|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
84-340 |
2.55e-29 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 118.98 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200 92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200 162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238
|
250
....*....|....*..
gi 564382884 324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200 239 EDGTIRVWDLRTGECVQ 255
|
|
| ACE1-Sec16-like super family |
cl14807 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
547-741 |
5.88e-09 |
|
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site. The actual alignment was detected with superfamily member cd09233:
Pssm-ID: 449359 [Multi-domain] Cd Length: 314 Bit Score: 59.19 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 547 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 618
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 619 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 688
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 689 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 741
Cdd:cd09233 208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
781-1133 |
2.96e-08 |
|
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 781 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPGFIMHGNVVPnS 858
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPPSPSPAANEPD-P 2640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 859 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQYSFGTGGSA-VYRPQQPVAPP-----ASNAYPNA----PYVSPVASYSGQP 928
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRPRRRAARPtvgslTSLADPPPppptPEPAPHALVSATP 2720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 929 QMYTAQPASSPTSSSAPLPPPPSSGAsfqhgGPGAPPSSSAYALPPGTTG----TPPAASELPASQRTENQSFQDQSSVL 1004
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPA-----GPATPGGPARPARPPTTAGppapAPPAAPAAGPPRRLTRPAVASLSESR 2795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1005 EGPQNGWND------------------------PPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQ---PQGLQQQPS 1057
Cdd:PHA03247 2796 ESLPSPWDPadppaavlapaaalppaaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKP 2875
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564382884 1058 ASGPRSSHASFPQPHLAggqpfhgiQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPDEHL 1133
Cdd:PHA03247 2876 AAPARPPVRRLARPAVS--------RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
84-340 |
2.55e-29 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 118.98 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200 92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200 162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238
|
250
....*....|....*..
gi 564382884 324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200 239 EDGTIRVWDLRTGECVQ 255
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
5.18e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 106.15 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 564382884 329 RVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
547-741 |
5.88e-09 |
|
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.
Pssm-ID: 187750 [Multi-domain] Cd Length: 314 Bit Score: 59.19 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 547 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 618
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 619 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 688
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 689 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 741
Cdd:cd09233 208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
781-1133 |
2.96e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 781 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPGFIMHGNVVPnS 858
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPPSPSPAANEPD-P 2640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 859 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQYSFGTGGSA-VYRPQQPVAPP-----ASNAYPNA----PYVSPVASYSGQP 928
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRPRRRAARPtvgslTSLADPPPppptPEPAPHALVSATP 2720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 929 QMYTAQPASSPTSSSAPLPPPPSSGAsfqhgGPGAPPSSSAYALPPGTTG----TPPAASELPASQRTENQSFQDQSSVL 1004
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPA-----GPATPGGPARPARPPTTAGppapAPPAAPAAGPPRRLTRPAVASLSESR 2795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1005 EGPQNGWND------------------------PPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQ---PQGLQQQPS 1057
Cdd:PHA03247 2796 ESLPSPWDPadppaavlapaaalppaaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKP 2875
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564382884 1058 ASGPRSSHASFPQPHLAggqpfhgiQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPDEHL 1133
Cdd:PHA03247 2876 AAPARPPVRRLARPAVS--------RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
547-741 |
7.23e-08 |
|
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.
Pssm-ID: 432884 Cd Length: 279 Bit Score: 55.26 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 547 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 616
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 617 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGARLESEGdslLRTQACLCYICAgNVERLVACWTKAQDGSNP 688
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382884 689 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYANLLAAQGSIAAAL 741
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
746-1114 |
2.22e-06 |
|
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: 52.08 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 746 DNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTwSDRTPTA 825
Cdd:pfam03154 159 DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL-IQQTPTL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 826 LPSHPPAACPSDTQGGNPPPPGFI---------MHGNVVPnSPAPLPTSPGHMHSQP-----PPYPQPQPYQPAQQYSFG 891
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVspqplpqpsLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 892 TGGSAVYRPQQPVA--------PPASNAYPNAPYVSP---VASYSGQPQMYTAQPASSPTSSSAPLPpppssgasFQHGG 960
Cdd:pfam03154 317 APGQSQQRIHTPPSqsqlqsqqPPREQPLPPAPLSMPhikPPPTTPIPQLPNPQSHKHPPHLSGPSP--------FQMNS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 961 PGAPP------SSSAYALPPgtTGTPPAASELPASQRTENQSFQ----DQSSVLEGPQNGWNDPPALNRVPKKKKLPENf 1030
Cdd:pfam03154 389 NLPPPpalkplSSLSTHHPP--SAHPPPLQLMPQSQQLPPPPAQppvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQH- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1031 mPPVPITSPIMNPGGDPQPQGLQQQPS----ASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGA 1106
Cdd:pfam03154 466 -PFVPGGPPPITPPSGPPTSTSSAMPGiqppSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEP 544
|
....*...
gi 564382884 1107 PIGNTIQH 1114
Cdd:pfam03154 545 TVVNTPSH 552
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
4.55e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVVQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564382884 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRIRVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
292-332 |
7.58e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 35.37 E-value: 7.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 564382884 292 TGEVLYELPTNTQWCFDIQWCPRNPAVLSAaSFDGRIRVYS 332
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASG-SDDGTIKLWD 40
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
84-340 |
2.55e-29 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 118.98 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 84 DVSGVLIAGGENGNIILYDPSkiiagDKEVVIAQKDkHTGPVRALDVnIFQTNLVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 19 PDGKLLATGSGDGTIKVWDLE-----TGELLRTLKG-HTGPVRDVAA-SADGTYLASGSSDKTIRLWDLETGECVRTLTG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 164 KTQppeDISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRLpvVQM 243
Cdd:cd00200 92 HTS---YVSSVAFSPD-GRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAAS 323
Cdd:cd00200 162 WDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASGS 238
|
250
....*....|....*..
gi 564382884 324 FDGRIRVYSIMGGSIDG 340
Cdd:cd00200 239 EDGTIRVWDLRTGECVQ 255
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
2.11e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 107.81 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVVQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 564382884 324 FDGRIRVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
5.18e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 106.15 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 564382884 329 RVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
2.12e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 101.14 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvVQMWDL 246
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 247 RfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319 276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352
|
....*..
gi 564382884 327 RIRVYSI 333
Cdd:COG2319 353 TVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-338 |
3.85e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 94.59 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvVQMWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCG 280
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 564382884 281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRIRVYSIMGGSI 338
Cdd:COG2319 224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGEL 280
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
171-337 |
3.50e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 83.54 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDvATQMVLASEDDrlpVVQMWDLRfAS 250
Cdd:cd00200 12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 251 SPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRIRV 330
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161
|
....*..
gi 564382884 331 YSIMGGS 337
Cdd:cd00200 162 WDLRTGK 168
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
547-741 |
5.88e-09 |
|
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat complex plays an important role in vesicular traffic of newly synthezised proteins from the endoplasmatic reticulum (ER) to the Golgi apparatus by mediating the formation of transport vesicles. COPII consists of an outer coat, made up of the scaffold proteins Sec31 and Sec13, and the cargo adaptor complex, Sec23 and Sec24, which are recruited by the small GTPase Sar1. Sec16 is involved in the early steps of the assembly process. Sec16 forms elongated heterotetramers with Sec13, Sec13-(Sec16)2-Sec13. It interacts with Sec13 by insertion of a single beta-blade to close the six-bladded beta propeller of Sec13. In the same way Sec13 interacts with Sec31 and Nup145C, a nuclear pore protein, all of these contain a structurally related ancestral coatomer element 1 (ACE1). Sec16 is believed to be a key component in maintaining the integrity of the ER exit site.
Pssm-ID: 187750 [Multi-domain] Cd Length: 314 Bit Score: 59.19 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 547 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 618
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 619 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgarleseGDSLLRTQ----ACLCYICAGnverlvacwtkAQDGSNP 688
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG-----------VPLGPYP 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 689 LS-------LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYANLLAAQGSIAAAL 741
Cdd:cd09233 208 SSpsscllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
8.99e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 59.15 E-value: 8.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564382884 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvVQMWDLR 247
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPD-GRTLASGSADGT---VRLWDLA 402
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
781-1133 |
2.96e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 58.80 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 781 QPLPKGGPGPLAGHPQVsrvQSQQYYPQVRIAPTV--TTWSDRTPTALPShPPAACPSDTQGGNPPPPGFIMHGNVVPnS 858
Cdd:PHA03247 2566 RSVPPPRPAPRPSEPAV---TSRARRPDAPPQSARprAPVDDRGDPRGPA-PPSPLPPDTHAPDPPPPSPSPAANEPD-P 2640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 859 PAPLPTSPGHMHSQPPPYPQPQPYQPAQQYSFGTGGSA-VYRPQQPVAPP-----ASNAYPNA----PYVSPVASYSGQP 928
Cdd:PHA03247 2641 HPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSpPQRPRRRAARPtvgslTSLADPPPppptPEPAPHALVSATP 2720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 929 QMYTAQPASSPTSSSAPLPPPPSSGAsfqhgGPGAPPSSSAYALPPGTTG----TPPAASELPASQRTENQSFQDQSSVL 1004
Cdd:PHA03247 2721 LPPGPAAARQASPALPAAPAPPAVPA-----GPATPGGPARPARPPTTAGppapAPPAAPAAGPPRRLTRPAVASLSESR 2795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1005 EGPQNGWND------------------------PPALNRVPKKKKLPENFMPPVPITSPIMNPGGDPQ---PQGLQQQPS 1057
Cdd:PHA03247 2796 ESLPSPWDPadppaavlapaaalppaaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRrrpPSRSPAAKP 2875
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564382884 1058 ASGPRSSHASFPQPHLAggqpfhgiQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKKPIPDEHL 1133
Cdd:PHA03247 2876 AAPARPPVRRLARPAVS--------RSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
547-741 |
7.23e-08 |
|
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal region is the part that binds to Sec23, a COPII vesicle coat protein. This association is part of the transport vesicle coat structure.
Pssm-ID: 432884 Cd Length: 279 Bit Score: 55.26 E-value: 7.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 547 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 616
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 617 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGARLESEGdslLRTQACLCYICAgNVERLVACWTKAQDGSNP 688
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564382884 689 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYANLLAAQGSIAAAL 741
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
725-1100 |
8.55e-08 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 57.26 E-value: 8.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 725 SQYANLLAAQGSIAAALAFLPDNTNQPDIVQLRDRlCRAQGRsvPGQESSrssyegqplPKGGPGPLAGHPQVSRVQS-- 802
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGR--AAQASS---------PPQRPRRRAARPTVGSLTSla 2699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 803 QQYYPQVRIAPTVTTWSDRTPTAL-PSHPPAACPSDTQGGNPPPPGfimHGNVVPNSPAPLPT------SPGHMHSQPPP 875
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALVSATPLPPgPAAARQASPALPAAPAPPAVP---AGPATPGGPARPARppttagPPAPAPPAAPA 2776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 876 YPQPQPYQPAQQYSFGTGGSAVYRPQQPVAPPASNAYPNAPYVSPVASYSGQPQMYTAQPASSPTSSSAPLPPPPSsgas 955
Cdd:PHA03247 2777 AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPL---- 2852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 956 fqhGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTENQSFQDQSSVLEGPQNGWNDPPALNRVPKKKKLPENFMPPVP 1035
Cdd:PHA03247 2853 ---GGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564382884 1036 ITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQ---PFHGIQQPLAQTGMPPSFSKPNT 1100
Cdd:PHA03247 2930 QPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRvavPRFRVPQPAPSREAPASSTPPLT 2997
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
8.10e-07 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 52.34 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRIRVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 564382884 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
746-1114 |
2.22e-06 |
|
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: 52.08 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 746 DNTNQPDIVQLRDRLCRAQGRSVPGQESSRSSYEGQPLPKGGPGPLAGHPQVSRVQSQQYYPQVRIAPTVTTwSDRTPTA 825
Cdd:pfam03154 159 DSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTL-IQQTPTL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 826 LPSHPPAACPSDTQGGNPPPPGFI---------MHGNVVPnSPAPLPTSPGHMHSQP-----PPYPQPQPYQPAQQYSFG 891
Cdd:pfam03154 238 HPQRLPSPHPPLQPMTQPPPPSQVspqplpqpsLHGQMPP-MPHSLQTGPSHMQHPVppqpfPLTPQSSQSQVPPGPSPA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 892 TGGSAVYRPQQPVA--------PPASNAYPNAPYVSP---VASYSGQPQMYTAQPASSPTSSSAPLPpppssgasFQHGG 960
Cdd:pfam03154 317 APGQSQQRIHTPPSqsqlqsqqPPREQPLPPAPLSMPhikPPPTTPIPQLPNPQSHKHPPHLSGPSP--------FQMNS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 961 PGAPP------SSSAYALPPgtTGTPPAASELPASQRTENQSFQ----DQSSVLEGPQNGWNDPPALNRVPKKKKLPENf 1030
Cdd:pfam03154 389 NLPPPpalkplSSLSTHHPP--SAHPPPLQLMPQSQQLPPPPAQppvlTQSQSLPPPAASHPPTSGLHQVPSQSPFPQH- 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1031 mPPVPITSPIMNPGGDPQPQGLQQQPS----ASGPRSSHASFPQPHLAGGQPFHGIQQPLAQTGMPPSFSKPNTEGAPGA 1106
Cdd:pfam03154 466 -PFVPGGPPPITPPSGPPTSTSSAMPGiqppSSASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEP 544
|
....*...
gi 564382884 1107 PIGNTIQH 1114
Cdd:pfam03154 545 TVVNTPSH 552
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
4.55e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 203 PIIKVSdhsNRMHCSGLAWHPDVATQMVLASEDDrlpVVQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 564382884 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRIRVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| PHA03307 |
PHA03307 |
transcriptional regulator ICP4; Provisional |
784-1109 |
6.05e-03 |
|
transcriptional regulator ICP4; Provisional
Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 40.92 E-value: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 784 PKGGPGPLAGHPQVSrvqsqqyypqvriapTVTTWSDRTPTAL-PSHPPAACPSDTQGGNPPPPGFimhgnvVPNSPAPl 862
Cdd:PHA03307 71 PPPGPGTEAPANESR---------------STPTWSLSTLAPAsPAREGSPTPPGPSSPDPPPPTP------PPASPPP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 863 ptSPGHMHSQPPPYPQPQPYQPAQQYSFGTGGSAvyRPQQPVAPPASNAYPnAPYVSPVASYSGQPQmytaqpassptss 942
Cdd:PHA03307 129 --SPAPDLSEMLRPVGSPGPPPAASPPAAGASPA--AVASDAASSRQAALP-LSSPEETARAPSSPP------------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 943 saplPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTENQSFQDQSSVLEGPQNGWNDP-PALNRVP 1021
Cdd:PHA03307 191 ----AEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPrPAPITLP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564382884 1022 KKKKLPENFMPPVPITSPIMNPGGDPQPQGLQQQPSASGPRSSHASFPQPHLAGGQPfhgiqqplaqTGMPPSFSKPNTE 1101
Cdd:PHA03307 267 TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRE----------SSSSSTSSSSESS 336
|
....*...
gi 564382884 1102 GAPGAPIG 1109
Cdd:PHA03307 337 RGAAVSPG 344
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
292-332 |
7.58e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 35.37 E-value: 7.58e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 564382884 292 TGEVLYELPTNTQWCFDIQWCPRNPAVLSAaSFDGRIRVYS 332
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASG-SDDGTIKLWD 40
|
|
|