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Conserved domains on  [gi|755528923|ref|XP_011240859|]
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probable C-mannosyltransferase DPY19L2 isoform X4 [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 ...
1-499 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: 917.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNV 80
Cdd:cd20179  154 MMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNV 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  81 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKI 160
Cdd:cd20179  234 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEI 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 161 QKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKT 240
Cdd:cd20179  314 QKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKT 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 241 LLLPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQR 320
Cdd:cd20179  394 LLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQ 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 321 LFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPI 400
Cdd:cd20179  474 LFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPI 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 401 VNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSIL 480
Cdd:cd20179  554 VNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVL 633
                        490
                 ....*....|....*....
gi 755528923 481 LKDSRPYFTTVFQNSMYRV 499
Cdd:cd20179  634 LEDARPYFTTVFQNSVYRV 652
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
1-499 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: 917.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNV 80
Cdd:cd20179  154 MMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNV 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  81 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKI 160
Cdd:cd20179  234 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEI 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 161 QKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKT 240
Cdd:cd20179  314 QKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKT 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 241 LLLPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQR 320
Cdd:cd20179  394 LLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQ 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 321 LFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPI 400
Cdd:cd20179  474 LFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPI 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 401 VNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSIL 480
Cdd:cd20179  554 VNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVL 633
                        490
                 ....*....|....*....
gi 755528923 481 LKDSRPYFTTVFQNSMYRV 499
Cdd:cd20179  634 LEDARPYFTTVFQNSVYRV 652
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-502 0e+00

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: 622.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923    1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT----STVHKKHYMALC 76
Cdd:pfam10034 118 YVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLS 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   77 FSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQK 156
Cdd:pfam10034 198 ASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  157 KSKIQKLG-GTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEQAT 233
Cdd:pfam10034 278 QPNMKKGRfSFRLLKLLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKET 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  234 PLRYIKTLLLPLILVITYLIFKKIVRDIMCVLY---------------TNTYVRKQLLDNAELIFHTLQLLAFTGLAILI 298
Cdd:pfam10034 358 FLRLTKTLLLPFYILVLLILLIKVLQSIYRRLKryklsqapmqeslplEDGRIGERPELNGEVVYHVLQLLAFGLLALLI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  299 MRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRP 378
Cdd:pfam10034 438 MRLKLLWTPHMCVFASLGASKQLWHFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPK 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  379 DAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTK-PGC 457
Cdd:pfam10034 518 DAVFAGSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGC 597
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 755528923  458 SMLEIWDVED---PSNAANPPLCS-ILLKDSRPYFTTVFQNSMYRVLKI 502
Cdd:pfam10034 598 RMLDIWDVEDghcPANRKGPRFCHeIKLSNYVPYFTRVFWNRSYHVYKV 646
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
1-499 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: 917.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNV 80
Cdd:cd20179  154 MMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPFIALCLSNV 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  81 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKI 160
Cdd:cd20179  234 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEI 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 161 QKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKT 240
Cdd:cd20179  314 QKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKT 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 241 LLLPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQR 320
Cdd:cd20179  394 LLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQ 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 321 LFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPI 400
Cdd:cd20179  474 LFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPI 553
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 401 VNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSIL 480
Cdd:cd20179  554 VNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVL 633
                        490
                 ....*....|....*....
gi 755528923 481 LKDSRPYFTTVFQNSMYRV 499
Cdd:cd20179  634 LEDARPYFTTVFQNSVYRV 652
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
1-500 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: 709.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNV 80
Cdd:cd20178  152 MMSLFFIYGTYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVTYILRAPNLGRGSLIALCISNV 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  81 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKI 160
Cdd:cd20178  232 LFMLPWQFAQFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKF 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 161 QKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKT 240
Cdd:cd20178  312 LKVNKSEVSLWVIQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKT 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 241 LLLPLILVITYLIFKKIVRDIMCVLYTN-TYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQ 319
Cdd:cd20178  392 LLLPVVLVVFAAIARKTIKDLWGVLAKKaTHTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSR 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 320 RLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRP 399
Cdd:cd20178  472 QLFGWLFCKVHPQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRP 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 400 IVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSI 479
Cdd:cd20178  552 IVNHPHYEDAGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTL 631
                        490       500
                 ....*....|....*....|.
gi 755528923 480 LLKDSRPYFTTVFQNSMYRVL 500
Cdd:cd20178  632 MSKDSRPHFTTVFENSVYKVL 652
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
1-499 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: 667.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRTSTVHKKHYMALCFSNV 80
Cdd:cd20177  151 VAGLLFLYGWLLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYLRSNIGKRFHLLAISISTF 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  81 AFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKI 160
Cdd:cd20177  231 LFMLMWQFSQFALLTQILSLFALYVLGYIPSSKVQTIILSHLISLLLAFVLLFGNEMLLTSLYLSSLLAFLIILYLQLRL 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 161 QKLGGTELQFWLIQGCFWWCGTIILKFLTSKICGVSD--HIRlsDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYI 238
Cdd:cd20177  311 KKSFKFKLIIWLLQLILVFLGTLGLKLLLSKLLNVEDdaHIF--KILKSKFGDYRDFDTRLYTCAAEFDFLSLETFLRLS 388
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 239 KTLLLPLILVITYLIFKKIVRDIMCVLYTNTYV------RKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIM 312
Cdd:cd20177  389 KTLLLPLYIVVLVVIAFLFLRVRLLTLNDSTLKesvnftDSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCIL 468
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 313 ASLICSQRLFGWLFCR-IHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMAS 391
Cdd:cd20177  469 ASLLLSKKLLWKLLLKkIFRLAVLFALLASMSYPGIPNLQEELSILGEFSNPDTEELMEWIKDNTPPDAVFAGSMPLMAN 548
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 392 IKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNA 471
Cdd:cd20177  549 VKLSTGRPIVNHPHYEDAGLRERTKQVYSMYSRRPAEEVYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNR 628
                        490       500
                 ....*....|....*....|....*....
gi 755528923 472 ANPPLC-SILLKDSRPYFTTVFQNSMYRV 499
Cdd:cd20177  629 GKPPLCiRLLLEDYVPYFKLVFSNKTYRV 657
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-502 0e+00

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: 622.32  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923    1 MMGLFFIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT----STVHKKHYMALC 76
Cdd:pfam10034 118 YVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLRENFALPFFALQMLALTYILKRknisSASELFCYILLS 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   77 FSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQK 156
Cdd:pfam10034 198 ASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  157 KSKIQKLG-GTELQFWLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEQAT 233
Cdd:pfam10034 278 QPNMKKGRfSFRLLKLLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKET 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  234 PLRYIKTLLLPLILVITYLIFKKIVRDIMCVLY---------------TNTYVRKQLLDNAELIFHTLQLLAFTGLAILI 298
Cdd:pfam10034 358 FLRLTKTLLLPFYILVLLILLIKVLQSIYRRLKryklsqapmqeslplEDGRIGERPELNGEVVYHVLQLLAFGLLALLI 437
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  299 MRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRP 378
Cdd:pfam10034 438 MRLKLLWTPHMCVFASLGASKQLWHFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPK 517
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  379 DAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTK-PGC 457
Cdd:pfam10034 518 DAVFAGSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGC 597
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 755528923  458 SMLEIWDVED---PSNAANPPLCS-ILLKDSRPYFTTVFQNSMYRVLKI 502
Cdd:pfam10034 598 RMLDIWDVEDghcPANRKGPRFCHeIKLSNYVPYFTRVFWNRSYHVYKV 646
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
6-502 1.40e-49

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: 180.42  E-value: 1.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   6 FIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILRT--STVHKKHYMALCF-SNVAF 82
Cdd:cd20181  130 YITSWLLSGTWLSGLLAAVWYITNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPnlQPLQERLTLLAIFiSTFLF 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  83 MLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLlVTWAIMQKKSKIQK 162
Cdd:cd20181  210 SLTWQFNQFMMLIQALVLFTLDCLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFN-LSVLIVRKLQKNLK 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 163 LGGTELQFW--LIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARI-LRYT-DFDTLIYTCAPEFDFMEQATPLRYI 238
Cdd:cd20181  289 TGSFLNRLGklLLHLALVLCLTLFLNNIIKKILNLKSDEHIFKFLKAKFgFGATrDFDANLYLCEEAFGLLPFNTFERLS 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 239 KTLL-------LPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCI 311
Cdd:cd20181  369 DTLLfyayifvLLLTVIVAAVVAFHNLSDSTNQQSMGKMEKGTVDLKPEVAYNLIHTILFGFLALSTMRMKYLWTSHMCV 448
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 312 MASL-ICSQRLFGWLFCRIHFEN----------VVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDA 380
Cdd:cd20181  449 FASFgLCSTELWELLLKSVHLYNpkrirvmrysVPILTLLYLCYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKA 528
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 381 VFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRT-KPGCSM 459
Cdd:cd20181  529 VFAGSMQLLAGVKLCTGRTLTNHPHYEDKSLRERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYERRhRRGCRL 608
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755528923 460 LEIWDVE-------------DPSNAANPPLCSILLKDSRPY---FTTVFQNSMYRVLKI 502
Cdd:cd20181  609 RDLLDIAnghimdgpgendpDLKPADHPRFCEEIKRNLPSYaayFTRVFQNKTFHVYKL 667
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
6-501 4.04e-33

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: 133.43  E-value: 4.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923   6 FIYSTYLSGSQLGGLITVACYFFNHGEATRVMWTPPLRESFSYPFLVLQMYILTIILR---TSTVHKKHYMALCFSNVAF 82
Cdd:cd20180  130 FVTSWLMSGTWLAGMLTVAWFIINRVDTTRIEYSIPLRENWALPYFACQVAALTGYLKsnlNTYAERFCYLLMSASTYTF 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923  83 MLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLS--SYYSSCLLVTWAIMQ---KK 157
Cdd:cd20180  210 MMMWEYSHYVLFLQAISLFLLDSFSLEQSDKVYEVYKVYLFSLFLGYLLQFENPALLVspLLSLVAALMLAKCLQlnmKK 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 158 SKIQKLGGTELQFWLIqgcfwWCGTIILKFLTSKICGVSDHIRLSDLIAARI-LRYT-DFDTLIYTCAPEFDFMEQATPL 235
Cdd:cd20180  290 GPFVAKMIKVLHFYLV-----CTLTITLNFIMKMFVPHKENEHLLKFLEVKFgLNTTkNFTMNWLLCQESLQAPSQDFFL 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 236 RYIKTLLLP---LILVITYLIFKKIVRDIMCVLYTNTYVR---KQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHM 309
Cdd:cd20180  365 RLTQSSLLPfyiLVLIICLLSMLQVIFRRLSGKPLKETVTledGRIGERPEIVYHVIHTILLGSLAMLFEGMKYLWTPYV 444
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 310 CIMASL-ICSQRL----FGWLFCRIHFENVVFGILTMM--SIQG-------CANLHNQWSIMGEFTNLPQEELIHWIKHS 375
Cdd:cd20180  445 CMLAAFgVCSPELwmtlFKWLRLRTVHPILLALILSMAvpTIIGfslwkefFPRLMTELSELQEFYDPDTVELMTWIKRQ 524
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 376 TRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCV-VRTK 454
Cdd:cd20180  525 APVAAVFAGSPQLMGTIKLCTGWMVTSLPLYNDDDLLKRNENIYQIYSKRSAEDIYKILTSYKANYLIIEDAICNeVGPV 604
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755528923 455 PGCSMLEIWDV----------EDPSNAANPPLCSILLKDSRP---YFTTVFQNSMYRVLK 501
Cdd:cd20180  605 RGCRVKDLLDIanghvvceegDKYTYSKYGRFCHEIKINYSPyvnYFTRVYWNRSYFVYK 664
 
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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