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Conserved domains on  [gi|224006580|ref|XP_002292250|]
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histidine decarboxylase, partial [Thalassiosira pseudonana CCMP1335]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03032 PLN03032
serine decarboxylase; Provisional
1-366 0e+00

serine decarboxylase; Provisional


:

Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 739.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   1 SDILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWG 80
Cdd:PLN03032   9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  81 YVTTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVN 160
Cdd:PLN03032  89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 161 IGTTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 241 KEHVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 224006580 321 LERPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECK 366
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVEVR 374
 
Name Accession Description Interval E-value
PLN03032 PLN03032
serine decarboxylase; Provisional
1-366 0e+00

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 739.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   1 SDILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWG 80
Cdd:PLN03032   9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  81 YVTTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVN 160
Cdd:PLN03032  89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 161 IGTTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 241 KEHVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 224006580 321 LERPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECK 366
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVEVR 374
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
41-365 3.31e-54

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 184.88  E-value: 3.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  41 NNLGDPFITSNygvhSRQFECSVIDFFAKLWKAePDSYWGYVTTCGTEGNLHGILLARE--CHPDG-----------ILY 107
Cdd:COG0076   88 KNLGDPDESPA----AAELEERVVNMLSDLLGA-PEEASGTFTSGGTEANLLALLAARErwRKRALaesgkpggkpnIVC 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 108 SSrETHYSVFKAARYYRMDAKAIPTLP-MGEIDYDALQSEIAKNRDRPVIInVNIGTTVKGAVDNLDRILRILKTLGIPr 186
Cdd:COG0076  163 SE-TAHFSFEKAARYLGLGLRRVPTVPtDYRIDVDALEEAIDENTIGGVVV-GTAGTTDTGSIDDIEELADIAEEYGIW- 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 187 erfhIHCDGALFAMMMPFVDWAPEVSFQ-KPIDSIAVSGHKMLGCPMPCGIALTR-KEHVKKVEQKIDYLNS----VDTT 260
Cdd:COG0076  240 ----LHVDAAFGGFLLPFLEPDGRWDFGlEGVDSITVDGHKYGLAPIGCGVVLFRdEEALRRILIFADYYLPgggiPNFT 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 261 IMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG------------LTCRLNDLSSTVVLERPMDDA 328
Cdd:COG0076  316 ILGSRPGRQALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGdfelvnepelpiVAFRLKDDEDTLADLSERLDR 395
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 224006580 329 FIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVEC 365
Cdd:COG0076  396 RGWQVPAQLLPKGLAIVFGTHVTGRQGLKFIVANLLI 432
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
20-303 1.59e-34

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: 130.02  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  20 GYPYNLMYNHEELyEFMKYSINNLGDPFitSNYGVhSRQFECSVIDFFAKLWKAEPDSYWGYVTTCGTEGNLHGILLAR- 98
Cdd:cd06450    4 GFVTTMDPPALLL-EMLTSAKNAIDFTW--DESPA-ATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  99 -------ECHPDGI----LYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDR---PVIINVNIGTT 164
Cdd:cd06450   80 rarkrlkAGGGRGIdklvIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 165 VKGAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRkehv 244
Cdd:cd06450  160 DTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 224006580 245 kkveqkidylnsvdttimgsrngqaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKI 303
Cdd:cd06450  231 -------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELI 264
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
60-307 8.59e-23

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 98.26  E-value: 8.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   60 ECSVIDFFAKLWKAePDSYW-----GYVTTCGTEGNLHGILLAR--------ECHPDG---------ILYSSRETHYSVF 117
Cdd:pfam00282  81 ENVVMNWLGEMLGL-PAEFLgqeggGVLQPGSSESNLLALLAARtkwikrmkAAGKPAdssgilaklVAYTSDQAHSSIE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  118 KAARYYRMDAKAIPTLPMGEIDYDALQSEIA---KNRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEedkENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLW-----LHVD 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  195 GAL--FAMMMPF-------VDWApevsfqkpiDSIAVSGHKMLGCPMPCGIALTRKEHvkKVEQ----KIDYL----NSV 257
Cdd:pfam00282 235 AAYggSAFICPEfrhwlfgIERA---------DSITFNPHKWMLVLLDCSAVWVKDKE--ALQQafqfNPLYLghtdSAY 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224006580  258 DT---TIMGSRnGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG 307
Cdd:pfam00282 304 DTghkQIPLSR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
SepCysS TIGR02539
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine ...
100-250 5.70e-03

O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine biosynthesis in the process, happens in Methanocaldococcus jannaschii and several other archaea by misacylation of tRNA(Cys) with O-phosphoserine (Sep), followed by modification of the phosphoserine to cysteine. In some species, direct tRNA-cys aminoacylation also occurs but this pathway is required for Cys biosynthesis. Members of this protein catalyze the second step in this two step pathway, using pyridoxal phosphate and a sulfur donor to synthesize Cys from Sep while attached to the tRNA.


Pssm-ID: 274187  Cd Length: 369  Bit Score: 38.27  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  100 CHPDGILYSSRETHYSVFKAARYYRMDAKAIPTL--PMGEIDYDALQSEIAKNRDRPVIINVNIGTTVKGAVDNL---DR 174
Cdd:TIGR02539  87 CKEGDYVVLDGNAHYTSYVAAERAGLNVAEVPETghPEYKVNPEGYKEVIDEVEDEGKPVGLALLTHVDGEYGNLndaKK 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224006580  175 ILRILKTLGIPrerFHIHCdgALFAMMMPFVDWAPEVSFqkpidsIAVSGHKMLGCPMPCGIALTRKEHVKKVEQK 250
Cdd:TIGR02539 167 VAKICREKGVP---LLLNC--AYTVGRMPVNGKEVKADF------IVGSGHKSMAASAPCGVLAMSEEWEDKVLRT 231
 
Name Accession Description Interval E-value
PLN03032 PLN03032
serine decarboxylase; Provisional
1-366 0e+00

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 739.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   1 SDILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWG 80
Cdd:PLN03032   9 ADILASYDKLLAEKSSVHFGYPYNLDFDYGELSQLMKYSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWELEKDEYWG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  81 YVTTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVN 160
Cdd:PLN03032  89 YITTCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMEAVKVPTLPSGEIDYDDLERALAKNRDKPAILNVN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 161 IGTTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTR 240
Cdd:PLN03032 169 IGTTVKGAVDDLDRILRILKELGYTEDRFYIHCDGALFGLMMPFVSRAPEVTFRKPIGSVSVSGHKFLGCPMPCGVALTR 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 241 KEHVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVV 320
Cdd:PLN03032 249 KKHVKALSQNVEYLNSRDATIMGSRNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCRLNELSSTVV 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 224006580 321 LERPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECK 366
Cdd:PLN03032 329 FERPMDEAFIKKWQLACEGDIAHVVVMPNVTVEKLDEFVEELVEVR 374
PLN02263 PLN02263
serine decarboxylase
3-369 0e+00

serine decarboxylase


Pssm-ID: 177904 [Multi-domain]  Cd Length: 470  Bit Score: 568.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   3 ILASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWGYV 82
Cdd:PLN02263  78 VLARYRKTLVERTKHHLGYPYNLDFDYGALGQLQHFSINNLGDPFIESNYGVHSRQFEVGVLDWFARLWEIEKNEYWGYI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  83 TTCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVNIG 162
Cdd:PLN02263 158 TNCGTEGNLHGILVGREVFPDGILYASRESHYSVFKAARMYRMECVKVDTLVSGEIDCADFKAKLLANKDKPAIINVNIG 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 163 TTVKGAVDNLDRILRILKTLGIPRERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRKE 242
Cdd:PLN02263 238 TTVKGAVDDLDLVIKTLEECGFSQDRFYIHCDGALFGLMMPFVKRAPKVTFKKPIGSVSVSGHKFVGCPMPCGVQITRME 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 243 HVKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVVLE 322
Cdd:PLN02263 318 HINVLSSNVEYLASRDATIMGSRNGHAPIFLWYTLNRKGYRGFQKEVQKCLRNAHYLKDRLREAGISAMLNELSSTVVFE 397
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 224006580 323 RPMDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVECKNVY 369
Cdd:PLN02263 398 RPKDEEFVRRWQLACQGNIAHVVVMPSVTIEKLDYFLKELVEKRSTW 444
PRK02769 PRK02769
histidine decarboxylase; Provisional
4-364 4.84e-170

histidine decarboxylase; Provisional


Pssm-ID: 235068 [Multi-domain]  Cd Length: 380  Bit Score: 479.15  E-value: 4.84e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   4 LASYDKLLKRKSSVHFGYPYNLMYNHEELYEFMKYSINNLGDPFITSNYGVHSRQFECSVIDFFAKLWKAEPDSYWGYVT 83
Cdd:PRK02769  11 IEDFWLYLRHNQYFNVGYPEAADFDYSALKRFFSFSINNCGDPYSKSNYPLNSFDFERDVMNFFAELFKIPFNESWGYIT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  84 TCGTEGNLHGILLARECHPDGILYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDRPVIINVNIGT 163
Cdd:PRK02769  91 NGGTEGNLYGCYLARELFPDGTLYYSKDTHYSVSKIARLLRIKSRVITSLPNGEIDYDDLISKIKENKNQPPIIFANIGT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 164 TVKGAVDNLDRILRILKTLGIprERFHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRKEH 243
Cdd:PRK02769 171 TMTGAIDNIKEIQEILKKIGI--DDYYIHADAALSGMILPFVNNPPPFSFADGIDSIAISGHKFIGSPMPCGIVLAKKKY 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 244 VKKVEQKIDYLNSVDTTIMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAGLTCRLNDLSSTVVLER 323
Cdd:PRK02769 249 VERISVDVDYIGSRDQTISGSRNGHTALLLWAAIRSLGSKGLRQRVQHCLDMAQYAVDRLQANGIPAWRNPNSITVVFPC 328
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 224006580 324 PmDDAFIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVE 364
Cdd:PRK02769 329 P-SERIWKKWHLATSGNQAHIITMPHHNKQQIDSLIDELIF 368
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
41-365 3.31e-54

Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism];


Pssm-ID: 223154 [Multi-domain]  Cd Length: 460  Bit Score: 184.88  E-value: 3.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  41 NNLGDPFITSNygvhSRQFECSVIDFFAKLWKAePDSYWGYVTTCGTEGNLHGILLARE--CHPDG-----------ILY 107
Cdd:COG0076   88 KNLGDPDESPA----AAELEERVVNMLSDLLGA-PEEASGTFTSGGTEANLLALLAARErwRKRALaesgkpggkpnIVC 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 108 SSrETHYSVFKAARYYRMDAKAIPTLP-MGEIDYDALQSEIAKNRDRPVIInVNIGTTVKGAVDNLDRILRILKTLGIPr 186
Cdd:COG0076  163 SE-TAHFSFEKAARYLGLGLRRVPTVPtDYRIDVDALEEAIDENTIGGVVV-GTAGTTDTGSIDDIEELADIAEEYGIW- 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 187 erfhIHCDGALFAMMMPFVDWAPEVSFQ-KPIDSIAVSGHKMLGCPMPCGIALTR-KEHVKKVEQKIDYLNS----VDTT 260
Cdd:COG0076  240 ----LHVDAAFGGFLLPFLEPDGRWDFGlEGVDSITVDGHKYGLAPIGCGVVLFRdEEALRRILIFADYYLPgggiPNFT 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 261 IMGSRNGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG------------LTCRLNDLSSTVVLERPMDDA 328
Cdd:COG0076  316 ILGSRPGRQALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGdfelvnepelpiVAFRLKDDEDTLADLSERLDR 395
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 224006580 329 FIKRWQLACEEDIAHVVVMPNVTRFKIDKFVEELVEC 365
Cdd:COG0076  396 RGWQVPAQLLPKGLAIVFGTHVTGRQGLKFIVANLLI 432
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
20-303 1.59e-34

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: 130.02  E-value: 1.59e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  20 GYPYNLMYNHEELyEFMKYSINNLGDPFitSNYGVhSRQFECSVIDFFAKLWKAEPDSYWGYVTTCGTEGNLHGILLAR- 98
Cdd:cd06450    4 GFVTTMDPPALLL-EMLTSAKNAIDFTW--DESPA-ATEMEAEVVNWLAKLFGLPSEDADGVFTSGGSESNLLALLAARd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  99 -------ECHPDGI----LYSSRETHYSVFKAARYYRMDAKAIPTLPMGEIDYDALQSEIAKNRDR---PVIINVNIGTT 164
Cdd:cd06450   80 rarkrlkAGGGRGIdklvIVCSDQAHVSVEKAAAYLDVKVRLVPVDEDGRMDPEALEAAIDEDKAEglnPIMVVATAGTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 165 VKGAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGIALTRkehv 244
Cdd:cd06450  160 DTGAIDPLEEIADLAEKYDLW-----LHVDAAYGGFLLPFPEPRHLDFGIERVDSISVDPHKYGLVPLGCSAVLVR---- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 224006580 245 kkveqkidylnsvdttimgsrngqaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKI 303
Cdd:cd06450  231 -------------------------ALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELI 264
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
60-307 8.59e-23

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 98.26  E-value: 8.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   60 ECSVIDFFAKLWKAePDSYW-----GYVTTCGTEGNLHGILLAR--------ECHPDG---------ILYSSRETHYSVF 117
Cdd:pfam00282  81 ENVVMNWLGEMLGL-PAEFLgqeggGVLQPGSSESNLLALLAARtkwikrmkAAGKPAdssgilaklVAYTSDQAHSSIE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  118 KAARYYRMDAKAIPTLPMGEIDYDALQSEIA---KNRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCD 194
Cdd:pfam00282 160 KAALYGGVKLREIPSDDNGKMRGMDLEKAIEedkENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLW-----LHVD 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  195 GAL--FAMMMPF-------VDWApevsfqkpiDSIAVSGHKMLGCPMPCGIALTRKEHvkKVEQ----KIDYL----NSV 257
Cdd:pfam00282 235 AAYggSAFICPEfrhwlfgIERA---------DSITFNPHKWMLVLLDCSAVWVKDKE--ALQQafqfNPLYLghtdSAY 303
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 224006580  258 DT---TIMGSRnGQAALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITEAG 307
Cdd:pfam00282 304 DTghkQIPLSR-RFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDG 355
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
75-236 9.32e-08

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: 53.40  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580   75 PDSYWGYVTTCGTEG-NLHGILLARECHP-DGILYSSREtHYSVF----KAARYYRMDAKAIPTLPMGEIDYDALQSEIa 148
Cdd:pfam00266  59 PSNDEIIFTSGTTEAiNLVALSLGRSLKPgDEIVITEME-HHANLvpwqELAKRTGARVRVLPLDEDGLLDLDELEKLI- 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  149 knRDRPVIINVNIGTTVKGAVDNLDRILRILKTLGIprerfHIHCDGALFAMMMPfvdwapeVSFQK-PIDSIAVSGHKM 227
Cdd:pfam00266 137 --TPKTKLVAITHVSNVTGTIQPVPEIGKLAHQYGA-----LVLVDAAQAIGHRP-------IDVQKlGVDFLAFSGHKL 202

                  ....*....
gi 224006580  228 LGcpmPCGI 236
Cdd:pfam00266 203 YG---PTGI 208
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
80-240 5.27e-06

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: 46.22  E-value: 5.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  80 GYVTTCGTEGNLHGILLAREchPDGILYSSRETHYSvfkaaRYYRMDAKA------IPTLPMGEIDYDALQSEIAKNRDR 153
Cdd:cd01494   20 AVFVPSGTGANEAALLALLG--PGDEVIVDANGHGS-----RYWVAAELAgakpvpVPVDDAGYGGLDVAILEELKAKPN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 154 PVIINVNIGTTVKGAVDNLDRILRILKTLGIPrerfhIHCDGA--LFAMMMPFVdwapEVSFQkPIDSIAVSGHKMLGCP 231
Cdd:cd01494   93 VALIVITPNTTSGGVLVPLKEIRKIAKEYGIL-----LLVDAAsaGGASPAPGV----LIPEG-GADVVTFSLHKNLGGE 162

                 ....*....
gi 224006580 232 MpCGIALTR 240
Cdd:cd01494  163 G-GGVVIVK 170
PLN02590 PLN02590
probable tyrosine decarboxylase
32-305 1.22e-04

probable tyrosine decarboxylase


Pssm-ID: 178200 [Multi-domain]  Cd Length: 539  Bit Score: 43.93  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  32 LYEFMKYSINNLGDPFITSNygvHSRQFECSVIDFFAKLWKAePDSYW------GYVTTCGTEGNLHGILLARE------ 99
Cdd:PLN02590 147 LGEMLNAGLSVVGFTWLTSP---AATELEIIVLDWLAKLLQL-PDHFLstgnggGVIQGTGCEAVLVVVLAARDrilkkv 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 100 ---CHPDGILYSSRETHYSVFKAA----------RYYRMDAKAIPTLPMGEIDyDALQSEIAKNRdRPVIINVNIGTTVK 166
Cdd:PLN02590 223 gktLLPQLVVYGSDQTHSSFRKACliggiheeniRLLKTDSSTNYGMPPESLE-EAISHDLAKGF-IPFFICATVGTTSS 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 167 GAVDNLDRILRILKTLGIprerfHIHCDGALFAMMMPFVDWAPEVSFQKPIDSIAVSGHKMLGCPMPCGI---------- 236
Cdd:PLN02590 301 AAVDPLVPLGNIAKKYGI-----WLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPlwvkdrysli 375
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 224006580 237 -AL-TRKEHVK-KVEQKIDYLNSVDTTIMGSRNGQaALYLWYSLRKKGIAGIKRDVVHCMETAQYLRDKITE 305
Cdd:PLN02590 376 dALkTNPEYLEfKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQ 446
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
80-232 3.33e-04

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: 41.93  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  80 GYVTTCGTEGNLhgILLARECHPDGILYSSRETHYSVFKA---ARYYRMDAKAIPTlPMGEIDYDALQSEIAKNRD---- 152
Cdd:cd06502   50 ALFVPSGTAANQ--LALAAHTQPGGSVICHETAHIYTDEAgapEFLSGVKLLPVPG-ENGKLTPEDLEAAIRPRDDihfp 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580 153 RPVIINVNIGTTVKG--AVDNLDRILRILKTLGIPrerfhIHCDGALF-----AMMMPFVDWApevsfqKPIDSIAVSGH 225
Cdd:cd06502  127 PPSLVSLENTTEGGTvyPLDELKAISALAKENGLP-----LHLDGARLanaaaALGVALKTYK------SGVDSVSFCLS 195

                 ....*..
gi 224006580 226 KMLGCPM 232
Cdd:cd06502  196 KGGGAPV 202
PRK02948 PRK02948
IscS subfamily cysteine desulfurase;
81-229 7.53e-04

IscS subfamily cysteine desulfurase;


Pssm-ID: 179511 [Multi-domain]  Cd Length: 381  Bit Score: 41.25  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  81 YVTTCGTEGN---LHGILLARECHPDGILYSSREtHYSVFKAARYYRMDAKAIPTLPM---GEIDYDALQSEIaknrdRP 154
Cdd:PRK02948  64 YFTSGGTESNylaIQSLLNALPQNKKHIITTPME-HASIHSYFQSLESQGYTVTEIPVdksGLIRLVDLERAI-----TP 137
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224006580 155 VIINVNI--GTTVKGAVDNLDRILRILKTLGIPrerfhIHCDGA-LFAMMmpfvdwaPEVSFQKPIDSIAVSGHKMLG 229
Cdd:PRK02948 138 DTVLASIqhANSEIGTIQPIAEIGALLKKYNVL-----FHSDCVqTFGKL-------PIDVFEMGIDSLSVSAHKIYG 203
GLY1 COG2008
Threonine aldolase [Amino acid transport and metabolism];
86-232 1.11e-03

Threonine aldolase [Amino acid transport and metabolism];


Pssm-ID: 224919 [Multi-domain]  Cd Length: 342  Bit Score: 40.34  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  86 GTEGNLhgILLARECHPDGILYSSRETHYSVFK--AARYYRMDAK-AIPTLPMGEIDYDALQSEIAKN-RDRPV------ 155
Cdd:COG2008   59 GTQANQ--LALAAHCQPGESVICHETAHIYTDEcgAPEFFGGGQKlPIVPGADGKLTPEDVEAAIRPDdIHHAPtplavl 136
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 224006580 156 IINVNIGTTVKgAVDNLDRILRILKTLGIPrerfhIHCDGALFAMMMPFVDwAPEVSFQKPIDSIAVSGHKMLGCPM 232
Cdd:COG2008  137 ENTATEGGTVY-PLDELEAISAVCKEHGLP-----LHMDGARLANALVALG-VALKTIKSYVDSVSFCLTKGGGAPV 206
SepCysS TIGR02539
O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine ...
100-250 5.70e-03

O-phospho-L-seryl-tRNA:Cys-tRNA synthase; Aminoacylation of tRNA(Cys) with Cys, and cysteine biosynthesis in the process, happens in Methanocaldococcus jannaschii and several other archaea by misacylation of tRNA(Cys) with O-phosphoserine (Sep), followed by modification of the phosphoserine to cysteine. In some species, direct tRNA-cys aminoacylation also occurs but this pathway is required for Cys biosynthesis. Members of this protein catalyze the second step in this two step pathway, using pyridoxal phosphate and a sulfur donor to synthesize Cys from Sep while attached to the tRNA.


Pssm-ID: 274187  Cd Length: 369  Bit Score: 38.27  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224006580  100 CHPDGILYSSRETHYSVFKAARYYRMDAKAIPTL--PMGEIDYDALQSEIAKNRDRPVIINVNIGTTVKGAVDNL---DR 174
Cdd:TIGR02539  87 CKEGDYVVLDGNAHYTSYVAAERAGLNVAEVPETghPEYKVNPEGYKEVIDEVEDEGKPVGLALLTHVDGEYGNLndaKK 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 224006580  175 ILRILKTLGIPrerFHIHCdgALFAMMMPFVDWAPEVSFqkpidsIAVSGHKMLGCPMPCGIALTRKEHVKKVEQK 250
Cdd:TIGR02539 167 VAKICREKGVP---LLLNC--AYTVGRMPVNGKEVKADF------IVGSGHKSMAASAPCGVLAMSEEWEDKVLRT 231
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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