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Conserved domains on  [gi|1034594007|ref|XP_016878549|]
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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) ...
181-403 3.25e-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: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594007 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
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 ...
181-403 3.25e-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: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594007 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
Cdd:cd06450   227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
173-403 6.42e-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: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 173 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 252
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 253 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 321
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 322 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 387
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1034594007 388 ILVEDELssPVVVFRF 403
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
180-402 2.24e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.37  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 180 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 258
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 259 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 336
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 337 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 401
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1034594007 402 R 402
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
221-416 3.50e-08

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 56.43  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 221 SQHQMDVAFLEKLIKDDIergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 296
Cdd:PRK13520  135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 297 AAAkcDSMTMTPGPwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPtdKLRALPLWLSLQYLGLDGFVE 364
Cdd:PRK13520  209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRS--GAGVAATYAVMKYLGREGYRK 283
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034594007 365 RIKHACQLSQRLQESLKKVNYiKILVEDELssPVVVFrffqELPGSDPVFKA 416
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 ...
181-403 3.25e-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: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 181 KKPVIYLSAAARPGL---GQYLCNQLglpfpclCRVPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:cd06450    94 DKLVIVCSDQAHVSVekaAAYLDVKV-------RLVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLaaakcdsMTMTPGPWL-GLPAVPAVT------LYKHDDPAL 330
Cdd:cd06450   163 AIDPLEEIADLAEKYDLWLHVDA------AYG---GFLL-------PFPEPRHLDfGIERVDSISvdphkyGLVPLGCSA 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034594007 331 TLVagltsnkptdklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVFRF 403
Cdd:cd06450   227 VLV------------RALKLWATLRRFGRDGYGEHIDRIVDLAKYLAELIRADPGFELLGEPNL--SLVCFRL 285
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
173-403 6.42e-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: 6.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 173 DGFNVLYNKKPVIYLSAAARPGLgQYLCNQLGLPFPCLCRVPCNtvfgsqHQMDVAFLEKLIKDDIERGrlplLLVANAG 252
Cdd:COG0076   148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 253 TAAVGHTDKIGRLKELCEQYGIWLHVEGvnlatlALGyvsSSVLAAAKC-----------DSMTMTPGPWLGLPAVPAVT 321
Cdd:COG0076   217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPdgrwdfglegvDSITVDGHKYGLAPIGCGVV 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 322 LYK----------HDDPALT----LVAGLTSNKPTDklRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIK 387
Cdd:COG0076   288 LFRdeealrriliFADYYLPgggiPNFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELEKLGDFE 365
                         250
                  ....*....|....*.
gi 1034594007 388 ILVEDELssPVVVFRF 403
Cdd:COG0076   366 LVNEPEL--PIVAFRL 379
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
180-402 2.24e-12

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 69.37  E-value: 2.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 180 NKKPVIYLSAAArpglgQYLCNQLGLPFPCLCR-VPCNtvfgSQHQMDVAFLEKLIKDDIERGRLPLLLVANAGTAAVGH 258
Cdd:pfam00282 143 LAKLVAYTSDQA-----HSSIEKAALYGGVKLReIPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 259 TDKIGRLKELCEQYGIWLHVEGVNLATLALG-YVSSSVLAAAKCDSMTMTPGPWLGLPAvPAVTLYKHDDPALTLVAGL- 336
Cdd:pfam00282 214 FDDLQELGDICAKHNLWLHVDAAYGGSAFICpEFRHWLFGIERADSITFNPHKWMLVLL-DCSAVWVKDKEALQQAFQFn 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 337 -----TSNKPTD----------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKILVEDELssPVVVF 401
Cdd:pfam00282 293 plylgHTDSAYDtghkqiplsrRFRILKLWFVIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFEICAEVGL--GLVCF 370

                  .
gi 1034594007 402 R 402
Cdd:pfam00282 371 R 371
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
221-416 3.50e-08

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 56.43  E-value: 3.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 221 SQHQMDVAFLEKLIKDDIergrlpLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVE----GVNLATLALGYVSSSVL 296
Cdd:PRK13520  135 DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHVDaafgGFVIPFLDDPPNFDFSL 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 297 AAAkcDSMTMTPGPwLGLPAVPA-VTLYKH---------DDPALT--LVAGLTSNKPtdKLRALPLWLSLQYLGLDGFVE 364
Cdd:PRK13520  209 PGV--DSITIDPHK-MGLAPIPAgGILFRDesyldalavDTPYLTskKQATLTGTRS--GAGVAATYAVMKYLGREGYRK 283
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034594007 365 RIKHACQLSQRLQESLKKVNYiKILVEDELssPVVVFrffqELPGSDPVFKA 416
Cdd:PRK13520  284 VVERCMENTRWLAEELKERGF-EPVIEPVL--NIVAF----DDPNPDEVREK 328
PLN02880 PLN02880
tyrosine decarboxylase
181-438 2.53e-06

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 50.68  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 181 KKPVIYLSAAARPGLgQYLCnQLGLPFPCLCRV---PCNTVFGSQHQMdvafLEKLIKDDIERGRLPLLLVANAGTAAVG 257
Cdd:PLN02880  180 EKLVVYASDQTHSAL-QKAC-QIAGIHPENCRLlktDSSTNYALAPEL----LSEAISTDLSSGLIPFFLCATVGTTSST 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 258 HTDKIGRLKELCEQYGIWLHVEGvnlatlalGYVSSSVL---------AAAKCDSMTMTPGPWLgLPAVPAVTLYKHDDP 328
Cdd:PLN02880  254 AVDPLLELGKIAKSNGMWFHVDA--------AYAGSACIcpeyrhyidGVEEADSFNMNAHKWF-LTNFDCSLLWVKDRN 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 329 ALTLVAG----LTSNKPTD----------------KLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQEslkkvnyiki 388
Cdd:PLN02880  325 ALIQSLStnpeFLKNKASQansvvdykdwqiplgrRFRSLKLWMVLRLYGVENLQSYIRNHIKLAKEFEQ---------- 394
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034594007 389 LVEDELSSPVVVFRFFqelpgSDPVFKAVPVPNMTPSGVGRERHSCDALN 438
Cdd:PLN02880  395 LVAQDSRFEVVTPRIF-----SLVCFRLVPPKNNEDNGNKLNHDLLDAVN 439
PLN02590 PLN02590
probable tyrosine decarboxylase
230-417 3.48e-04

probable tyrosine decarboxylase


Pssm-ID: 178200  Cd Length: 539  Bit Score: 43.93  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 230 LEKLIKDDIERGRLPLLLVANAGTAAVGHTDKIGRLKELCEQYGIWLHVEGVNLATLAL-GYVSSSVLAAAKCDSMTMTP 308
Cdd:PLN02590  274 LEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACIcPEYRKFIDGIENADSFNMNA 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 309 GPWLgLPAVPAVTLYKHDDPALtlvagltsnkpTDKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQeSLKKVNYIKI 388
Cdd:PLN02590  354 HKWL-FANQTCSPLWVKDRYSL-----------IDALKTNPEYLEFKVSKKDTVVNYKDWQISLSRRFR-SLKLWMVLRL 420
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1034594007 389 LVEDELSS----PVVVFRFFQELPGSDPVFKAV 417
Cdd:PLN02590  421 YGSENLRNfirdHVNLAKHFEDYVAQDPSFEVV 453
PLN03032 PLN03032
serine decarboxylase; Provisional
244-423 8.39e-04

serine decarboxylase; Provisional


Pssm-ID: 166673 [Multi-domain]  Cd Length: 374  Bit Score: 42.51  E-value: 8.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 244 PLLLVANAGTAAVGHTDKIGRLKELCEQYGI-----WLHVEGVnLATLALGYVSSSVLAAAK--CDSMTMTPGPWLGLPa 316
Cdd:PLN03032  162 PAILNVNIGTTVKGAVDDLDRILRILKELGYtedrfYIHCDGA-LFGLMMPFVSRAPEVTFRkpIGSVSVSGHKFLGCP- 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034594007 317 VP---AVTLYKHDDPALTLVAGLTSNKPT-----DKLRALPLWLSLQYLGLDGFVERIKHACQLSQRLQESLKKVNYIKI 388
Cdd:PLN03032  240 MPcgvALTRKKHVKALSQNVEYLNSRDATimgsrNGHAPLYLWYTLRRKGYRGIKRDVQHCMRNAHYLKDRLTEAGLTCR 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034594007 389 LveDELSSPVVVFRFFQE-------LPGSDPVFKAVPVPNMT 423
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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