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Conserved domains on  [gi|578834024|ref|XP_006723108|]
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protein C-mannosyl-transferase DPY19L3 isoform X5 [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 ...
1-516 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 cd20181:

Pssm-ID: 455131  Cd Length: 667  Bit Score: 964.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   1 MSQIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLD 80
Cdd:cd20181  152 TNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLQERLTLLAIFISTFLFSLTWQFNQFMMLIQALVLFTLD 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  81 SLDMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTL 160
Cdd:cd20181  232 CLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFNLSVLIVRKLQKNLKTGSFLNRLGKLLLHLALVLCLTL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 161 FLNNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVA 240
Cdd:cd20181  312 FLNNIIKKILNLKSDEHIFKFLKAKFGFGATRDFDANLYLCEEAFGLLPFNTFERLSDTLLFYAYIFVLLLTVIVAAVVA 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 241 FHNLSDSTNQQSVGKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSVHLYN 320
Cdd:cd20181  392 FHNLSDSTNQQSMGKMEKGTVDLKPEVAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSTELWELLLKSVHLYN 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 321 PKRICIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 400
Cdd:cd20181  472 PKRIRVMRYSVPILTLLYLCYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 401 PHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHMMDGPGENDPDLK 480
Cdd:cd20181  552 PHYEDKSLRERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHIMDGPGENDPDLK 631
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 578834024 481 PADHPRFCEEIKRNLPPYVAYFTRVFQNKTFHVYKL 516
Cdd:cd20181  632 PADHPRFCEEIKRNLPSYAAYFTRVFQNKTFHVYKL 667
 
Name Accession Description Interval E-value
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
1-516 0e+00

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: 964.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   1 MSQIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLD 80
Cdd:cd20181  152 TNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLQERLTLLAIFISTFLFSLTWQFNQFMMLIQALVLFTLD 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  81 SLDMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTL 160
Cdd:cd20181  232 CLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFNLSVLIVRKLQKNLKTGSFLNRLGKLLLHLALVLCLTL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 161 FLNNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVA 240
Cdd:cd20181  312 FLNNIIKKILNLKSDEHIFKFLKAKFGFGATRDFDANLYLCEEAFGLLPFNTFERLSDTLLFYAYIFVLLLTVIVAAVVA 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 241 FHNLSDSTNQQSVGKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSVHLYN 320
Cdd:cd20181  392 FHNLSDSTNQQSMGKMEKGTVDLKPEVAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSTELWELLLKSVHLYN 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 321 PKRICIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 400
Cdd:cd20181  472 PKRIRVMRYSVPILTLLYLCYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 401 PHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHMMDGPGENDPDLK 480
Cdd:cd20181  552 PHYEDKSLRERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHIMDGPGENDPDLK 631
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 578834024 481 PADHPRFCEEIKRNLPPYVAYFTRVFQNKTFHVYKL 516
Cdd:cd20181  632 PADHPRFCEEIKRNLPSYAAYFTRVFQNKTFHVYKL 667
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
4-516 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: 630.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024    4 IDTTRVEFTIPLRENWALPFFAIQIAAITYFLRP-NLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSL 82
Cdd:pfam10034 148 GETTRVEWTPPLRENFALPFFALQMLALTYILKRkNISSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   83 DMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTLFL 162
Cdd:pfam10034 228 GLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRFSFRLLKLLLHGLLVLFGTLTL 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  163 NNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVAFH 242
Cdd:pfam10034 308 KLLIKKLLNVEDDAHIFDFLKAKFGLNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKVLQSIYR 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  243 NL----SDSTNQQSVGKMEKGTVDLKPET----AYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGlCSPEIWELLLK 314
Cdd:pfam10034 388 RLkrykLSQAPMQESLPLEDGRIGERPELngevVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLG-ASKQLWHFLFK 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  315 svhlynpkriCIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTG 394
Cdd:pfam10034 467 ----------KIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTG 536
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  395 RTLTNHPHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHmmdgpge 474
Cdd:pfam10034 537 RPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRRRGCRMLDIWDVEDGH------- 609
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 578834024  475 ndpDLKPADHPRFCEEIKrnLPPYVAYFTRVFQNKTFHVYKL 516
Cdd:pfam10034 610 ---CPANRKGPRFCHEIK--LSNYVPYFTRVFWNRSYHVYKV 646
 
Name Accession Description Interval E-value
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
1-516 0e+00

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: 964.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   1 MSQIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLD 80
Cdd:cd20181  152 TNRIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLQERLTLLAIFISTFLFSLTWQFNQFMMLIQALVLFTLD 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  81 SLDMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTL 160
Cdd:cd20181  232 CLDMLPTAKVTWLYGIQISGLLLVCILQFFNSMILGSLLLSFNLSVLIVRKLQKNLKTGSFLNRLGKLLLHLALVLCLTL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 161 FLNNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVA 240
Cdd:cd20181  312 FLNNIIKKILNLKSDEHIFKFLKAKFGFGATRDFDANLYLCEEAFGLLPFNTFERLSDTLLFYAYIFVLLLTVIVAAVVA 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 241 FHNLSDSTNQQSVGKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSVHLYN 320
Cdd:cd20181  392 FHNLSDSTNQQSMGKMEKGTVDLKPEVAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSTELWELLLKSVHLYN 471
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 321 PKRICIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 400
Cdd:cd20181  472 PKRIRVMRYSVPILTLLYLCYKFWPGLMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNH 551
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 401 PHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHMMDGPGENDPDLK 480
Cdd:cd20181  552 PHYEDKSLRERTRQVYQIYAKRSPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHIMDGPGENDPDLK 631
                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 578834024 481 PADHPRFCEEIKRNLPPYVAYFTRVFQNKTFHVYKL 516
Cdd:cd20181  632 PADHPRFCEEIKRNLPSYAAYFTRVFQNKTFHVYKL 667
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
4-516 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: 630.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024    4 IDTTRVEFTIPLRENWALPFFAIQIAAITYFLRP-NLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSL 82
Cdd:pfam10034 148 GETTRVEWTPPLRENFALPFFALQMLALTYILKRkNISSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   83 DMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLGKLLLHLFMVLCLTLFL 162
Cdd:pfam10034 228 GLVPSKKVAKIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQPNMKKGRFSFRLLKLLLHGLLVLFGTLTL 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  163 NNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVAFH 242
Cdd:pfam10034 308 KLLIKKLLNVEDDAHIFDFLKAKFGLNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLLPFYILVLLILLIKVLQSIYR 387
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  243 NL----SDSTNQQSVGKMEKGTVDLKPET----AYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGlCSPEIWELLLK 314
Cdd:pfam10034 388 RLkrykLSQAPMQESLPLEDGRIGERPELngevVYHVLQLLAFGLLALLIMRLKLLWTPHMCVFASLG-ASKQLWHFLFK 466
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  315 svhlynpkriCIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTG 394
Cdd:pfam10034 467 ----------KIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDTEELMEWIKSNTPKDAVFAGSMPLMATVKLSTG 536
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  395 RTLTNHPHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHmmdgpge 474
Cdd:pfam10034 537 RPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRRRGCRMLDIWDVEDGH------- 609
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 578834024  475 ndpDLKPADHPRFCEEIKrnLPPYVAYFTRVFQNKTFHVYKL 516
Cdd:pfam10034 610 ---CPANRKGPRFCHEIK--LSNYVPYFTRVFWNRSYHVYKV 646
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
5-513 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: 580.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   5 DTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLqplSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSLDM 84
Cdd:cd20177  182 EATRVQWTPPLRESFAYPFLLLQILLITIYLRSNI---GKRFHLLAISISTFLFMLMWQFSQFALLTQILSLFALYVLGY 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  85 LPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTgSFLNRLGKLLLHLFMVLCLTLFLNN 164
Cdd:cd20177  259 IPSSKVQTIILSHLISLLLAFVLLFGNEMLLTSLYLSSLLAFLIILYLQLRLKK-SFKFKLIIWLLQLILVFLGTLGLKL 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 165 IIKKILNLKSDEHIFKFLKAKFGLGatRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVAFHNL 244
Cdd:cd20177  338 LLSKLLNVEDDAHIFKILKSKFGDY--RDFDTRLYTCAAEFDFLSLETFLRLSKTLLLPLYIVVLVVIAFLFLRVRLLTL 415
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 245 SDSTNQQSVgKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSvhlynpkri 324
Cdd:cd20177  416 NDSTLKESV-NFTDSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLKK--------- 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 325 cIMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYE 404
Cdd:cd20177  486 -IFRLAVLFALLASMSYPGIPNLQEELSILGEFSNPDTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPHYE 564
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 405 DSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYErRHRRGCRLRDLLDIANGHMMDGPGendpdlkpadh 484
Cdd:cd20177  565 DAGLRERTKQVYSMYSRRPAEEVYNILKKLGVNYIILEDSICLS-RRRDGCSLPDIWDLEDPHNRGKPP----------- 632
                        490       500
                 ....*....|....*....|....*....
gi 578834024 485 prfcEEIKRNLPPYVAYFTRVFQNKTFHV 513
Cdd:cd20177  633 ----LCIRLLLEDYVPYFKLVFSNKTYRV 657
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
1-515 1.13e-145

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: 433.50  E-value: 1.13e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   1 MSQIDTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLD 80
Cdd:cd20180  152 INRVDTTRIEYSIPLRENWALPYFACQVAALTGYLKSNLNTYAERFCYLLMSASTYTFMMMWEYSHYVLFLQAISLFLLD 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  81 SLDMLPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLKTGSFLNRLgKLLLHLFMVLCLTL 160
Cdd:cd20180  232 SFSLEQSDKVYEVYKVYLFSLFLGYLLQFENPALLVSPLLSLVAALMLAKCLQLNMKKGPFVAKM-IKVLHFYLVCTLTI 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 161 FLNNIIKKILNLKSDEHIFKFLKAKFGLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVA 240
Cdd:cd20180  311 TLNFIMKMFVPHKENEHLLKFLEVKFGLNTTKNFTMNWLLCQESLQAPSQDFFLRLTQSSLLPFYILVLIICLLSMLQVI 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 241 FHNLSDSTNQQSVgKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFGLCSPEIWELLLKSVHLYN 320
Cdd:cd20180  391 FRRLSGKPLKETV-TLEDGRIGERPEIVYHVIHTILLGSLAMLFEGMKYLWTPYVCMLAAFGVCSPELWMTLFKWLRLRT 469
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 321 PKRIC---IMRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTL 397
Cdd:cd20180  470 VHPILlalILSMAVPTIIGFSLWKEFFPRLMTELSELQEFYDPDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMV 549
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 398 TNHPHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHRRGCRLRDLLDIANGHMMDGPGENdp 477
Cdd:cd20180  550 TSLPLYNDDDLLKRNENIYQIYSKRSAEDIYKILTSYKANYLIIEDAICNEVGPVRGCRVKDLLDIANGHVVCEEGDK-- 627
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 578834024 478 dLKPADHPRFCEEIKRNLPPYVAYFTRVFQNKTFHVYK 515
Cdd:cd20180  628 -YTYSKYGRFCHEIKINYSPYVNYFTRVYWNRSYFVYK 664
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
5-513 2.43e-59

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: 207.39  E-value: 2.43e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   5 DTTRVEFTIPLRENWALPFFAIQIAAITYFLRpnlQPLSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSLDM 84
Cdd:cd20178  183 ECTRVMWTPPLRESFSYPFLVLQMLLVTYILR---APNLGRGSLIALCISNVLFMLPWQFAQFVLLTQIASLFAVYVVGY 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  85 LPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIARKLQKNLkTGSFLNRLGKLLLHLFMVLCLTLFLNN 164
Cdd:cd20178  260 IDSCKLQKILYAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRPKF-LKVNKSEVSLWVIQGCAWLFGTVILKY 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 165 IIKKILNLKSDEHIFKFLKAKFGlgATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLFYAYIFVLSITVIVAFVVAFHNL 244
Cdd:cd20178  339 LTSKVFGIADDAHIGNLLKSKFT--SYKDFDTLMYTCAAEFDFMEKETPLRYTKTLLLPVVLVVFAAIARKTIKDLWGVL 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 245 SDSTNQQSVGKMEKGtvdlkpETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFgLCSPEIWELLLKSVHlynpkri 324
Cdd:cd20178  417 AKKATHTRKEQFAHG------ELVYHALQLLAYAVLAILIMRLKLFLTPHMCVMASL-VCSRQLFGWLFCKVH------- 482
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 325 cimRYSVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYE 404
Cdd:cd20178  483 ---PQAVVFAILAAMAIQGSANLQTQWNIIGEFSNLPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYE 559
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 405 DSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYERRHrrgcrlrdlldianghmmdgPGENDPDLKPADH 484
Cdd:cd20178  560 DAGLRARTKIVYSMYSRKPAEEVKRELMKLGVNYYILEESWCVRRSK--------------------PGCSMPEIWDVED 619
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 578834024 485 PR------FCEEIKRNLPPyvaYFTRVFQNKTFHV 513
Cdd:cd20178  620 PDnagktpLCTLMSKDSRP---HFTTVFENSVYKV 651
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
5-513 6.84e-38

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: 147.50  E-value: 6.84e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024   5 DTTRVEFTIPLRENWALPFFAIQIAAITYFLRPNLqplSERLTLLAIFISTFLFSLTWQFNQFMMLMQALVLFTLDSLDM 84
Cdd:cd20179  185 EATRVMWTPPLRESFSYPFLVLQMCILTLILRTSS---NDRRPFIALCLSNVAFMLPWQFAQFILFTQIASLFPMYVVGY 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024  85 LPAVKATWLYGIQITSLLLVCILQFFNSMILGSLLISFNLSVFIArkLQKNLKtgsfLNRLGKLLLHLFMV-----LCLT 159
Cdd:cd20179  262 IEPSKFQKIIYMNMISVTLSFILMFGNSMYLSSYYSSSLLMTWAI--ILKRNE----IQKLGVSKLNFWLIqgsawWCGT 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 160 LFLNNIIKKILNLKSDEHIFKFLKAKfgLGATRDFDANLYLCEEAFGLLPFNTFGRLSDTLLfyayifvLSITVIVAFVV 239
Cdd:cd20179  336 IILKFLTSKILGVSDHIRLSDLIAAR--ILRYTDFDTLIYTCAPEFDFMEKATPLRYTKTLL-------LPVVMVITCFI 406
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 240 AFHNLSDSTNQQSVGKMEKGTVDLKPETAYNLIHTILFGFLALSTMRMKYLWTSHMCVFASFgLCSPEIWELLLKSVHLY 319
Cdd:cd20179  407 FKKTVRDISYVLATNIYLRKQLLEHSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASL-ICSRQLFGWLFRRVRFE 485
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 320 NpkricimrysVPILILLYLCYKFWPGMMDELSELREFYDPDTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTN 399
Cdd:cd20179  486 K----------VIFGILTVMSIQGYANLRNQWSIIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVN 555
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578834024 400 HPHYEDSSLRERTRAVYQIYAKRAPEEVHALLRSFGTDYVILEDSICYeRRHRRGCRLRDLLDIAnghmmdgpgendpDL 479
Cdd:cd20179  556 HPHYEDADLRARTKIVYSTYSRKSAKEVRDKLLELHVNYYVLEEAWCV-VRTKPGCSMLEIWDVE-------------DP 621
                        490       500       510
                 ....*....|....*....|....*....|....
gi 578834024 480 KPADHPRFCEEIKRNLPPyvaYFTRVFQNKTFHV 513
Cdd:cd20179  622 SNAANPPLCSVLLEDARP---YFTTVFQNSVYRV 652
 
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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