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Conserved domains on  [gi|1226099802|gb|ASP21593|]
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methyltransferase type 12 [Antarctobacter heliothermus]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11467871)

SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

CATH:  2.20.25.110
EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008757|GO:0008168|GO:1904047
PubMed:  12826405|12504684
SCOP:  3000118

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-138 1.07e-17

Trans-aconitate methyltransferase [Energy production and conversion];


:

Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  35 EGAVICDAAAGPGADVDALAQAVPGAQVLAFDKQTAFVAQMTARFsgaPNVAVQQADLAQIAdlPQAPFDMIWCAGALYF 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL---PNVRFVVADLRDLD--PPEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1226099802 115 LG-LDQGLQIMRRALKAGGVLAFSE 138
Cdd:COG4106    76 LPdHAALLARLAAALAPGGVLAVQV 100
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-138 1.07e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  35 EGAVICDAAAGPGADVDALAQAVPGAQVLAFDKQTAFVAQMTARFsgaPNVAVQQADLAQIAdlPQAPFDMIWCAGALYF 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL---PNVRFVVADLRDLD--PPEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1226099802 115 LG-LDQGLQIMRRALKAGGVLAFSE 138
Cdd:COG4106    76 LPdHAALLARLAAALAPGGVLAVQV 100
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-132 2.06e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.43  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  39 ICDAAAGPGADVDALAQAVpGAQVLAFDKQTAFVAQMTARFSGA-PNVAVQQADLAQIaDLPQAPFDMIWCAGALYFLG- 116
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAgLNVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPd 78

                          90
                  ....*....|....*...
gi 1226099802 117 --LDQGLQIMRRALKAGG 132
Cdd:pfam13649  79 pdLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-137 4.07e-09

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: 52.82  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  39 ICDAAAGPGADVDALAQAvPGAQVLAFD---KQTAFVAQMTARFsGAPNVAVQQADLAQIADLPQAPFDMIWCAGALYFL 115
Cdd:cd02440     2 VLDLGCGTGALALALASG-PGARVTGVDispVALELARKAAAAL-LADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....
gi 1226099802 116 GLDQ--GLQIMRRALKAGGVLAFS 137
Cdd:cd02440    80 VEDLarFLEEARRLLKPGGVLVLT 103
rADc smart00650
Ribosomal RNA adenine dimethylases;
29-106 2.16e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.57  E-value: 2.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1226099802   29 DLAGLAEGAVICDAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARFSGAPNVAVQQADLAQiADLPQAPFDMI 106
Cdd:smart00650   7 RAANLRPGDTVLEIGPGKGALTEELLER--AKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALK-FDLPKLQPYKV 81
PRK08317 PRK08317
hypothetical protein; Provisional
 26-139 1.46e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  26 WATDLAGLAEGAVICDAAAGPGADVDALAQAV-PGAQVLAFDKQTAFVAQMTARFSG-APNVAVQQADLAQIaDLPQAPF 103
Cdd:PRK08317   10 RTFELLAVQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGlGPNVEFVRGDADGL-PFPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1226099802 104 DMIWCAGAL-YFLGLDQGLQIMRRALKAGGVLAFSEP 139
Cdd:PRK08317   89 DAVRSDRVLqHLEDPARALAEIARVLRPGGRVVVLDT 125
 
Name Accession Description Interval E-value
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
35-138 1.07e-17

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 75.63  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  35 EGAVICDAAAGPGADVDALAQAVPGAQVLAFDKQTAFVAQMTARFsgaPNVAVQQADLAQIAdlPQAPFDMIWCAGALYF 114
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARL---PNVRFVVADLRDLD--PPEPFDLVVSNAALHW 75

                          90       100
                  ....*....|....*....|....*
gi 1226099802 115 LG-LDQGLQIMRRALKAGGVLAFSE 138
Cdd:COG4106    76 LPdHAALLARLAAALAPGGVLAVQV 100
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 29-138 6.70e-14

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: 66.56  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  29 DLAGLAEGAVICDAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARFSGAP-NVAVQQADLAQIaDLPQAPFDMIW 107
Cdd:COG2226    16 AALGLRPGARVLDLGCGTGRLALALAER--GARVTGVDISPEMLELARERAAEAGlNVEFVVGDAEDL-PFPDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1226099802 108 CAGALYFLG-LDQGLQIMRRALKAGGVLAFSE 138
Cdd:COG2226    93 SSFVLHHLPdPERALAEIARVLKPGGRLVVVD 124
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 26-139 7.96e-14

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: 66.19  E-value: 7.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  26 WATDLAG-----LAEGAVICDAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARFSgAPNVAVQQADLAQIaDLPQ 100
Cdd:COG2227    10 WDRRLAAllarlLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAA-ELNVDFVQGDLEDL-PLED 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1226099802 101 APFDMIWCAGALYFL-GLDQGLQIMRRALKAGGVLAFSEP 139
Cdd:COG2227    86 GSFDLVICSEVLEHLpDPAALLRELARLLKPGGLLLLSTP 125
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 26-137 1.50e-13

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 67.25  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  26 WATDLAGLAEGAVICDAAAGPGADVDALAQAvPGAQVLAFDKQTAFVAQMTARFS--GAPNVAVQQADLAQIADLPQAPF 103
Cdd:COG0500    17 LLALLERLPKGGRVLDLGCGTGRNLLALAAR-FGGRVIGIDLSPEAIALARARAAkaGLGNVEFLVADLAELDPLPAESF 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1226099802 104 DMIWCAGALYFLG---LDQGLQIMRRALKAGGVLAFS 137
Cdd:COG0500    96 DLVVAFGVLHHLPpeeREALLRELARALKPGGVLLLS 132
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 39-132 2.06e-12

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 61.43  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  39 ICDAAAGPGADVDALAQAVpGAQVLAFDKQTAFVAQMTARFSGA-PNVAVQQADLAQIaDLPQAPFDMIWCAGALYFLG- 116
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRG-GARVTGVDLSPEMLERARERAAEAgLNVEFVQGDAEDL-PFPDGSFDLVVSSGVLHHLPd 78

                          90
                  ....*....|....*...
gi 1226099802 117 --LDQGLQIMRRALKAGG 132
Cdd:pfam13649  79 pdLEAALREIARVLKPGG 96
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-134 1.54e-10

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 56.22  E-value: 1.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  41 DAAAGPGADVDALAQAVPGAQVLAFDKQTAFVAQMTARFSGAPNVAVQQADLAQ--IADLPQAPFDMIWCAGALYFLG-L 117
Cdd:pfam08242   2 EIGCGTGTLLRALLEALPGLEYTGLDISPAALEAARERLAALGLLNAVRVELFQldLGELDPGSFDVVVASNVLHHLAdP 81

                          90
                  ....*....|....*..
gi 1226099802 118 DQGLQIMRRALKAGGVL 134
Cdd:pfam08242  82 RAVLRNIRRLLKPGGVL 98
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 35-148 6.75e-10

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 55.89  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  35 EGAVICDAAAGPGADVDALAQAV-PGAQVLAFDKQTAFVAQMTARFS--GAPNVAVQQADlaqIADLPQA----PFDMIW 107
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELAEELgPNAEVVGIDISEEAIEKARENAQklGFDNVEFEQGD---IEELPELleddKFDVVI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1226099802 108 CAGALYFLG-LDQGLQIMRRALKAGGVLAFSEPCYFTETPGP 148
Cdd:pfam13847  80 SNCVLNHIPdPDKVLQEILRVLKPGGRLIISDPDSLAELPAH 121
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 29-139 7.99e-10

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.71  E-value: 7.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  29 DLAGLAEGAVICDAAAGPGADVDALAQAVpGAQVLAFD---KQTAFVAQMTARFSGAPNVAVQQADLAQIAdlPQAPFDM 105
Cdd:COG2230    45 RKLGLKPGMRVLDIGCGWGGLALYLARRY-GVRVTGVTlspEQLEYARERAAEAGLADRVEVRLADYRDLP--ADGQFDA 121

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1226099802 106 IWCAGALYFLG---LDQGLQIMRRALKAGGVLAFSEP 139
Cdd:COG2230   122 IVSIGMFEHVGpenYPAYFAKVARLLKPGGRLLLHTP 158
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 39-137 4.07e-09

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: 52.82  E-value: 4.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  39 ICDAAAGPGADVDALAQAvPGAQVLAFD---KQTAFVAQMTARFsGAPNVAVQQADLAQIADLPQAPFDMIWCAGALYFL 115
Cdd:cd02440     2 VLDLGCGTGALALALASG-PGARVTGVDispVALELARKAAAAL-LADNVEVLKGDAEELPPEADESFDVIISDPPLHHL 79

                          90       100
                  ....*....|....*....|....
gi 1226099802 116 GLDQ--GLQIMRRALKAGGVLAFS 137
Cdd:cd02440    80 VEDLarFLEEARRLLKPGGVLVLT 103
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
2-137 3.84e-07

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 48.84  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802   2 DWRTFFEVH--KDLPREGPGTSGDVIWATdlAGLAEGAVICDAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARF 79
Cdd:COG4976    13 QYADSYDAAlvEDLGYEAPALLAEELLAR--LPPGPFGRVLDLGCGTGLLGEALRPR--GYRLTGVDLSEEMLAKAREKG 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1226099802  80 SGapnVAVQQADLAQIADLPqAPFDMIWCAGALYFLG-LDQGLQIMRRALKAGGVLAFS 137
Cdd:COG4976    89 VY---DRLLVADLADLAEPD-GRFDLIVAADVLTYLGdLAAVFAGVARALKPGGLFIFS 143
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 41-136 3.95e-06

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 44.19  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  41 DAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARFSGAPnVAVQQADLAQIaDLPQAPFDMIWCAGALYFLG-LDQ 119
Cdd:pfam08241   2 DVGCGTGLLTELLARL--GARVTGVDISPEMLELAREKAPREG-LTFVVGDAEDL-PFPDNSFDLVLSSEVLHHVEdPER 77

                          90
                  ....*....|....*..
gi 1226099802 120 GLQIMRRALKAGGVLAF 136
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
 52-134 1.43e-04

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: 41.33  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  52 ALAQAVPGAQVLAFDKQTAFV--AQMTARFSGAPNVAVQQADLAqiADLPQAPFDMIWC-----AGAlyFLGLDQGLQIM 124
Cdd:COG2813    66 ALAKRNPEARVTLVDVNARAVelARANAAANGLENVEVLWSDGL--SGVPDGSFDLILSnppfhAGR--AVDKEVAHALI 141

                          90
                  ....*....|...
gi 1226099802 125 RRA---LKAGGVL 134
Cdd:COG2813   142 ADAarhLRPGGEL 154
rADc smart00650
Ribosomal RNA adenine dimethylases;
29-106 2.16e-04

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 40.57  E-value: 2.16e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1226099802   29 DLAGLAEGAVICDAAAGPGADVDALAQAvpGAQVLAFDKQTAFVAQMTARFSGAPNVAVQQADLAQiADLPQAPFDMI 106
Cdd:smart00650   7 RAANLRPGDTVLEIGPGKGALTEELLER--AKRVTAIEIDPRLAPRLREKFAAADNLTVIHGDALK-FDLPKLQPYKV 81
PRK08317 PRK08317
hypothetical protein; Provisional
 26-139 1.46e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 38.76  E-value: 1.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1226099802  26 WATDLAGLAEGAVICDAAAGPGADVDALAQAV-PGAQVLAFDKQTAFVAQMTARFSG-APNVAVQQADLAQIaDLPQAPF 103
Cdd:PRK08317   10 RTFELLAVQPGDRVLDVGCGPGNDARELARRVgPEGRVVGIDRSEAMLALAKERAAGlGPNVEFVRGDADGL-PFPDGSF 88

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1226099802 104 DMIWCAGAL-YFLGLDQGLQIMRRALKAGGVLAFSEP 139
Cdd:PRK08317   89 DAVRSDRVLqHLEDPARALAEIARVLRPGGRVVVLDT 125
 
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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