|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
295-1090 |
1.52e-179 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 546.70 E-value: 1.52e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 295 PGYQnSAPPVAGMPPPSLSYPSgpQAFTQTPLGANHLTASMSglslhpeglrvvnllqernmlpstPLQPPVPNLLEDIQ 374
Cdd:COG5028 92 PYGG-SMADGTAPKPTNPLVPV--DLFEDQPPPISDLFLPPP------------------------PIVPPLTTNFVGSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 375 KLNCNPELFRCTLTSVPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVNFLDQ-RRWKC 449
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRC 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 450 NLCYRVNDVPEEFmYNPLTRV--YGEPHKRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAIETGYLNSVCQSLL 527
Cdd:COG5028 225 NICRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 528 DNLDLLPG-NTRTKIGFITFDSTIHFYSLQEGLSQpQMLIVSDIDDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTK 605
Cdd:COG5028 304 ENLDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQD 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 606 TLETQSALGPALQAAFKLISPTGGRMSVFQTQLPTLGVGALKPREEPNQRssakeiHLTPSTDFYKKLALDCSGQQAAVD 685
Cdd:COG5028 383 NKSPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVD 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 686 LFLLSGQYSDLASLGCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELHRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFV 765
Cdd:COG5028 457 LFLTSEDYIDVATLSHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 766 RSTDLLSLPNVNPDAGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNEVFLGADVQAISGLLA 845
Cdd:COG5028 536 RSSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 846 NMAVDRSVTASLSDARDALVNAVIDSLSAYRSSVLSGQQPGLMV-PFSLRLFPLFVLALLKQKSFQTGtSIRLDERIFAM 924
Cdd:COG5028 615 KKASTKALNSSLKEARVLINKSMVDILKAYKKELVKSNTSTQLPlPANLKLLPLLMLALLKSSAFRSG-STPSDIRISAL 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 925 CQVKSQPLVHLMLTTHPSLYRVDNLSDEGALNINDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSLLMLWVGRNCSQNFLS 1003
Cdd:COG5028 694 NRLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQ 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 1004 QVLGVQNYASIPQTMTDLPELDTPESARIAAFISWLREQRPFF-PVLYVIRE--ESLMKAAFLQSLVEDRTESALSYYEF 1080
Cdd:COG5028 772 DLFGVDSLSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDStLPLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDY 851
|
810
....*....|
gi 85687567 1081 LLHIQQQVNK 1090
Cdd:COG5028 852 LQILHEKIKS 861
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
498-740 |
2.19e-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: 2.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIP 576
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 577 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLISPTGGRMSVFQTQLPTLGVGALKPREEPNQRS 656
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 657 SAKE-IHLTPSTDFYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELHRY 735
Cdd:cd01479 161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239
|
....*
gi 85687567 736 LTRKI 740
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
498-736 |
1.23e-104 |
|
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: 327.67 E-value: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 578 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLI--SPTGGRMSVFQTQLPTLGV-GALKPREEPNQ 654
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 655 RSSAKE-IHLTPSTD-FYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 732
Cdd:pfam04811 161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 85687567 733 HRYL 736
Cdd:pfam04811 238 QRYF 241
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
463-1090 |
3.72e-49 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 191.06 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 463 MYNPLTRVYGEPHKRPEVQNATIEFMAPSEYMLrppqPPVYLFVFDVSHNAIetgyLNSVCQSLLDNLDLLPGNTR---T 539
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNSFLAKYPQVKNML----PPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqT 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 540 KIGFITFDSTIHFYSLQEGLSQP-------------QMLIVSDIDDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTK 605
Cdd:PTZ00395 991 KIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTT 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 606 TLETQSALGPALQAAFKLISPTGGRMSV--FQTQLPTLGVGALKPREEPNQRSSAKeihlTPSTDFYKKLALDCSGQQAA 683
Cdd:PTZ00395 1071 MQSYGSCGNSALKIAMDMLKERNGLGSIcmFYTTTPNCGIGAIKELKKDLQENFLE----VKQKIFYDSLLLDLYAFNIS 1146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 684 VDLFLLSGQYSDLA--SLGCISRYSAGSVYYYPSYHHQHNpvqVQKLQKELHRYLTRK-IGFEAVMRIRCTKGLSIHTF- 759
Cdd:PTZ00395 1147 VDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLf 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 760 --HGNF-FVRSTDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNEVFLGAD 836
Cdd:PTZ00395 1224 ccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTD 1303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 837 VQAisglLANMAVDRSVTASLSDarDALVNAVIDSLSA----YR----SSVLSGQqpgLMVPFSLRLFPLFVLALLKQKS 908
Cdd:PTZ00395 1304 AEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRincaSSAHSGQ---LILPDTLKLLPLFTSSLLKHNV 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 909 fqTGTSIRLDERIFAMCQVKSQPLVHLMLTTHPSLY--RVDNLSDE-GALNIND-----RTIPQppilqlSVEKLSRDGA 980
Cdd:PTZ00395 1375 --TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDdlfipKTIPS------SAEKIYSNGI 1446
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 981 FLMDAGSLLMLWVGRNCSQNFLSQVLGvqnyaSIP--QTMTDLPELDTPESARIAAFISWLREQRPF--FPVLYVIREES 1056
Cdd:PTZ00395 1447 YLLDACTHFYLYFGFHSDANFAKEIVG-----DIPteKNAHELNLTDTPNAQKVQRIIKNLSRIHHFnkYVPLVMVAPKS 1521
|
650 660 670
....*....|....*....|....*....|....
gi 85687567 1057 LMKAAFLQSLVEDRTESALSYYEFLLHIQQQVNK 1090
Cdd:PTZ00395 1522 NEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
5-367 |
7.92e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 5 RIPAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGsyPRPMPAKTlnpfsaqsnyggsqgsgq 84
Cdd:PHA03247 2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--PTPEPAPH------------------ 2713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 85 tlnsPLVTSGPVLPSLHSGPVPRMPLPTSqnPAATPMPSGSFLPGANPPPPlnwqynypsTGPQTNHFPHVAPPTLP-GN 163
Cdd:PHA03247 2714 ----ALVSATPLPPGPAAARQASPALPAA--PAPPAVPAGPATPGGPARPA---------RPPTTAGPPAPAPPAAPaAG 2778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 164 PNLTADHQYVSSGDPALQTSFKKPGSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQKTPPRAAPPPSFNSAVNQ 243
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 244 EG-ITSNANNGSTAAHNTYDEIEGGGFLATPQLVNQ-NPKTSRSVGSAYPSLPPGYQNSAPPVAGMPPPSLSYPSGPQAF 321
Cdd:PHA03247 2859 GGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 85687567 322 TQTPLGANHLTASMSGLSLHPEGLRVVNLLQERNMLPSTPLQPPVP 367
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
16-180 |
1.58e-04 |
|
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: 45.91 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 16 LQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGSYPRPMPAKTLNPFSAQSnyggsqgSGQTLNSPLvtsgp 95
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQ-------QTPTLHPQR----- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 96 vLPSLHSG--PVPRMPLPTSQNPAATPMPSgsfLPGANPPPPLNWQynypsTGPqtNHFPHVAPPTLPGNPNLTADHQYV 173
Cdd:pfam03154 242 -LPSPHPPlqPMTQPPPPSQVSPQPLPQPS---LHGQMPPMPHSLQ-----TGP--SHMQHPVPPQPFPLTPQSSQSQVP 310
|
....*..
gi 85687567 174 SSGDPAL 180
Cdd:pfam03154 311 PGPSPAA 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5028 |
COG5028 |
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking ... |
295-1090 |
1.52e-179 |
|
Vesicle coat complex COPII, subunit SEC24/subunit SFB2/subunit SFB3 [Intracellular trafficking and secretion];
Pssm-ID: 227361 [Multi-domain] Cd Length: 861 Bit Score: 546.70 E-value: 1.52e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 295 PGYQnSAPPVAGMPPPSLSYPSgpQAFTQTPLGANHLTASMSglslhpeglrvvnllqernmlpstPLQPPVPNLLEDIQ 374
Cdd:COG5028 92 PYGG-SMADGTAPKPTNPLVPV--DLFEDQPPPISDLFLPPP------------------------PIVPPLTTNFVGSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 375 KLNCNPELFRCTLTSVPQTQALLNKAKLPLGLLLHPFKDLV----QLPVVTSSTIVRCRSCRTYINPFVNFLDQ-RRWKC 449
Cdd:COG5028 145 QSNCSPKYVRSTMYAIPETNDLLKKSKIPFGLVIRPFLELYpeedPVPLVEDGSIVRCRRCRSYINPFVQFIEQgRKWRC 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 450 NLCYRVNDVPEEFmYNPLTRV--YGEPHKRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAIETGYLNSVCQSLL 527
Cdd:COG5028 225 NICRSKNDVPEGF-DNPSGPNdpRSDRYSRPELKSGVVDFLAPKEYSLRQPPPPVYVFLIDVSFEAIKNGLVKAAIRAIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 528 DNLDLLPG-NTRTKIGFITFDSTIHFYSLQEGLSQpQMLIVSDIDDVFIPMPENLLV-NLNESKELVQDLLKTLPQMFTK 605
Cdd:COG5028 304 ENLDQIPNfDPRTKIAIICFDSSLHFFKLSPDLDE-QMLIVSDLDEPFLPFPSGLFVlPLKSCKQIIETLLDRVPRIFQD 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 606 TLETQSALGPALQAAFKLISPTGGRMSVFQTQLPTLGVGALKPREEPNQRssakeiHLTPSTDFYKKLALDCSGQQAAVD 685
Cdd:COG5028 383 NKSPKNALGPALKAAKSLIGGTGGKIIVFLSTLPNMGIGKLQLREDKESS------LLSCKDSFYKEFAIECSKVGISVD 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 686 LFLLSGQYSDLASLGCISRYSAGSVYYYPSYHhQHNPVQVQKLQKELHRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFV 765
Cdd:COG5028 457 LFLTSEDYIDVATLSHLCRYTGGQTYFYPNFS-ATRPNDATKLANDLVSHLSMEIGYEAVMRVRCSTGLRVSSFYGNFFN 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 766 RSTDLLSLPNVNPDAGYAVQMSVEESLTdTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNEVFLGADVQAISGLLA 845
Cdd:COG5028 536 RSSDLCAFSTMPRDTSLLVEFSIDEKLM-TSDVYFQVALLYTLNDGERRIRVVNLSLPTSSSIREVYASADQLAIACILA 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 846 NMAVDRSVTASLSDARDALVNAVIDSLSAYRSSVLSGQQPGLMV-PFSLRLFPLFVLALLKQKSFQTGtSIRLDERIFAM 924
Cdd:COG5028 615 KKASTKALNSSLKEARVLINKSMVDILKAYKKELVKSNTSTQLPlPANLKLLPLLMLALLKSSAFRSG-STPSDIRISAL 693
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 925 CQVKSQPLVHLMLTTHPSLYRVDNLSDEGALNINDRTI-PQPpiLQLSVEKLSRDGAFLMDAGSLLMLWVGRNCSQNFLS 1003
Cdd:COG5028 694 NRLTSLPLKQLMRNIYPTLYALHDMPIEAGLPDEGLLVlPSP--INATSSLLESGGLYLIDTGQKIFLWFGKDAVPSLLQ 771
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 1004 QVLGVQNYASIPQTMTDLPELDTPESARIAAFISWLREQRPFF-PVLYVIRE--ESLMKAAFLQSLVEDRTESALSYYEF 1080
Cdd:COG5028 772 DLFGVDSLSDIPSGKFTLPPTGNEFNERVRNIIGELRSVNDDStLPLVLVRGggDPSLRLWFFSTLVEDKTLNIPSYLDY 851
|
810
....*....|
gi 85687567 1081 LLHIQQQVNK 1090
Cdd:COG5028 852 LQILHEKIKS 861
|
|
| Sec24-like |
cd01479 |
Sec24-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the ... |
498-740 |
2.19e-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: 2.19e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGN-TRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIP 576
Cdd:cd01479 1 PQPAVYVFLIDVSYNAIKSGLLATACEALLSNLDNLPGDdPRTRVGFITFDSTLHFFNLKSSLEQPQMMVVSDLDDPFLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 577 MPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLISPTGGRMSVFQTQLPTLGVGALKPREEPNQRS 656
Cdd:cd01479 81 LPDGLLVNLKESRQVIEDLLDQIPEMFQDTKETESALGPALQAAFLLLKETGGKIIVFQSSLPTLGAGKLKSREDPKLLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 657 SAKE-IHLTPSTDFYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSyHHQHNPVQVQKLQKELHRY 735
Cdd:cd01479 161 TDKEkQLLQPQTDFYKKLALECVKSQISVDLFLFSNQYVDVATLGCLSRLTGGQVYYYPS-FNFSAPNDVEKLVNELARY 239
|
....*
gi 85687567 736 LTRKI 740
Cdd:cd01479 240 LTRKI 244
|
|
| Sec23_trunk |
pfam04811 |
Sec23/Sec24 trunk domain; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
498-736 |
1.23e-104 |
|
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: 327.67 E-value: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:pfam04811 1 PQPPVFLFVIDVSYNAIKSGLLAALKESLLQSLDLLPGDPRARVGFITFDSTVHFFNLGSSLRQPQMLVVSDLQDMFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 578 PENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLI--SPTGGRMSVFQTQLPTLGV-GALKPREEPNQ 654
Cdd:pfam04811 81 PDRFLVPLSECRFVLEDLLEQLPPMFPVTKRPERCLGPALQAAFLLLkaAFTGGKIMVFQGGLPTVGPgGKLKSRLDESH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 655 RSSAKE-IHLTPSTD-FYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHnpvQVQKLQKEL 732
Cdd:pfam04811 161 HGTDKEkAKLVKKADkFYKSLAKECVKQGHSVDLFAFSLDYVDVATLGQLSRLTGGQVYLYPSFQADV---DGSKFKQDL 237
|
....
gi 85687567 733 HRYL 736
Cdd:pfam04811 238 QRYF 241
|
|
| trunk_domain |
cd01468 |
trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi ... |
498-734 |
1.13e-100 |
|
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: 317.26 E-value: 1.13e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYSLQEGLSQPQMLIVSDIDDVFIPM 577
Cdd:cd01468 1 PQPPVFVFVIDVSYEAIKEGLLQALKESLLASLDLLPGDPRARVGLITYDSTVHFYNLSSDLAQPKMYVVSDLKDVFLPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 578 PENLLVNLNESKELVQDLLKTLPQMFTK--TLETQSALGPALQAAFKLISPT--GGRMSVFQTQLPTLGVGALKPREEPN 653
Cdd:cd01468 81 PDRFLVPLSECKKVIHDLLEQLPPMFWPvpTHRPERCLGPALQAAFLLLKGTfaGGRIIVFQGGLPTVGPGKLKSREDKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 654 QRSSAKE-IHLTPSTDFYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHqhnPVQVQKLQKEL 732
Cdd:cd01468 161 PIRSHDEaQLLKPATKFYKSLAKECVKSGICVDLFAFSLDYVDVATLKQLAKSTGGQVYLYDSFQA---PNDGSKFKQDL 237
|
..
gi 85687567 733 HR 734
Cdd:cd01468 238 QR 239
|
|
| PTZ00395 |
PTZ00395 |
Sec24-related protein; Provisional |
463-1090 |
3.72e-49 |
|
Sec24-related protein; Provisional
Pssm-ID: 185594 [Multi-domain] Cd Length: 1560 Bit Score: 191.06 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 463 MYNPLTRVYGEPHKRPEVQNATIEFMAPSEYMLrppqPPVYLFVFDVSHNAIetgyLNSVCQSLLDNLDLLPGNTR---T 539
Cdd:PTZ00395 919 MKNLICEKNGEPDSAKIRRNSFLAKYPQVKNML----PPYFVFVVECSYNAI----YNNITYTILEGIRYAVQNVKcpqT 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 540 KIGFITFDSTIHFYSLQEGLSQP-------------QMLIVSDIDDVFIPMP-ENLLVNLNESKELVQDLLKTLPQMFTK 605
Cdd:PTZ00395 991 KIAIITFNSSIYFYHCKGGKGVSgeegdggggsgnhQVIVMSDVDDPFLPLPlEDLFFGCVEEIDKINTLIDTIKSVSTT 1070
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 606 TLETQSALGPALQAAFKLISPTGGRMSV--FQTQLPTLGVGALKPREEPNQRSSAKeihlTPSTDFYKKLALDCSGQQAA 683
Cdd:PTZ00395 1071 MQSYGSCGNSALKIAMDMLKERNGLGSIcmFYTTTPNCGIGAIKELKKDLQENFLE----VKQKIFYDSLLLDLYAFNIS 1146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 684 VDLFLLSGQYSDLA--SLGCISRYSAGSVYYYPSYHHQHNpvqVQKLQKELHRYLTRK-IGFEAVMRIRCTKGLSIHTF- 759
Cdd:PTZ00395 1147 VDIFIISSNNVRVCvpSLQYVAQNTGGKILFVENFLWQKD---YKEIYMNIMDTLTSEdIAYCCELKLRYSHHMSVKKLf 1223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 760 --HGNF-FVRSTDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNEVFLGAD 836
Cdd:PTZ00395 1224 ccNNNFnSIISVDTIKIPKIRHDQTFAFLLNYSDISESKKQIYFQCACIYTNLWGDRFVRLHTTHMNLTSSLSTVFRYTD 1303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 837 VQAisglLANMAVDRSVTASLSDarDALVNAVIDSLSA----YR----SSVLSGQqpgLMVPFSLRLFPLFVLALLKQKS 908
Cdd:PTZ00395 1304 AEA----LMNILIKQLCTNILHN--DNYSKIIIDNLAAilfsYRincaSSAHSGQ---LILPDTLKLLPLFTSSLLKHNV 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 909 fqTGTSIRLDERIFAMCQVKSQPLVHLMLTTHPSLY--RVDNLSDE-GALNIND-----RTIPQppilqlSVEKLSRDGA 980
Cdd:PTZ00395 1375 --TKKEILHDLKVYSLIKLLSMPIISSLLYVYPVMYviHIKGKTNEiDSMDVDDdlfipKTIPS------SAEKIYSNGI 1446
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 981 FLMDAGSLLMLWVGRNCSQNFLSQVLGvqnyaSIP--QTMTDLPELDTPESARIAAFISWLREQRPF--FPVLYVIREES 1056
Cdd:PTZ00395 1447 YLLDACTHFYLYFGFHSDANFAKEIVG-----DIPteKNAHELNLTDTPNAQKVQRIIKNLSRIHHFnkYVPLVMVAPKS 1521
|
650 660 670
....*....|....*....|....*....|....
gi 85687567 1057 LMKAAFLQSLVEDRTESALSYYEFLLHIQQQVNK 1090
Cdd:PTZ00395 1522 NEEEHLISLCVEDKADKEYSYVNFLCFIHKLVHK 1555
|
|
| Sec23_BS |
pfam08033 |
Sec23/Sec24 beta-sandwich domain; |
741-825 |
2.30e-32 |
|
Sec23/Sec24 beta-sandwich domain;
Pssm-ID: 429794 [Multi-domain] Cd Length: 86 Bit Score: 120.72 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 741 GFEAVMRIRCTKGLSIHTFHGNFFVRS-TDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHT 819
Cdd:pfam08033 1 GFNAVLRVRTSKGLKVSGFIGNFVSRSsGDTWKLPSLDPDTSYAFEFDIDEPLPNGSNAYIQFALLYTHSSGERRIRVTT 80
|
....*.
gi 85687567 820 LCLPVV 825
Cdd:pfam08033 81 VALPVT 86
|
|
| Sec23_helical |
pfam04815 |
Sec23/Sec24 helical domain; COPII-coated vesicles carry proteins from the endoplasmic ... |
836-937 |
2.57e-32 |
|
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: 121.07 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 836 DVQAISGLLANMAVDRSVTASLSDARDALVNAVIDSLSAYRSSVLSGQQPG-LMVPFSLRLFPLFVLALLKQKSFQTGTS 914
Cdd:pfam04815 1 DQEAIAVLLAKKAVEKALSSSLSDAREALDNKLVDILAAYRKYCASSSSPGqLILPESLKLLPLYMLALLKSPALRGGNS 80
|
90 100
....*....|....*....|...
gi 85687567 915 IRLDERIFAMCQVKSQPLVHLML 937
Cdd:pfam04815 81 SPSDERAYARHLLLSLPVEELLL 103
|
|
| zf-Sec23_Sec24 |
pfam04810 |
Sec23/Sec24 zinc finger; COPII-coated vesicles carry proteins from the endoplasmic reticulum ... |
425-461 |
3.95e-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: 72.86 E-value: 3.95e-16
10 20 30
....*....|....*....|....*....|....*...
gi 85687567 425 IVRCRSCRTYINPFVNFLDQ-RRWKCNLCYRVNDVPEE 461
Cdd:pfam04810 1 PVRCRRCRAYLNPFCQFDFGgKKWTCNFCGTRNPVPPE 38
|
|
| PLN00162 |
PLN00162 |
transport protein sec23; Provisional |
384-555 |
7.81e-16 |
|
transport protein sec23; Provisional
Pssm-ID: 215083 [Multi-domain] Cd Length: 761 Bit Score: 82.68 E-value: 7.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 384 RCTLTSVPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIvRCRSCRTYINPF--VNFlDQRRWKCNLCYRVNDVPEE 461
Cdd:PLN00162 13 RMSWNVWPSSKIEASKCVIPLAALYTPLKPLPELPVLPYDPL-RCRTCRAVLNPYcrVDF-QAKIWICPFCFQRNHFPPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 462 FMYNPLTRVYGE--PhkrpevQNATIEFMAPSEYMLRPPqPPVYLFVFDVSHNAIETGYLNSvcqSLLDNLDLLPGNTRt 539
Cdd:PLN00162 91 YSSISETNLPAElfP------QYTTVEYTLPPGSGGAPS-PPVFVFVVDTCMIEEELGALKS---ALLQAIALLPENAL- 159
|
170
....*....|....*.
gi 85687567 540 kIGFITFDSTIHFYSL 555
Cdd:PLN00162 160 -VGLITFGTHVHVHEL 174
|
|
| SEC23 |
COG5047 |
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion]; |
384-859 |
2.20e-15 |
|
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion];
Pssm-ID: 227380 [Multi-domain] Cd Length: 755 Bit Score: 81.08 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 384 RCTLTSVPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVNFLDQRR-WKCNLCYRVNDVPEEF 462
Cdd:COG5047 13 RLTWNVFPATRGDATRTVIPIACLYTPLHEDDALTVNYYEPVKCTAPCKAVLNPYCHIDERNQsWICPFCNQRNTLPPQY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 463 MYNPLTRVYGEPHKrpevQNATIEFMAPseymlRPPQ-PPVYLFVFDVshnAIETGYLNSVCQSLLDNLDLLPGNTRtkI 541
Cdd:COG5047 93 RDISNANLPLELLP----QSSTIEYTLS-----KPVIlPPVFFFVVDA---CCDEEELTALKDSLIVSLSLLPPEAL--V 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 542 GFITFDSTIHF----------------------YSLQE--GLSQPQMLIV--SDIDDVFIPMPENLLVNLNESKELVQDL 595
Cdd:COG5047 159 GLITYGTSIQVhelnaenhrrsyvfsgnkeytkENLQEllALSKPTKSGGfeSKISGIGQFASSRFLLPTQQCEFKLLNI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 596 LKTL---PQMFTKTLETQSALGPALQAAFKLIS----PTGGRMSVFQTQLPTLGVGALKPRE--EPnQRS-----SAKEI 661
Cdd:COG5047 239 LEQLqpdPWPVPAGKRPLRCTGSALNIASSLLEqcfpNAGCHIVLFAGGPCTVGPGTVVSTElkEP-MRShhdieSDSAQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 662 HLTPSTDFYKKLALDCSGQQAAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHNPVQVQK-LQKELHRYLtrKI 740
Cdd:COG5047 318 HSKKATKFYKGLAERVANQGHALDIFAGCLDQIGIMEMEPLTTSTGGALVLSDSFTTSIFKQSFQRiFNRDSEGYL--KM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 741 GFEAVMRIRCTKGLSIHTFHGN---------------FFVRSTDLLSLPNVNPDAGYAV------QMSVEESLTDTQ-LV 798
Cdd:COG5047 396 GFNANMEVKTSKNLKIKGLIGHavsvkkkannisdseIGIGATNSWKMASLSPKSNYALyfeialGAASGSAQRPAEaYI 475
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85687567 799 SFQSalLYTSSKGERRIRVHTLCLPVVSTLNEVFLGA-DVQAISGLLANMAVDRSVTASLSD 859
Cdd:COG5047 476 QFIT--TYQHSSGTYRIRVTTVARMFTDGGLPKINRSfDQEAAAVFMARIAAFKAETEDIID 535
|
|
| Gelsolin |
pfam00626 |
Gelsolin repeat; |
961-1036 |
3.67e-11 |
|
Gelsolin repeat;
Pssm-ID: 395501 [Multi-domain] Cd Length: 76 Bit Score: 60.01 E-value: 3.67e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 85687567 961 TIPQPPILQLSVEKLSRDGAFLMDAGSLLMLWVGRNcsQNFLSQVLGVQNYASIPQTM-TDLPELDT-PESARIAAFI 1036
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 ... |
498-687 |
4.55e-05 |
|
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: 46.60 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 498 PQPPVYLFVFDVSHNAIETGYLNSvcqSLLDNLDLLPGNTRtkIGFITFDSTIHFYSL---------------------- 555
Cdd:cd01478 1 TSPPVFLFVVDTCMDEEELDALKE---SLIMSLSLLPPNAL--VGLITFGTMVQVHELgfeecsksyvfrgnkdytakqi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 556 --QEGLSQPQM----LIVSDIDDVFIPMPEN-LLVNLNESKELVQDLLKTL---PQMFTKTLETQSALGPALQAAFKLIS 625
Cdd:cd01478 76 qdMLGLGGPAMrpsaSQHPGAGNPLPSAAASrFLLPVSQCEFTLTDLLEQLqpdPWPVPAGHRPLRCTGVALSIAVGLLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 85687567 626 P----TGGRMSVFQTQLPTLGVGALKPREEPNQRSSAKEI------HLTPSTDFYKKLALDCSGQQAAVDLF 687
Cdd:cd01478 156 AcfpnTGARIMLFAGGPCTVGPGAVVSTELKDPIRSHHDIdkdnakYYKKAVKFYDSLAKRLAANGHAVDIF 227
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
5-367 |
7.92e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.24 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 5 RIPAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGsyPRPMPAKTlnpfsaqsnyggsqgsgq 84
Cdd:PHA03247 2654 DDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPP--PTPEPAPH------------------ 2713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 85 tlnsPLVTSGPVLPSLHSGPVPRMPLPTSqnPAATPMPSGSFLPGANPPPPlnwqynypsTGPQTNHFPHVAPPTLP-GN 163
Cdd:PHA03247 2714 ----ALVSATPLPPGPAAARQASPALPAA--PAPPAVPAGPATPGGPARPA---------RPPTTAGPPAPAPPAAPaAG 2778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 164 PNLTADHQYVSSGDPALQTSFKKPGSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQKTPPRAAPPPSFNSAVNQ 243
Cdd:PHA03247 2779 PPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 244 EG-ITSNANNGSTAAHNTYDEIEGGGFLATPQLVNQ-NPKTSRSVGSAYPSLPPGYQNSAPPVAGMPPPSLSYPSGPQAF 321
Cdd:PHA03247 2859 GGdVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRStESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 85687567 322 TQTPLGANHLTASMSGLSLHPEGLRVVNLLQERNMLPSTPLQPPVP 367
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
16-180 |
1.58e-04 |
|
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: 45.91 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 16 LQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGSYPRPMPAKTLNPFSAQSnyggsqgSGQTLNSPLvtsgp 95
Cdd:pfam03154 174 LQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQ-------QTPTLHPQR----- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 96 vLPSLHSG--PVPRMPLPTSQNPAATPMPSgsfLPGANPPPPLNWQynypsTGPqtNHFPHVAPPTLPGNPNLTADHQYV 173
Cdd:pfam03154 242 -LPSPHPPlqPMTQPPPPSQVSPQPLPQPS---LHGQMPPMPHSLQ-----TGP--SHMQHPVPPQPFPLTPQSSQSQVP 310
|
....*..
gi 85687567 174 SSGDPAL 180
Cdd:pfam03154 311 PGPSPAA 317
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
2-372 |
2.58e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.31 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 2 AQPRIPAARGAAASLQAQNGAASASGSPYTNGPVHNTlmSPQVsssqgydsqPPGSYPRPMPAKTLNPFSAQSNYGGSQG 81
Cdd:PHA03247 2734 ALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPA--PPAA---------PAAGPPRRLTRPAVASLSESRESLPSPW 2802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 82 SGQTLNSPLVTSGPVLPSlHSGPVPRMPLPTSQNPAATPMPSGSflpganPPPPLNWQYNYPSTGPQTNHFPHVAPPTLP 161
Cdd:PHA03247 2803 DPADPPAAVLAPAAALPP-AASPAGPLPPPTSAQPTAPPPPPGP------PPPSLPLGGSVAPGGDVRRRPPSRSPAAKP 2875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 162 GNPNltadHQYVSS-GDPALQTSFKKpgSALPLQNPPLPPTFQPGAPPGPPPAGGPPPSRGPAPQkTPPRAAPPPSFNSA 240
Cdd:PHA03247 2876 AAPA----RPPVRRlARPAVSRSTES--FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPP-PPPRPQPPLAPTTD 2948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 241 vnqegiTSNANNGSTAAHNTYDEIEGGGFLATPQLVNQNPKTSRSVGSayPSLPPGYQNSAPPVAGMpPPSLSY----PS 316
Cdd:PHA03247 2949 ------PAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPA--SSTPPLTGHSLSRVSSW-ASSLALheetDP 3019
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 85687567 317 GPQAFTQT---PLGANHLTASMSGLSlHPEGLRVVNLLQERNMLPSTPLQPPVPNLLED 372
Cdd:PHA03247 3020 PPVSLKQTlwpPDDTEDSDADSLFDS-DSERSDLEALDPLPPEPHDPFAHEPDPATPEA 3077
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
7-135 |
6.65e-04 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 85687567 7 PAARGAAASLQAQNGAASASGSPYTNGPVHNTLMSPQVSSSQGYDSQPPGSYPRPMPAKTLNPFSAQSNYGGSQGSGQTL 86
Cdd:PHA03307 334 ESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPR 413
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 85687567 87 NSPLVTSGPvlpslHSGPVPRMPLPtsqnpaatpMPSGSFLPGANPPPP 135
Cdd:PHA03307 414 PSPLDAGAA-----SGAFYARYPLL---------TPSGEPWPGSPPPPP 448
|
|
| |
