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Conserved domains on  [gi|31560202|ref|NP_080220|]
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post-GPI attachment to proteins factor 4 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
25-395 1.04e-179

Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.


:

Pssm-ID: 409191  Cd Length: 379  Bit Score: 504.83  E-value: 1.04e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202  25 VQLFILTVVTFGLLAPLACHRLLHSYFYLRHWHLNQMSQDFLQQSLKEGEAALHYFEELPSANGSVPIVWQATPRPWLVI 104
Cdd:cd22190   3 RHLLILYVVTFLVILPLLCHRLPFSYYYSRHLSLDDLSDKALQENDERGAKALQYFESLDPKSSSQFSPLEKQGKPDLAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 105 TIITVDRQPG---FHYVLQVVSQFHRLLQQCgPQCEGHQLFLCNVERS-VSHFDAKLLSKYVPVANRYEGTEDDygDDPS 180
Cdd:cd22190  83 TIITVSRQSGtksPHYLLQVVARLLRLLKEC-GLCNTTRLFICNVDSDpSSHEEAVFLSKYVPVVSRYGNEERS--DVTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 181 TNSFEKEKQDYVYCLESSLQtYNPDYVLMVEDDAIPEEQIFPVLEHLLRARFSE---PHLQDALYLKLYHPERLQHYINP 257
Cdd:cd22190 160 DNRFEKEKQDYVFCLESSLK-LNPKYVLLLEDDALPHPDFFPVLEHLLRYRLEKkytPNRRDWAYLKLYHPERLQGYGNP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 258 EPMRILEWVGVGMLLGPVLTWIYMRFA--CRPGFSWPVMLFFCLYSMGLVELVGRHYFLELRRLSPSLYSVVPASQCCTP 335
Cdd:cd22190 239 EPMRILELLGLGLLGGTILVLIYLRLLskSRRRFSWLVFLFFFVYFMLLAELIGRPHLLELRRLSPHLYSVVPAPECCTP 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 336 AMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLR 395
Cdd:cd22190 319 AMLYPKSSARRLLDYLSSVTCSPGYPKDFALDDFLRKKGLRAYLVEPNLFSHIGLYSSLR 378
 
Name Accession Description Interval E-value
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
25-395 1.04e-179

Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.


Pssm-ID: 409191  Cd Length: 379  Bit Score: 504.83  E-value: 1.04e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202  25 VQLFILTVVTFGLLAPLACHRLLHSYFYLRHWHLNQMSQDFLQQSLKEGEAALHYFEELPSANGSVPIVWQATPRPWLVI 104
Cdd:cd22190   3 RHLLILYVVTFLVILPLLCHRLPFSYYYSRHLSLDDLSDKALQENDERGAKALQYFESLDPKSSSQFSPLEKQGKPDLAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 105 TIITVDRQPG---FHYVLQVVSQFHRLLQQCgPQCEGHQLFLCNVERS-VSHFDAKLLSKYVPVANRYEGTEDDygDDPS 180
Cdd:cd22190  83 TIITVSRQSGtksPHYLLQVVARLLRLLKEC-GLCNTTRLFICNVDSDpSSHEEAVFLSKYVPVVSRYGNEERS--DVTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 181 TNSFEKEKQDYVYCLESSLQtYNPDYVLMVEDDAIPEEQIFPVLEHLLRARFSE---PHLQDALYLKLYHPERLQHYINP 257
Cdd:cd22190 160 DNRFEKEKQDYVFCLESSLK-LNPKYVLLLEDDALPHPDFFPVLEHLLRYRLEKkytPNRRDWAYLKLYHPERLQGYGNP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 258 EPMRILEWVGVGMLLGPVLTWIYMRFA--CRPGFSWPVMLFFCLYSMGLVELVGRHYFLELRRLSPSLYSVVPASQCCTP 335
Cdd:cd22190 239 EPMRILELLGLGLLGGTILVLIYLRLLskSRRRFSWLVFLFFFVYFMLLAELIGRPHLLELRRLSPHLYSVVPAPECCTP 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 336 AMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLR 395
Cdd:cd22190 319 AMLYPKSSARRLLDYLSSVTCSPGYPKDFALDDFLRKKGLRAYLVEPNLFSHIGLYSSLR 378
 
Name Accession Description Interval E-value
PGAP4 cd22190
Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), ...
25-395 1.04e-179

Post-GPI attachment to proteins factor 4; Post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246), has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases (GTs), it contains three transmembrane domains. Structural modeling suggests that PGAP4 adopts a GT-A fold split by an insertion of tandem transmembrane domains.


Pssm-ID: 409191  Cd Length: 379  Bit Score: 504.83  E-value: 1.04e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202  25 VQLFILTVVTFGLLAPLACHRLLHSYFYLRHWHLNQMSQDFLQQSLKEGEAALHYFEELPSANGSVPIVWQATPRPWLVI 104
Cdd:cd22190   3 RHLLILYVVTFLVILPLLCHRLPFSYYYSRHLSLDDLSDKALQENDERGAKALQYFESLDPKSSSQFSPLEKQGKPDLAV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 105 TIITVDRQPG---FHYVLQVVSQFHRLLQQCgPQCEGHQLFLCNVERS-VSHFDAKLLSKYVPVANRYEGTEDDygDDPS 180
Cdd:cd22190  83 TIITVSRQSGtksPHYLLQVVARLLRLLKEC-GLCNTTRLFICNVDSDpSSHEEAVFLSKYVPVVSRYGNEERS--DVTS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 181 TNSFEKEKQDYVYCLESSLQtYNPDYVLMVEDDAIPEEQIFPVLEHLLRARFSE---PHLQDALYLKLYHPERLQHYINP 257
Cdd:cd22190 160 DNRFEKEKQDYVFCLESSLK-LNPKYVLLLEDDALPHPDFFPVLEHLLRYRLEKkytPNRRDWAYLKLYHPERLQGYGNP 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 258 EPMRILEWVGVGMLLGPVLTWIYMRFA--CRPGFSWPVMLFFCLYSMGLVELVGRHYFLELRRLSPSLYSVVPASQCCTP 335
Cdd:cd22190 239 EPMRILELLGLGLLGGTILVLIYLRLLskSRRRFSWLVFLFFFVYFMLLAELIGRPHLLELRRLSPHLYSVVPAPECCTP 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 336 AMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLR 395
Cdd:cd22190 319 AMLYPKSSARRLLDYLSSVTCSPGYPKDFALDDFLRKKGLRAYLVEPNLFSHIGLYSSLR 378
PGAP4-like cd21105
Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI ...
27-396 1.92e-98

Post-GPI attachment to proteins factor 4 and similar proteins; This family includes post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. This family also includes uncharacterized fungal proteins with similarity to PGAP4.


Pssm-ID: 409189  Cd Length: 364  Bit Score: 297.75  E-value: 1.92e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202  27 LFILTVVTFGLLAP--LACHRLLHSYFYLR--HWHLNQMSQDFLQQSLKEGEAALHYFEELPSangsvpivwQATPRPWL 102
Cdd:cd21105   1 LIVLAIIFLTLLFLvrLVSPRLGHSVFFLAsqELLLRRLEELRLAQALKLLESLKNSSQALGF---------RLSPKPDL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 103 VITIITVDRQPGfHYVLQVVSQFHRLLQQCGPQCEGHQLFLCNVER-SVSHFDAKLLSKYVPVANRYEGTEDDYgdDPST 181
Cdd:cd21105  72 CIVIIAVNRRPH-SYLTQTVASLLRGIQSDLASYSNVSLSICNTESpPATFSELERLSELVPVDSIKRRLEEDK--DDSS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 182 NSFEKEKQDYVYCLESSLQTyNPDYVLMVEDDAIPEEQIFPVLEHLLRARFSepHLQDALYLKLYHPERLQHYINPEPmR 261
Cdd:cd21105 149 SWFRKETLDYAYCLRACTES-GSRYTLLLEDDAIATPRFLQRLLSLLEDLES--PRRKWLFVKLYYPEYWRGFELYFP-S 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 262 ILEWVGVGMLLGPVLTWIYMRFACRPGF------SWPVMLFFCLYSMGLVELVGRHYFLELRRLSPSLYSVVPASqCCTP 335
Cdd:cd21105 225 ILELVSLSVLAGLLTTLLWLALLRRLRRpfplrtNLILVFVLFLLSGFVLFAVGRQNLLGLLFRKPSGLVSIPEG-CCTV 303
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31560202 336 AMLFPAPAARRTLTYLSQVYCHKGFGKDMALYSLLRAKGERAYVVEPNLVKHIGLFSSLRY 396
Cdd:cd21105 304 AVLFPNSSVARLLEYFTLLDARQGKPKDHLLDEYLFTSGLSIYELVPNLVQHIGLFSSYRK 364
PGAP4-like_fungal cd22189
uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This ...
27-393 2.04e-10

uncharacterized fungal proteins similar to Post-GPI attachment to proteins factor 4; This subfamily contains uncharacterized fungal proteins with similarity to animal post-GPI attachment to proteins factor 4 (PGAP4), also known as post-GPI attachment to proteins GalNAc transferase 4 or transmembrane protein 246 (TMEM246). PGAP4 has been shown to be a Golgi-resident GPI-GalNAc transferase. Many eukaryotic proteins are anchored to the cell surface through glycolipid glycosylphosphatidylinositol (GPI). GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications. PGAP4 knockout cells lose GPI-GalNAc structures. PGAP4 is most likely involved in the initial steps of GPI-GalNAc biosynthesis. In contrast to other Golgi glycotransferases, it contains three transmembrane domains. Proteins from this subfamily contain the putative catalytic site of PGAP4 and may have similar activities.


Pssm-ID: 409190  Cd Length: 375  Bit Score: 61.79  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202  27 LFILTVVTFGLL---APLACHRLLHSYFYlrhwhlnQMSQDFLQQ-SLKEGEAALHYFEELPSANGSvPIVWQATPRPWL 102
Cdd:cd22189   4 LLLVFALLYLLLfqyCRSNSYRDPTSAFF-------DPERAYEPRySATREQEADAFIDSANATPPP-PNSTKAGSNPSL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 103 VITIITVDRqPGFHYVLQ-VVSQFHRLLQQcgpqcEGHQLFLcNVerSVSH--------FDAKLLSKyvpVANRYEGTED 173
Cdd:cd22189  76 CVGIPTVKR-PGEQYLDTtVGSLLDGLTPE-----ERADIHL-VV--LIAHtdptqhpaYGEPWLHN---LADEVLTYNV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 174 DYGDDPSTNSFEKEKQ--------DYVYCLESSLQTyNPDYVLMVEDDAIPEEQIFPvleHLLRA------RFSEPHLQD 239
Cdd:cd22189 144 SDEDLEHLRELEEEGGnfrekglfDYTYLLEACYET-GAPYIAMFEDDVVAADGWYH---RTLQAlrdierKTARKGASD 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 240 ALYLKLYHPERLQHYiNPEPMRILEWVGVGMLLGPVLTWIYMRFACRPGF---SWPVMLFFCLYSM----GLVELVGRhy 312
Cdd:cd22189 220 WLYLRLFYTETFLGW-NSEEWPTYLFWSLLVVALVALALLLLRRRRRPARrslTNPTIAVICLVCVpaliLLFFAAGR-- 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31560202 313 fLELRRLSPSLySVVPASQCCTPAMLFPAPAARRTLTYLSQVycHKGFGkDMALYSLLRAKGERAYVVEPNLVKHIGLFS 392
Cdd:cd22189 297 -VTVLPLPPGV-HEMNRFGCCSQALVFPREQVPDLIDYLEER--GDGQV-DSLIEDYADERGLDRWALTPSVLQHVGAKS 371

                .
gi 31560202 393 S 393
Cdd:cd22189 372 S 372
 
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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