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Conserved domains on  [gi|342804159|gb|EGU39490|]
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type 11 methyltransferase [Vibrio splendidus ATCC 33789]

Protein Classification

class I SAM-dependent methyltransferase( domain architecture ID 11454890)

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

EC:  2.1.1.-
Gene Ontology:  GO:0032259|GO:0008168|GO:1904047
PubMed:  12504684|12826405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 48-150 1.34e-20

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: 84.30  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  48 QGKSLLHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHANslKQALDLKADFIESDVVQFGHENkQQFDIVFtSYGVLCW 127
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED-GSFDLVI-CSEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 342804159 128 LPNLVDWAQTIAKSLKVGGEFHL 150
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 48-150 1.34e-20

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: 84.30  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  48 QGKSLLHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHANslKQALDLKADFIESDVVQFGHENkQQFDIVFtSYGVLCW 127
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED-GSFDLVI-CSEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 342804159 128 LPNLVDWAQTIAKSLKVGGEFHL 150
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-146 4.46e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.35  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   57 CHFGQDTLSWA-RLGAEVTGVDLSANAIKHANSLKQALDLKADFIESDVVQFGHENkQQFDIVFtSYGVLCWL--PNLVD 133
Cdd:pfam13649   6 CGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD-GSFDLVV-SSGVLHHLpdPDLEA 83

                          90
                  ....*....|...
gi 342804159  134 WAQTIAKSLKVGG 146
Cdd:pfam13649  84 ALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-151 1.30e-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: 54.36  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  60 GQDTLSWARL-GAEVTGVDLSANAIKHANSLKQA-LDLKADFIESDVVQFGHENKQQFDIVFTSYGVLCWLPNLVDWAQT 137
Cdd:cd02440   10 GALALALASGpGARVTGVDISPVALELARKAAAAlLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDLARFLEE 89

                         90
                 ....*....|....
gi 342804159 138 IAKSLKVGGEFHLV 151
Cdd:cd02440   90 ARRLLKPGGVLVLT 103
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 42-155 3.99e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.52  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  42 KQVGNVQGKSLLHLQCHFGQDTLSWARLG---AEVTGVDLSAN--AIKHANSLKQALDLKADFIESDVVQFGHENkQQFD 116
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGmlAVGREKLRDLGLSGNVEFVQGDAEALPFPD-NSFD 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 342804159 117 IVFTSYGvlcwLPNLVDWAQT---IAKSLKVGGEFHLVEFHT 155
Cdd:PRK00216 124 AVTIAFG----LRNVPDIDKAlreMYRVLKPGGRLVILEFSK 161
 
Name Accession Description Interval E-value
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 48-150 1.34e-20

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: 84.30  E-value: 1.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  48 QGKSLLHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHANslKQALDLKADFIESDVVQFGHENkQQFDIVFtSYGVLCW 127
Cdd:COG2227   24 AGGRVLDVGCGTGRLALALARRGADVTGVDISPEALEIAR--ERAAELNVDFVQGDLEDLPLED-GSFDLVI-CSEVLEH 99

                         90       100
                 ....*....|....*....|...
gi 342804159 128 LPNLVDWAQTIAKSLKVGGEFHL 150
Cdd:COG2227  100 LPDPAALLRELARLLKPGGLLLL 122
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 41-154 5.82e-17

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: 75.42  E-value: 5.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  41 LKQVGNVQGKSLLHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHANSLKQALDLKADFIESDVVQFGHENkQQFDIVFT 120
Cdd:COG2226   15 LAALGLRPGARVLDLGCGTGRLALALAERGARVTGVDISPEMLELARERAAEAGLNVEFVVGDAEDLPFPD-GSFDLVIS 93

                         90       100       110
                 ....*....|....*....|....*....|....
gi 342804159 121 SYgVLCWLPNLVDWAQTIAKSLKVGGEFHLVEFH 154
Cdd:COG2226   94 SF-VLHHLPDPERALAEIARVLKPGGRLVVVDFS 126
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 57-146 4.46e-13

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 63.35  E-value: 4.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   57 CHFGQDTLSWA-RLGAEVTGVDLSANAIKHANSLKQALDLKADFIESDVVQFGHENkQQFDIVFtSYGVLCWL--PNLVD 133
Cdd:pfam13649   6 CGTGRLTLALArRGGARVTGVDLSPEMLERARERAAEAGLNVEFVQGDAEDLPFPD-GSFDLVV-SSGVLHHLpdPDLEA 83

                          90
                  ....*....|...
gi 342804159  134 WAQTIAKSLKVGG 146
Cdd:pfam13649  84 ALREIARVLKPGG 96
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-148 2.41e-12

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 61.53  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   53 LHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHANSLKQALDLKadFIESDVVQFGHENKqQFDIVFtSYGVLCWLPNLV 132
Cdd:pfam08241   1 LDVGCGTGLLTELLARLGARVTGVDISPEMLELAREKAPREGLT--FVVGDAEDLPFPDN-SFDLVL-SSEVLHHVEDPE 76

                          90
                  ....*....|....*.
gi 342804159  133 DWAQTIAKSLKVGGEF 148
Cdd:pfam08241  77 RALREIARVLKPGGIL 92
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 53-148 6.02e-12

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 60.46  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   53 LHLQCHFGQDTLSWARL--GAEVTGVDLSANAIKHA-NSLKQALDLKADFIESDVVQFGHENKQQFDIVfTSYGVLCWLP 129
Cdd:pfam08242   1 LEIGCGTGTLLRALLEAlpGLEYTGLDISPAALEAArERLAALGLLNAVRVELFQLDLGELDPGSFDVV-VASNVLHHLA 79

                          90
                  ....*....|....*....
gi 342804159  130 NLVDWAQTIAKSLKVGGEF 148
Cdd:pfam08242  80 DPRAVLRNIRRLLKPGGVL 98
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
41-214 5.92e-11

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 59.63  E-value: 5.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  41 LKQVGNVQGKSLLHLQCHFGQDTLSWARLGAEVTGVDLSANAIKHAnslkQALDLKADFIESDVVQFGHENKqQFDIVfT 120
Cdd:COG4976   39 LARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLTGVDLSEEMLAKA----REKGVYDRLLVADLADLAEPDG-RFDLI-V 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159 121 SYGVLCWLPNLVDWAQTIAKSLKVGGEFHLvefhtfndllsgypyfpdSRPDVEEEGTYtencdgtktttvtwSHPISEV 200
Cdd:COG4976  113 AADVLTYLGDLAAVFAGVARALKPGGLFIF------------------SVEDADGSGRY--------------AHSLDYV 160

                        170
                 ....*....|....
gi 342804159 201 INALIDAGLKIESF 214
Cdd:COG4976  161 RDLLAAAGFEVPGL 174
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
48-146 8.31e-10

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 54.44  E-value: 8.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  48 QGKSLLHLQCHFGQDTLSWARL--GAEVTGVDLSANAIKHAnslKQALDlKADFIESDVVQFghENKQQFDIVFTSYgVL 125
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERfpGARVTGVDLSPEMLARA---RARLP-NVRFVVADLRDL--DPPEPFDLVVSNA-AL 73

                         90       100
                 ....*....|....*....|.
gi 342804159 126 CWLPNLVDWAQTIAKSLKVGG 146
Cdd:COG4106   74 HWLPDHAALLARLAAALAPGG 94
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 67-151 1.29e-09

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


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 56.46  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  67 ARLGAEVTGVDLSANAIKHANSLKQALDLK-ADFIESDVVQFGHENKQQFDIVFtSYGVLCWLP--NLVDWAQTIAKSLK 143
Cdd:COG0500   46 ARFGGRVIGIDLSPEAIALARARAAKAGLGnVEFLVADLAELDPLPAESFDLVV-AFGVLHHLPpeEREALLRELARALK 124


                 ....*...
gi 342804159 144 VGGEFHLV 151
Cdd:COG0500  125 PGGVLLLS 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 60-151 1.30e-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: 54.36  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  60 GQDTLSWARL-GAEVTGVDLSANAIKHANSLKQA-LDLKADFIESDVVQFGHENKQQFDIVFTSYGVLCWLPNLVDWAQT 137
Cdd:cd02440   10 GALALALASGpGARVTGVDISPVALELARKAAAAlLADNVEVLKGDAEELPPEADESFDVIISDPPLHHLVEDLARFLEE 89

                         90
                 ....*....|....
gi 342804159 138 IAKSLKVGGEFHLV 151
Cdd:cd02440   90 ARRLLKPGGVLVLT 103
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 49-150 1.82e-09

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


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 55.32  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  49 GKSLLHLQCHFGQDTLSWA-RLGAEVTGVDLSANAIKHANSLKQA--LDLKADFIESDVVQFGHEnkQQFDIVFtSYGVL 125
Cdd:COG2230   52 GMRVLDIGCGWGGLALYLArRYGVRVTGVTLSPEQLEYARERAAEagLADRVEVRLADYRDLPAD--GQFDAIV-SIGMF 128

                         90       100
                 ....*....|....*....|....*..
gi 342804159 126 CWLP--NLVDWAQTIAKSLKVGGEFHL 150
Cdd:COG2230  129 EHVGpeNYPAYFAKVARLLKPGGRLLL 155
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 49-160 5.14e-08

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 50.88  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   49 GKSLLHLQCHFGQDTLSWARL---GAEVTGVDLSANAIKHANSLKQALDLK-ADFIESDVVQFG-HENKQQFDIVFtSYG 123
Cdd:pfam13847   4 GMRVLDLGCGTGHLSFELAEElgpNAEVVGIDISEEAIEKARENAQKLGFDnVEFEQGDIEELPeLLEDDKFDVVI-SNC 82

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 342804159  124 VLCWLPNLVDWAQTIAKSLKVGGEFHLVEFHTFNDLL 160
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDPDSLAELP 119
RlmK COG1092
23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure ...
 47-119 2.79e-05

23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI [Translation, ribosomal structure and biogenesis]; 23S rRNA G2069 N7-methylase RlmK or C1962 C5-methylase RlmI is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 440709 [Multi-domain]  Cd Length: 392  Bit Score: 44.79  E-value: 2.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  47 VQGKSLLHLQCHFGqdtlSW----ARLGA-EVTGVDLSANAIKHAnslKQALDL-----KADFIESDVVQF---GHENKQ 113
Cdd:COG1092  215 AKGKRVLNLFSYTG----GFsvhaAAGGAkSVTSVDLSATALEWA---KENAALnglddRHEFVQADAFDWlreLAREGE 287


                 ....*.
gi 342804159 114 QFDIVF 119
Cdd:COG1092  288 RFDLII 293
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 67-157 6.48e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 42.42  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159   67 ARLGAEVTGVDLSANAIKHAnslkqaldLKADFIESDVVQFGHENKQQFDIVfTSYGVLCWLPNLVDWAQTIAKSLKVGG 146
Cdd:pfam13489  41 RAQGFSVTGVDPSPIAIERA--------LLNVRFDQFDEQEAAVPAGKFDVI-VAREVLEHVPDPPALLRQIAALLKPGG 111

                          90
                  ....*....|.
gi 342804159  147 efhLVEFHTFN 157
Cdd:pfam13489 112 ---LLLLSTPL 119
ubiE PRK00216
bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol ...
 42-155 3.99e-04

bifunctional demethylmenaquinone methyltransferase/2-methoxy-6-polyprenyl-1,4-benzoquinol methylase UbiE;


Pssm-ID: 234689 [Multi-domain]  Cd Length: 239  Bit Score: 40.52  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342804159  42 KQVGNVQGKSLLHLQCHFGQDTLSWARLG---AEVTGVDLSAN--AIKHANSLKQALDLKADFIESDVVQFGHENkQQFD 116
Cdd:PRK00216  45 KWLGVRPGDKVLDLACGTGDLAIALAKAVgktGEVVGLDFSEGmlAVGREKLRDLGLSGNVEFVQGDAEALPFPD-NSFD 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 342804159 117 IVFTSYGvlcwLPNLVDWAQT---IAKSLKVGGEFHLVEFHT 155
Cdd:PRK00216 124 AVTIAFG----LRNVPDIDKAlreMYRVLKPGGRLVILEFSK 161
 
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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