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Conserved domains on  [gi|2468907794|ref|WP_276984764|]
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N-acetylmannosamine-6-phosphate 2-epimerase [Actinobacillus porcinus]

Protein Classification

N-acetylmannosamine-6-phosphate 2-epimerase( domain architecture ID 10011628)

N-acetylmannosamine-6-phosphate 2-epimerase converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
11-226 4.41e-125

putative N-acetylmannosamine-6-phosphate 2-epimerase;


:

Pssm-ID: 234907  Cd Length: 221  Bit Score: 352.91  E-value: 4.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  11 ERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITPFLDD 90
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  91 IDALATAGADIIAVDGTNRPRP--VSIKEAVERIHQK-GCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGG-EVPEEP 166
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPdgETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEEtKKPEEP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468907794 167 DYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWFAQAIQQ 226
Cdd:PRK01130  161 DFALLKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
11-226 4.41e-125

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 352.91  E-value: 4.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  11 ERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITPFLDD 90
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  91 IDALATAGADIIAVDGTNRPRP--VSIKEAVERIHQK-GCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGG-EVPEEP 166
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPdgETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEEtKKPEEP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468907794 167 DYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWFAQAIQQ 226
Cdd:PRK01130  161 DFALLKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
7-227 1.40e-121

Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 442247  Cd Length: 226  Bit Score: 344.39  E-value: 1.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794   7 QNVLERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITP 86
Cdd:COG3010     1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  87 FLDDIDALATAGADIIAVDGTNRPRP--VSIKEAVERIHQK-GCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGGEVP 163
Cdd:COG3010    81 TLEEVDALAEAGADIIALDATRRPRPdgETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468907794 164 -EEPDYQLVKDL-KAAGCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWFAQAIQQA 227
Cdd:COG3010   161 tDGPDLELLKELvAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
35-226 4.84e-120

Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.


Pssm-ID: 427732  Cd Length: 192  Bit Score: 339.03  E-value: 4.84e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  35 VAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITPFLDDIDALATAGADIIAVDGTNRPRPVS 114
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794 115 IKEAVERIHQKGCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGGEVPEEPDYQLVKDLKAAGCFVMGEGRYNTPELAR 194
Cdd:pfam04131  81 IEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAEPDFQLVKTLSEAGCFVIAEGRYNTPELAK 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2468907794 195 SAIEAGADCVTVGSALTRLEHIVSWFAQAIQQ 226
Cdd:pfam04131 161 KAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
7-220 1.47e-116

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 331.46  E-value: 1.47e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794   7 QNVLERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITP 86
Cdd:cd04729     1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  87 FLDDIDALATAGADIIAVDGTNRPRPV--SIKEAVERIHQKG-CLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTG-GEV 162
Cdd:cd04729    81 TIEEVDALAAAGADIIALDATDRPRPDgeTLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEeTAK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468907794 163 PEEPDYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWF 220
Cdd:cd04729   161 TEDPDFELLKELRKAlGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
 
Name Accession Description Interval E-value
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
11-226 4.41e-125

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 352.91  E-value: 4.41e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  11 ERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITPFLDD 90
Cdd:PRK01130    1 EQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIKAIRAVVDVPIIGIIKRDYPDSEVYITPTLKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  91 IDALATAGADIIAVDGTNRPRP--VSIKEAVERIHQK-GCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGG-EVPEEP 166
Cdd:PRK01130   81 VDALAAAGADIIALDATLRPRPdgETLAELVKRIKEYpGQLLMADCSTLEEGLAAQKLGFDFIGTTLSGYTEEtKKPEEP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468907794 167 DYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWFAQAIQQ 226
Cdd:PRK01130  161 DFALLKELLKAvGCPVIAEGRINTPEQAKKALELGAHAVVVGGAITRPEEITKWFVDALKK 221
NanE COG3010
Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];
7-227 1.40e-121

Putative N-acetylmannosamine-6-phosphate epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 442247  Cd Length: 226  Bit Score: 344.39  E-value: 1.40e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794   7 QNVLERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITP 86
Cdd:COG3010     1 NELLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIKKAVDLPIIGIIKRDYPDSDVYITP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  87 FLDDIDALATAGADIIAVDGTNRPRP--VSIKEAVERIHQK-GCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGGEVP 163
Cdd:COG3010    81 TLEEVDALAEAGADIIALDATRRPRPdgETLAELIARIHEEpGALVMADISTLEEALAAAELGADIVGTTLSGYTGETKG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468907794 164 -EEPDYQLVKDL-KAAGCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWFAQAIQQA 227
Cdd:COG3010   161 tDGPDLELLKELvAALGVPVIAEGRIHTPEQAAAALELGAHAVVVGTAITRPELITKRFVDALKKA 226
NanE pfam04131
Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ...
35-226 4.84e-120

Putative N-acetylmannosamine-6-phosphate epimerase; This family represents a putative ManNAc-6-P-to-GlcNAc-6P epimerase in the N-acetylmannosamine (ManNAc) utilization pathway found mainly in pathogenic bacteria.


Pssm-ID: 427732  Cd Length: 192  Bit Score: 339.03  E-value: 4.84e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  35 VAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITPFLDDIDALATAGADIIAVDGTNRPRPVS 114
Cdd:pfam04131   1 VSAMALAAEQAGAVGIRIEGVNNLKATRAVVDVPIIGIVKRDLPDSPVRITPFMKDIDELANAGADIIALDGTSRPRPVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794 115 IKEAVERIHQKGCLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTGGEVPEEPDYQLVKDLKAAGCFVMGEGRYNTPELAR 194
Cdd:pfam04131  81 IEDFIKRIKEKGCLAMADCSTFEEGLNADKLGVDIIGTTLSGYTGGENPAEPDFQLVKTLSEAGCFVIAEGRYNTPELAK 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2468907794 195 SAIEAGADCVTVGSALTRLEHIVSWFAQAIQQ 226
Cdd:pfam04131 161 KAIEIGADAVTVGSAITRLEHITQWFNNAIKS 192
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
7-220 1.47e-116

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 331.46  E-value: 1.47e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794   7 QNVLERIRYGLIASCQPVDNGPMDHPNIVAAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRDLPDSPIRITP 86
Cdd:cd04729     1 MKLLEQLKGGLIVSCQALPGEPLHSPEIMAAMALAAVQGGAVGIRANGVEDIRAIRARVDLPIIGLIKRDYPDSEVYITP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  87 FLDDIDALATAGADIIAVDGTNRPRPV--SIKEAVERIHQKG-CLAMADCSNLEEGLYCQQLGFDIVGSTMSGYTG-GEV 162
Cdd:cd04729    81 TIEEVDALAAAGADIIALDATDRPRPDgeTLAELIKRIHEEYnCLLMADISTLEEALNAAKLGFDIIGTTLSGYTEeTAK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468907794 163 PEEPDYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSALTRLEHIVSWF 220
Cdd:cd04729   161 TEDPDFELLKELRKAlGIPVIAEGRINSPEQAAKALELGADAVVVGSAITRPEHITGWF 219
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
36-208 4.02e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 46.04  E-value: 4.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  36 AAMAQASVIGGAAGLRIEGVDNLKATRPTVSVPIIGIVKRdLPDSPI--------RITPFLDDIDALATAGADIIAVDGT 107
Cdd:cd04722    15 VELAKAAAEAGADAIIVGTRSSDPEEAETDDKEVLKEVAA-ETDLPLgvqlaindAAAAVDIAAAAARAAGADGVEIHGA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794 108 NRPRPVSIKEAVERIHQK--GCLAMADCSNLEEGL--YCQQLGFDIVGSTMSGYTGGEVPEEPDYQLVKDLKAAGCF--V 181
Cdd:cd04722    94 VGYLAREDLELIRELREAvpDVKVVVKLSPTGELAaaAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKvpV 173
                         170       180
                  ....*....|....*....|....*..
gi 2468907794 182 MGEGRYNTPELARSAIEAGADCVTVGS 208
Cdd:cd04722   174 IAGGGINDPEDAAEALALGADGVIVGS 200
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
23-210 1.37e-05

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 44.78  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  23 PVDNGPMDH---PNIVAAMAQASVIG--GAAGLRIEGVDN-LKATRPTVSVPI-IGIVkrdlpdSPIRITPFLDDIDALA 95
Cdd:cd04730     4 PIIQAPMAGvstPELAAAVSNAGGLGfiGAGYLTPEALRAeIRKIRALTDKPFgVNLL------VPSSNPDFEALLEVAL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  96 TAGADIIAVdGTNRPRPVsikeaVERIHQKGCLAMADCSNLEEGLYCQQLGFDIV---GSTMSGYTGGevPEEPDYQLVK 172
Cdd:cd04730    78 EEGVPVVSF-SFGPPAEV-----VERLKAAGIKVIPTVTSVEEARKAEAAGADALvaqGAEAGGHRGT--FDIGTFALVP 149
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2468907794 173 DLKAA-GCFVMGEGRYNTPELARSAIEAGADCVTVGSAL 210
Cdd:cd04730   150 EVRDAvDIPVIAAGGIADGRGIAAALALGADGVQMGTRF 188
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
95-212 6.95e-04

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 40.00  E-value: 6.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468907794  95 ATAGADIIAVDGTNRPrpVSIKEAVERIHQKGCLAMADCSNLEE----GLYCQQLGFDIVG------STMSGYTGGEVPE 164
Cdd:PRK07028   78 AKAGADIVCILGLADD--STIEDAVRAARKYGVRLMADLINVPDpvkrAVELEELGVDYINvhvgidQQMLGKDPLELLK 155
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2468907794 165 EPDYQLVKDLKAAGCFvmgegrynTPELARSAIEAGADCVTVGSALTR 212
Cdd:PRK07028  156 EVSEEVSIPIAVAGGL--------DAETAAKAVAAGADIVIVGGNIIK 195
FadH COG1902
2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family ...
162-210 6.67e-03

2,4-dienoyl-CoA reductase or related NADH-dependent reductase, Old Yellow Enzyme (OYE) family [Energy production and conversion];


Pssm-ID: 441506 [Multi-domain]  Cd Length: 365  Bit Score: 37.07  E-value: 6.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468907794 162 VPEEPDYQLVKDLKAA-GCFVMGEGRYNTPELARSAIEAG-ADCVTVGSAL 210
Cdd:COG1902   270 VPEGYQLPFAARIRKAvGIPVIAVGGITTPEQAEAALASGdADLVALGRPL 320
 
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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