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Conserved domains on  [gi|301616568|ref|XP_002937727|]
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pyridoxal-dependent decarboxylase domain-containing protein 1 [Xenopus tropicalis]

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) ...
205-469 1.28e-18

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: 88.03  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 205 RVPCNtmfgSQHQMDVALLDRLIKDDIQSGKCPLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHVEGvnlatlALGyv 284
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 285 sSSVLaatkcdsMTLTLGPWL-GLPAVPAVTLyrheDPSLSLAAGLTSSqpVEKLRALPLWLSLQYLGHSGIVERIKHAS 363
Cdd:cd06450  189 -GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGCS--AVLVRALKLWATLRRFGRDGYGEHIDRIV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 364 QLSQKLLESLKNLSSVKtsVENDGSSPVVVFRFvyegcKSDSTLNLsTIERDSDALNQWLGDQLAALvPLCGVDIVELed 443
Cdd:cd06450  255 DLAKYLAELIRADPGFE--LLGEPNLSLVCFRL-----KPSVKLDE-LNYDLSDRLNERGGWHVPAT-TLGGPNVLRF-- 323
                        250       260
                 ....*....|....*....|....*.
gi 301616568 444 egtCVRfNPLMTTAVLGTTAEDVEQL 469
Cdd:cd06450  324 ---VVT-NPLTTRDDADALLEDIERA 345
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
608-758 3.07e-03

Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains.


The actual alignment was detected with superfamily member PRK10997:

Pssm-ID: 412136  Cd Length: 487  Bit Score: 40.67  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 608 ILEAEVQLYKANEERLLEEgVLRQIPLVGSMLNWFSPvQTTPKGRTFNLTAGSLETTETTYISKaqttgltppstpTSAH 687
Cdd:PRK10997 144 TTTLNQQLLEQEREQLLAE-LQQRMTLSGQLEPVLAE-NDEAAGRLWDMSAGQLKRGDYQLIVQ------------YGEF 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301616568 688 AKRQPG-QKLFKRLSRNSDAMSETSSISHLEEVESLEALPmpdtqqfDSTADELSATAENSAIPSVVPTETS 758
Cdd:PRK10997 210 LKQQPElQKLAEQLGRSREAKSVPRNDAPMETFRTMVREP-------DTVPEQVVGIHQSDDILRLLPPELA 274
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
205-469 1.28e-18

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: 88.03  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 205 RVPCNtmfgSQHQMDVALLDRLIKDDIQSGKCPLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHVEGvnlatlALGyv 284
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 285 sSSVLaatkcdsMTLTLGPWL-GLPAVPAVTLyrheDPSLSLAAGLTSSqpVEKLRALPLWLSLQYLGHSGIVERIKHAS 363
Cdd:cd06450  189 -GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGCS--AVLVRALKLWATLRRFGRDGYGEHIDRIV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 364 QLSQKLLESLKNLSSVKtsVENDGSSPVVVFRFvyegcKSDSTLNLsTIERDSDALNQWLGDQLAALvPLCGVDIVELed 443
Cdd:cd06450  255 DLAKYLAELIRADPGFE--LLGEPNLSLVCFRL-----KPSVKLDE-LNYDLSDRLNERGGWHVPAT-TLGGPNVLRF-- 323
                        250       260
                 ....*....|....*....|....*.
gi 301616568 444 egtCVRfNPLMTTAVLGTTAEDVEQL 469
Cdd:cd06450  324 ---VVT-NPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
166-397 3.05e-16

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: 82.03  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 166 DGFNALYNKQPVIYISAASRPGLgQSICNQLGLPLSCLCRVPCNtmfgsqHQMDVALLDRLIKDDIQSGkcplLLVANAG 245
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 246 TPGAGHTDKLGRLKELCDQYNIWLHVEGvnlatlALGyvsSSVLAATKCDsmtltlGPWL-GLPAVPAVT---------- 314
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPD------GRWDfGLEGVDSITvdghkyglap 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 315 ------LYR----------HEDPSLSLA----AGLTSSQPVEklRALPLWLSLQYLGHSGIVERIKHASQLSQKLLESLK 374
Cdd:COG0076  282 igcgvvLFRdeealrriliFADYYLPGGgipnFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELE 359
                        250       260
                 ....*....|....*....|...
gi 301616568 375 NLSSVKtsVENDGSSPVVVFRFV 397
Cdd:COG0076  360 KLGDFE--LVNEPELPIVAFRLK 380
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
206-397 1.53e-07

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 54.35  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568  206 VPCNtmfgSQHQMDVALLDRLIKDDIQSGKCPLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHVEGVNLATLALG-YV 284
Cdd:pfam00282 172 IPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICpEF 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568  285 SSSVLAATKCDSMTLTLGPWLGLPA------------------VPAVTLyRHEDPSLSLAA-GLTSSQPVeklRALPLWL 345
Cdd:pfam00282 248 RHWLFGIERADSITFNPHKWMLVLLdcsavwvkdkealqqafqFNPLYL-GHTDSAYDTGHkQIPLSRRF---RILKLWF 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 301616568  346 SLQYLGHSGIVERIKHASQLSQKLLESLKNLSSVKtsVENDGSSPVVVFRFV 397
Cdd:pfam00282 324 VIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFE--ICAEVGLGLVCFRLK 373
PLN02880 PLN02880
tyrosine decarboxylase
167-272 1.44e-03

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 41.82  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 167 GFNALynKQPVIYISAASRPGLgQSICNQLGL-PLSC-LCRVPCNTMFGsqhqMDVALLDRLIKDDIQSGKCPLLLVANA 244
Cdd:PLN02880 175 GKNAL--EKLVVYASDQTHSAL-QKACQIAGIhPENCrLLKTDSSTNYA----LAPELLSEAISTDLSSGLIPFFLCATV 247
                         90       100
                 ....*....|....*....|....*...
gi 301616568 245 GTPGAGHTDKLGRLKELCDQYNIWLHVE 272
Cdd:PLN02880 248 GTTSSTAVDPLLELGKIAKSNGMWFHVD 275
yieM PRK10997
ATPase RavA stimulator ViaA;
608-758 3.07e-03

ATPase RavA stimulator ViaA;


Pssm-ID: 236815  Cd Length: 487  Bit Score: 40.67  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 608 ILEAEVQLYKANEERLLEEgVLRQIPLVGSMLNWFSPvQTTPKGRTFNLTAGSLETTETTYISKaqttgltppstpTSAH 687
Cdd:PRK10997 144 TTTLNQQLLEQEREQLLAE-LQQRMTLSGQLEPVLAE-NDEAAGRLWDMSAGQLKRGDYQLIVQ------------YGEF 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301616568 688 AKRQPG-QKLFKRLSRNSDAMSETSSISHLEEVESLEALPmpdtqqfDSTADELSATAENSAIPSVVPTETS 758
Cdd:PRK10997 210 LKQQPElQKLAEQLGRSREAKSVPRNDAPMETFRTMVREP-------DTVPEQVVGIHQSDDILRLLPPELA 274
 
Name Accession Description Interval E-value
DOPA_deC_like cd06450
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
205-469 1.28e-18

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: 88.03  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 205 RVPCNtmfgSQHQMDVALLDRLIKDDIQSGKCPLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHVEGvnlatlALGyv 284
Cdd:cd06450  121 LVPVD----EDGRMDPEALEAAIDEDKAEGLNPIMVVATAGTTDTGAIDPLEEIADLAEKYDLWLHVDA------AYG-- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 285 sSSVLaatkcdsMTLTLGPWL-GLPAVPAVTLyrheDPSLSLAAGLTSSqpVEKLRALPLWLSLQYLGHSGIVERIKHAS 363
Cdd:cd06450  189 -GFLL-------PFPEPRHLDfGIERVDSISV----DPHKYGLVPLGCS--AVLVRALKLWATLRRFGRDGYGEHIDRIV 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 364 QLSQKLLESLKNLSSVKtsVENDGSSPVVVFRFvyegcKSDSTLNLsTIERDSDALNQWLGDQLAALvPLCGVDIVELed 443
Cdd:cd06450  255 DLAKYLAELIRADPGFE--LLGEPNLSLVCFRL-----KPSVKLDE-LNYDLSDRLNERGGWHVPAT-TLGGPNVLRF-- 323
                        250       260
                 ....*....|....*....|....*.
gi 301616568 444 egtCVRfNPLMTTAVLGTTAEDVEQL 469
Cdd:cd06450  324 ---VVT-NPLTTRDDADALLEDIERA 345
GadA COG0076
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ...
166-397 3.05e-16

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: 82.03  E-value: 3.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 166 DGFNALYNKQPVIYISAASRPGLgQSICNQLGLPLSCLCRVPCNtmfgsqHQMDVALLDRLIKDDIQSGkcplLLVANAG 245
Cdd:COG0076  148 LAESGKPGGKPNIVCSETAHFSF-EKAARYLGLGLRRVPTVPTD------YRIDVDALEEAIDENTIGG----VVVGTAG 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 246 TPGAGHTDKLGRLKELCDQYNIWLHVEGvnlatlALGyvsSSVLAATKCDsmtltlGPWL-GLPAVPAVT---------- 314
Cdd:COG0076  217 TTDTGSIDDIEELADIAEEYGIWLHVDA------AFG---GFLLPFLEPD------GRWDfGLEGVDSITvdghkyglap 281
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 315 ------LYR----------HEDPSLSLA----AGLTSSQPVEklRALPLWLSLQYLGHSGIVERIKHASQLSQKLLESLK 374
Cdd:COG0076  282 igcgvvLFRdeealrriliFADYYLPGGgipnFTILGSRPGR--QALALYANLRRLGREGYRKLLDRTLELARYLAEELE 359
                        250       260
                 ....*....|....*....|...
gi 301616568 375 NLSSVKtsVENDGSSPVVVFRFV 397
Cdd:COG0076  360 KLGDFE--LVNEPELPIVAFRLK 380
Pyridoxal_deC pfam00282
Pyridoxal-dependent decarboxylase conserved domain;
206-397 1.53e-07

Pyridoxal-dependent decarboxylase conserved domain;


Pssm-ID: 395219  Cd Length: 373  Bit Score: 54.35  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568  206 VPCNtmfgSQHQMDVALLDRLIKDDIQSGKCPLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHVEGVNLATLALG-YV 284
Cdd:pfam00282 172 IPSD----DNGKMRGMDLEKAIEEDKENGLIPFFVVATLGTTGSGAFDDLQELGDICAKHNLWLHVDAAYGGSAFICpEF 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568  285 SSSVLAATKCDSMTLTLGPWLGLPA------------------VPAVTLyRHEDPSLSLAA-GLTSSQPVeklRALPLWL 345
Cdd:pfam00282 248 RHWLFGIERADSITFNPHKWMLVLLdcsavwvkdkealqqafqFNPLYL-GHTDSAYDTGHkQIPLSRRF---RILKLWF 323
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 301616568  346 SLQYLGHSGIVERIKHASQLSQKLLESLKNLSSVKtsVENDGSSPVVVFRFV 397
Cdd:pfam00282 324 VIRSLGVEGLQNQIRRHVELAQYLEALIRKDGRFE--ICAEVGLGLVCFRLK 373
PLN02880 PLN02880
tyrosine decarboxylase
167-272 1.44e-03

tyrosine decarboxylase


Pssm-ID: 215475  Cd Length: 490  Bit Score: 41.82  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 167 GFNALynKQPVIYISAASRPGLgQSICNQLGL-PLSC-LCRVPCNTMFGsqhqMDVALLDRLIKDDIQSGKCPLLLVANA 244
Cdd:PLN02880 175 GKNAL--EKLVVYASDQTHSAL-QKACQIAGIhPENCrLLKTDSSTNYA----LAPELLSEAISTDLSSGLIPFFLCATV 247
                         90       100
                 ....*....|....*....|....*...
gi 301616568 245 GTPGAGHTDKLGRLKELCDQYNIWLHVE 272
Cdd:PLN02880 248 GTTSSTAVDPLLELGKIAKSNGMWFHVD 275
yieM PRK10997
ATPase RavA stimulator ViaA;
608-758 3.07e-03

ATPase RavA stimulator ViaA;


Pssm-ID: 236815  Cd Length: 487  Bit Score: 40.67  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 608 ILEAEVQLYKANEERLLEEgVLRQIPLVGSMLNWFSPvQTTPKGRTFNLTAGSLETTETTYISKaqttgltppstpTSAH 687
Cdd:PRK10997 144 TTTLNQQLLEQEREQLLAE-LQQRMTLSGQLEPVLAE-NDEAAGRLWDMSAGQLKRGDYQLIVQ------------YGEF 209
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 301616568 688 AKRQPG-QKLFKRLSRNSDAMSETSSISHLEEVESLEALPmpdtqqfDSTADELSATAENSAIPSVVPTETS 758
Cdd:PRK10997 210 LKQQPElQKLAEQLGRSREAKSVPRNDAPMETFRTMVREP-------DTVPEQVVGIHQSDDILRLLPPELA 274
PRK13520 PRK13520
tyrosine decarboxylase MfnA;
192-271 7.33e-03

tyrosine decarboxylase MfnA;


Pssm-ID: 237409  Cd Length: 371  Bit Score: 39.48  E-value: 7.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301616568 192 ICNQLGLPLSclcRVPCNtmfgSQHQMDVALLDRLIKDDIqsgkcpLLLVANAGTPGAGHTDKLGRLKELCDQYNIWLHV 271
Cdd:PRK13520 120 AADMLGVELR---RAPLD----DDYRVDVKAVEDLIDDNT------IGIVGIAGTTELGQVDPIPELSKIALENGIFLHV 186
 
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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