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Conserved domains on  [gi|1370461710|ref|XP_024304717|]
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probable C-mannosyltransferase DPY19L2 isoform X10 [Homo sapiens]

Protein Classification

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 ...
103-527 0e+00

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: 703.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 103 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 182
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 183 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 262
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 263 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 342
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 343 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 422
Cdd:cd20179   241 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 423 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 502
Cdd:cd20179   321 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 400
                         410       420
                  ....*....|....*....|....*
gi 1370461710 503 VITCFIFKKTVRDISYVLATNIYLR 527
Cdd:cd20179   401 VITCFIFKKTVRDISYVLATNIYLR 425
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
103-527 0e+00

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: 703.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 103 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 182
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 183 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 262
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 263 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 342
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 343 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 422
Cdd:cd20179   241 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 423 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 502
Cdd:cd20179   321 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 400
                         410       420
                  ....*....|....*....|....*
gi 1370461710 503 VITCFIFKKTVRDISYVLATNIYLR 527
Cdd:cd20179   401 VITCFIFKKTVRDISYVLATNIYLR 425
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
114-520 1.18e-175

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: 511.38  E-value: 1.18e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 114 VFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHL 193
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 194 YPEVIIASWYCTFMGIMNLfgletktcwnvtrieplnevqscegLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLG 273
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNY-------------------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 274 GLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRT----SSNDRRPFIALCLSNVAFMLPWQFAQFILF 349
Cdd:pfam10034 136 GILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 350 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLG-VSKLNFWLI 428
Cdd:pfam10034 216 TQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLKLLL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 429 QGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITC 506
Cdd:pfam10034 296 HGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLL 375
                         410
                  ....*....|....
gi 1370461710 507 FIFKKTVRDISYVL 520
Cdd:pfam10034 376 ILLIKVLQSIYRRL 389
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
103-527 0e+00

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: 703.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 103 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 182
Cdd:cd20179     1 RFSSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 183 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 262
Cdd:cd20179    81 LIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 263 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 342
Cdd:cd20179   161 YGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 343 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 422
Cdd:cd20179   241 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSK 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 423 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 502
Cdd:cd20179   321 LNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 400
                         410       420
                  ....*....|....*....|....*
gi 1370461710 503 VITCFIFKKTVRDISYVLATNIYLR 527
Cdd:cd20179   401 VITCFIFKKTVRDISYVLATNIYLR 425
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
108-521 0e+00

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: 603.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 108 TTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINA 187
Cdd:cd20178     4 VTLLLAALAGVLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLVINT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 188 IKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVTRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYL 267
Cdd:cd20178    84 LKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTVNRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYGTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 268 SGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFI 347
Cdd:cd20178   164 SGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFAQFV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 348 LFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWL 427
Cdd:cd20178   244 LLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVSLWV 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 428 IQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCF 507
Cdd:cd20178   324 IQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFAA 403
                         410
                  ....*....|....
gi 1370461710 508 IFKKTVRDISYVLA 521
Cdd:cd20178   404 IARKTIKDLWGVLA 417
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
105-549 0e+00

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: 583.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 105 SSRTTLGIAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLI 184
Cdd:cd20177     1 KILLGLLLALLVGVLYSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 185 INAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNVtRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYG 264
Cdd:cd20177    81 INTLKRFNLYPEVILAILYRVFPSIANYFGIPTKQCWQV-RGEDLPPVESCEGLGEPAYFYIYVVFGLNGLVAGLLFLYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 265 AYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFA 344
Cdd:cd20177   160 WLLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYLRSNIGKRFHLLAISISTFLFMLMWQFS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 345 QFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLN 424
Cdd:cd20177   240 QFALLTQILSLFALYVLGYIPSSKVQTIILSHLISLLLAFVLLFGNEMLLTSLYLSSLLAFLIILYLQLRLKKSFKFKLI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 425 FWLIQGSAWWCGTIILKFLTSKILGVSD--HIRlsDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVM 502
Cdd:cd20177   320 IWLLQLILVFLGTLGLKLLLSKLLNVEDdaHIF--KILKSKFGDYRDFDTRLYTCAAEFDFLSLETFLRLSKTLLLPLYI 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1370461710 503 VITCFIFKKTVRDISYVLATNIYLRCCLCRCHAYNGKHQAVYTSSHC 549
Cdd:cd20177   398 VVLVVIAFLFLRVRLLTLNDSTLKESVNFTDSRLILNPEIVYNVLQL 444
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
114-520 1.18e-175

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: 511.38  E-value: 1.18e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 114 VFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHL 193
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 194 YPEVIIASWYCTFMGIMNLfgletktcwnvtrieplnevqscegLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLG 273
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNY-------------------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLG 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 274 GLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRT----SSNDRRPFIALCLSNVAFMLPWQFAQFILF 349
Cdd:pfam10034 136 GILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 350 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLG-VSKLNFWLI 428
Cdd:pfam10034 216 TQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLKLLL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 429 QGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITC 506
Cdd:pfam10034 296 HGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLL 375
                         410
                  ....*....|....
gi 1370461710 507 FIFKKTVRDISYVL 520
Cdd:pfam10034 376 ILLIKVLQSIYRRL 389
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
108-504 5.00e-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: 145.75  E-value: 5.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 108 TTLG--IAVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLII 185
Cdd:cd20181     2 TTVGgtVALCIGLLTSVYVATLHENDLWFSNIKEVEREISFRTECGLYYSYYKQMLQAPSIQQGFHGLIYDNKTESMRTI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 186 NAIKRFHLYPEVIIASWYctfmgimnlfgletktcwnvtRIEPLNEVQsceglgDPACFYVGVIFILNGLMMGLFFMYGA 265
Cdd:cd20181    82 NLLQRMNIYQEVFLSVLY---------------------RVLPIQKYL------EPVYFYIYTLFGLQAVYVIALYITSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 266 YLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSN---DRRPFIALCLSNVAFMLPWQ 342
Cdd:cd20181   135 LLSGTWLSGLLAAVWYITNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQplqERLTLLAIFISTFLFSLTWQ 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 343 FAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWaIILKRNEIQKLG--V 420
Cdd:cd20181   215 FNQFMMLIQALVLFTLDCLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFNLSVL-IVRKLQKNLKTGsfL 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 421 SKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARI-LRYT-DFDTLIYTCAPEFDFMEKATPLRYTKTLLL 498
Cdd:cd20181   294 NRLGKLLLHLALVLCLTLFLNNIIKKILNLKSDEHIFKFLKAKFgFGATrDFDANLYLCEEAFGLLPFNTFERLSDTLLF 373

                  ....*.
gi 1370461710 499 PVVMVI 504
Cdd:cd20181   374 YAYIFV 379
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
113-390 1.13e-30

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: 126.88  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 113 AVFVAILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFH 192
Cdd:cd20180     9 AVTSGMMYAVYLSTYHERKFWFSNRQELEREITFQGDSAIYYSYYKDMLKAPSFERGVYELTHNNKTVSLKTINAVQQMS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 193 LYPEVIIASWYctfmgimnlfgletktcwnvtrieplnEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQL 272
Cdd:cd20180    89 LYPELIASVLY---------------------------QATGSNEVIEPVYFYIGIVFGLQGIYVTALFVTSWLMSGTWL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461710 273 GGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILR---TSSNDRRPFIALCLSNVAFMLPWQFAQFILF 349
Cdd:cd20180   142 AGMLTVAWFIINRVDTTRIEYSIPLRENWALPYFACQVAALTGYLKsnlNTYAERFCYLLMSASTYTFMMMWEYSHYVLF 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370461710 350 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGN 390
Cdd:cd20180   222 LQAISLFLLDSFSLEQSDKVYEVYKVYLFSLFLGYLLQFEN 262
 
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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