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Conserved domains on  [gi|505093354|ref|WP_015280456|]
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methyltransferase [Thioflavicoccus mobilis]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 10008106)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Homo sapiens electron transfer flavoprotein beta subunit lysine methyltransferase

CATH:  3.40.50.150
EC:  2.1.1.-
Gene Ontology:  GO:1904047|GO:0008168|GO:0032259|GO:0008757
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 3-193 4.17e-53

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 169.29  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354   3 VEHVRI-SCGIRILQQKHPLIRSLRKAG---SEPTIYGTRVWQSSLMLIEYLREHPLIERQRIIEIGCGWGLVGIFCAKR 78
Cdd:COG3897   12 LETVLVpEIRLHLAADAHPLWDATEEALgesGAPPPFWAFLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  79 FAADVLLTDVDEQVFPYALAHANLNEVTVQTERACFDSLAEAslRGRNVIVGADVCFWPELTSQLRRLIARAASFGIErV 158
Cdd:COG3897   92 GAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAA--GGFDLILGGDVLYERDLAEPLLPFLDRLAAPGGE-V 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505093354 159 VIADPGRTTFMRLAEYCQRHFMATMTPYRMSTRTK 193
Cdd:COG3897  169 LIGDPGRGYLPAFRERLEALAGYEVVTRELEDTEK 203
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 3-193 4.17e-53

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 169.29  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354   3 VEHVRI-SCGIRILQQKHPLIRSLRKAG---SEPTIYGTRVWQSSLMLIEYLREHPLIERQRIIEIGCGWGLVGIFCAKR 78
Cdd:COG3897   12 LETVLVpEIRLHLAADAHPLWDATEEALgesGAPPPFWAFLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  79 FAADVLLTDVDEQVFPYALAHANLNEVTVQTERACFDSLAEAslRGRNVIVGADVCFWPELTSQLRRLIARAASFGIErV 158
Cdd:COG3897   92 GAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAA--GGFDLILGGDVLYERDLAEPLLPFLDRLAAPGGE-V 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505093354 159 VIADPGRTTFMRLAEYCQRHFMATMTPYRMSTRTK 193
Cdd:COG3897  169 LIGDPGRGYLPAFRERLEALAGYEVVTRELEDTEK 203
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 35-103 9.04e-06

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.12  E-value: 9.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354   35 YGTRVwqsslmLIEYLrehPLIERQRIIEIGCGWGLVGIFCAKRFA-ADVLLTDVDEqvfpYALAHANLN 103
Cdd:pfam05175  18 IGSRL------LLEHL---PKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINA----RALESAREN 74
PRK14968 PRK14968
putative methyltransferase; Provisional
 43-106 4.31e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 4.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505093354  43 SLMLIEYLREHPlieRQRIIEIGCGWGLVGIFCAKRfAADVLLTDVDeqvfPYA----LAHANLNEVT 106
Cdd:PRK14968  12 SFLLAENAVDKK---GDRVLEVGTGSGIVAIVAAKN-GKKVVGVDIN----PYAvecaKCNAKLNNIR 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-150 4.09e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 38.57  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  60 RIIEIGCGWGLVGIFCAKRFAADVLLTDVDEQVFPYAL-AHANLNEVTVQTERACFDSLAEASLRGRNVIVGADVCFW-P 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90
                 ....*....|...
gi 505093354 138 ELTSQLRRLIARA 150
Cdd:cd02440   81 EDLARFLEEARRL 93
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 41-103 3.61e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 3.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505093354   41 QSSLMLIEYLREhplIERQRIIEIGCGWGLVGIFCAKRfAADVLLTDVDeqvfPYALAHANLN 103
Cdd:TIGR00537   6 EDSLLLEANLRE---LKPDDVLEIGAGTGLVAIRLKGK-GKCILTTDIN----PFAVKELREN 60
 
Name Accession Description Interval E-value
Nnt1 COG3897
Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, ...
 3-193 4.17e-53

Protein N-terminal and lysine N-methylase, NNT1/EFM7 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443104 [Multi-domain]  Cd Length: 216  Bit Score: 169.29  E-value: 4.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354   3 VEHVRI-SCGIRILQQKHPLIRSLRKAG---SEPTIYGTRVWQSSLMLIEYLREHPLIERQRIIEIGCGWGLVGIFCAKR 78
Cdd:COG3897   12 LETVLVpEIRLHLAADAHPLWDATEEALgesGAPPPFWAFLWPSGQALARYLLDHPEVAGKRVLELGCGLGLVGIAAAKA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  79 FAADVLLTDVDEQVFPYALAHANLNEVTVQTERACFDSLAEAslRGRNVIVGADVCFWPELTSQLRRLIARAASFGIErV 158
Cdd:COG3897   92 GAADVTATDYDPEALAALRLNAALNGVAITTRLGDWRDPPAA--GGFDLILGGDVLYERDLAEPLLPFLDRLAAPGGE-V 168

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 505093354 159 VIADPGRTTFMRLAEYCQRHFMATMTPYRMSTRTK 193
Cdd:COG3897  169 LIGDPGRGYLPAFRERLEALAGYEVVTRELEDTEK 203
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 35-103 5.61e-08

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 50.57  E-value: 5.61e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  35 YGTRVwqsslmLIEYLrehPLIERQRIIEIGCGWGLVGIFCAKRFA-ADVLLTDVDEQvfpyALAHANLN 103
Cdd:COG2813   36 IGTRL------LLEHL---PEPLGGRVLDLGCGYGVIGLALAKRNPeARVTLVDVNAR----AVELARAN 92
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
 35-103 9.04e-06

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 44.12  E-value: 9.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354   35 YGTRVwqsslmLIEYLrehPLIERQRIIEIGCGWGLVGIFCAKRFA-ADVLLTDVDEqvfpYALAHANLN 103
Cdd:pfam05175  18 IGSRL------LLEHL---PKDLSGKVLDLGCGAGVLGAALAKESPdAELTMVDINA----RALESAREN 74
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 46-163 1.50e-05

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 42.70  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  46 LIEYLREHpLIERQRIIEIGCGWGLVGIFCAKRFaADVLLTDVDEQVfpYALAHANLNEVTVQTERACFDSLAEASlrGR 125
Cdd:COG2227   14 LAALLARL-LPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEA--LEIARERAAELNVDFVQGDLEDLPLED--GS 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 505093354 126 -NVIVGADVCFW-PELTSQLRRLIARAASFGieRVVIADP 163
Cdd:COG2227   88 fDLVICSEVLEHlPDPAALLRELARLLKPGG--LLLLSTP 125
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
 36-90 3.30e-05

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 42.70  E-value: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505093354   36 GTRVWQSSLMLIEYLrEHPLI--------ERQRIIEIGCGWGLVGIFCAKRFA-ADVLLTDVDE 90
Cdd:pfam10294  18 GGHVWDAAVVLSKYL-EMKIFkelgannlSGLNVLELGSGTGLVGIAVALLLPgASVTITDLEE 80
PRK14968 PRK14968
putative methyltransferase; Provisional
 43-106 4.31e-05

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 42.58  E-value: 4.31e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505093354  43 SLMLIEYLREHPlieRQRIIEIGCGWGLVGIFCAKRfAADVLLTDVDeqvfPYA----LAHANLNEVT 106
Cdd:PRK14968  12 SFLLAENAVDKK---GDRVLEVGTGSGIVAIVAAKN-GKKVVGVDIN----PYAvecaKCNAKLNNIR 71
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 45-101 5.51e-05

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 41.84  E-value: 5.51e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505093354  45 MLIEYLREHPLIERQRIIEIGCGWGLVGIFCAKRFAADVLLTDVDEQvfpyALAHAN 101
Cdd:COG2230   39 KLDLILRKLGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPE----QLEYAR 91
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 61-117 1.83e-04

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 39.08  E-value: 1.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 505093354   61 IIEIGCGWGLVGIFCAKRFAADVLLTDVDEQVFPYALAHANLNEVTVQTERACFDSL 117
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDL 57
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-150 4.09e-04

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 38.57  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  60 RIIEIGCGWGLVGIFCAKRFAADVLLTDVDEQVFPYAL-AHANLNEVTVQTERACFDSLAEASLRGRNVIVGADVCFW-P 137
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARkAAAALLADNVEVLKGDAEELPPEADESFDVIISDPPLHHlV 80

                         90
                 ....*....|...
gi 505093354 138 ELTSQLRRLIARA 150
Cdd:cd02440   81 EDLARFLEEARRL 93
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
43-106 6.55e-04

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 39.39  E-value: 6.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505093354  43 SLMLiEYLREHPLiERQRIIEIGCGWGLVGIFCAKRFAADVLLTDVDEQVFPYALAHANLNEVT 106
Cdd:COG2264  136 RLCL-EALEKLLK-PGKTVLDVGCGSGILAIAAAKLGAKRVLAVDIDPVAVEAARENAELNGVE 197
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
29-110 8.11e-04

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 38.98  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  29 GSEPTiygTRvwqssLMLiEYLREHPLiERQRIIEIGCGWGLVGIFCAKRFAADVLLTDVDEQVFPYALAHANLNEVTVQ 108
Cdd:PRK00517 101 GTHPT---TR-----LCL-EALEKLVL-PGKTVLDVGCGSGILAIAAAKLGAKKVLAVDIDPQAVEAARENAELNGVELN 170


                 ..
gi 505093354 109 TE 110
Cdd:PRK00517 171 VY 172
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 58-102 1.76e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 38.20  E-value: 1.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 505093354  58 RQRIIEIGCGWGLVGIFCAKRF-AADVLLTDVDEQVfpYALAHANL 102
Cdd:COG4123   38 GGRVLDLGTGTGVIALMLAQRSpGARITGVEIQPEA--AELARRNV 81
hemK_rel_arch TIGR00537
HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme ...
 41-103 3.61e-03

HemK-related putative methylase; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. This model represents an archaeal and eukaryotic protein family that lacks an N-terminal domain found in HemK and its eubacterial homologs. It is found in a single copy in the first six completed archaeal and eukaryotic genomes. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129628 [Multi-domain]  Cd Length: 179  Bit Score: 36.76  E-value: 3.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505093354   41 QSSLMLIEYLREhplIERQRIIEIGCGWGLVGIFCAKRfAADVLLTDVDeqvfPYALAHANLN 103
Cdd:TIGR00537   6 EDSLLLEANLRE---LKPDDVLEIGAGTGLVAIRLKGK-GKCILTTDIN----PFAVKELREN 60
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 46-177 8.70e-03

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 35.35  E-value: 8.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505093354  46 LIEYLREHPlieRQRIIEIGCGWGLVGIFCAKRfAADVLLTDVDEQVFPYALAHANLNEVTVQTERACFDSL--AEASLr 123
Cdd:COG2226   14 LLAALGLRP---GARVLDLGCGTGRLALALAER-GARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLpfPDGSF- 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 505093354 124 grNVIVGADV-CFWPELTSQLRRlIARAASFGIeRVVIADPGRTTFMRLAEYCQR 177
Cdd:COG2226   89 --DLVISSFVlHHLPDPERALAE-IARVLKPGG-RLVVVDFSPPDLAELEELLAE 139
 
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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