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Conserved domains on  [gi|20129045|ref|NP_573317|]
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uncharacterized protein Dmel_CG6659, isoform A [Drosophila melanogaster]

Protein Classification

C-mannosyltransferase dpy-19 family protein( domain architecture ID 10562139)

C-mannosyltransferase dpy-19 family protein similar to Caenorhabditis elegans C-mannosyltransferase dpy-19 (dumpy-19) that mediates C-mannosylation of tryptophan residues on target proteins such as unc-5 and mig-21

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
17-853 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: 689.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    17 CGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYV 96
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    97 LPELVTAYFFHVVRSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKIYERPLAR 176
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNYLGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   177 ENFAFPFIFLQMFYLCICIGRIihRQRHTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTALVNaf 256
Cdd:pfam10034 161 ENFALPFFALQMLALTYILKRK--NISSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVA-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   257 vlDYSLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRqlRHVRSRRlghaqdllngdlFSLKFLMLTLLLASS 336
Cdd:pfam10034 237 --KIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQ--PNMKKGR------------FSFRLLKLLLHGLLV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   337 VQTTLIELFNRAGVVSVTEGDqqHFFDI-CAHWALQVNVGFVAHLSACNPQYARVAWSELWQLVKTMIVkpycmYGVVML 415
Cdd:pfam10034 301 LFGTLTLKLLIKKLLNVEDDA--HIFDFlKAKFGLNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLL-----PFYILV 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   416 AMFFrrwrksgapvsalteeqrerarkyvledfieehfvsmsdmssketekqlykCFRLLKSCDYDYERYKRAQASLRKE 495
Cdd:pfam10034 374 LLIL---------------------------------------------------LIKVLQSIYRRLKRYKLSQAPMQES 402
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   496 QPPARDDFMQDikrlraqinrnsvkqrkeraqetkeaatdgastpteeedkdpeaeseskkknqepgsgetetesaadpt 575
Cdd:pfam10034 403 LPLEDGRIGER--------------------------------------------------------------------- 413
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   576 etppsrsadneeeeeehsataagcgsnssghrqrkrsssrrssvvptanaQILNMHYVYSFLQMLVFTLIGLAVRKLFFL 655
Cdd:pfam10034 414 --------------------------------------------------PELNGEVVYHVLQLLAFGLLALLIMRLKLL 443
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   656 SFTQGCVIAPTVCSKLWYHRQRN-IFWSVSLAVFLLSMFDPGMVNIREEYFPTRYSKSGDDlDSMLEWIKLNTERDAVFA 734
Cdd:pfam10034 444 WTPHMCVFASLGASKQLWHFLFKkIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDT-EELMEWIKSNTPKDAVFA 522
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   735 GPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDIYNQCAQLKIQYLIISLDECTNEVR-DDCDLLAI 813
Cdd:pfam10034 523 GSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDI 602
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 20129045   814 WDDKQ---PAYQKYPQFCHEL-LHKNVPSFLKVFANDHYGIIKM 853
Cdd:pfam10034 603 WDVEDghcPANRKGPRFCHEIkLSNYVPYFTRVFWNRSYHVYKV 646
 
Name Accession Description Interval E-value
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
17-853 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: 689.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    17 CGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYV 96
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    97 LPELVTAYFFHVVRSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKIYERPLAR 176
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNYLGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   177 ENFAFPFIFLQMFYLCICIGRIihRQRHTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTALVNaf 256
Cdd:pfam10034 161 ENFALPFFALQMLALTYILKRK--NISSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVA-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   257 vlDYSLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRqlRHVRSRRlghaqdllngdlFSLKFLMLTLLLASS 336
Cdd:pfam10034 237 --KIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQ--PNMKKGR------------FSFRLLKLLLHGLLV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   337 VQTTLIELFNRAGVVSVTEGDqqHFFDI-CAHWALQVNVGFVAHLSACNPQYARVAWSELWQLVKTMIVkpycmYGVVML 415
Cdd:pfam10034 301 LFGTLTLKLLIKKLLNVEDDA--HIFDFlKAKFGLNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLL-----PFYILV 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   416 AMFFrrwrksgapvsalteeqrerarkyvledfieehfvsmsdmssketekqlykCFRLLKSCDYDYERYKRAQASLRKE 495
Cdd:pfam10034 374 LLIL---------------------------------------------------LIKVLQSIYRRLKRYKLSQAPMQES 402
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   496 QPPARDDFMQDikrlraqinrnsvkqrkeraqetkeaatdgastpteeedkdpeaeseskkknqepgsgetetesaadpt 575
Cdd:pfam10034 403 LPLEDGRIGER--------------------------------------------------------------------- 413
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   576 etppsrsadneeeeeehsataagcgsnssghrqrkrsssrrssvvptanaQILNMHYVYSFLQMLVFTLIGLAVRKLFFL 655
Cdd:pfam10034 414 --------------------------------------------------PELNGEVVYHVLQLLAFGLLALLIMRLKLL 443
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   656 SFTQGCVIAPTVCSKLWYHRQRN-IFWSVSLAVFLLSMFDPGMVNIREEYFPTRYSKSGDDlDSMLEWIKLNTERDAVFA 734
Cdd:pfam10034 444 WTPHMCVFASLGASKQLWHFLFKkIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDT-EELMEWIKSNTPKDAVFA 522
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   735 GPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDIYNQCAQLKIQYLIISLDECTNEVR-DDCDLLAI 813
Cdd:pfam10034 523 GSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDI 602
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 20129045   814 WDDKQ---PAYQKYPQFCHEL-LHKNVPSFLKVFANDHYGIIKM 853
Cdd:pfam10034 603 WDVEDghcPANRKGPRFCHEIkLSNYVPYFTRVFWNRSYHVYKV 646
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
8-850 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: 640.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   8 VILSHALIGCGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHS 87
Cdd:cd20177   1 KILLGLLLALLVGVLYSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  88 VNVLQRFYVLPELVTAYFFHVVRSGFN------------------------PMVQPMQFYLEFVWLMGGVTLLVLYLYGT 143
Cdd:cd20177  81 INTLKRFNLYPEVILAILYRVFPSIANyfgiptkqcwqvrgedlppvesceGLGEPAYFYIYVVFGLNGLVAGLLFLYGW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 144 LLSENIFGGIYGVISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCICIgriihrQRHTSRMFMIFAMSLFTACALL 223
Cdd:cd20177 161 LLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYL------RSNIGKRFHLLAISISTFLFML 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 224 SWQFSTFIFTTQILIMMTSWNASALPTALvnafVLDYSLSHLLGHALAFVMSHGNSqLLLTWQLSISLFLFLITMVRQLR 303
Cdd:cd20177 235 MWQFSQFALLTQILSLFALYVLGYIPSSK----VQTIILSHLISLLLAFVLLFGNE-MLLTSLYLSSLLAFLIILYLQLR 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 304 HVRSRRLGHAQDLLNGDLFSLkflmltlllassvqTTLIelFNRAGVVSVTEGDQQHFFDI-CAHWALQVNvgFVAHLSA 382
Cdd:cd20177 310 LKKSFKFKLIIWLLQLILVFL--------------GTLG--LKLLLSKLLNVEDDAHIFKIlKSKFGDYRD--FDTRLYT 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 383 CNPQYARvAWSELWQLVKTMIVKPYCMYGVVMLAMFFRRWRKSGAPVSALTEEqrerarkyvledfieehfvsmsdmssk 462
Cdd:cd20177 372 CAAEFDF-LSLETFLRLSKTLLLPLYIVVLVVIAFLFLRVRLLTLNDSTLKES--------------------------- 423
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 463 etekqlykcfrllkscdydyerykraqaslrkeqpparddfmqdikrlraqinrnsvkqrkeraqetkeaatdgastpte 542
Cdd:cd20177     --------------------------------------------------------------------------------
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 543 eedkdpeaeseskkknqepgsgetetesaadptetppsrsadneeeeeehsataagcgsnssghrqrkrsssrrssVVPT 622
Cdd:cd20177 424 ----------------------------------------------------------------------------VNFT 427
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 623 ANAQILNMHYVYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAPTVCSKLWYHRQRN--IFWSVSLAVFLLSMFDPGMVNI 700
Cdd:cd20177 428 DSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLkkIFRLAVLFALLASMSYPGIPNL 507
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 701 REEYFPTRYSKSGdDLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSD 780
Cdd:cd20177 508 QEELSILGEFSNP-DTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPHYEDAGLRERTKQVYSMYSRRPAEE 586
                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129045 781 IYNQCAQLKIQYLIISLDECTNEVRDDCDLLAIWDDKQPAYQKYPQFC-HELLHKNVPSFLKVFANDHYGI 850
Cdd:cd20177 587 VYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGKPPLCiRLLLEDYVPYFKLVFSNKTYRV 657
 
Name Accession Description Interval E-value
Dpy19 pfam10034
Q-cell neuroblast polarization; Dyp-19, formerly known as DUF2211, is a transmembrane domain ...
17-853 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: 689.73  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    17 CGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYV 96
Cdd:pfam10034   1 VGSGILYALHVSTLFENDRWFSHLSELEREISFRTEMGLYYSYYKTIIEAPSFLEGLYQLMNDNRTEYPDTINALQRFNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045    97 LPELVTAYFFHVVRSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKIYERPLAR 176
Cdd:pfam10034  81 YPEVILAILYRIFRGIQNYLGEPVYFYIYFVFGLQGVYVSALFLYGWYLSGSWLGGILAVLWFFFNHGETTRVEWTPPLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   177 ENFAFPFIFLQMFYLCICIGRIihRQRHTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTALVNaf 256
Cdd:pfam10034 161 ENFALPFFALQMLALTYILKRK--NISSASELFCYILLSASTFLFLLTWQFSQFVLLTQILSLFLLDSLGLVPSKKVA-- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   257 vlDYSLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRqlRHVRSRRlghaqdllngdlFSLKFLMLTLLLASS 336
Cdd:pfam10034 237 --KIYLSHLISLLLAFVLQFGNSMLLTSPLLSSLISILLIRYLQ--PNMKKGR------------FSFRLLKLLLHGLLV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   337 VQTTLIELFNRAGVVSVTEGDqqHFFDI-CAHWALQVNVGFVAHLSACNPQYARVAWSELWQLVKTMIVkpycmYGVVML 415
Cdd:pfam10034 301 LFGTLTLKLLIKKLLNVEDDA--HIFDFlKAKFGLNSTRDFDTNLYTCAEEFDFLSKETFLRLTKTLLL-----PFYILV 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   416 AMFFrrwrksgapvsalteeqrerarkyvledfieehfvsmsdmssketekqlykCFRLLKSCDYDYERYKRAQASLRKE 495
Cdd:pfam10034 374 LLIL---------------------------------------------------LIKVLQSIYRRLKRYKLSQAPMQES 402
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   496 QPPARDDFMQDikrlraqinrnsvkqrkeraqetkeaatdgastpteeedkdpeaeseskkknqepgsgetetesaadpt 575
Cdd:pfam10034 403 LPLEDGRIGER--------------------------------------------------------------------- 413
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   576 etppsrsadneeeeeehsataagcgsnssghrqrkrsssrrssvvptanaQILNMHYVYSFLQMLVFTLIGLAVRKLFFL 655
Cdd:pfam10034 414 --------------------------------------------------PELNGEVVYHVLQLLAFGLLALLIMRLKLL 443
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   656 SFTQGCVIAPTVCSKLWYHRQRN-IFWSVSLAVFLLSMFDPGMVNIREEYFPTRYSKSGDDlDSMLEWIKLNTERDAVFA 734
Cdd:pfam10034 444 WTPHMCVFASLGASKQLWHFLFKkIFSSAVPTVILASMSYKGFPNIQEELSILGEFYNPDT-EELMEWIKSNTPKDAVFA 522
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   735 GPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDIYNQCAQLKIQYLIISLDECTNEVR-DDCDLLAI 813
Cdd:pfam10034 523 GSMPLMATVKLSTGRPIVNHPHYEDAGLRERTEDVYSVYSRKPAEDVYKILTSLKVNYVILEDSICSERSRrRGCRMLDI 602
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....
gi 20129045   814 WDDKQ---PAYQKYPQFCHEL-LHKNVPSFLKVFANDHYGIIKM 853
Cdd:pfam10034 603 WDVEDghcPANRKGPRFCHEIkLSNYVPYFTRVFWNRSYHVYKV 646
Dpy19 cd20177
C-mannosyltransferase Dpy19; Dpy19 proteins are C-mannosyltransferases that mediate ...
8-850 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: 640.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045   8 VILSHALIGCGFFFLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHS 87
Cdd:cd20177   1 KILLGLLLALLVGVLYSLHLSTLFENDRHFSHLSELEREMTFRTEMGLYYSYYKQLIEAPSFLEGLYKLTHDNVTEYPHT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  88 VNVLQRFYVLPELVTAYFFHVVRSGFN------------------------PMVQPMQFYLEFVWLMGGVTLLVLYLYGT 143
Cdd:cd20177  81 INTLKRFNLYPEVILAILYRVFPSIANyfgiptkqcwqvrgedlppvesceGLGEPAYFYIYVVFGLNGLVAGLLFLYGW 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 144 LLSENIFGGIYGVISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCICIgriihrQRHTSRMFMIFAMSLFTACALL 223
Cdd:cd20177 161 LLSGSILGGLLTVAFFFFNHGEATRVQWTPPLRESFAYPFLLLQILLITIYL------RSNIGKRFHLLAISISTFLFML 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 224 SWQFSTFIFTTQILIMMTSWNASALPTALvnafVLDYSLSHLLGHALAFVMSHGNSqLLLTWQLSISLFLFLITMVRQLR 303
Cdd:cd20177 235 MWQFSQFALLTQILSLFALYVLGYIPSSK----VQTIILSHLISLLLAFVLLFGNE-MLLTSLYLSSLLAFLIILYLQLR 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 304 HVRSRRLGHAQDLLNGDLFSLkflmltlllassvqTTLIelFNRAGVVSVTEGDQQHFFDI-CAHWALQVNvgFVAHLSA 382
Cdd:cd20177 310 LKKSFKFKLIIWLLQLILVFL--------------GTLG--LKLLLSKLLNVEDDAHIFKIlKSKFGDYRD--FDTRLYT 371
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 383 CNPQYARvAWSELWQLVKTMIVKPYCMYGVVMLAMFFRRWRKSGAPVSALTEEqrerarkyvledfieehfvsmsdmssk 462
Cdd:cd20177 372 CAAEFDF-LSLETFLRLSKTLLLPLYIVVLVVIAFLFLRVRLLTLNDSTLKES--------------------------- 423
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 463 etekqlykcfrllkscdydyerykraqaslrkeqpparddfmqdikrlraqinrnsvkqrkeraqetkeaatdgastpte 542
Cdd:cd20177     --------------------------------------------------------------------------------
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 543 eedkdpeaeseskkknqepgsgetetesaadptetppsrsadneeeeeehsataagcgsnssghrqrkrsssrrssVVPT 622
Cdd:cd20177 424 ----------------------------------------------------------------------------VNFT 427
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 623 ANAQILNMHYVYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAPTVCSKLWYHRQRN--IFWSVSLAVFLLSMFDPGMVNI 700
Cdd:cd20177 428 DSRLILNPEIVYNVLQLLAFGLLAILIMRLKLFWTPHMCILASLLLSKKLLWKLLLkkIFRLAVLFALLASMSYPGIPNL 507
                       730       740       750       760       770       780       790       800
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 701 REEYFPTRYSKSGdDLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSD 780
Cdd:cd20177 508 QEELSILGEFSNP-DTEELMEWIKDNTPPDAVFAGSMPLMANVKLSTGRPIVNHPHYEDAGLRERTKQVYSMYSRRPAEE 586
                       810       820       830       840       850       860       870
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129045 781 IYNQCAQLKIQYLIISLDECTNEVRDDCDLLAIWDDKQPAYQKYPQFC-HELLHKNVPSFLKVFANDHYGI 850
Cdd:cd20177 587 VYNILKKLGVNYIILEDSICLSRRRDGCSLPDIWDLEDPHNRGKPPLCiRLLLEDYVPYFKLVFSNKTYRV 657
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
21-301 1.27e-31

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: 131.89  E-value: 1.27e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  21 FLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQRFYVLPEL 100
Cdd:cd20178  14 VLHWSHITHLFENDRHFSHLSTLEREMAFRTEMGLYYSYFKTIIEAPSFLNGVWMIMNDRLTEYPLVINTLKRFNLYPEV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 101 VTAYFFHVVRS-------------------GFNP------MVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYG 155
Cdd:cd20178  94 VLASWYRIYTGimdffgiqtktcwtvnrgeGLSPvescegLGDPAYFYVAVIFLLNGLMMSLFFIYGTYLSGSRLGGVVT 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 156 VISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCicigrIIHRQRHTSRMFMIfAMSLFTACALLSWQFSTFIFTTQ 235
Cdd:cd20178 174 VLCFFFNHGECTRVMWTPPLRESFSYPFLVLQMLLVT-----YILRAPNLGRGSLI-ALCISNVLFMLPWQFAQFVLLTQ 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129045 236 ILIMMTSWNASALPTALVNAFVldysLSHLLGHALAFVMSHGNSQLLLTWQLSISLFLFLITMVRQ 301
Cdd:cd20178 248 IASLFAVYVVGYIDSCKLQKIL----YAHMISLVVCFVLMFGNSMLLTSYYASSLVIIWGILALRP 309
Dpy19L1 cd20178
C-mannosyltransferase Dpy-19-like protein 1 (Dpy19L1); Dpy19 proteins are ...
633-851 2.54e-28

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: 121.49  E-value: 2.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 633 VYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAPTVCSKL---W----YHRQRNIFwsvslaVFLLSMFDPGMVNIReeyf 705
Cdd:cd20178 434 VYHALQLLAYAVLAILIMRLKLFLTPHMCVMASLVCSRQlfgWlfckVHPQAVVF------AILAAMAIQGSANLQ---- 503
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 706 pTRYSKSGD----DLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDI 781
Cdd:cd20178 504 -TQWNIIGEfsnlPQEELLEWIKYNTKPDAVFAGAMPTMASVKLSALRPIVNHPHYEDAGLRARTKIVYSMYSRKPAEEV 582
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 782 YNQCAQLKIQYLIISLDECTNEVRDDCDLLAIWDDKQPAYQKYPQFCHELLHKNVPSFLKVFANDHYGII 851
Cdd:cd20178 583 KRELMKLGVNYYILEESWCVRRSKPGCSMPEIWDVEDPDNAGKTPLCTLMSKDSRPHFTTVFENSVYKVL 652
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
14-296 1.18e-25

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: 113.22  E-value: 1.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  14 LIGCGFF--FLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVL 91
Cdd:cd20179   7 TLGIAVFvaILHWLHLVTLFENDRHFSHLSSLEREMTFRTEMGLYYSYFKTIIEAPSFLEGLWMIMNDRLTEYPLIINAI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  92 QRFYVLPELVTAYFFHVVRSGFN----------------PMVQ---------PMQFYLEFVWLMGGVTLLVLYLYGTLLS 146
Cdd:cd20179  87 KRFHLYPEVIIASWYCTFMGIMNlfgletktcwnvtriePLNEvqsceglgdPACFYVGVIFILNGLMMGLFFMYGAYLS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 147 ENIFGGIYGVISYLMFHSFVAKIYERPLARENFAFPFIFLQMFYLCICIGRIIHRQRHTsrMFMIFAMSLFtacaLLSWQ 226
Cdd:cd20179 167 GTQLGGLITVLCFFFNHGEATRVMWTPPLRESFSYPFLVLQMCILTLILRTSSNDRRPF--IALCLSNVAF----MLPWQ 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20129045 227 FSTFIFTTQILIMMTSWNASAL-PTALVNAFVLDYSlshllGHALAFVMSHGNSQLLLTWQLSISLFLFLI 296
Cdd:cd20179 241 FAQFILFTQIASLFPMYVVGYIePSKFQKIIYMNMI-----SVTLSFILMFGNSMYLSSYYSSSLLMTWAI 306
Dpy19L2 cd20179
C-mannosyltransferase Dpy-19-like protein 2 (Dpy19L2); Dpy19 proteins are ...
629-850 5.71e-23

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: 104.74  E-value: 5.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 629 NMHYVYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAPTVCSKLWYHRQ--RNIFWSVSLAVFLLsMFDPGMVNIREEYfP 706
Cdd:cd20179 431 HSELAFHTLQLLVFTALAILIMRLKMFLTPHMCVMASLICSRQLFGWLfrRVRFEKVIFGILTV-MSIQGYANLRNQW-S 508
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 707 TRYSKSGDDLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQQSSDIYNQCA 786
Cdd:cd20179 509 IIGEFNNLPQEELLQWIKYSTTSDAVFAGAMPTMASIKLSTLHPIVNHPHYEDADLRARTKIVYSTYSRKSAKEVRDKLL 588
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20129045 787 QLKIQYLIISLDECTNEVRDDCDLLAIWDDKQPAYQKYPQFCHELLHKNVPSFLKVFANDHYGI 850
Cdd:cd20179 589 ELHVNYYVLEEAWCVVRTKPGCSMLEIWDVEDPSNAANPPLCSVLLEDARPYFTTVFQNSVYRV 652
Dpy19L3 cd20181
C-mannosyltransferase Dpy-19-like protein 3 (Dpy19L3); Dpy19 proteins are ...
634-853 3.18e-16

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: 83.35  E-value: 3.18e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 634 YSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAP-TVCS-KLW---------YHRQRniFWSVSLAVFLLSM------FDPG 696
Cdd:cd20181 420 YNLIHTILFGFLALSTMRMKYLWTSHMCVFASfGLCStELWelllksvhlYNPKR--IRVMRYSVPILTLlylcykFWPG 497
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 697 MVN----IREEYFPtrysksgdDLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSV 772
Cdd:cd20181 498 LMDelseLREFYDP--------DTVELMNWINSNTPRKAVFAGSMQLLAGVKLCTGRTLTNHPHYEDKSLRERTRQVYQI 569
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 773 YSRQQSSDIYNQCAQLKIQYLIISLDECTNEV-RDDC---DLLAIWD------------DKQPAyqKYPQFCHElLHKNV 836
Cdd:cd20181 570 YAKRSPEEVHALLRSFGTDYVILEDSICYERRhRRGCrlrDLLDIANghimdgpgendpDLKPA--DHPRFCEE-IKRNL 646
                       250       260
                ....*....|....*....|.
gi 20129045 837 PS----FLKVFANDHYGIIKM 853
Cdd:cd20181 647 PSyaayFTRVFQNKTFHVYKL 667
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
13-301 2.91e-15

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: 79.88  E-value: 2.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  13 ALIGCGFffLYVQHVRVIFETRTNIQQLNQLEREALLRREDALYYAFYKQLAEGPDFWHGYEQLKNVTDIEYPHSVNVLQ 92
Cdd:cd20180   8 AAVTSGM--MYAVYLSTYHERKFWFSNRQELEREITFQGDSAIYYSYYKDMLKAPSFERGVYELTHNNKTVSLKTINAVQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045  93 RFYVLPELVTAYFFHVvrSGFNPMVQPMQFYLEFVWLMGGVTLLVLYLYGTLLSENIFGGIYGVISYLMFHSFVAKI-YE 171
Cdd:cd20180  86 QMSLYPELIASVLYQA--TGSNEVIEPVYFYIGIVFGLQGIYVTALFVTSWLMSGTWLAGMLTVAWFIINRVDTTRIeYS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 172 RPLaRENFAFPFIFLQMFYLCICIGRIIHRqrhTSRMFMIFAMSLFTACALLSWQFSTFIFTTQILIMMTSWNASALPTA 251
Cdd:cd20180 164 IPL-RENWALPYFACQVAALTGYLKSNLNT---YAERFCYLLMSASTYTFMMMWEYSHYVLFLQAISLFLLDSFSLEQSD 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20129045 252 LVNAFVLDYSLSHLLGHALAFvmshGNSQLLLTWQLSISLFLFLITMVRQ 301
Cdd:cd20180 240 KVYEVYKVYLFSLFLGYLLQF----ENPALLVSPLLSLVAALMLAKCLQL 285
Dpy19L4 cd20180
C-mannosyltransferase Dpy-19-like protein 4 (Dpy19L4); Dpy19 proteins are ...
633-852 1.15e-09

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: 62.16  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 633 VYSFLQMLVFTLIGLAVRKLFFLSFTQGCVIAP-TVCS-KLW-----YHRQRNIFwSVSLAVfLLSMFDPGMV--NIREE 703
Cdd:cd20180 417 VYHVIHTILLGSLAMLFEGMKYLWTPYVCMLAAfGVCSpELWmtlfkWLRLRTVH-PILLAL-ILSMAVPTIIgfSLWKE 494
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 704 YFPTRYSKSGD-------DLDSMLEWIKLNTERDAVFAGPVDIIGTVHLTTKRPIVNHAHLEMRQIAERTEHVYSVYSRQ 776
Cdd:cd20180 495 FFPRLMTELSElqefydpDTVELMTWIKRQAPVAAVFAGSPQLMGTIKLCTGWMVTSLPLYNDDDLLKRNENIYQIYSKR 574
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129045 777 QSSDIYNQCAQLKIQYLIISLDECTN-------EVRDDCDLL---AIWDDKQP-AYQKYPQFCHELLHKNVP---SFLKV 842
Cdd:cd20180 575 SAEDIYKILTSYKANYLIIEDAICNEvgpvrgcRVKDLLDIAnghVVCEEGDKyTYSKYGRFCHEIKINYSPyvnYFTRV 654
                       250
                ....*....|
gi 20129045 843 FANDHYGIIK 852
Cdd:cd20180 655 YWNRSYFVYK 664
DUF6798 pfam20604
Domain of unknown function (DUF6798); This presumed domain is functionally uncharacterized. ...
719-752 1.00e-02

Domain of unknown function (DUF6798); This presumed domain is functionally uncharacterized. This domain family is mainly found in bacteria and archaea, and is approximately 60 amino acids in length. There is a conserved WxxR sequence motif and a conserved Lys residue. Members of this entry may be transmembrane proteins.


Pssm-ID: 466753 [Multi-domain]  Cd Length: 60  Bit Score: 35.26  E-value: 1.00e-02
                          10        20        30
                  ....*....|....*....|....*....|....
gi 20129045   719 MLEWIKLNTERDAVFAGPVDiIGTVHLTTKRPIV 752
Cdd:pfam20604   5 LCEWIRENTPADAVFLTPPG-QQTFRWYAQRAEV 37
 
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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