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Conserved domains on  [gi|612906875|gb|EZV18536|]
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hypothetical protein U926_01775 [Staphylococcus aureus 12S00881]

Protein Classification

aminotransferase class IV( domain architecture ID 10471046)

aminotransferase class IV similar to similar to Legionella pneumophila putative 4-amino-4-deoxychorismate lyase that converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate in one of the crucial steps in the folate-biosynthesis pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
2-201 6.40e-41

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


:

Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 138.26  E-value: 6.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875    2 QLFETMKIDNGHIPRLTYHTNRIKCSSERLN--FKFDEHAWRNELNDVTTKYHSGQYRLKIVLHA----------ESEFE 69
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGipLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRgpggfglptsDPTLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   70 TIVSPLPEKSSFTAK-----------FQVLPKAVNPTFINNKTTERKHLAHNHetDLILLTSEDGKVLEFDIGNVVIEED 138
Cdd:pfam01063  81 IFVSALPPPPESKKKgvisslvrrnpPSPLPGAKTLNYLENVLARREAKAQGA--DDALLLDEDGNVTEGSTSNVFLVKG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612906875  139 GKWYTPSYKDDFLKGCMRDYLIDSDK-----LVEKDFNKNELIykyhnNEIRLFLINSLREVADVHLC 201
Cdd:pfam01063 159 GTLYTPPLESGILPGITRQALLDLAKalgleVEERPITLADLQ-----EADEAFLTNSLRGVTPVSSI 221
 
Name Accession Description Interval E-value
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
2-201 6.40e-41

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 138.26  E-value: 6.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875    2 QLFETMKIDNGHIPRLTYHTNRIKCSSERLN--FKFDEHAWRNELNDVTTKYHSGQYRLKIVLHA----------ESEFE 69
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGipLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRgpggfglptsDPTLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   70 TIVSPLPEKSSFTAK-----------FQVLPKAVNPTFINNKTTERKHLAHNHetDLILLTSEDGKVLEFDIGNVVIEED 138
Cdd:pfam01063  81 IFVSALPPPPESKKKgvisslvrrnpPSPLPGAKTLNYLENVLARREAKAQGA--DDALLLDEDGNVTEGSTSNVFLVKG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612906875  139 GKWYTPSYKDDFLKGCMRDYLIDSDK-----LVEKDFNKNELIykyhnNEIRLFLINSLREVADVHLC 201
Cdd:pfam01063 159 GTLYTPPLESGILPGITRQALLDLAKalgleVEERPITLADLQ-----EADEAFLTNSLRGVTPVSSI 221
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
3-199 6.63e-16

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 74.07  E-value: 6.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   3 LFETMKIDNGHIPRLTYHTNRIKCSSERLNFK--FDEHAWRNELNDVTTKYHSGQYRLKIVL--------HAESEFET-- 70
Cdd:COG0115   30 VFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPipYTEEELLEAIRELVAANGLEDGYIRPQVtrgvggrgVFAEEYEPtv 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  71 --IVSPLPEKSS---------FTAKFQvlpKAVNPTFINNKTTER------KHLAHNHETDLILLTSEDGKVLEFDIGNV 133
Cdd:COG0115  110 iiIASPLPAYPAeayekgvrvITSPYR---RAAPGGLGGIKTGNYlnnvlaKQEAKEAGADEALLLDTDGYVAEGSGSNV 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612906875 134 VIEEDGKWYTPSYKDDFLKGCMRDYLID--SD---KLVEKDFNKNELiykYHNNEIrlFLINSLREVADVH 199
Cdd:COG0115  187 FIVKDGVLVTPPLSGGILPGITRDSVIElaRElgiPVEERPISLEEL---YTADEV--FLTGTAAEVTPVT 252
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
3-199 1.30e-15

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 72.73  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   3 LFETMKIDNGHIPRLTYHTNRIKCSSERLNF-KFDEHAWRNELNDVTTKYHSGQYRLKIVLHAESEFETIVSPLPEKSSF 81
Cdd:cd01559   10 VFETMRALDGRLFLLDAHLARLERSARRLGIpEPDLPRLRAALESLLAANDIDEGRIRLILSRGPGGRGYAPSVCPGPAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  82 TAKFQVLPKAVNPTFINNKTTER-----------KHL-----------AHNHETDLILLTSEDGKVLEFDIGNVVIEEDG 139
Cdd:cd01559   90 YVSVIPLPPAWRQDGVRLITCPVrlgeqpllaglKHLnylenvlakreARDRGADEALFLDTDGRVIEGTASNLFFVKDG 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612906875 140 KWYTPSYKDDFLKGCMRDYLIDSDK-----LVEKDFNKNELiykYHNNEIrlFLINSLREVADVH 199
Cdd:cd01559  170 ELVTPSLDRGGLAGITRQRVIELAAakgyaVDERPLRLEDL---LAADEA--FLTNSLLGVAPVT 229
PRK07101 PRK07101
hypothetical protein; Provisional
1-187 5.21e-14

hypothetical protein; Provisional


Pssm-ID: 235934  Cd Length: 187  Bit Score: 67.27  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   1 MQLFETMKIDNGHIPRLTYHTNRIKcSSERLNFKFDEHAWRNELNDVTTKYHSGQYRLKIVLHAEsEFETIVSPLPEK-- 78
Cdd:PRK07101   3 FPLFETIAIEDGEIQNLSYHQQRYE-RTLAEFYGKEAPFDLAEIIQPPTELQEGLVRCRIDYNAE-IYQVQYFPYQRRpi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  79 SSFtakfqvlpKAVNPTFIN--NKTTERKHL----AHNHETDLILLTsEDGKVLEFDIGNVVIEEDGKWYTPsyKDDFLK 152
Cdd:PRK07101  81 RSF--------QPVYCDDIDysLKYTDRSALnelfAQKGECDEIIII-KNGLVTDTSIGNLAFFDGKQWFTP--KKPLLK 149
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 612906875 153 GCMRDYLIDSDKLVEKDFNKNELiYKYHnnEIRLF 187
Cdd:PRK07101 150 GTQRARLLDEGKIKEKDITVEDL-LQYE--EIRLI 181
 
Name Accession Description Interval E-value
Aminotran_4 pfam01063
Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to ...
2-201 6.40e-41

Amino-transferase class IV; The D-amino acid transferases (D-AAT) are required by bacteria to catalyze the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.


Pssm-ID: 395844 [Multi-domain]  Cd Length: 221  Bit Score: 138.26  E-value: 6.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875    2 QLFETMKIDNGHIPRLTYHTNRIKCSSERLN--FKFDEHAWRNELNDVTTKYHSGQYRLKIVLHA----------ESEFE 69
Cdd:pfam01063   1 GVFETLRVYNGKIFFLDEHLARLRRSAKLLGipLPFDEEDLRKIIEELLKANGLGVGRLRLTVSRgpggfglptsDPTLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   70 TIVSPLPEKSSFTAK-----------FQVLPKAVNPTFINNKTTERKHLAHNHetDLILLTSEDGKVLEFDIGNVVIEED 138
Cdd:pfam01063  81 IFVSALPPPPESKKKgvisslvrrnpPSPLPGAKTLNYLENVLARREAKAQGA--DDALLLDEDGNVTEGSTSNVFLVKG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 612906875  139 GKWYTPSYKDDFLKGCMRDYLIDSDK-----LVEKDFNKNELIykyhnNEIRLFLINSLREVADVHLC 201
Cdd:pfam01063 159 GTLYTPPLESGILPGITRQALLDLAKalgleVEERPITLADLQ-----EADEAFLTNSLRGVTPVSSI 221
IlvE COG0115
Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid ...
3-199 6.63e-16

Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Branched-chain amino acid aminotransferase/4-amino-4-deoxychorismate lyase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439885 [Multi-domain]  Cd Length: 285  Bit Score: 74.07  E-value: 6.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   3 LFETMKIDNGHIPRLTYHTNRIKCSSERLNFK--FDEHAWRNELNDVTTKYHSGQYRLKIVL--------HAESEFET-- 70
Cdd:COG0115   30 VFEGIRAYDGRLFRLDEHLARLNRSAKRLGIPipYTEEELLEAIRELVAANGLEDGYIRPQVtrgvggrgVFAEEYEPtv 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  71 --IVSPLPEKSS---------FTAKFQvlpKAVNPTFINNKTTER------KHLAHNHETDLILLTSEDGKVLEFDIGNV 133
Cdd:COG0115  110 iiIASPLPAYPAeayekgvrvITSPYR---RAAPGGLGGIKTGNYlnnvlaKQEAKEAGADEALLLDTDGYVAEGSGSNV 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 612906875 134 VIEEDGKWYTPSYKDDFLKGCMRDYLID--SD---KLVEKDFNKNELiykYHNNEIrlFLINSLREVADVH 199
Cdd:COG0115  187 FIVKDGVLVTPPLSGGILPGITRDSVIElaRElgiPVEERPISLEEL---YTADEV--FLTGTAAEVTPVT 252
ADCL_like cd01559
ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent ...
3-199 1.30e-15

ADCL_like: 4-Amino-4-deoxychorismate lyase: is a member of the fold-type IV of PLP dependent enzymes that converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate. Based on the information available from the crystal structure, most members of this subgroup are likely to function as dimers. The enzyme from E.Coli, the structure of which is available, is a homodimer that is folded into a small and a larger domain. The coenzyme pyridoxal 5; -phosphate resides at the interface of the two domains that is linked by a flexible loop. Members of this subgroup are found in Eukaryotes and bacteria.


Pssm-ID: 238800 [Multi-domain]  Cd Length: 249  Bit Score: 72.73  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   3 LFETMKIDNGHIPRLTYHTNRIKCSSERLNF-KFDEHAWRNELNDVTTKYHSGQYRLKIVLHAESEFETIVSPLPEKSSF 81
Cdd:cd01559   10 VFETMRALDGRLFLLDAHLARLERSARRLGIpEPDLPRLRAALESLLAANDIDEGRIRLILSRGPGGRGYAPSVCPGPAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  82 TAKFQVLPKAVNPTFINNKTTER-----------KHL-----------AHNHETDLILLTSEDGKVLEFDIGNVVIEEDG 139
Cdd:cd01559   90 YVSVIPLPPAWRQDGVRLITCPVrlgeqpllaglKHLnylenvlakreARDRGADEALFLDTDGRVIEGTASNLFFVKDG 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 612906875 140 KWYTPSYKDDFLKGCMRDYLIDSDK-----LVEKDFNKNELiykYHNNEIrlFLINSLREVADVH 199
Cdd:cd01559  170 ELVTPSLDRGGLAGITRQRVIELAAakgyaVDERPLRLEDL---LAADEA--FLTNSLLGVAPVT 229
PRK07101 PRK07101
hypothetical protein; Provisional
1-187 5.21e-14

hypothetical protein; Provisional


Pssm-ID: 235934  Cd Length: 187  Bit Score: 67.27  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   1 MQLFETMKIDNGHIPRLTYHTNRIKcSSERLNFKFDEHAWRNELNDVTTKYHSGQYRLKIVLHAEsEFETIVSPLPEK-- 78
Cdd:PRK07101   3 FPLFETIAIEDGEIQNLSYHQQRYE-RTLAEFYGKEAPFDLAEIIQPPTELQEGLVRCRIDYNAE-IYQVQYFPYQRRpi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  79 SSFtakfqvlpKAVNPTFIN--NKTTERKHL----AHNHETDLILLTsEDGKVLEFDIGNVVIEEDGKWYTPsyKDDFLK 152
Cdd:PRK07101  81 RSF--------QPVYCDDIDysLKYTDRSALnelfAQKGECDEIIII-KNGLVTDTSIGNLAFFDGKQWFTP--KKPLLK 149
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 612906875 153 GCMRDYLIDSDKLVEKDFNKNELiYKYHnnEIRLF 187
Cdd:PRK07101 150 GTQRARLLDEGKIKEKDITVEDL-LQYE--EIRLI 181
PLPDE_IV cd00449
PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, ...
2-199 1.73e-12

PyridoxaL 5'-Phosphate Dependent Enzymes class IV (PLPDE_IV). This D-amino acid superfamily, one of five classes of PLPDE, consists of branched-chain amino acid aminotransferases (BCAT), D-amino acid transferases (DAAT), and 4-amino-4-deoxychorismate lyases (ADCL). BCAT catalyzes the reversible transamination reaction between the L-branched-chain amino and alpha-keto acids. DAAT catalyzes the synthesis of D-glutamic acid and D-alanine, and ADCL converts 4-amino-4-deoxychorismate to p-aminobenzoate and pyruvate. Except for a few enzymes, i. e., Escherichia coli and Salmonella BCATs, which are homohexamers arranged as a double trimer, the class IV PLPDEs are homodimers. Homodimer formation is required for catalytic activity.


Pssm-ID: 238254 [Multi-domain]  Cd Length: 256  Bit Score: 64.16  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   2 QLFETMKIDNGHIPRLTYHTNRIKCSSERLNFK--FDEHAWRNELNDVTTKYHSGQYRLKIVLHAESEFETIVSPLPEKS 79
Cdd:cd00449    9 GVFEGLRAGKGRLFRLDEHLDRLNRSAKRLGLPipYDREELREALKELVAANNGASLYIRPLLTRGVGGLGVAPPPSPEP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  80 SFT-------AKFQVLPKAVN----PTF---INNKTTERKHL-----------AHNHETDLILLTSEDGKVLEFDIGNVV 134
Cdd:cd00449   89 TFVvfaspvgAYAKGGEKGVRlitsPDRrraAPGGTGDAKTGgnlnsvlakqeAAEAGADEALLLDDNGYVTEGSASNVF 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875 135 IEEDGKWYTPSYKDDFLKGCMRDYLID-----SDKLVEKDFNKNELiykYHNNEIrlFLINSLREVADVH 199
Cdd:cd00449  169 IVKDGELVTPPLDGGILPGITRDSVIElakelGIKVEERPISLDEL---YAADEV--FLTGTAAEVTPVT 233
PRK07546 PRK07546
hypothetical protein; Provisional
2-193 4.46e-08

hypothetical protein; Provisional


Pssm-ID: 169002 [Multi-domain]  Cd Length: 209  Bit Score: 51.13  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875   2 QLFETMKIDNGH-IPRLTYHTNRIKCSSERLNFKFDEHAWRNELNDVTTKyHSGQYRLKIVL--HAESEFETIV-SPLPE 77
Cdd:PRK07546   5 ELIETLRWEPGAgFPRLDRHLARLERSARALGFPCDPAAVRAKLAEAVAG-AQGPLRLRLTLarDGRLTVETAPlPPLPP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612906875  78 KSSFTAKFQVLPKAVNPTFINNKTTERKHLAH------NHETDLILLTSEDGKVLEFDIGNVVIEEDGKWY-TPSYKDDF 150
Cdd:PRK07546  84 DTVWRVAIARTRLDSADPLLRYKTTRRAAYDAaraelpPAEADEVILLNERGEVCEGTITNVFLDRGGGMLtTPPLSCGL 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 612906875 151 LKGCMRDYLIDSDKLVEKDFNKNELiykyhNNEIRLFLINSLR 193
Cdd:PRK07546 164 LPGVLRAELLDAGRAREAVLTVDDL-----KSARAIWVGNSLR 201
PRK07849 PRK07849
aminodeoxychorismate lyase;
108-153 1.35e-03

aminodeoxychorismate lyase;


Pssm-ID: 236114 [Multi-domain]  Cd Length: 292  Bit Score: 38.40  E-value: 1.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 612906875 108 AHNHETDLILLTSEDGKVLEFDIGNVVIEEDGKWYTPSYKDDFLKG 153
Cdd:PRK07849 173 AARRGADDVIFTSTDGYVLEGPTSTVVIATDDRLLTPPPWYGILPG 218
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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