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Conserved domains on  [gi|2203290782|ref|NP_001388962|]
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RNA N6-adenosine-methyltransferase METTL16 [Rattus norvegicus]

Protein Classification

RNA N6-adenosine-methyltransferase METTL16( domain architecture ID 11161135)

RNA N6-adenosine-methyltransferase METTL16 acts as a RNA N6-methyltransferase that methylates adenosine residues at the N(6) position of a subset of RNAs and is involved in S-adenosyl-L-methionine homeostasis by regulating expression of MAT2A transcripts

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
1-291 3.03e-178

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


:

Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 503.97  E-value: 3.03e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   1 MALSKSMHARNRYKDKPpDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTV 79
Cdd:pfam05971   1 MALKSGLHPRNRHKGRY-DFAYLISVYPELKQHVQLNPNGRQSINFADPEAVKALNKALLREFYGVSIwDIPDGFLCPPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  80 PLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDLIKVV 158
Cdd:pfam05971  80 PGRADYIHWVADLLGHQDSDIPTLRRALDIGTGANCIYPLLGVTEYGWRFVGSEVDPQSLNSAKAIVESNpNLSDAIELR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 159 KVPQKTLLMDALKEESEIvYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQL 238
Cdd:pfam05971 160 RQPQSTLIFNGLIGENER-YDFTLCNPPFHASLAEAKGGSSRKPGRPPPSLNFGGQIAELWCEGGEAAFIKKMIEESLQF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2203290782 239 KKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 291
Cdd:pfam05971 239 AKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
 
Name Accession Description Interval E-value
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
1-291 3.03e-178

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 503.97  E-value: 3.03e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   1 MALSKSMHARNRYKDKPpDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTV 79
Cdd:pfam05971   1 MALKSGLHPRNRHKGRY-DFAYLISVYPELKQHVQLNPNGRQSINFADPEAVKALNKALLREFYGVSIwDIPDGFLCPPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  80 PLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDLIKVV 158
Cdd:pfam05971  80 PGRADYIHWVADLLGHQDSDIPTLRRALDIGTGANCIYPLLGVTEYGWRFVGSEVDPQSLNSAKAIVESNpNLSDAIELR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 159 KVPQKTLLMDALKEESEIvYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQL 238
Cdd:pfam05971 160 RQPQSTLIFNGLIGENER-YDFTLCNPPFHASLAEAKGGSSRKPGRPPPSLNFGGQIAELWCEGGEAAFIKKMIEESLQF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2203290782 239 KKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 291
Cdd:pfam05971 239 AKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
RlmF COG3129
23S rRNA A1618 N6-methylase RlmF [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
7-289 2.48e-62

23S rRNA A1618 N6-methylase RlmF [Translation, ribosomal structure and biogenesis]; 23S rRNA A1618 N6-methylase RlmF is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442363  Cd Length: 292  Bit Score: 206.56  E-value: 2.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   7 MHARNRYKdKPPDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTVPLRLNY 85
Cdd:COG3129     1 LHPRNRHR-GRYDFPALIKSCPELAPFVFLNPYGDESIDFANPKAVKALNKALLKHFYGIKHwDIPDGYLCPPIPGRADY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  86 IHWVEDLIGhQDSDKTTLR----RGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDLIKVVKV 160
Cdd:COG3129    80 IHYLADLLA-ESNNGVIPTgkkiKVLDIGTGANCIYPIIGNREYGWRFVGSDIDPVALASAQKIIDANpGLKGKIELRLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 161 PQKTLLMDALKEESEIvYDFCMCNPPFFANQLEAKGVNSR-----NSRRPPPSSVNTGGI-TEIMAEGGELEFVKRIIHD 234
Cdd:COG3129   159 KNPKNIFKGIIKPGER-FDLTLCNPPFHASAEEAAAGTQRklknlGKKKAKKPVLNFGGQsNELWCEGGELAFIKRMIKE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2203290782 235 SLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQG-RTMRWaLAWSF 289
Cdd:COG3129   238 SKQFAKQVLWFTSLVSKKENLPPLYKALKKLGATEVKTIEMAQGqKQSRF-VAWTF 292
PRK11727 PRK11727
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
1-292 2.42e-58

23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;


Pssm-ID: 236964  Cd Length: 321  Bit Score: 197.01  E-value: 2.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   1 MALSKSMHARNRYKDKPpDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTV 79
Cdd:PRK11727   10 SAQKPGLHPRNRHRGRY-DFAALIQSHPELKPFVILNPYGEQSIDFANPLAVKALNKALLAHFYGVAHwDIPAGYLCPPI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  80 PLRLNYIHWVEDLIGhQDSDKTTLR----RGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDL 154
Cdd:PRK11727   89 PGRADYIHHLADLLA-EDNGGVIPRganvRVLDIGVGANCIYPLIGVHEYGWRFVGSDIDPQALASAQAIISANpGLNGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 155 IKVVKVPQKTLLMDALKEESEiVYDFCMCNPPFFANQLEAKGVNSRNSR-----RPPPSSVNTGGI-TEIMAEGGELEFV 228
Cdd:PRK11727  168 IRLRLQKDSKAIFKGIIHKNE-RFDATLCNPPFHASAAEARAGSQRKLRnlglnKDKKKVLNFGGQqAELWCEGGEVAFI 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203290782 229 KRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDD 292
Cdd:PRK11727  247 KRMIEESKAFAKQVLWFTSLVSKKENLPPLYRALKKVGAVEVKTIEMAQGQKQSRFIAWTFLDD 310
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
105-215 1.75e-05

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: 43.96  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 105 RGIDIGTGASCIYPLLgATLNGWYFLATEVDDMCFNYAKKNvEQNNLSDLIKVVKVPQKTLLMDALKEeseivYDFCMCN 184
Cdd:cd02440     1 RVLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADES-----FDVIISD 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2203290782 185 PPFFANQLEAKGVNSRNSRRPPPssvntGGI 215
Cdd:cd02440    74 PPLHHLVEDLARFLEEARRLLKP-----GGV 99
 
Name Accession Description Interval E-value
Methyltransf_10 pfam05971
RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, ...
1-291 3.03e-178

RNA methyltransferase; This family includes ribosomal RNA large subunit methyltransferase F, and related proteins, including methyltransferase-like protein 16 (METTL16). METTL16 is a conserved RNA methyltransferase which interacts specifically with the MALAT1 triple helix. METTL16 shows nuclear localization. Another functional study indicates that METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Furthermore, results indicate that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA) and it has evolved an additional function in vertebrates to control SAM homeostasis by post-transcriptionally regulating SAM synthetase gene expression.


Pssm-ID: 399160 [Multi-domain]  Cd Length: 291  Bit Score: 503.97  E-value: 3.03e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   1 MALSKSMHARNRYKDKPpDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTV 79
Cdd:pfam05971   1 MALKSGLHPRNRHKGRY-DFAYLISVYPELKQHVQLNPNGRQSINFADPEAVKALNKALLREFYGVSIwDIPDGFLCPPV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  80 PLRLNYIHWVEDLIGHQDSDKTTLRRGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDLIKVV 158
Cdd:pfam05971  80 PGRADYIHWVADLLGHQDSDIPTLRRALDIGTGANCIYPLLGVTEYGWRFVGSEVDPQSLNSAKAIVESNpNLSDAIELR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 159 KVPQKTLLMDALKEESEIvYDFCMCNPPFFANQLEAKGVNSRNSRRPPPSSVNTGGITEIMAEGGELEFVKRIIHDSLQL 238
Cdd:pfam05971 160 RQPQSTLIFNGLIGENER-YDFTLCNPPFHASLAEAKGGSSRKPGRPPPSLNFGGQIAELWCEGGEAAFIKKMIEESLQF 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2203290782 239 KKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYD 291
Cdd:pfam05971 239 AKQVRWFTTLVSKGCNLPPLKEELRILGAPKVTVTEMAQGQKQSRFIAWSFYD 291
RlmF COG3129
23S rRNA A1618 N6-methylase RlmF [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
7-289 2.48e-62

23S rRNA A1618 N6-methylase RlmF [Translation, ribosomal structure and biogenesis]; 23S rRNA A1618 N6-methylase RlmF is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 442363  Cd Length: 292  Bit Score: 206.56  E-value: 2.48e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   7 MHARNRYKdKPPDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTVPLRLNY 85
Cdd:COG3129     1 LHPRNRHR-GRYDFPALIKSCPELAPFVFLNPYGDESIDFANPKAVKALNKALLKHFYGIKHwDIPDGYLCPPIPGRADY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  86 IHWVEDLIGhQDSDKTTLR----RGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDLIKVVKV 160
Cdd:COG3129    80 IHYLADLLA-ESNNGVIPTgkkiKVLDIGTGANCIYPIIGNREYGWRFVGSDIDPVALASAQKIIDANpGLKGKIELRLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 161 PQKTLLMDALKEESEIvYDFCMCNPPFFANQLEAKGVNSR-----NSRRPPPSSVNTGGI-TEIMAEGGELEFVKRIIHD 234
Cdd:COG3129   159 KNPKNIFKGIIKPGER-FDLTLCNPPFHASAEEAAAGTQRklknlGKKKAKKPVLNFGGQsNELWCEGGELAFIKRMIKE 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2203290782 235 SLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQG-RTMRWaLAWSF 289
Cdd:COG3129   238 SKQFAKQVLWFTSLVSKKENLPPLYKALKKLGATEVKTIEMAQGqKQSRF-VAWTF 292
PRK11727 PRK11727
23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;
1-292 2.42e-58

23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF;


Pssm-ID: 236964  Cd Length: 321  Bit Score: 197.01  E-value: 2.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782   1 MALSKSMHARNRYKDKPpDFAYLASKYPDFKQHIQINLNGRVSLNFKDPEAVRALTCTLLREDFGLSI-DIPLERLIPTV 79
Cdd:PRK11727   10 SAQKPGLHPRNRHRGRY-DFAALIQSHPELKPFVILNPYGEQSIDFANPLAVKALNKALLAHFYGVAHwDIPAGYLCPPI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782  80 PLRLNYIHWVEDLIGhQDSDKTTLR----RGIDIGTGASCIYPLLGATLNGWYFLATEVDDMCFNYAKKNVEQN-NLSDL 154
Cdd:PRK11727   89 PGRADYIHHLADLLA-EDNGGVIPRganvRVLDIGVGANCIYPLIGVHEYGWRFVGSDIDPQALASAQAIISANpGLNGA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 155 IKVVKVPQKTLLMDALKEESEiVYDFCMCNPPFFANQLEAKGVNSRNSR-----RPPPSSVNTGGI-TEIMAEGGELEFV 228
Cdd:PRK11727  168 IRLRLQKDSKAIFKGIIHKNE-RFDATLCNPPFHASAAEARAGSQRKLRnlglnKDKKKVLNFGGQqAELWCEGGEVAFI 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2203290782 229 KRIIHDSLQLKKRLRWYSCMLGKKCSLAPLKEELRIQGVPKVTFTEFCQGRTMRWALAWSFYDD 292
Cdd:PRK11727  247 KRMIEESKAFAKQVLWFTSLVSKKENLPPLYRALKKVGAVEVKTIEMAQGQKQSRFIAWTFLDD 310
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
104-204 1.64e-06

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: 49.37  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 104 RRGIDIGTGaSCIYPLLGAT-LNGWYFLATEVDDMCFNYAKKNVEQNNLSDLIKVVKVPqktlLMDALKEESEIVYDFCM 182
Cdd:COG4123    39 GRVLDLGTG-TGVIALMLAQrSPGARITGVEIQPEAAELARRNVALNGLEDRITVIHGD----LKEFAAELPPGSFDLVV 113
                          90       100
                  ....*....|....*....|..
gi 2203290782 183 CNPPFFAnqlEAKGVNSRNSRR 204
Cdd:COG4123   114 SNPPYFK---AGSGRKSPDEAR 132
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
105-215 1.75e-05

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: 43.96  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2203290782 105 RGIDIGTGASCIYPLLgATLNGWYFLATEVDDMCFNYAKKNvEQNNLSDLIKVVKVPQKTLLMDALKEeseivYDFCMCN 184
Cdd:cd02440     1 RVLDLGCGTGALALAL-ASGPGARVTGVDISPVALELARKA-AAALLADNVEVLKGDAEELPPEADES-----FDVIISD 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2203290782 185 PPFFANQLEAKGVNSRNSRRPPPssvntGGI 215
Cdd:cd02440    74 PPLHHLVEDLARFLEEARRLLKP-----GGV 99
 
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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