|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
237-1093 |
1.44e-176 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 539.38 E-value: 1.44e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 237 PLFNSAVNQEGITSNtnnGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGATGVPPSS 314
Cdd:COG5028 10 PQAQSQVHTGAASSK---KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVMSPAFQSQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 315 LNYPS---GPQAFTQTPLGANHLTTSMSGLSLQPEglrvvnllQERNMLPSTPLKPPVPNLHEDIQKLNCNPELFRCTLT 391
Cdd:COG5028 87 QKFSSpygGSMADGTAPKPTNPLVPVDLFEDQPPP--------ISDLFLPPPPIVPPLTTNFVGSEQSNCSPKYVRSTMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 392 SIPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEEFl 466
Cdd:COG5028 159 AIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKNDVPEGF- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 467 YNPLTRV--YGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPG-NTRTK 543
Cdd:COG5028 238 DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIPNfDPRTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 544 IGFITFDSTIHFYGLQESLSQpQMLIVSDIEDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTKTLETQSALGPALQA 622
Cdd:COG5028 318 IAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQDNKSPKNALGPALKA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 623 AFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRssakdiHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASL 702
Cdd:COG5028 397 AKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVDLFLTSEDYIDVATL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 703 GCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLSLPNVNPD 782
Cdd:COG5028 471 SHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCAFSTMPRD 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 783 AGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRSMTASLSD 862
Cdd:COG5028 550 TSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKALNSSLKE 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 863 ARDALVNAVIDSLSAYRSS-VLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNaRLDERIFAMCQVKNQPLVYLMLT 941
Cdd:COG5028 629 ARVLINKSMVDILKAYKKElVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGST-PSDIRISALNRLTSLPLKQLMRN 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 942 THPSLYRVDNLSDEGALNISDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQNYASIPQP 1020
Cdd:COG5028 708 IYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDLFGVDSLSDIPSG 785
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160331913 1021 MTDLPELDTPESARIIAFISWLREQRPFFPI-LYVIRD--ESPMKANFLQNMIEDRTESALSYYEFLLHIQQQVNK 1093
Cdd:COG5028 786 KFTLPPTGNEFNERVRNIIGELRSVNDDSTLpLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYLQILHEKIKS 861
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
501-743 |
2.41e-128 |
|
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 24 is very similar to Sec23. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238756 [Multi-domain] Cd Length: 244 Bit Score: 390.48 E-value: 2.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 579
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 580 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRS 659
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 660 SAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELQRY 738
Cdd:cd01479 161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239
|
....*
gi 160331913 739 LTRKI 743
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
501-739 |
3.91e-107 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 334.60 E-value: 3.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 581 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM--SPTGGRMSVFQTQLPTLGV-GALKPREEPNH 657
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 658 RSSAKD-IHMTPSTD-FYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 735
Cdd:pfam04811 161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 160331913 736 QRYL 739
Cdd:pfam04811 238 QRYF 241
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
491-1093 |
6.74e-45 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 177.57 E-value: 6.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 491 MAPSEYMLRPPQ-----PPVYLFVFDVSHNAVetgyLNSVCQSLLDNLDLLPGNTR---TKIGFITFDSTIHFYGLQESL 562
Cdd:PTZ00395 935 IRRNSFLAKYPQvknmlPPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqTKIAIITFNSSIYFYHCKGGK 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 563 SQP-------------QMLIVSDIEDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMS 628
Cdd:PTZ00395 1011 GVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTTMQSYGSCGNSALKIAMDMLK 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 629 PTGGRMSV--FQTQLPTLGVGALKPREepnhRSSAKDIHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLA--SLGC 704
Cdd:PTZ00395 1091 ERNGLGSIcmFYTTTPNCGIGAIKELK----KDLQENFLEVKQKIFYDSLLLDLYAFNISVDIFIISSNNVRVCvpSLQY 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 705 ISRYSAGSVYYYPSYHHQHNpvqVQKLQKELQRYLTRK-IGFEAVMRIRCTKGLSIHTF---HGNF-FVRSTDLLSLPNV 779
Cdd:PTZ00395 1167 VAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLfccNNNFnSIISVDTIKIPKI 1243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 780 NPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAisglLANMAVDRSMTAS 859
Cdd:PTZ00395 1244 RHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTDAEA----LMNILIKQLCTNI 1319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 860 LSDarDALVNAVIDSLSA----YRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSfqTGTNARLDERIFAMCQVKNQP 934
Cdd:PTZ00395 1320 LHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPLFTSSLLKHNV--TKKEILHDLKVYSLIKLLSMP 1395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 935 LVYLMLTTHPSLY---------RVDNLSDEGALNISdRTIPQppilqlSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFL 1005
Cdd:PTZ00395 1396 IISSLLYVYPVMYvihikgktnEIDSMDVDDDLFIP-KTIPS------SAEKIYSNGIYLLDACTHFYLYFGFHSDANFA 1468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 1006 SQVLGvqnyaSIPQPMT--DLPELDTPES---ARIIAFISWLREQRPFFPiLYVIRDESPMKANFLQNMIEDRTESALSY 1080
Cdd:PTZ00395 1469 KEIVG-----DIPTEKNahELNLTDTPNAqkvQRIIKNLSRIHHFNKYVP-LVMVAPKSNEEEHLISLCVEDKADKEYSY 1542
|
650
....*....|...
gi 160331913 1081 YEFLLHIQQQVNK 1093
Cdd:PTZ00395 1543 VNFLCFIHKLVHK 1555
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
55-159 |
9.14e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.14 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 55 PGSYPHPIPAK--TLNPVSGQSNY---GGSQGSGQTLNRPpvASNPVTPSLHSGPAPR--------MPLPASQNPATTPM 121
Cdd:pfam03154 286 PSHMQHPVPPQpfPLTPQSSQSQVppgPSPAAPGQSQQRI--HTPPSQSQLQSQQPPReqplppapLSMPHIKPPPTTPI 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 160331913 122 PS----------------SSFLPEANLPPPLNWQynyPSTASQTNHCPRASSQP 159
Cdd:pfam03154 364 PQlpnpqshkhpphlsgpSPFQMNSNLPPPPALK---PLSSLSTHHPPSAHPPP 414
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
237-1093 |
1.44e-176 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 539.38 E-value: 1.44e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 237 PLFNSAVNQEGITSNtnnGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSV--GYSYPSLPPGYQNTTPPGATGVPPSS 314
Cdd:COG5028 10 PQAQSQVHTGAASSK---KSARPHRAYANFSAGQMGMPPYTTPPLQQQSRRQidQAATAMHNTGANNPAPSVMSPAFQSQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 315 LNYPS---GPQAFTQTPLGANHLTTSMSGLSLQPEglrvvnllQERNMLPSTPLKPPVPNLHEDIQKLNCNPELFRCTLT 391
Cdd:COG5028 87 QKFSSpygGSMADGTAPKPTNPLVPVDLFEDQPPP--------ISDLFLPPPPIVPPLTTNFVGSEQSNCSPKYVRSTMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 392 SIPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEEFl 466
Cdd:COG5028 159 AIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRCNICRSKNDVPEGF- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 467 YNPLTRV--YGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPG-NTRTK 543
Cdd:COG5028 238 DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAILENLDQIPNfDPRTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 544 IGFITFDSTIHFYGLQESLSQpQMLIVSDIEDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTKTLETQSALGPALQA 622
Cdd:COG5028 318 IAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQDNKSPKNALGPALKA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 623 AFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRssakdiHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASL 702
Cdd:COG5028 397 AKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVDLFLTSEDYIDVATL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 703 GCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLSLPNVNPD 782
Cdd:COG5028 471 SHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFNRSSDLCAFSTMPRD 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 783 AGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRSMTASLSD 862
Cdd:COG5028 550 TSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILAKKASTKALNSSLKE 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 863 ARDALVNAVIDSLSAYRSS-VLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNaRLDERIFAMCQVKNQPLVYLMLT 941
Cdd:COG5028 629 ARVLINKSMVDILKAYKKElVKSNTSTQLPLPANLKLLPLLMLALLKSSAFRSGST-PSDIRISALNRLTSLPLKQLMRN 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 942 THPSLYRVDNLSDEGALNISDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQNYASIPQP 1020
Cdd:COG5028 708 IYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQDLFGVDSLSDIPSG 785
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160331913 1021 MTDLPELDTPESARIIAFISWLREQRPFFPI-LYVIRD--ESPMKANFLQNMIEDRTESALSYYEFLLHIQQQVNK 1093
Cdd:COG5028 786 KFTLPPTGNEFNERVRNIIGELRSVNDDSTLpLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDYLQILHEKIKS 861
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
501-743 |
2.41e-128 |
|
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 24 is very similar to Sec23. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup carry a partial MIDAS motif and have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238756 [Multi-domain] Cd Length: 244 Bit Score: 390.48 E-value: 2.41e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIP 579
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 580 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRS 659
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 660 SAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELQRY 738
Cdd:cd01479 161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239
|
....*
gi 160331913 739 LTRKI 743
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
501-739 |
3.91e-107 |
|
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
Pssm-ID: 398467 [Multi-domain] Cd Length: 241 Bit Score: 334.60 E-value: 3.91e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 581 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM--SPTGGRMSVFQTQLPTLGV-GALKPREEPNH 657
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 658 RSSAKD-IHMTPSTD-FYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 735
Cdd:pfam04811 161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 160331913 736 QRYL 739
Cdd:pfam04811 238 QRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
501-737 |
1.99e-102 |
|
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface. Some members of this family possess a partial MIDAS motif that is a characteristic feature of most vWA domain proteins.
Pssm-ID: 238745 [Multi-domain] Cd Length: 239 Bit Score: 321.89 E-value: 1.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPM 580
Cdd:cd01468 1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 581 PENLLVNLNESKELVQDLLKTLPQMFTK--TLETQSALGPALQAAFKLMSPT--GGRMSVFQTQLPTLGVGALKPREEPN 656
Cdd:cd01468 81 PDRFLVPLSECKKVIHDLLEQLPPMFWPvpTHRPERCLGPALQAAFLLLKGTfaGGRIIVFQGGLPTVGPGKLKSREDKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 657 HRSSAKD-IHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHqhnPVQVQKLQKEL 735
Cdd:cd01468 161 PIRSHDEaQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQA---PNDGSKFKQDL 237
|
..
gi 160331913 736 QR 737
Cdd:cd01468 238 QR 239
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
491-1093 |
6.74e-45 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 177.57 E-value: 6.74e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 491 MAPSEYMLRPPQ-----PPVYLFVFDVSHNAVetgyLNSVCQSLLDNLDLLPGNTR---TKIGFITFDSTIHFYGLQESL 562
Cdd:PTZ00395 935 IRRNSFLAKYPQvknmlPPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqTKIAIITFNSSIYFYHCKGGK 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 563 SQP-------------QMLIVSDIEDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMS 628
Cdd:PTZ00395 1011 GVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTTMQSYGSCGNSALKIAMDMLK 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 629 PTGGRMSV--FQTQLPTLGVGALKPREepnhRSSAKDIHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLA--SLGC 704
Cdd:PTZ00395 1091 ERNGLGSIcmFYTTTPNCGIGAIKELK----KDLQENFLEVKQKIFYDSLLLDLYAFNISVDIFIISSNNVRVCvpSLQY 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 705 ISRYSAGSVYYYPSYHHQHNpvqVQKLQKELQRYLTRK-IGFEAVMRIRCTKGLSIHTF---HGNF-FVRSTDLLSLPNV 779
Cdd:PTZ00395 1167 VAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLfccNNNFnSIISVDTIKIPKI 1243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 780 NPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAisglLANMAVDRSMTAS 859
Cdd:PTZ00395 1244 RHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTDAEA----LMNILIKQLCTNI 1319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 860 LSDarDALVNAVIDSLSA----YRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSfqTGTNARLDERIFAMCQVKNQP 934
Cdd:PTZ00395 1320 LHN--DNYSKIIIDNLAAilfsYRINCASSAHSGqLILPDTLKLLPLFTSSLLKHNV--TKKEILHDLKVYSLIKLLSMP 1395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 935 LVYLMLTTHPSLY---------RVDNLSDEGALNISdRTIPQppilqlSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFL 1005
Cdd:PTZ00395 1396 IISSLLYVYPVMYvihikgktnEIDSMDVDDDLFIP-KTIPS------SAEKIYSNGIYLLDACTHFYLYFGFHSDANFA 1468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 1006 SQVLGvqnyaSIPQPMT--DLPELDTPES---ARIIAFISWLREQRPFFPiLYVIRDESPMKANFLQNMIEDRTESALSY 1080
Cdd:PTZ00395 1469 KEIVG-----DIPTEKNahELNLTDTPNAqkvQRIIKNLSRIHHFNKYVP-LVMVAPKSNEEEHLISLCVEDKADKEYSY 1542
|
650
....*....|...
gi 160331913 1081 YEFLLHIQQQVNK 1093
Cdd:PTZ00395 1543 VNFLCFIHKLVHK 1555
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
744-828 |
6.79e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 119.18 E-value: 6.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 744 GFEAVMRIRCTKGLSIHTFHGNFFVRS-TDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHT 822
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSsGDTWKLPSLDPDTSYAFEFDIDEPLPNGSNAYIQFALLYTHSSGERRIRVTT 80
|
....*.
gi 160331913 823 LCLPVV 828
Cdd:pfam08033 81 VALPVT 86
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
839-940 |
1.22e-31 |
|
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is composed of five alpha helices.
Pssm-ID: 461441 [Multi-domain] Cd Length: 103 Bit Score: 119.14 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 839 DVQAISGLLANMAVDRSMTASLSDARDALVNAVIDSLSAYRSSVLSNQQPG-LMVPFSLRLFPLFVLALLKQKSFQTGTN 917
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASSSSPGqLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 160331913 918 ARLDERIFAMCQVKNQPLVYLML 940
Cdd:pfam04815 81 SPSDERAYARHLLLSLPVEELLL 103
|
|
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
387-690 |
3.93e-18 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 90.00 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 387 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VSFlDQRRWKCNLCYRVNDVPEE 464
Cdd:PLN00162 13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 465 FLYNPLTRVYGE--PhrrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRt 542
Cdd:PLN00162 91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 543 kIGFITFDSTIHFYGL----------------------QESLS------QPQMLIVSDIEDVFIPMPEN-LLVNLNESK- 592
Cdd:PLN00162 160 -VGLITFGTHVHVHELgfsecsksyvfrgnkevskdqiLEQLGlggkkrRPAGGGIAGARDGLSSSGVNrFLLPASECEf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 593 --ELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLM---SP-TGGRMSVFQTQLPTLGVGAL--KPREEP--NHRSSAK 662
Cdd:PLN00162 239 tlNSALEELQKDPWPVPPGHRPARCTGAALSVAAGLLgacVPgTGARIMAFVGGPCTEGPGAIvsKDLSEPirSHKDLDK 318
|
330 340 350
....*....|....*....|....*....|
gi 160331913 663 DI--HMTPSTDFYKKLALDCSGQQVAVDLF 690
Cdd:PLN00162 319 DAapYYKKAVKFYEGLAKQLVAQGHVLDVF 348
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
387-862 |
1.17e-16 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 85.32 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 387 RCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVSFLDQRR-WKCNLCYRVNDVPEEf 465
Cdd:COG5047 13 RLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHIDERNQsWICPFCNQRNTLPPQ- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 466 lYNPLTRVYGEPhrRPEVQNATIEFMAPseymlRPPQ-PPVYLFVFDVshnAVETGYLNSVCQSLLDNLDLLPGNTRtkI 544
Cdd:COG5047 92 -YRDISNANLPL--ELLPQSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEAL--V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 545 GFITFDSTIHF----------------------YGLQESLSQPQML----IVSDIEDVFIPMPENLLVNLNESKELVQDL 598
Cdd:COG5047 159 GLITYGTSIQVhelnaenhrrsyvfsgnkeytkENLQELLALSKPTksggFESKISGIGQFASSRFLLPTQQCEFKLLNI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 599 LKTL---PQMFTKTLETQSALGPALQAAFKLMS----PTGGRMSVFQTQLPTLGVGALKPRE--EP----NHRSSAKDIH 665
Cdd:COG5047 239 LEQLqpdPWPVPAGKRPLRCTGSALNIASSLLEqcfpNAGCHIVLFAGGPCTVGPGTVVSTElkEPmrshHDIESDSAQH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 666 MTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYhhqhnpvQVQKLQKELQRYLTR---- 741
Cdd:COG5047 319 SKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSF-------TTSIFKQSFQRIFNRdseg 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 742 --KIGFEAVMRIRCTKGLSIHTFHGN---------------FFVRSTDLLSLPNVNPDAGYAV------QMSVEESLTDT 798
Cdd:COG5047 392 ylKMGFNANMEVKTSKNLKIKGLIGHavsvkkkannisdseIGIGATNSWKMASLSPKSNYALyfeialGAASGSAQRPA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 160331913 799 Q-LVSFQSalLYTSSKGERRIRVHTLCLPVVSTLNDVFLGA-DVQAISGLLANMAVDRSMTASLSD 862
Cdd:COG5047 472 EaYIQFIT--TYQHSSGTYRIRVTTVARMFTDGGLPKINRSfDQEAAAVFMARIAAFKAETEDIID 535
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
428-464 |
6.78e-16 |
|
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is found to be zinc binding domain.
Pssm-ID: 461437 [Multi-domain] Cd Length: 38 Bit Score: 72.09 E-value: 6.78e-16
10 20 30
....*....|....*....|....*....|....*...
gi 160331913 428 IVRCRSCRTYINPFVSFLDQ-RRWKCNLCYRVNDVPEE 464
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
964-1039 |
7.08e-11 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 59.24 E-value: 7.08e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 160331913 964 TIPQPPILQLSVEKLSRDGAFLMDAGSVLMLWVGKNctQNFLSQVLGVQNYASIPQPM-TDLPELDT-PESARIIAFI 1039
Cdd:pfam00626 1 KFVLPPPVPLSQESLNSGDCYLLDNGFTIFLWVGKG--SSLLEKLFAALLAAQLDDDErFPLPEVIRvPQGKEPARFL 76
|
|
| Sec23-like |
cd01478 |
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
501-690 |
8.46e-07 |
|
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
Pssm-ID: 238755 [Multi-domain] Cd Length: 267 Bit Score: 51.60 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 501 PQPPVYLFVFDVSHNAVETGYLNSvcqSLLDNLDLLPGNTRtkIGFITFDSTIHFY------------------------ 556
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKE---SLIMSLSLLPPNAL--VGLITFGTMVQVHelgfeecsksyvfrgnkdytakqi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 557 ----GLQESLSQPQMLIVSDIEDVFIPMPEN-LLVNLNESKELVQDLLKTL---PQMFTKTLETQSALGPALQAAFKLMS 628
Cdd:cd01478 76 qdmlGLGGPAMRPSASQHPGAGNPLPSAAASrFLLPVSQCEFTLTDLLEQLqpdPWPVPAGHRPLRCTGVALSIAVGLLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160331913 629 P----TGGRMSVFQTQLPTLGVGALKPREEPNHRSSAKDI------HMTPSTDFYKKLALDCSGQQVAVDLF 690
Cdd:cd01478 156 AcfpnTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIdkdnakYYKKAVKFYDSLAKRLAANGHAVDIF 227
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
55-159 |
9.14e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 40.14 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160331913 55 PGSYPHPIPAK--TLNPVSGQSNY---GGSQGSGQTLNRPpvASNPVTPSLHSGPAPR--------MPLPASQNPATTPM 121
Cdd:pfam03154 286 PSHMQHPVPPQpfPLTPQSSQSQVppgPSPAAPGQSQQRI--HTPPSQSQLQSQQPPReqplppapLSMPHIKPPPTTPI 363
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 160331913 122 PS----------------SSFLPEANLPPPLNWQynyPSTASQTNHCPRASSQP 159
Cdd:pfam03154 364 PQlpnpqshkhpphlsgpSPFQMNSNLPPPPALK---PLSSLSTHHPPSAHPPP 414
|
|
| |
