPELQIDGDIRRNLMPGVTTWHSPHFH-AYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   181 CNLFH-----GNSASCGTMTTGGTESIVMA-MKAYRDFAREYK---------GIT-RPNIVVPKTVHAAFDKGGQYFNIH 244
Cdd:pfam00282  89 GEMLGlpaefLGQEGGGVLQPGSSESNLLAlLAARTKWIKRMKaagkpadssGILaKLVAYTSDQAHSSIEKAALYGGVK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   245 VRSVDVDPE--TYEVDIKKFKRAINRNTILLVGSAPNFP---YGTIDDIEAIAALGVKYDIPVHVDACL-GSFVVAlvrn 318
Cdd:pfam00282 169 LREIPSDDNgkMRGMDLEKAIEEDKENGLIPFFVVATLGttgSGAFDDLQELGDICAKHNLWLHVDAAYgGSAFIC---- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   319 agYKLRPFDFEVKGVTSISADTHKYGFAPKGSSVILYSDKKYKDHQFTVTTDWPGGVYGSP-----TVNGSRaGGIIAAC 393
Cdd:pfam00282 245 --PEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSR-RFRILKL 321

                         330       340       350
                  ....*....|....*....|....*....|.
gi 21355963   394 WATMMSFGYDGYLEATKRIVDTARYIERGVR 424
Cdd:pfam00282 322 WFVIRSLGVEGLQNQIRRHVELAQYLEALIR 352
PRK02769 PRK02769
histidine decarboxylase; Provisional
 171-418 2.14e-10

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 62.37  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  171 KMEAEVVRMACNLFHGNSA-SCGTMTTGGTESIVMAMkaYrdFAREYkgitRPN--IVVPKTVHAAFDKGGQYFNIHVRS 247
Cdd:PRK02769  65 DFERDVMNFFAELFKIPFNeSWGYITNGGTEGNLYGC--Y--LAREL----FPDgtLYYSKDTHYSVSKIARLLRIKSRV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  248 VDVDPETyEVD----IKKFKRAINRNTILL--VGSAPNfpyGTIDDIEAIAALGVKY---DIPVHVDACLGSFVVALVRN 318
Cdd:PRK02769 137 ITSLPNG-EIDyddlISKIKENKNQPPIIFanIGTTMT---GAIDNIKEIQEILKKIgidDYYIHADAALSGMILPFVNN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  319 AgyklRPFDFEvKGVTSISADTHKYGFAPKGSSVILySDKKYKDhQFTVTTDWPGGvyGSPTVNGSRAGGIIAACWATMM 398
Cdd:PRK02769 213 P----PPFSFA-DGIDSIAISGHKFIGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIR 283

                        250       260
                 ....*....|....*....|
gi 21355963  399 SFGYDGYLEATKRIVDTARY 418
Cdd:PRK02769 284 SLGSKGLRQRVQHCLDMAQY 303
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 173-312 5.14e-06

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 48.88  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   173 EAEVVRMACNLFHGNSASCGTMTTGGTESIVMAMKAyrdfareykgITRP--NIVVPKTVHAAFDKGGQYFNIHVRSVDV 250
Cdd:TIGR01265  80 EAVAEYLSSDLPGKLTADDVVLTSGCSQAIEICIEA----------LANPgaNILVPRPGFPLYDTRAAFSGLEVRLYDL 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355963   251 DPET-YEVDIKKFKRAINRNTILLVGSAPNFPYGTI---DDIEAIAALGVKYDIPVHVDACLGSFV 312
Cdd:TIGR01265 150 LPEKdWEIDLDGLESLADEKTVAIVVINPSNPCGSVfsrDHLQKIAEVAEKLGIPIIADEIYGHMV 215
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 132-494 1.24e-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: 340.72  E-value: 1.24e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 132 RVSGAVYGYKPDLVELVTEVYGKASYTNPlhADLFPGVCKMEAEVVRMACNLFHG-NSASCGTMTTGGTESIVMAMKAYR 210
Cdd:cd06450   1 FLAGFVTTMDPPALLLEMLTSAKNAIDFT--WDESPAATEMEAEVVNWLAKLFGLpSEDADGVFTSGGSESNLLALLAAR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 211 DFAREY------KGITRPNIVVPKTVHAAFDKGGQYFNIHVRSVDVDPETyEVDIKKFKRAINR------NTILLVGSAP 278
Cdd:cd06450  79 DRARKRlkagggRGIDKLVIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDG-RMDPEALEAAIDEdkaeglNPIMVVATAG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 279 NFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFVVALVRNAGYklrpfDFEVKGVTSISADTHKYGFAPKGSSVILYSdk 358
Cdd:cd06450 158 TTDTGAIDPLEEIADLAEKYDLWLHVDAAYGGFLLPFPEPRHL-----DFGIERVDSISVDPHKYGLVPLGCSAVLVR-- 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 359 kykdhqftvttdwpggvygsptvngsraggiIAACWATMMSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATS 438
Cdd:cd06450 231 -------------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNLS 279

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355963 439 VIALGSNV-----FDIFRLSDSLCKLG-WNLNALQF--PSGIHLCVTDMHTQPGVADKFIADVR 494
Cdd:cd06450 280 LVCFRLKPsvkldELNYDLSDRLNERGgWHVPATTLggPNVLRFVVTNPLTTRDDADALLEDIE 343
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
 100-499 1.83e-90

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: 285.19  E-value: 1.83e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 100 SETLPEKGLSKEEILRLVDEHLKTGHYNWRDGRVSGAVYGYkPDLVELVTEVYGKASYTNPLHADLFPGVCKMEAEVVRM 179
Cdd:COG0076  37 DEPLPEEGLPPEEALAELEDLVLPGSVDWNHPRFLAFVTGG-TTPAALAADLLASALNQNMGDWDTSPAATELEREVVRW 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 180 ACNLFHGNSASCGTMTTGGTESIVMAMKAYRDFAREY-------KGITRPNIVVPKTVHAAFDKGGQYFNI---HVRSVD 249
Cdd:COG0076 116 LADLLGLPEGAGGVFTSGGTEANLLALLAARDRALARrvraeglPGAPRPRIVVSEEAHSSVDKAARLLGLgrdALRKVP 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 250 VDPEtYEVDIKKFKRAINR------NTILLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFvvALVRNAGYKL 323
Cdd:COG0076 196 VDED-GRMDPDALEAAIDEdraaglNPIAVVATAGTTNTGAIDPLAEIADIAREHGLWLHVDAAYGGF--ALPSPELRHL 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 324 rpFDfEVKGVTSISADTHKYGFAPKGSSVILYSDKKYKDHQFTVTTD-WPGGVYGSP-----TVNGSRAGGIIAAcWATM 397
Cdd:COG0076 273 --LD-GIERADSITVDPHKWLYVPYGCGAVLVRDPELLREAFSFHASyLGPADDGVPnlgdyTLELSRRFRALKL-WATL 348

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 398 MSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATSVIAlgsnvfdiFRL-SDSLCKLGWNLNALQ--------- 467
Cdd:COG0076 349 RALGREGYRELIERCIDLARYLAEGIAALPGFELLAPPELNIVC--------FRYkPAGLDEEDALNYALRdrlrargra 420

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 21355963 468 FPSG--------IHLCVTDMHTQPGVADKFIADVRSCTAE 499
Cdd:COG0076 421 FLSPtkldgrvvLRLVVLNPRTTEDDVDALLDDLREAAAE 460
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
101-424 1.10e-17

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 84.78  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   101 ETLPEKGLSKEEILRLVDEHLKTGHYNWRDGRVSgAVYGYKPDLVELVTEVYGKASYTNPLHADLFPGVCKMEAEVVRMA 180
Cdd:pfam00282  10 LAAPIIPEPELQIDGDIRRNLMPGVTTWHSPHFH-AYMPTGNSYPSLLGDMLTDAINCNGFTWESSPACTELENVVMNWL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   181 CNLFH-----GNSASCGTMTTGGTESIVMA-MKAYRDFAREYK---------GIT-RPNIVVPKTVHAAFDKGGQYFNIH 244
Cdd:pfam00282  89 GEMLGlpaefLGQEGGGVLQPGSSESNLLAlLAARTKWIKRMKaagkpadssGILaKLVAYTSDQAHSSIEKAALYGGVK 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   245 VRSVDVDPE--TYEVDIKKFKRAINRNTILLVGSAPNFP---YGTIDDIEAIAALGVKYDIPVHVDACL-GSFVVAlvrn 318
Cdd:pfam00282 169 LREIPSDDNgkMRGMDLEKAIEEDKENGLIPFFVVATLGttgSGAFDDLQELGDICAKHNLWLHVDAAYgGSAFIC---- 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   319 agYKLRPFDFEVKGVTSISADTHKYGFAPKGSSVILYSDKKYKDHQFTVTTDWPGGVYGSP-----TVNGSRaGGIIAAC 393
Cdd:pfam00282 245 --PEFRHWLFGIERADSITFNPHKWMLVLLDCSAVWVKDKEALQQAFQFNPLYLGHTDSAYdtghkQIPLSR-RFRILKL 321

                         330       340       350
                  ....*....|....*....|....*....|.
gi 21355963   394 WATMMSFGYDGYLEATKRIVDTARYIERGVR 424
Cdd:pfam00282 322 WFVIRSLGVEGLQNQIRRHVELAQYLEALIR 352
NifS COG1104
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ...
 195-349 2.54e-11

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: 65.45  E-value: 2.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 195 TTGGTESIVMAMKAyrdFAREYKGiTRPNIVVPKTVHAAFDKGGQYF---NIHVRSVDVDPETyEVDIKKFKRAINRNTI 271
Cdd:COG1104  68 TSGGTEANNLAIKG---AARAYRK-KGKHIITSAIEHPAVLETARFLekeGFEVTYLPVDEDG-RVDLEALEAALRPDTA 142

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355963 272 LL-VGSApNFPYGTIDDIEAIAALGVKYDIPVHVDAclgsfvvalVRNAGyKLrPFDFEVKGVTSISADTHKYGfAPKG 349
Cdd:COG1104 143 LVsVMHA-NNETGTIQPIAEIAEIAKEHGVLFHTDA---------VQAVG-KI-PVDVKELGVDLLSLSAHKIY-GPKG 208
PRK02769 PRK02769
histidine decarboxylase; Provisional
 171-418 2.14e-10

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 62.37  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  171 KMEAEVVRMACNLFHGNSA-SCGTMTTGGTESIVMAMkaYrdFAREYkgitRPN--IVVPKTVHAAFDKGGQYFNIHVRS 247
Cdd:PRK02769  65 DFERDVMNFFAELFKIPFNeSWGYITNGGTEGNLYGC--Y--LAREL----FPDgtLYYSKDTHYSVSKIARLLRIKSRV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  248 VDVDPETyEVD----IKKFKRAINRNTILL--VGSAPNfpyGTIDDIEAIAALGVKY---DIPVHVDACLGSFVVALVRN 318
Cdd:PRK02769 137 ITSLPNG-EIDyddlISKIKENKNQPPIIFanIGTTMT---GAIDNIKEIQEILKKIgidDYYIHADAALSGMILPFVNN 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  319 AgyklRPFDFEvKGVTSISADTHKYGFAPKGSSVILySDKKYKDhQFTVTTDWPGGvyGSPTVNGSRAGGIIAACWATMM 398
Cdd:PRK02769 213 P----PPFSFA-DGIDSIAISGHKFIGSPMPCGIVL-AKKKYVE-RISVDVDYIGS--RDQTISGSRNGHTALLLWAAIR 283

                        250       260
                 ....*....|....*....|
gi 21355963  399 SFGYDGYLEATKRIVDTARY 418
Cdd:PRK02769 284 SLGSKGLRQRVQHCLDMAQY 303
PLN02651 PLN02651
cysteine desulfurase
 195-349 3.70e-07

cysteine desulfurase


Pssm-ID: 178257 [Multi-domain]  Cd Length: 364  Bit Score: 52.35  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  195 TTGGTESIVMAMKAYRDFAREYKgitrPNIVVPKTVHAA-------FDKGGqyfnIHVRSVDVDPETYeVDIKKFKRAIN 267
Cdd:PLN02651  66 TSGATESNNLAIKGVMHFYKDKK----KHVITTQTEHKCvldscrhLQQEG----FEVTYLPVKSDGL-VDLDELAAAIR 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  268 RNTILLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDAclgsfvvalVRNAGyKLrPFDFEVKGVTSISADTHKYGfAP 347
Cdd:PLN02651 137 PDTALVSVMAVNNEIGVIQPVEEIGELCREKKVLFHTDA---------AQAVG-KI-PVDVDDLGVDLMSISGHKIY-GP 204


                 ..
gi 21355963  348 KG 349
Cdd:PLN02651 205 KG 206
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
145-349 4.09e-06

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 48.96  E-value: 4.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  145 VELVTEVYGKASytnPLH-----ADLFPGVCKMEAevvrmaCNLFHGnSASCGTMTTGGTESIVMA----MKAYRDFARE 215
Cdd:PRK02948  21 QKAASQYFGNES---SLHdiggtASSLLQVCRKTF------AEMIGG-EEQGIYFTSGGTESNYLAiqslLNALPQNKKH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  216 YkgITRPniVVPKTVHAAF----DKGgqyFNIHVRSVDvdpETYEVDIKKFKRAINRNTILLVGSAPNFPYGTIDDIEAI 291
Cdd:PRK02948  91 I--ITTP--MEHASIHSYFqsleSQG---YTVTEIPVD---KSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 21355963  292 AALGVKYDIPVHVDaCLGSFVvalvrnagyKLrPFDFEVKGVTSISADTHK-YGfaPKG 349
Cdd:PRK02948 161 GALLKKYNVLFHSD-CVQTFG---------KL-PIDVFEMGIDSLSVSAHKiYG--PKG 206
tyr_nico_aTase TIGR01265
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ...
 173-312 5.14e-06

tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.


Pssm-ID: 188123  Cd Length: 403  Bit Score: 48.88  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   173 EAEVVRMACNLFHGNSASCGTMTTGGTESIVMAMKAyrdfareykgITRP--NIVVPKTVHAAFDKGGQYFNIHVRSVDV 250
Cdd:TIGR01265  80 EAVAEYLSSDLPGKLTADDVVLTSGCSQAIEICIEA----------LANPgaNILVPRPGFPLYDTRAAFSGLEVRLYDL 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355963   251 DPET-YEVDIKKFKRAINRNTILLVGSAPNFPYGTI---DDIEAIAALGVKYDIPVHVDACLGSFV 312
Cdd:TIGR01265 150 LPEKdWEIDLDGLESLADEKTVAIVVINPSNPCGSVfsrDHLQKIAEVAEKLGIPIIADEIYGHMV 215
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 194-312 1.00e-05

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: 47.72  E-value: 1.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963 194 MTTGGTESIVMAMKAYRDFAREykgitrpnIVVPKTVHAAFDKGGQYFNIHVRSVDVDPE-TYEVDIKKFKRAINRNTIL 272
Cdd:cd00609  64 VTNGAQEALSLLLRALLNPGDE--------VLVPDPTYPGYEAAARLAGAEVVPVPLDEEgGFLLDLELLEAAKTPKTKL 135

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 21355963 273 LVGSAPNFPYGTI---DDIEAIAALGVKYDIPVHVDACLGSFV 312
Cdd:cd00609 136 LYLNNPNNPTGAVlseEELEELAELAKKHGILIISDEAYAELV 178
DegT_DnrJ_EryC1 pfam01041
DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all ...
 195-310 1.40e-05

DegT/DnrJ/EryC1/StrS aminotransferase family; The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA, StsC and StsS. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyzes the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin.


Pssm-ID: 395827  Cd Length: 360  Bit Score: 47.28  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   195 TTGGTESIVMAMKAyrdfareyKGITRPNIVV------PKTVHAAfdkggqyfnIHVRS----VDVDPETYEVDIKKFKR 264
Cdd:pfam01041  45 VSSGTAALHLALRA--------LGVGPGDEVItpsftfVATANAA---------LRLGAkpvfVDIDPDTYNIDPEAIEA 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 21355963   265 AINRNT--ILLVGSapnfpYGTIDDIEAIAALGVKYDIPVHVDAC--LGS 310
Cdd:pfam01041 108 AITPRTkaIIPVHL-----YGQPADMDAIRAIAARHGLPVIEDAAhaLGA 152
PRK14012 PRK14012
IscS subfamily cysteine desulfurase;
195-349 2.09e-05

IscS subfamily cysteine desulfurase;


Pssm-ID: 184450 [Multi-domain]  Cd Length: 404  Bit Score: 46.86  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  195 TTGGTESIVMAMKAYRDFAREyKGitrPNIVVPKTVH-AAFDKGGQYFN--IHVRSVDVDPETYeVDIKKFKRAINRNTI 271
Cdd:PRK14012  72 TSGATESDNLAIKGAAHFYQK-KG---KHIITSKTEHkAVLDTCRQLERegFEVTYLDPQSNGI-IDLEKLEAAMRDDTI 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355963  272 LLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDAclgsfvvalVRNAGyKLrPFDFEVKGVTSISADTHK-YGfaPKG 349
Cdd:PRK14012 147 LVSIMHVNNEIGVIQDIAAIGEICRERGIIFHVDA---------AQSVG-KV-PIDLSKLKVDLMSFSAHKiYG--PKG 212
WecE COG0399
dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];
248-310 2.17e-05

dTDP-4-amino-4,6-dideoxygalactose transaminase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440168  Cd Length: 364  Bit Score: 46.60  E-value: 2.17e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355963 248 VDVDPETYEVDIKKFKRAINRNT--ILLVgsapNFpYGTIDDIEAIAALGVKYDIPVHVDAC--LGS 310
Cdd:COG0399  97 VDIDPDTYNIDPEALEAAITPRTkaIIPV----HL-YGQPADMDAIMAIAKKHGLKVIEDAAqaLGA 158
PRK00451 PRK00451
aminomethyl-transferring glycine dehydrogenase subunit GcvPA;
197-294 2.63e-05

aminomethyl-transferring glycine dehydrogenase subunit GcvPA;


Pssm-ID: 234769 [Multi-domain]  Cd Length: 447  Bit Score: 46.67  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  197 GGT---ESIVMAMkayrdfareykGITRPN-IVVPKTVHAAFDK------GGQyfNIHVRSVDVDPETyeVDIKKFKRAI 266
Cdd:PRK00451 137 GATalaEAALMAV-----------RITKRKkVLVSGAVHPEYREvlktylKGQ--GIEVVEVPYEDGV--TDLEALEAAV 201

                         90       100
                 ....*....|....*....|....*...
gi 21355963  267 NRNTILLVGSAPNFpYGTIDDIEAIAAL 294
Cdd:PRK00451 202 DDDTAAVVVQYPNF-FGVIEDLEEIAEI 228
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
241-307 5.99e-05

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 45.52  E-value: 5.99e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355963 241 FNIHVRSVDVDpETYEVDIKKFKRAINRNTILL-VGSAPNFpYGTIDDIEAIAALGVKYDIPVHVDAC 307
Cdd:COG0520 127 TGAEVRVIPLD-EDGELDLEALEALLTPRTKLVaVTHVSNV-TGTVNPVKEIAALAHAHGALVLVDGA 192
PRK05994 PRK05994
O-acetylhomoserine aminocarboxypropyltransferase; Validated
 234-328 1.01e-04

O-acetylhomoserine aminocarboxypropyltransferase; Validated


Pssm-ID: 180344 [Multi-domain]  Cd Length: 427  Bit Score: 44.70  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  234 FDKGGQYFNIHVRSVDVDpetyevDIKKFKRAINRNT-ILLVGSAPNfPYGTIDDIEAIAALGVKYDIPVHVDACLGSfv 312
Cdd:PRK05994 119 FGHAFKSFGWQVRWADAD------DPASFERAITPRTkAIFIESIAN-PGGTVTDIAAIAEVAHRAGLPLIVDNTLAS-- 189

                         90
                 ....*....|....*.
gi 21355963  313 valvrnaGYKLRPFDF 328
Cdd:PRK05994 190 -------PYLIRPIEH 198
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 171-355 1.40e-04

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: 44.16  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   171 KMEA--EVVRmacNLFHGNSASCGTMTTGGTESIVMAMKAYRDFAREYKGItrpnIVVPKTVHAAF-------DKGGqyF 241
Cdd:pfam00266  44 AYEEarEKVA---EFINAPSNDEIIFTSGTTEAINLVALSLGRSLKPGDEI----VITEMEHHANLvpwqelaKRTG--A 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   242 NIHVRSVDvdpETYEVDIKKFKRAINRNTILLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDAclgsfvvalVRNAGY 321
Cdd:pfam00266 115 RVRVLPLD---EDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDA---------AQAIGH 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 21355963   322 klRPFDFEVKGVTSISADTHK-YGfaPKGSSViLY 355
Cdd:pfam00266 183 --RPIDVQKLGVDFLAFSGHKlYG--PTGIGV-LY 212
PRK06225 PRK06225
pyridoxal phosphate-dependent aminotransferase;
194-300 2.37e-04

pyridoxal phosphate-dependent aminotransferase;


Pssm-ID: 235749 [Multi-domain]  Cd Length: 380  Bit Score: 43.59  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  194 MTTGGTESIVMAMKAYrdfareykgiTRP--NIVVPKTVHAAFDKGGQYFNIHVRSVDV-DPE-TYEVDIKKFKRAINRN 269
Cdd:PRK06225  88 ITAGATESLYLVMRAF----------LSPgdNAVTPDPGYLIIDNFASRFGAEVIEVPIySEEcNYKLTPELVKENMDEN 157

                         90       100       110
                 ....*....|....*....|....*....|....
gi 21355963  270 TILLVGSAPNFPYG---TIDDIEAIAALGVKYDI 300
Cdd:PRK06225 158 TRLIYLIDPLNPLGssyTEEEIKEFAEIARDNDA 191
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 245-307 6.84e-04

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


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 42.07  E-value: 6.84e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355963 245 VRSVDVDPEtYEVDIKKFKRAINRNTILL-VGSAPNFpYGTIDDIEAIAALGVKYDIPVHVDAC 307
Cdd:cd06453 116 LKVVPVDDD-GQLDLEALEKLLTERTKLVaVTHVSNV-LGTINPVKEIGEIAHEAGVPVLVDGA 177
PLN02656 PLN02656
tyrosine transaminase
 194-309 1.06e-03

tyrosine transaminase


Pssm-ID: 178262 [Multi-domain]  Cd Length: 409  Bit Score: 41.45  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  194 MTTGGTESIVMAMKAyrdfareykgITRP--NIVVPKTVHAAFDKGGQYFNIHVRSVDVDPET-YEVDIKKFKRAINRNT 270
Cdd:PLN02656 101 ITSGCTQAIDVALSM----------LARPgaNILLPRPGFPIYELCAAFRHLEVRYVDLLPEKgWEVDLDAVEALADQNT 170

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 21355963  271 ILLVGSAPNFPYGTI---DDIEAIAALGVKYDIPVHVDACLG 309
Cdd:PLN02656 171 VALVIINPGNPCGNVysyQHLKKIAETAEKLKILVIADEVYG 212
PLN02187 PLN02187
rooty/superroot1
 216-305 1.19e-03

rooty/superroot1


Pssm-ID: 215119 [Multi-domain]  Cd Length: 462  Bit Score: 41.64  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  216 YKGITRPN--IVVPKTVHAAFDKGGQYFNIHVRSVDVDPET-YEVDIKKFKRAINRNTILLVGSAPNFPYGTI---DDIE 289
Cdd:PLN02187 148 FESLARPNanILLPRPGFPHYDARAAYSGLEVRKFDLLPEKeWEIDLEGIEAIADENTVAMVVINPNNPCGNVyshDHLK 227

                         90
                 ....*....|....*.
gi 21355963  290 AIAALGVKYDIPVHVD 305
Cdd:PLN02187 228 KVAETARKLGIMVISD 243
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
194-305 1.37e-03

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 41.14  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   194 MTTGGTESIVMAMKAYRDFAREykgitrpnIVVPKTVHAAFDKGGQYFNIHVRSVDV-DPETYEVDIKKFKRAINRNTIL 272
Cdd:pfam00155  68 FGSGAGANIEALIFLLANPGDA--------ILVPAPTYASYIRIARLAGGEVVRYPLyDSNDFHLDFDALEAALKEKPKV 139

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 21355963   273 LVGSAPNFPYGTI---DDIEAIAALGVKYDIPVHVD 305
Cdd:pfam00155 140 VLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVD 175
PLN03032 PLN03032
serine decarboxylase; Provisional
 192-425 1.50e-03

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 40.96  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  192 GTMTTGGTES----IVMAMKAYRDfareykGItrpnIVVPKTVHAAFDKGGQYFNIHVRSVDVDPeTYEVDIKKFKRAIN 267
Cdd:PLN03032  88 GYITTCGTEGnlhgILVGREVFPD------GI----LYASRESHYSVFKAARMYRMEAVKVPTLP-SGEIDYDDLERALA 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  268 RN----TILLVGSAPNFPyGTIDDIEAIAALGVKYDIP-----VHVDACLGSFVVALVRNAgyklrPFDFEVKGVTSISA 338
Cdd:PLN03032 157 KNrdkpAILNVNIGTTVK-GAVDDLDRILRILKELGYTedrfyIHCDGALFGLMMPFVSRA-----PEVTFRKPIGSVSV 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963  339 DTHKYGFAPKGSSVILYSDKKYKDHQFTVttDWPGGVygSPTVNGSRAGGIIAACWATMMSFGYDGYLEATKRIVDTARY 418
Cdd:PLN03032 231 SGHKFLGCPMPCGVALTRKKHVKALSQNV--EYLNSR--DATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHY 306


                 ....*..
gi 21355963  419 IERGVRD 425
Cdd:PLN03032 307 LKDRLTE 313
SepSecS pfam05889
O-phosphoseryl-tRNA(Sec) selenium transferase, SepSecS; Early annotation suggested this family, ...
 241-427 1.68e-03

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: 41.04  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   241 FNIHVRSVDVDPETYEVDIKKFKRAINR---NTILLVGSAPNFPYGTI-DDIEAIAALGVKYDIPVHVDACLG--SFVVA 314
Cdd:pfam05889 123 FEPRLVETVLDGDYLITDVNDVETIIEEkgeEVILAVLSTTSCFAPRSpDNVKEIAKICAEYDVPHLVNGAYGiqSEEYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   315 LVRNAGYKLRPFDFEVKgvtSISADThkygFAPKGSSVILYSDkkyKDHQFTVTTDWPGGVYGSPTVNGSRaggiiaacw 394
Cdd:pfam05889 203 RKIAAAHKCGRVDAVVQ---SLDKNF----IVPVGGAIIAAFD---ESFIQEISEEYPGRASARPSKDKLI--------- 263

                         170       180       190
                  ....*....|....*....|....*....|...
gi 21355963   395 aTMMSFGYDGYLEATKRIVDTARYIERGVRDID 427
Cdd:pfam05889 264 -SLLSLGCKAYLALMKEQKEMFPLLRELLKDLA 295
tyr_amTase_E TIGR01264
tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found ...
 194-312 2.16e-03

tyrosine aminotransferase, eukaryotic; This model describes tyrosine aminotransferase as found in animals and Trypanosoma cruzi. It is the first enzyme of a pathway of tyrosine degradation via homogentisate. Several plant enzyme designated as probable tyrosine aminotransferases are very closely related to an experimentally demonstrated nicotianamine aminotransferase, an enzyme in a siderophore (iron uptake chelator) biosynthesis pathway. These plant sequences are excluded from the model seed and score between the trusted an noise cutoffs. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273529 [Multi-domain]  Cd Length: 401  Bit Score: 40.54  E-value: 2.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355963   194 MTTGGTESIVMAMKAYRDFAReykgitrpNIVVPKTVHAAFDKGGQYFNIHVRSVDVDPE-TYEVDIKKFKRAINRNTIL 272
Cdd:TIGR01264 100 LCSGCSHAIEMCIAALANAGQ--------NILVPRPGFPLYETLAESMGIEVKLYNLLPDkSWEIDLKQLESLIDEKTAA 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 21355963   273 LVGSAPNFPYGTIDD---IEAIAALGVKYDIPVHVDACLGSFV 312
Cdd:TIGR01264 172 LIVNNPSNPCGSVFSrqhLEEILAVAERQCLPIIADEIYGDMV 214
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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