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Conserved domains on  [gi|550544169|ref|NP_001272373|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
145-367 3.03e-21

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).


The actual alignment was detected with superfamily member cd06450:

Pssm-ID: 418510  Cd Length: 345  Bit Score: 95.73  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 145 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 221
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 222 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 294
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544169 295 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 367
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
145-367 3.03e-21

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  Cd Length: 345  Bit Score: 95.73  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 145 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 221
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 222 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 294
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544169 295 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 367
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
137-367 5.95e-18

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: 87.43  E-value: 5.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 137 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 216
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 217 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 285
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 286 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 351
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        250
                 ....*....|....*.
gi 550544169 352 ILVEDELssPVVVFRF 367
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
144-366 2.10e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.37  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  144 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 222
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  223 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 300
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  301 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 365
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 550544169  366 R 366
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
185-380 3.29e-08

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 56.43  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 185 SQHQMDVAFLEKLIKDDIergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 260
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 261 AAAkcDSMTMTPGPwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPtdKLRALPLWLSLQYLGLDGFVE 328
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRS--GAGVAATYAVMKYLGREGYRK 283
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550544169 329 RIKHACQLSQRLQESLKKVNYiKILVEDELssPVVVFrffqELPGSDPVFKA 380
Cdd:PRK13520 284 VVERCMENTRWLAEELKERGF-EPVIEPVL--NIVAF----DDPNPDEVREK 328
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
145-367 3.03e-21

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  Cd Length: 345  Bit Score: 95.73  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 145 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 221
Cdd:cd06450   94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 222 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 294
Cdd:cd06450  163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550544169 295 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 367
Cdd:cd06450  227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
137-367 5.95e-18

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: 87.43  E-value: 5.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 137 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 216
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 217 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 285
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 286 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 351
Cdd:COG0076  288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                        250
                 ....*....|....*.
gi 550544169 352 ILVEDELssPVVVFRF 367
Cdd:COG0076  366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
144-366 2.10e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.37  E-value: 2.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  144 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 222
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  223 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 300
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169  301 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 365
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 550544169  366 R 366
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
185-380 3.29e-08

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 56.43  E-value: 3.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 185 SQHQMDVAFLEKLIKDDIergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 260
Cdd:PRK13520 135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 261 AAAkcDSMTMTPGPwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPtdKLRALPLWLSLQYLGLDGFVE 328
Cdd:PRK13520 209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRS--GAGVAATYAVMKYLGREGYRK 283
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 550544169 329 RIKHACQLSQRLQESLKKVNYiKILVEDELssPVVVFrffqELPGSDPVFKA 380
Cdd:PRK13520 284 VVERCMENTRWLAEELKERGF-EPVIEPVL--NIVAF----DDPNPDEVREK 328
PLN02880 PLN02880
tyrosine decarboxylase
145-402 2.40e-06

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 50.68  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 145 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 221
Cdd:PLN02880 180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 222 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 292
Cdd:PLN02880 254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 293 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 352
Cdd:PLN02880 325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 550544169 353 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 402
Cdd:PLN02880 395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
PLN02590 PLN02590
probable tyrosine decarboxylase
194-381 3.29e-04

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 43.93  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 194 LEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLAL-GYVSSSVLAAAKCDSMTMTP 272
Cdd:PLN02590 274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIcPEYRKFIDGIENADSFNMNA 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 273 GPWLgLPAVPAVTLYKHDDPALtlvagltsnkpTDKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQeSLKKVNYIKI 352
Cdd:PLN02590 354 HKWL-FANQTCSPLWVKDRYSL-----------IDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRL 420
                        170       180       190
                 ....*....|....*....|....*....|...
gi 550544169 353 LVEDELSS----PVVVFRFFQELPGSDPVFKAV 381
Cdd:PLN02590 421 YGSENLRNfirdHVNLAKHFEDYVAQDPSFEVV 453
PLN03032 PLN03032
serine decarboxylase; Provisional
208-387 7.93e-04

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 42.51  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 208 PLLLVANAGTAAVGHTDKIGRLKELCEQYGI-----WLHVEGVnLATLALGYVSSSVLAAAK--CDSMTMTPGPWLGLPa 280
Cdd:PLN03032 162 PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGA-LFGLMMPFVSRAPEVTFRkpIGSVSVSGHKFLGCP- 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550544169 281 VP---AVTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKI 352
Cdd:PLN03032 240 MPcgvALTRKKHVKALSQNVEYLNSRDATimgsrNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCR 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 550544169 353 LveDELSSPVVVFRFFQE-------LPGSDPVFKAVPVPNMT 387
Cdd:PLN03032 320 L--NELSSTVVFERPMDEafikkwqLACEGDIAHVVVMPNVT 359
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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