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Conserved domains on  [gi|1370461704|ref|XP_024304715|]
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probable C-mannosyltransferase DPY19L2 isoform X6 [Homo sapiens]

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 ...
1-611 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: 991.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 80
Cdd:cd20179    42 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20179   122 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 240
Cdd:cd20179   202 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 241 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 320
Cdd:cd20179   282 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 321 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 400
Cdd:cd20179   362 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 401 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 480
Cdd:cd20179   442 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 521
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 481 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 560
Cdd:cd20179   522 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 601
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370461704 561 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 611
Cdd:cd20179   602 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 652
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
1-611 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: 991.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 80
Cdd:cd20179    42 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20179   122 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 240
Cdd:cd20179   202 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 241 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 320
Cdd:cd20179   282 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 321 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 400
Cdd:cd20179   362 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 401 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 480
Cdd:cd20179   442 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 521
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 481 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 560
Cdd:cd20179   522 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 601
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370461704 561 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 611
Cdd:cd20179   602 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 652
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-614 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: 772.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLfgletktcwnv 80
Cdd:pfam10034  31 ISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNLYPEVILAILYRIFRGIQNY----------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 trieplnevqscegLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:pfam10034 100 --------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLRENFAL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRT----SSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMIS 236
Cdd:pfam10034 166 PFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVAKIYLSHLIS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 237 VTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLG-VSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSD 315
Cdd:pfam10034 246 LLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLKLLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 316 LIAARI--LRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDI-----SYVLATNIYLRKQLL 388
Cdd:pfam10034 326 FLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKVLQSIyrrlkRYKLSQAPMQESLPL 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 389 E----------HSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQG 458
Cdd:pfam10034 406 EdgrigerpelNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLGASKQLWHFLFKKIFSSAVPTVILASMSYKG 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 459 YANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKS 538
Cdd:pfam10034 486 FPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKP 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 539 AKEVRDKLLELHVNYYVLEEAWCVVRTK-PGCSMLEIWDVED---PSNAANPPLCSVL-LEDARPYFTTVFQNSVYRVLK 613
Cdd:pfam10034 566 AEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPANRKGPRFCHEIkLSNYVPYFTRVFWNRSYHVYK 645

                  .
gi 1370461704 614 V 614
Cdd:pfam10034 646 V 646
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
1-611 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: 991.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 80
Cdd:cd20179    42 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20179   122 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 240
Cdd:cd20179   202 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 241 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 320
Cdd:cd20179   282 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 321 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 400
Cdd:cd20179   362 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQL 441
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 401 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 480
Cdd:cd20179   442 LVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEEL 521
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 481 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 560
Cdd:cd20179   522 LQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAW 601
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370461704 561 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 611
Cdd:cd20179   602 CVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 652
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
1-612 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: 899.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 80
Cdd:cd20178    40 MAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLVINTLKRFNLYPEVVLASWYRIYTGIMDFFGIQTKTCWTV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 TRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20178   120 NRGEGLSPVESCEGLGDPAYFYVAVIFLLNGLMMSLFFIYGTYLSGSRLGGVVTVLCFFFNHGECTRVMWTPPLRESFSY 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 240
Cdd:cd20178   200 PFLVLQMLLVTYILRAPNLGRGSLIALCISNVLFMLPWQFAQFVLLTQIASLFAVYVVGYIDSCKLQKILYAHMISLVVC 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 241 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSDLIAAR 320
Cdd:cd20178   280 FVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVSLWVIQGCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSK 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 321 ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATN-IYLRKQLLEHSELAFHTLQ 399
Cdd:cd20178   360 FTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFAAIARKTIKDLWGVLAKKaTHTRKEQFAHGELVYHALQ 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 400 LLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEE 479
Cdd:cd20178   440 LLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCKVHPQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEE 519
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 480 LLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEA 559
Cdd:cd20178   520 LLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYEDAGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEES 599
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370461704 560 WCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRVL 612
Cdd:cd20178   600 WCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHFTTVFENSVYKVL 652
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
1-611 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: 850.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLFGLETKTCWNV 80
Cdd:cd20177    40 MTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHTINTLKRFNLYPEVILAILYRVFPSIANYFGIPTKQCWQV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 tRIEPLNEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20177   120 -RGEDLPPVESCEGLGEPAYFYIYVVFGLNGLVAGLLFLYGWLLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAY 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLS 240
Cdd:cd20177   199 PFLLLQILLITIYLRSNIGKRFHLLAISISTFLFMLMWQFSQFALLTQILSLFALYVLGYIPSSKVQTIILSHLISLLLA 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 241 FILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQGSAWWCGTIILKFLTSKILGVSD--HIRlsDLIA 318
Cdd:cd20177   279 FVLLFGNEMLLTSLYLSSLLAFLIILYLQLRLKKSFKFKLIIWLLQLILVFLGTLGLKLLLSKLLNVEDdaHIF--KILK 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 319 ARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDISYVLATNIYL------RKQLLEHSE 392
Cdd:cd20177   357 SKFGDYRDFDTRLYTCAAEFDFLSLETFLRLSKTLLLPLYIVVLVVIAFLFLRVRLLTLNDSTLKesvnftDSRLILNPE 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 393 LAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRR-VRFEKVIFGILTVMSIQGYANLRNQWSIIGE 471
Cdd:cd20177   437 IVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLKkIFRLAVLFALLASMSYPGIPNLQEELSILGE 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 472 FNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHV 551
Cdd:cd20177   517 FSNPDTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPHYEDAGLRERTKQVYSMYSRRPAEEVYNILKKLGV 596
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370461704 552 NYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLC-SVLLEDARPYFTTVFQNSVYRV 611
Cdd:cd20177   597 NYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGKPPLCiRLLLEDYVPYFKLVFSNKTYRV 657
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-614 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: 772.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYCTFMGIMNLfgletktcwnv 80
Cdd:pfam10034  31 ISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNLYPEVILAILYRIFRGIQNY----------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 trieplnevqscegLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:pfam10034 100 --------------LGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLRENFAL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRT----SSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMIS 236
Cdd:pfam10034 166 PFFALQMLALTYILKRknisSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVAKIYLSHLIS 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 237 VTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLG-VSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSD 315
Cdd:pfam10034 246 LLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLKLLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFD 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 316 LIAARI--LRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIFKKTVRDI-----SYVLATNIYLRKQLL 388
Cdd:pfam10034 326 FLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKVLQSIyrrlkRYKLSQAPMQESLPL 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 389 E----------HSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKVIFGILTVMSIQG 458
Cdd:pfam10034 406 EdgrigerpelNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLGASKQLWHFLFKKIFSSAVPTVILASMSYKG 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 459 YANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKS 538
Cdd:pfam10034 486 FPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKP 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 539 AKEVRDKLLELHVNYYVLEEAWCVVRTK-PGCSMLEIWDVED---PSNAANPPLCSVL-LEDARPYFTTVFQNSVYRVLK 613
Cdd:pfam10034 566 AEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPANRKGPRFCHEIkLSNYVPYFTRVFWNRSYHVYK 645

                  .
gi 1370461704 614 V 614
Cdd:pfam10034 646 V 646
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
1-613 1.10e-66

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: 230.11  E-value: 1.10e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYctfmgimnlfgletktcwnv 80
Cdd:cd20181    40 ISFRTECGLYYSYYKQMLQAPSIQQGFHGLIYDNKTESMRTINLLQRMNIYQEVFLSVLY-------------------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 tRIEPLNEVQsceglgDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20181   100 -RVLPIQKYL------EPVYFYIYTLFGLQAVYVIALYITSWLLSGTWLSGLLAAVWYITNRIDTTRVEFTIPLRENWAL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILRTSSN---DRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISV 237
Cdd:cd20181   173 PFFAIQIAAITYFLRPNLQplqERLTLLAIFISTFLFSLTWQFNQFMMLIQALVLFTLDCLDMLPTAKVTWLYGIQISGL 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 238 TLSFILMFGNSMYLSSYYSSSLLMTWaIILKRNEIQKLG--VSKLNFWLIQGSAWWCGTIILKFLTSKILGVSDHIRLSD 315
Cdd:cd20181   253 LLVCILQFFNSMILGSLLLSFNLSVL-IVRKLQKNLKTGsfLNRLGKLLLHLALVLCLTLFLNNIIKKILNLKSDEHIFK 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 316 LIAARI-LRYT-DFDTLIYTCAPEFDFMEKATPLRYTKTLLL-PVVMVITCFIFKKTVRDISYVLATNIYLRKQLLEHS- 391
Cdd:cd20181   332 FLKAKFgFGATrDFDANLYLCEEAFGLLPFNTFERLSDTLLFyAYIFVLLLTVIVAAVVAFHNLSDSTNQQSMGKMEKGt 411
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 392 -----ELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASL-ICSRQLFGWLFR--------RVRFEKVIFGILTV--MS 455
Cdd:cd20181   412 vdlkpEVAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFgLCSTELWELLLKsvhlynpkRIRVMRYSVPILTLlyLC 491
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 456 IQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYS 535
Cdd:cd20181   492 YKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYEDKSLRERTRQVYQIYA 571
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 536 RKSAKEVRDKLLELHVNYYVLEEAWCVVRT-KPGCSMLEIWDVE-------------DPSNAANPPLCSVLLEDARPY-- 599
Cdd:cd20181   572 KRSPEEVHALLRSFGTDYVILEDSICYERRhRRGCRLRDLLDIAnghimdgpgendpDLKPADHPRFCEEIKRNLPSYaa 651
                         650
                  ....*....|....*
gi 1370461704 600 -FTTVFQNSVYRVLK 613
Cdd:cd20181   652 yFTRVFQNKTFHVYK 666
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
1-613 1.72e-47

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: 176.95  E-value: 1.72e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704   1 MTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAIKRFHLYPEVIIASWYctfmgimnlfgletktcwnv 80
Cdd:cd20180    40 ITFQGDSAIYYSYYKDMLKAPSFERGVYELTHNNKTVSLKTINAVQQMSLYPELIASVLY-------------------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704  81 trieplnEVQSCEGLGDPACFYVGVIFILNGLMMGLFFMYGAYLSGTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSY 160
Cdd:cd20180   100 -------QATGSNEVIEPVYFYIGIVFGLQGIYVTALFVTSWLMSGTWLAGMLTVAWFIINRVDTTRIEYSIPLRENWAL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 161 PFLVLQMCILTLILR---TSSNDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGYIEPSKFQKIIYMNMISV 237
Cdd:cd20180   173 PYFACQVAALTGYLKsnlNTYAERFCYLLMSASTYTFMMMWEYSHYVLFLQAISLFLLDSFSLEQSDKVYEVYKVYLFSL 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 238 TLSFILMFGNSMYLS-----SYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIqgsawWCGTIILKFLTSKILGVSDHIR 312
Cdd:cd20180   253 FLGYLLQFENPALLVspllsLVAALMLAKCLQLNMKKGPFVAKMIKVLHFYLV-----CTLTITLNFIMKMFVPHKENEH 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 313 LSDLIAARI-LRYT-DFDTLIYTC-----APEFDFMekatpLRYTKTLLLP--VVMVITCFIFKKTV---RDISYVLATN 380
Cdd:cd20180   328 LLKFLEVKFgLNTTkNFTMNWLLCqeslqAPSQDFF-----LRLTQSSLLPfyILVLIICLLSMLQVifrRLSGKPLKET 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 381 IYLRK-QLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASL-ICSRQLFGWLFRRVRFEKVIFGILTVM---- 454
Cdd:cd20180   403 VTLEDgRIGERPEIVYHVIHTILLGSLAMLFEGMKYLWTPYVCMLAAFgVCSPELWMTLFKWLRLRTVHPILLALIlsma 482
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 455 --SIQGYA-------NLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRA 525
Cdd:cd20180   483 vpTIIGFSlwkeffpRLMTELSELQEFYDPDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMVTSLPLYNDDDLLK 562
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370461704 526 RTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCV-VRTKPGCSMLEIWDV----------EDPSNAANPPLCSVLLE 594
Cdd:cd20180   563 RNENIYQIYSKRSAEDIYKILTSYKANYLIIEDAICNeVGPVRGCRVKDLLDIanghvvceegDKYTYSKYGRFCHEIKI 642
                         650       660
                  ....*....|....*....|..
gi 1370461704 595 DARP---YFTTVFQNSVYRVLK 613
Cdd:cd20180   643 NYSPyvnYFTRVYWNRSYFVYK 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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