|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
8.44e-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: 105.88 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1318663329 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.29e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1318663329 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
572-766 |
1.73e-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: 60.73 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318663329 716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
792-1073 |
3.66e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 792 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 870
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 871 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 950
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 951 QHGGPGA--PPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFM--PPVPITSPIMNPSGDPQSQGLQQQPSTPG 1026
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1318663329 1027 PLSSHASFPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1073
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
769-1033 |
4.59e-09 |
|
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: 60.94 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 846
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 847 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 922
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 923 qmytaqQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAyalPPGTTGPqngwndppalnrVPKKKKMPenfMPPVPI 1002
Cdd:pfam03154 464 ------QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGP------------VPAAVSCP---LPPVQI 519
|
250 260 270
....*....|....*....|....*....|....*
gi 1318663329 1003 TSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 1033
Cdd:pfam03154 520 KEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
572-766 |
3.54e-07 |
|
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: 53.33 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663329 714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
894-1026 |
3.24e-04 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 44.80 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 894 PQQPVAPPASNAYPNTPYIS--PVASYSGQPQMYTAQQAssptsssaasFPPPSsgasfqhgGPGAPPSSSAYALPPgtt 971
Cdd:TIGR01628 383 RQLPMGSPMGGAMGQPPYYGqgPQQQFNGQPLGWPRMSM----------MPTPM--------GPGGPLRPNGLAPMN--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1318663329 972 gpQNGWNDPPALNRVPKKKKMPENFMPpvpitspimNPSGDPQSQGLQQQPSTPG 1026
Cdd:TIGR01628 442 --AVRAPSRNAQNAAQKPPMQPVMYPP---------NYQSLPLSQDLPQPQSTAS 485
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
13-332 |
8.44e-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: 105.88 E-value: 8.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1318663329 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.29e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1318663329 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.71e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.99 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 247 RfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319 276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352
|
....*..
gi 1318663329 327 RISVYSI 333
Cdd:COG2319 353 TVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-338 |
6.59e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.82 E-value: 6.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1318663329 281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGGSI 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 |
1.08e-16 |
|
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: 82.00 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDvATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200 12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 251 SPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161
|
....*..
gi 1318663329 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 ... |
572-766 |
1.73e-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: 60.73 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318663329 716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
3.32e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.31 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 1318663329 246 LR 247
Cdd:COG2319 401 LA 402
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
792-1073 |
3.66e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.49 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 792 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 870
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 871 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 950
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 951 QHGGPGA--PPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFM--PPVPITSPIMNPSGDPQSQGLQQQPSTPG 1026
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1318663329 1027 PLSSHASFPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1073
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
769-1033 |
4.59e-09 |
|
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: 60.94 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 846
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 847 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 922
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 923 qmytaqQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAyalPPGTTGPqngwndppalnrVPKKKKMPenfMPPVPI 1002
Cdd:pfam03154 464 ------QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGP------------VPAAVSCP---LPPVQI 519
|
250 260 270
....*....|....*....|....*....|....*
gi 1318663329 1003 TSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 1033
Cdd:pfam03154 520 KEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
788-1137 |
6.19e-09 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 60.41 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 788 AQGKPVSGQESSQSPYERQPLSK----GRPGPVAGHSQMPrvqtQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTApghm 863
Cdd:pfam09606 181 GQGQAGGMNGGQQGPMGGQMPPQmgvpGMPGPADAGAQMG----QQAQANGGMNPQQMGGAPNQVAMQQQQPQQQG---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 864 psqlPPYPQPQPYQPAQQYSFGTGGAA-AYRPQQPVAPPasnayPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFP 942
Cdd:pfam09606 253 ----QQSQLGMGINQMQQMPQGVGGGAgQGGPGQPMGPP-----GQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 943 PPSSGASFQHGGPGAPPSSSAYALPPGTTGPQN--GWNDPPALNRVPKKKKMPEnfmpPVPITSPI-MNPsgdPQSQGLQ 1019
Cdd:pfam09606 324 AAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNfgGLGANPMQRGQPGMMSSPS----PVPGQQVRqVTP---NQFMRQS 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 1020 QQPSTPGPLSSHASFPQQHLAGGQPF-HGVQQPLAQTG-MPPSFSKPNTEGaPGAPIGNTIQ---------HVQALPTEK 1088
Cdd:pfam09606 397 PQPSVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSqQPAQQRTIGQDS-PGGSLNTPGQsavnsplnpQEEQLYREK 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1318663329 1089 ---ITKKPIPEEHLILKTTfedliqrclssaTDPQTKRKLDDASKRLEFLYD 1137
Cdd:pfam09606 476 yrqLTKYIEPLKRMIAKME------------NDPGDIDKMNKMKRLLEILSN 515
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
806-1080 |
2.04e-07 |
|
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: 55.54 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 806 QPLSKGRPGPvaghsQMPRVQTQQYYPHGENPPPPGFIMQGNVI---PNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQY 882
Cdd:pfam03154 250 QPMTQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGPSHmqhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 883 SFGTGGAAAYRPQQPVA----PPASNAYPNT--PYISPVASY-SGQPQMYTAQQASSPTSSSAASFPPPS-----SGASF 950
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPReqplPPAPLSMPHIkpPPTTPIPQLpNPQSHKHPPHLSGPSPFQMNSNLPPPPalkplSSLST 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 951 QHGGPGAPPS----------SSAYALPPGTTGPQN----GWNDPP--ALNRVPKKKKMPEN-FMP--PVPITSPIMNPSG 1011
Cdd:pfam03154 405 HHPPSAHPPPlqlmpqsqqlPPPPAQPPVLTQSQSlpppAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITPPSGPPTS 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1318663329 1012 DPQSQGLQQQPSTpGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQH 1080
Cdd:pfam03154 485 TSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
572-766 |
3.54e-07 |
|
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: 53.33 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663329 714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
2.49e-06 |
|
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: 50.80 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 252 PLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 1318663329 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
790-1099 |
2.50e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 790 GKPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFimQGNVIPNPAAPL-----PTAPGHMP 864
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP--RRRAARPTVGSLtsladPPPPPPTP 2708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 865 SQLPpypqpQPYQPAQQYSFGTGGAAAYRPQQPVApPASNAYPNTPYISPVASYSGQPQMyTAQQASSPTSSSAASFPPP 944
Cdd:PHA03247 2709 EPAP-----HALVSATPLPPGPAAARQASPALPAA-PAPPAVPAGPATPGGPARPARPPT-TAGPPAPAPPAAPAAGPPR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 945 S----SGASFQHGGPGAPPSSSAYALPPGTTGPQNGWND--------PPALNRVPKKKKMPENFMPPVPITSPIMNPSGD 1012
Cdd:PHA03247 2782 RltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 1013 PQSQGLQQQPSTPGPLSSHAsfPQQHLAGGQPfhgVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKK 1092
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARP--PVRRLARPAV---SRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
....*..
gi 1318663329 1093 PIPEEHL 1099
Cdd:PHA03247 2937 PRPQPPL 2943
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
819-1098 |
4.06e-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: 51.31 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 819 HSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPqpqpyqpaqqysfgtggaaayrpQQPV 898
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQ-----------------------TQST 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 899 APPASnAYPNTPYISPVASYSGQPQMYTAQQassptsssaasfPPPSSGASFQhggpGAPPSSSAYALPPGTTGPQNGwn 978
Cdd:pfam03154 225 AAPHT-LIQQTPTLHPQRLPSPHPPLQPMTQ------------PPPPSQVSPQ----PLPQPSLHGQMPPMPHSLQTG-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 979 dppalnrvpkkkkmPENFMPPVPiTSPIMNPSGDPQSQGlqqqPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMP 1058
Cdd:pfam03154 286 --------------PSHMQHPVP-PQPFPLTPQSSQSQV----PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP 346
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1318663329 1059 PsfskpntegapgAPIgnTIQHVQALPTEKITKKPIPEEH 1098
Cdd:pfam03154 347 P------------APL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
890-1054 |
8.98e-05 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 46.95 E-value: 8.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 890 AAYRPQQPVAPPAsnaypntpyisPVASYSGQPQMYTAQQASSPTSssaasFPPPSSGASFQHGGPGAPPSSSAYALPPG 969
Cdd:pfam09770 201 AAMRAQAKKPAQQ-----------PAPAPAQPPAAPPAQQAQQQQQ-----FPPQIQQQQQPQQQPQQPQQHPGQGHPVT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 970 T-TGPQNGWNDPPALNRVPKKKKMPENfMPPVPI--TSPIMNPS--GDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQ- 1043
Cdd:pfam09770 265 IlQRPQSPQPDPAQPSIQPQAQQFHQQ-PPPVPVqpTQILQNPNrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQa 343
|
170
....*....|.
gi 1318663329 1044 PFHGVQQPLAQ 1054
Cdd:pfam09770 344 PIITHPQQLAQ 354
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
791-1070 |
2.31e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.46 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 791 KPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPY 870
Cdd:PRK10263 355 QPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 871 PQPQPYQPaqqysfgTGGAAAYRPQQPVAPPASNAYPNTPYISPVAsysgQPQMYTAQQASSPTSSSAasfPPPssgaSF 950
Cdd:PRK10263 435 APAPEQPV-------AGNAWQAEEQQSTFAPQSTYQTEQTYQQPAA----QEPLYQQPQPVEQQPVVE---PEP----VV 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 951 QHGGPGAPPSSSAYALPPGTTGPQN---GWNDPpalnrVPKKKKMPENFMPPVPITSPIMNP------SGDPQSQGLQQQ 1021
Cdd:PRK10263 497 EETKPARPPLYYFEEVEEKRAREREqlaAWYQP-----IPEPVKEPEPIKSSLKAPSVAAVPpveaaaAVSPLASGVKKA 571
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1318663329 1022 PSTPGPLSSHASfPQQHLAGGqpfhGVQQPLAQTGMPPSFSKPNTEGAP 1070
Cdd:PRK10263 572 TLATGAAATVAA-PVFSLANS----GGPRPQVKEGIGPQLPRPKRIRVP 615
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
894-1026 |
3.24e-04 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 44.80 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 894 PQQPVAPPASNAYPNTPYIS--PVASYSGQPQMYTAQQAssptsssaasFPPPSsgasfqhgGPGAPPSSSAYALPPgtt 971
Cdd:TIGR01628 383 RQLPMGSPMGGAMGQPPYYGqgPQQQFNGQPLGWPRMSM----------MPTPM--------GPGGPLRPNGLAPMN--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1318663329 972 gpQNGWNDPPALNRVPKKKKMPENFMPpvpitspimNPSGDPQSQGLQQQPSTPG 1026
Cdd:TIGR01628 442 --AVRAPSRNAQNAAQKPPMQPVMYPP---------NYQSLPLSQDLPQPQSTAS 485
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
837-1075 |
1.30e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 837 PPPPGfiMQGNVIPNPAAPLPTAPG-----HMPSQLppypqpqpyqpaqqysfgtggAAAYRPQQPVAPPASNAYPNTPY 911
Cdd:PHA03247 2559 APPAA--PDRSVPPPRPAPRPSEPAvtsraRRPDAP---------------------PQSARPRAPVDDRGDPRGPAPPS 2615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 912 ISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYAL--PPGTTGPQNGWNdPPALNrvPKK 989
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgrAAQASSPPQRPR-RRAAR--PTV 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 990 KKMPENFMPPVPITSPimNPSGDPQSQGLqqqPSTPGPLSSHASFPQQHLAGGQPF--HGVQQPLAQT--GMPPSFSKPN 1065
Cdd:PHA03247 2693 GSLTSLADPPPPPPTP--EPAPHALVSAT---PLPPGPAAARQASPALPAAPAPPAvpAGPATPGGPArpARPPTTAGPP 2767
|
250
....*....|
gi 1318663329 1066 TEGAPGAPIG 1075
Cdd:PHA03247 2768 APAPPAAPAA 2777
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
807-1087 |
1.45e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.13 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 807 PLSKGRPGPVAGHSQMPRVQTQQYYPhGENPPPPGFIMQGNVIPNPAAPLPTAP--------GHMPSQLPPYPQPQPYQP 878
Cdd:PHA03378 590 PSYAQTPWPVPHPSQTPEPPTTQSHI-PETSAPRQWPMPLRPIPMRPLRMQPITfnvlvfptPHQPPQVEITPYKPTWTQ 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 879 AQQYSFG--TGGAAAYRPQQ--------------PVAPPASnayPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFP 942
Cdd:PHA03378 669 IGHIPYQpsPTGANTMLPIQwapgtmqpppraptPMRPPAA---PPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 943 PPSSGASFQHGGPGAPPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENfMPPVPITSPIMNPSGDPQSQGLQQQ- 1021
Cdd:PHA03378 746 PPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQP-PPQAGPTSMQLMPRAAPGQQGPTKQi 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 1022 -------------PSTPGPLS---SHASFPQQHLAGGQPFHGVQQPLAqtgMPPSFSKPNTEGAPGAPIGNTIQHVQALP 1085
Cdd:PHA03378 825 lrqlltggvkrgrPSLKKPAAlerQAAAGPTPSPGSGTSDKIVQAPVF---YPPVLQPIQVMRQLGSVRAAAASTVTQAP 901
|
..
gi 1318663329 1086 TE 1087
Cdd:PHA03378 902 TE 903
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
788-1073 |
2.40e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 42.35 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 788 AQGKPVSGQESSQSPYERQPLSKGRPGPV-----AGH---------SQMPRVQTQQYYPH---GENPPPPGFIMQGNVIP 850
Cdd:PHA03379 468 AQLPPGPLQDLEPGDQLPGVVQDGRPACApvpapAGPivrpweaslSQVPGVAFAPVMPQpmpVEPVPVPTVALERPVCP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 851 NPAAPLPTAPGHMPSQLPPYPQPQPYQ-------PAQQYSFgTGGAAAYRPQ-QPVAPPASNAYPNTPYISPVASYSG-- 920
Cdd:PHA03379 548 APPLIAMQGPGETSGIVRVRERWRPAPwtpnpprSPSQMSV-RDRLARLRAEaQPYQASVEVQPPQLTQVSPQQPMEYpl 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 921 --QPQMYT----AQQASSPTSSSAASFPPPSSGASFQH----GGPGAPPSSSAYALPP-GTTGPQngWNDppalnrvpkk 989
Cdd:PHA03379 627 epEQQMFPgspfSQVADVMRAGGVPAMQPQYFDLPLQQpisqGAPLAPLRASMGPVPPvPATQPQ--YFD---------- 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 990 kkmpenfmppVPITSPImnPSGDPQSQGLQQQPSTPGPLSSHASFPqqhlaGGQPFHGVQQPLAQT---GMPpsFSKPNT 1066
Cdd:PHA03379 695 ----------IPLTEPI--NQGASAAHFLPQQPMEGPLVPERWMFQ-----GATLSQSVRPGVAQSqyfDLP--LTQPIN 755
|
....*..
gi 1318663329 1067 EGAPGAP 1073
Cdd:PHA03379 756 HGAPAAH 762
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
886-982 |
2.96e-03 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 41.28 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 886 TGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPtsssaasfPPPSSGASFQHGGPGAPPSSSAYA 965
Cdd:pfam16072 163 AGGQQPAAPAAPAYPVAPAAYPAQAPAAAPAPAPGAPQTPLAPLNPVA--------AAPAAAAGAAAAPVVAAAAPAAAA 234
|
90
....*....|....*..
gi 1318663329 966 LPPGTTGPQNGWNDPPA 982
Cdd:pfam16072 235 PPPPAPAAPPADAAPPA 251
|
|
| DUF3824 |
pfam12868 |
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ... |
794-910 |
3.27e-03 |
|
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.
Pssm-ID: 372351 [Multi-domain] Cd Length: 145 Bit Score: 39.34 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 794 SGQESSQSPYERQPLSKGRPGPVAGHsqmprvqtQQYYPHGEN-PPPPGFIMQGNVIPNPAAPL-PTAPGHMPSqlppyp 871
Cdd:pfam12868 47 DYRDYYEDPYSPSPYPPSPAGPYASQ--------GQYYPETNYfPPPPGSTPQPPVDPQPNAPPpPYNPADYPP------ 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 1318663329 872 qpqpyqpaqqysfGTGGAAAYRPQQPVAPPASNAYPNTP 910
Cdd:pfam12868 113 -------------PPGAAPPPQPYQYPPPPGPDPYAPRP 138
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
798-1095 |
6.81e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.81 E-value: 6.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 798 SSQSPyERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVI-PNPA-APLPTAPGHMpsqlppypqpqp 875
Cdd:PHA03379 439 SAQVP-EPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQdGRPAcAPVPAPAGPI------------ 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 876 yqpaqqysfgtggaaaYRPQQPvappasnAYPNTPYISPvASYSGQPqMYTAQQASSPTSSSAASFPPPSSGASfqhGGP 955
Cdd:PHA03379 506 ----------------VRPWEA-------SLSQVPGVAF-APVMPQP-MPVEPVPVPTVALERPVCPAPPLIAM---QGP 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 956 GAPPS----SSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMnpsgdpqSQGLQQQPSTpGPLSsh 1031
Cdd:PHA03379 558 GETSGivrvRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASVEVQPPQL-------TQVSPQQPME-YPLE-- 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1318663329 1032 asfPQQHLAGGQPFHGVQQPLAQTGM----PPSFS----KPNTEGAPGAPIGNTIQHVQALPTEKITKKPIP 1095
Cdd:PHA03379 628 ---PEQQMFPGSPFSQVADVMRAGGVpamqPQYFDlplqQPISQGAPLAPLRASMGPVPPVPATQPQYFDIP 696
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
954-1054 |
8.68e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.45 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 954 GPGAP---PSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGPLSS 1030
Cdd:PRK10263 739 GPHEPlftPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ 818
|
90 100
....*....|....*....|....
gi 1318663329 1031 HasfPQQHLAGGQPFHGVQQPLAQ 1054
Cdd:PRK10263 819 Q---PQQPVAPQPQYQQPQQPVAP 839
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
814-1053 |
8.95e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.24 E-value: 8.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 814 GPVAghSQMPRVQTQQYYPHGENPPPPgfimqgnVIPNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYR 893
Cdd:PRK12323 380 APVA--QPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 894 PQQPVAPPASNAYPNTPYISPVASYSGQPQmytAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTTGP 973
Cdd:PRK12323 451 APAPAAAPAAAARPAAAGPRPVAAAAAAAP---ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIP 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663329 974 QNGWNDPPAlNRVPKKKKMPENFMPPVPITSPIMNPSGDPQsqglQQQPSTPGplSSHASFPQqhLAGGQPFHGVQQPLA 1053
Cdd:PRK12323 528 DPATADPDD-AFETLAPAPAAAPAPRAAAATEPVVAPRPPR----ASASGLPD--MFDGDWPA--LAARLPVRGLAQQLA 598
|
|
|