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Conserved domains on  [gi|1039793541|ref|XP_017168925|]
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probable C-mannosyltransferase DPY19L2 isoform X6 [Mus musculus]

Protein Classification

Dpy19 superfamily-containing protein( domain architecture ID 1903530)

Dpy19 superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Dpy19 super family cl41786
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
118-366 1.48e-169

C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant.


The actual alignment was detected with superfamily member cd20179:

Pssm-ID: 455131  Cd Length: 652  Bit Score: 488.79  E-value: 1.48e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 118 RFSHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 197
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 198 LVINTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFI 277
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 278 YSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQ 357
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240

                  ....*....
gi 1039793541 358 FAQFILFTQ 366
Cdd:cd20179   241 FAQFILFTQ 249
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
118-366 1.48e-169

C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L2 (also called protein Dpy-19 homolog 2) deletion is a major cause of globozoospermia.


Pssm-ID: 439132  Cd Length: 652  Bit Score: 488.79  E-value: 1.48e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 118 RFSHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 197
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 198 LVINTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFI 277
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 278 YSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQ 357
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240

                  ....*....
gi 1039793541 358 FAQFILFTQ 366
Cdd:cd20179   241 FAQFILFTQ 249
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
129-387 7.61e-120

Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.


Pssm-ID: 462945  Cd Length: 646  Bit Score: 361.54  E-value: 7.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 129 IFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRFHL 208
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 209 YPEVVIAYWYRTIIGIMNLfgietktcwnvtrmeplnevqscegLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQLG 288
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNY-------------------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 289 GLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT----STVHKKHYMALCFSNVAFMLPWQFAQFILF 364
Cdd:pfam10034 136 GILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLL 215
                         250       260
                  ....*....|....*....|....*....
gi 1039793541 365 TQPL---FDYSCHVLH---LDSLIISHVC 387
Cdd:pfam10034 216 TQILslfLLDSLGLVPskkVAKIYLSHLI 244
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
118-366 1.48e-169

C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L2 (also called protein Dpy-19 homolog 2) deletion is a major cause of globozoospermia.


Pssm-ID: 439132  Cd Length: 652  Bit Score: 488.79  E-value: 1.48e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 118 RFSHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 197
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 198 LVINTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFI 277
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 278 YSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQ 357
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240

                  ....*....
gi 1039793541 358 FAQFILFTQ 366
Cdd:cd20179   241 FAQFILFTQ 249
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
120-387 1.17e-143

C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant.


Pssm-ID: 439130  Cd Length: 657  Bit Score: 422.83  E-value: 1.17e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 120 SHRTLFGLAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLV 199
Cdd:cd20177     1 KILLGLLLALLVGVLYSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 200 INTVKRFHLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVtRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFIYS 279
Cdd:cd20177    81 INTLKRFNLYPEVILAILYRVFPSIANYFGIPTKQCWQV-RGEDLPPVESCEGLGEPAYFYIYVVFGLNGLVAGLLFLYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 280 TYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQFA 359
Cdd:cd20177   160 WLLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYLRSNIGKRFHLLAISISTFLFMLMWQFS 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1039793541 360 QFILFTQPLFDYSCHVLHL------DSLIISHVC 387
Cdd:cd20177   240 QFALLTQILSLFALYVLGYipsskvQTIILSHLI 273
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
127-366 1.15e-141

C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. Dpy19L1 (also called protein Dpy-19 homolog 1) regulates neurite extension during development.


Pssm-ID: 439131  Cd Length: 652  Bit Score: 417.71  E-value: 1.15e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 127 LAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRF 206
Cdd:cd20178     8 LAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLVINTLKRF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 207 HLYPEVVIAYWYRTIIGIMNLFGIETKTCWNVTRMEPLNEVQSCEGLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQ 286
Cdd:cd20178    88 NLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYGTYLSGSR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 287 LGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNVAFMLPWQFAQFILFTQ 366
Cdd:cd20178   168 LGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFAQFVLLTQ 247
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
129-387 7.61e-120

Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain family that is required to orient the neuroblast cells, QR and QL accurately on the anterior-posterior axis: QL and QR are born in the same anterior-posterior position, but polarise and migrate left-right asymmetrically, QL migrating towards the posterior and QR migrating towards the anterior. It is also required, with unc-40, to express mab-5 correctly in the Q cell descendants. The Dpy-19 protein derives from the C. elegans DUMPY mutant, Swiss:P34413.


Pssm-ID: 462945  Cd Length: 646  Bit Score: 361.54  E-value: 7.61e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 129 IFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRFHL 208
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 209 YPEVVIAYWYRTIIGIMNLfgietktcwnvtrmeplnevqscegLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQLG 288
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNY-------------------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 289 GLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT----STVHKKHYMALCFSNVAFMLPWQFAQFILF 364
Cdd:pfam10034 136 GILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLL 215
                         250       260
                  ....*....|....*....|....*....
gi 1039793541 365 TQPL---FDYSCHVLH---LDSLIISHVC 387
Cdd:pfam10034 216 TQILslfLLDSLGLVPskkVAKIYLSHLI 244
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
127-368 4.95e-37

C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. In humans Dpy19L3 (also called protein Dpy-19 homolog 3) is a C-mannosyltransferase of R-spondin.


Pssm-ID: 439134  Cd Length: 667  Bit Score: 142.28  E-value: 4.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 127 LAIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRF 206
Cdd:cd20181     8 VALCIGLLTSVYVATLHENDLWFSNIKEVEREISFRTECGLYYSYYKQMLQAPSIQQGFHGLIYDNKTESMRTINLLQRM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 207 HLYPEVVIAYWYRtIIGIMNLFgietktcwnvtrmeplnevqsceglgDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQ 286
Cdd:cd20181    88 NIYQEVFLSVLYR-VLPIQKYL--------------------------EPVYFYIYTLFGLQAVYVIALYITSWLLSGTW 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 287 LGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT--STVHKKHYMALCF-SNVAFMLPWQFAQFIL 363
Cdd:cd20181   141 LSGLLAAVWYITNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPnlQPLQERLTLLAIFiSTFLFSLTWQFNQFMM 220

                  ....*
gi 1039793541 364 FTQPL 368
Cdd:cd20181   221 LIQAL 225
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
128-368 6.40e-31

C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are C-mannosyltransferases that mediate C-mannosylation of tryptophan residues on target proteins. C-mannosylation is the attachment of alpha-mannose to the indole C2 carbon of the first tryptophan residue in the consensus amino acid sequence Trp-Xaa-Xaa-Trp/Cys through a C-C bond. This reaction takes place in the endoplasmic reticulum (ER) lumen. Dpy19 is a transmembrane domain family whose name is derived from the Caenorhabditis elegans Dumpy mutant. The function of Dpy19L4 (also called protein Dpy-19 homolog 4) is unknown.


Pssm-ID: 439133  Cd Length: 664  Bit Score: 124.57  E-value: 6.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 128 AIFVGILHWLHLITLFENDHHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLVINTVKRFH 207
Cdd:cd20180     9 AVTSGMMYAVYLSTYHERKFWFSNRQELEREITFQGDSAIYYSYYKDMLKAPSFERGVYELTHNNKTVSLKTINAVQQMS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 208 LYPEVVIAYWYRtiigimnlfgietktcwnvtrmeplneVQSCEGLGDPACFYIGVIFILNGLMMGLFFIYSTYLSGSQL 287
Cdd:cd20180    89 LYPELIASVLYQ---------------------------ATGSNEVIEPVYFYIGIVFGLQGIYVTALFVTSWLMSGTWL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039793541 288 GGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILR---TSTVHKKHYMALCFSNVAFMLPWQFAQFILF 364
Cdd:cd20180   142 AGMLTVAWFIINRVDTTRIEYSIPLRENWALPYFACQVAALTGYLKsnlNTYAERFCYLLMSASTYTFMMMWEYSHYVLF 221

                  ....
gi 1039793541 365 TQPL 368
Cdd:cd20180   222 LQAI 225
 
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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