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Conserved domains on  [gi|1720431950|ref|XP_030100281|]
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probable C-mannosyltransferase DPY19L2 isoform X5 [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 ...
4-408 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: 743.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   4 TWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQ 83
Cdd:cd20179   248 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQ 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  84 GCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIF 163
Cdd:cd20179   328 GSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIF 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 164 KKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENV 243
Cdd:cd20179   408 KKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKV 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 244 VFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRAR 323
Cdd:cd20179   488 IFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRAR 567
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 324 TKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQN 403
Cdd:cd20179   568 TKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQN 647

                  ....*
gi 1720431950 404 SMYRV 408
Cdd:cd20179   648 SVYRV 652
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
4-408 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: 743.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   4 TWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQ 83
Cdd:cd20179   248 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQ 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  84 GCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIF 163
Cdd:cd20179   328 GSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIF 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 164 KKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENV 243
Cdd:cd20179   408 KKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKV 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 244 VFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRAR 323
Cdd:cd20179   488 IFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRAR 567
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 324 TKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQN 403
Cdd:cd20179   568 TKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQN 647

                  ....*
gi 1720431950 404 SMYRV 408
Cdd:cd20179   648 SVYRV 652
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-411 2.21e-162

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: 471.32  E-value: 2.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   1 MSSTWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLG-GTELQF 79
Cdd:pfam10034 213 VLLTQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLK 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  80 WLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILV 157
Cdd:pfam10034 293 LLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYIL 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 158 ITYLIFKKIVRDIMCVLYT------NTYVRKQLLD---------NAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMA 222
Cdd:pfam10034 373 VLLILLIKVLQSIYRRLKRyklsqaPMQESLPLEDgrigerpelNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFA 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 223 SLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIK 302
Cdd:pfam10034 453 SLGASKQLWHFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVK 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 303 LSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTK-PGCSMLEIWDVED---PS 378
Cdd:pfam10034 533 LSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPA 612
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1720431950 379 NAANPPLCS-ILLKDSRPYFTTVFQNSMYRVLKI 411
Cdd:pfam10034 613 NRKGPRFCHeIKLSNYVPYFTRVFWNRSYHVYKV 646
 
Name Accession Description Interval E-value
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
4-408 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: 743.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   4 TWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQ 83
Cdd:cd20179   248 TQIASLFPMYVVGYIEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAIILKRNEIQKLGVSKLNFWLIQ 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  84 GCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIF 163
Cdd:cd20179   328 GSAWWCGTIILKFLTSKILGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLLLPVVMVITCFIF 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 164 KKIVRDIMCVLYTNTYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFENV 243
Cdd:cd20179   408 KKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLFRRVRFEKV 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 244 VFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRAR 323
Cdd:cd20179   488 IFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRAR 567
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 324 TKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQN 403
Cdd:cd20179   568 TKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQN 647

                  ....*
gi 1720431950 404 SMYRV 408
Cdd:cd20179   648 SVYRV 652
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
4-409 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: 556.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   4 TWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQ 83
Cdd:cd20178   246 TQIASLFAVYVVGYIDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKFLKVNKSEVSLWVIQ 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  84 GCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYLIF 163
Cdd:cd20178   326 GCAWLFGTVILKYLTSKVFGIADDAHIGNLLKSKFTSYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFAAIA 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 164 KKIVRDIMCVLYTN-TYVRKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLFCRIHFEN 242
Cdd:cd20178   406 RKTIKDLWGVLAKKaTHTRKEQFAHGELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQLFGWLFCKVHPQA 485
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 243 VVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRA 322
Cdd:cd20178   486 VVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYEDAGLRA 565
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 323 RTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSILLKDSRPYFTTVFQ 402
Cdd:cd20178   566 RTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHFTTVFE 645

                  ....*..
gi 1720431950 403 NSMYRVL 409
Cdd:cd20178   646 NSVYKVL 652
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
4-408 1.80e-178

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: 512.58  E-value: 1.80e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   4 TWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLGGTELQFWLIQ 83
Cdd:cd20177   245 TQILSLFALYVLGYIPSSKVQTIILSHLISLLLAFVLLFGNEMLLTSLYLSSLLAFLIILYLQLRLKKSFKFKLIIWLLQ 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  84 GCFWWCGTIILKFLTSKICGVSD--HIRlsDLIAARILRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILVITYL 161
Cdd:cd20177   325 LILVFLGTLGLKLLLSKLLNVEDdaHIF--KILKSKFGDYRDFDTRLYTCAAEFDFLSLETFLRLSKTLLLPLYIVVLVV 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 162 IFKKIVRDIMCVLYTNTYV------RKQLLDNAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMASLICSQRLFGWLF 235
Cdd:cd20177   403 IAFLFLRVRLLTLNDSTLKesvnftDSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLL 482
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 236 CR-IHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPH 314
Cdd:cd20177   483 LKkIFRLAVLFALLASMSYPGIPNLQEELSILGEFSNPDTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPH 562
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 315 YEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLC-SILLKDS 393
Cdd:cd20177   563 YEDAGLRERTKQVYSMYSRRPAEEVYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGKPPLCiRLLLEDY 642
                         410
                  ....*....|....*
gi 1720431950 394 RPYFTTVFQNSMYRV 408
Cdd:cd20177   643 VPYFKLVFSNKTYRV 657
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
1-411 2.21e-162

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: 471.32  E-value: 2.21e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950   1 MSSTWIASLFPMYVVGYIEPSKFQKIIYVNMSSVALCFILMFGNSMYLSSYYSSCLLVTWAIMQKKSKIQKLG-GTELQF 79
Cdd:pfam10034 213 VLLTQILSLFLLDSLGLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRfSFRLLK 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950  80 WLIQGCFWWCGTIILKFLTSKICGVSDHIRLSDLIAARI--LRYTDFDTLIYTCAPEFDFMEQATPLRYIKTLLLPLILV 157
Cdd:pfam10034 293 LLLHGLLVLFGTLTLKLLIKKLLNVEDDAHIFDFLKAKFglNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYIL 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 158 ITYLIFKKIVRDIMCVLYT------NTYVRKQLLD---------NAELIFHTLQLLAFTGLAILIMRLKLFLTPHMCIMA 222
Cdd:pfam10034 373 VLLILLIKVLQSIYRRLKRyklsqaPMQESLPLEDgrigerpelNGEVVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFA 452
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 223 SLICSQRLFGWLFCRIHFENVVFGILTMMSIQGCANLHNQWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIK 302
Cdd:pfam10034 453 SLGASKQLWHFLFKKIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVK 532
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 303 LSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLLKLHVNYYVLEEAWCVVRTK-PGCSMLEIWDVED---PS 378
Cdd:pfam10034 533 LSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDIWDVEDghcPA 612
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1720431950 379 NAANPPLCS-ILLKDSRPYFTTVFQNSMYRVLKI 411
Cdd:pfam10034 613 NRKGPRFCHeIKLSNYVPYFTRVFWNRSYHVYKV 646
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
123-411 6.36e-32

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: 128.03  E-value: 6.36e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 123 DFDTLIYTCAPEFDFMEQATPLRYIKTLL-------LPLILVITYLIFKKIVRDIMCVLYTNTYVRKQLLDNAELIFHTL 195
Cdd:cd20181   344 DFDANLYLCEEAFGLLPFNTFERLSDTLLfyayifvLLLTVIVAAVVAFHNLSDSTNQQSMGKMEKGTVDLKPEVAYNLI 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 196 QLLAFTGLAILIMRLKLFLTPHMCIMASL-ICSQRLFGWLFCRIHFEN----------VVFGILTMMSIQGCANLHNQWS 264
Cdd:cd20181   424 HTILFGFLALSTMRMKYLWTSHMCVFASFgLCSTELWELLLKSVHLYNpkrirvmrysVPILTLLYLCYKFWPGLMDELS 503
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 265 IMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRNNLL 344
Cdd:cd20181   504 ELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYEDKSLRERTRQVYQIYAKRSPEEVHALLR 583
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 345 KLHVNYYVLEEAWCVVRT-KPGCSMLEIWDVE-------------DPSNAANPPLCSILLKDSRPY---FTTVFQNSMYR 407
Cdd:cd20181   584 SFGTDYVILEDSICYERRhRRGCRLRDLLDIAnghimdgpgendpDLKPADHPRFCEEIKRNLPSYaayFTRVFQNKTFH 663

                  ....
gi 1720431950 408 VLKI 411
Cdd:cd20181   664 VYKL 667
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
122-410 8.54e-19

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: 88.74  E-value: 8.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 122 TDFDTLIYTCAPEFDFMEQATPLRYIKTLLLP---LILVITYLIFKKIVRDIMCVLYTNTYVR---KQLLDNAELIFHTL 195
Cdd:cd20180   342 KNFTMNWLLCQESLQAPSQDFFLRLTQSSLLPfyiLVLIICLLSMLQVIFRRLSGKPLKETVTledGRIGERPEIVYHVI 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 196 QLLAFTGLAILIMRLKLFLTPHMCIMASL-ICSQRL----FGWLFCRIHFENVVFGILTMM--SIQG-------CANLHN 261
Cdd:cd20180   422 HTILLGSLAMLFEGMKYLWTPYVCMLAAFgVCSPELwmtlFKWLRLRTVHPILLALILSMAvpTIIGfslwkefFPRLMT 501
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 262 QWSIMGEFTNLPQEELIHWIKHSTRPDAVFAGAMPTMASIKLSTLRPIVNHPHYEDADLRARTKIVYSVYSRKSAVEVRN 341
Cdd:cd20180   502 ELSELQEFYDPDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMVTSLPLYNDDDLLKRNENIYQIYSKRSAEDIYK 581
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720431950 342 NLLKLHVNYYVLEEAWCV-VRTKPGCSMLEIWDV----------EDPSNAANPPLCSILLKDSRP---YFTTVFQNSMYR 407
Cdd:cd20180   582 ILTSYKANYLIIEDAICNeVGPVRGCRVKDLLDIanghvvceegDKYTYSKYGRFCHEIKINYSPyvnYFTRVYWNRSYF 661

                  ...
gi 1720431950 408 VLK 410
Cdd:cd20180   662 VYK 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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