|
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 ... |
13-332 |
3.13e-24 |
|
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: 104.34 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939775 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| ACE1-Sec16-like super family |
cl14807 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
534-657 |
4.57e-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: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 605
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939775 606 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 657
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 super family |
cl38111 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
904-1076 |
3.07e-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. The actual alignment was detected with superfamily member pfam03154:
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 54.77 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 904 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 971
Cdd:pfam03154 181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 972 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1037
Cdd:pfam03154 258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622939775 1038 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1076
Cdd:pfam03154 336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| PHA03247 super family |
cl33720 |
large tegument protein UL36; Provisional |
712-1053 |
5.15e-07 |
|
large tegument protein UL36; Provisional The actual alignment was detected with superfamily member PHA03247:
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 712 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 791
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 792 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 871
Cdd:PHA03247 2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 872 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 949
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 950 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1027
Cdd:PHA03247 2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
330 340
....*....|....*....|....*...
gi 1622939775 1028 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1053
Cdd:PHA03247 2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
|
|
|
|
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 |
3.13e-24 |
|
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: 104.34 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939775 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.73e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1622939775 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 ... |
534-657 |
4.57e-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: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 605
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939775 606 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 657
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
904-1076 |
3.07e-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: 54.77 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 904 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 971
Cdd:pfam03154 181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 972 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1037
Cdd:pfam03154 258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622939775 1038 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1076
Cdd:pfam03154 336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
712-1053 |
5.15e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 712 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 791
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 792 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 871
Cdd:PHA03247 2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 872 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 949
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 950 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1027
Cdd:PHA03247 2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
330 340
....*....|....*....|....*...
gi 1622939775 1028 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1053
Cdd:PHA03247 2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
534-728 |
5.70e-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: 52.56 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 603
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 604 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 672
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 673 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 728
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
854-1051 |
5.62e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 854 RPQQPVAPPTSnAYPNTPyissassysgqsqlyaaqhqassptSSPATSFPPPPSSGASFQHGGPGA--PPSSSAYALPp 931
Cdd:PHA03247 2823 SPAGPLPPPTS-AQPTAP-------------------------PPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKP- 2875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 932 gTTGTLPAASELPASQRTGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMlQQQPSAPIPlssqss 1011
Cdd:PHA03247 2876 -AAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLA------ 2944
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622939775 1012 fPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1051
Cdd:PHA03247 2945 -PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
3.93e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622939775 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
711-1115 |
2.40e-03 |
|
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: 41.92 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 711 MSQYANLLAAQGSIAAALAFLPDNTNQPNIVQLrdrlcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVGHHQMPrvQTQQ 790
Cdd:pfam09606 117 PGTASNLLASLGRPQMPMGGAGFPSQMSRVGRM------QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQG--QAGG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 791 YYPHGENPPppgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQPvAPPTSNAYPNt 870
Cdd:pfam09606 188 MNGGQQGPM-------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQQ-QQPQQQGQQS- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 871 pyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTTGTLPAASELPASQ 947
Cdd:pfam09606 256 ---QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQGGNHPAAHQQQMNQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 948 ------RTGPQNGWNDPPALNRV--------PKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFP 1013
Cdd:pfam09606 333 svgqggQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 1014 QPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLS 1092
Cdd:pfam09606 413 QSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMIAK 492
|
410 420
....*....|....*....|...
gi 1622939775 1093 SATDPQTKRKLDDASKRLEFLYD 1115
Cdd:pfam09606 493 MENDPGDIDKMNKMKRLLEILSN 515
|
|
|
|
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 |
3.13e-24 |
|
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: 104.34 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgpykmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 86 sgvLIAGGENGNIILYDPSKiiaGDKEVVIAQndkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET---GECVRTLTG---HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1622939775 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
121-340 |
1.84e-23 |
|
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: 102.03 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 121 HTGPVRALDVNIfQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQV-------------------- 180
Cdd:cd00200 8 HTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLasgssdktirlwdletgecv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 181 ------------------QHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDiaTQMVLASEDDRLpvIQ 242
Cdd:cd00200 87 rtltghtsyvssvafspdGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS--VAFSPD--GTFVASSSQDGT--IK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 243 MWDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAA 322
Cdd:cd00200 161 LWDLR-TGKCVATLTGHTGEVNSVAFS-PDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSP-DGYLLASG 237
|
250
....*....|....*...
gi 1622939775 323 SFDGRISVYSIMGGSTDG 340
Cdd:cd00200 238 SEDGTIRVWDLRTGECVQ 255
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.73e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 89 LIAGGENGNIILYDpskiIAGDKEvvIAQNDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDiATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 249 ASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1622939775 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.29e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.83 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKLLRTLTG--HSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQM 243
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPDgrlLAS----GSADGT---VRL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 244 WDLRfASSPLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:COG2319 273 WDLA-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GS 349
|
250
....*....|
gi 1622939775 324 FDGRISVYSI 333
Cdd:COG2319 350 DDGTVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-336 |
1.97e-19 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 92.28 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 201 NEPIIKVSDHSNRMHCsgLAWHPD---IATqmvlASEDDRlpvIQMWDLRfASSPLRVLENHARGILAIAWSmADPELLL 277
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPDgklLAS----GSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLA 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622939775 278 SCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGG 336
Cdd:COG2319 221 SGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATG 278
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
2.15e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.08 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 89 LIAGGENGNIILYDpskiIAGDKEVVIAQNdkHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRTLTG--HSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---IATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 1622939775 246 LR 247
Cdd:COG2319 401 LA 402
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
534-657 |
4.57e-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: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKyFAKSQSKIT---RLITAVVMKNWKEIVESC---- 605
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622939775 606 -----DLKNWREALAAVLTYAKPD-EFSALCDLlgtrleneGDSLLQTQ----ACLCYICAG 657
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALVEL--------GDLLAQRGlveaAHICYLLAG 200
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
904-1076 |
3.07e-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: 54.77 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 904 PPPPSSGASFQHGGPGAPPSSSAYALPPGTTgtlPAASELPASQRT--GPQNGWNDPPALN--RVPK--------KKKTP 971
Cdd:pfam03154 181 ASPPSPPPPGTTQAATAGPTPSAPSVPPQGS---PATSQPPNQTQStaAPHTLIQQTPTLHpqRLPSphpplqpmTQPPP 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 972 ENFMPPVPITSPIMNPLGDPQSQMLQQQPS--------APIPLSSQSS------FPQPHLSgGQPFHGIQQPLGQTgMPP 1037
Cdd:pfam03154 258 PSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSqsqvppGPSPAAP-GQSQQRIHTPPSQS-QLQ 335
|
170 180 190
....*....|....*....|....*....|....*....
gi 1622939775 1038 SFSKPNIEGAPGAPIgnTFQHVQSLPTKKITKKPIPDEH 1076
Cdd:pfam03154 336 SQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
712-1053 |
5.15e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 54.56 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 712 SQYANLLAAQGSIAAALAFLPDNTNQPNIVQLRDRlCRAQGEPVAGHESPKIPYekqqlPKGRPGPVGhhqmPRVQTQQY 791
Cdd:PHA03247 2632 SPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR-ARRLGRAAQASSPPQRPR-----RRAARPTVG----SLTSLADP 2701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 792 YPHGENPPPPgfimhgnvNPNAAGQLPTSPGhmhTQVPPYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTSnAYPNTP 871
Cdd:PHA03247 2702 PPPPPTPEPA--------PHALVSATPLPPG---PAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT-AGPPAP 2769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 872 YISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPAASELPA--SQRT 949
Cdd:PHA03247 2770 APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPgpPPPS 2849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 950 GPQNGWNDP--PALNRVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFPQPHLSGGQPFHGIQ 1027
Cdd:PHA03247 2850 LPLGGSVAPggDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
330 340
....*....|....*....|....*...
gi 1622939775 1028 QPLGQT-GMPPSFSKPNIEGAP-GAPIG 1053
Cdd:PHA03247 2930 QPPPPPpPRPQPPLAPTTDPAGaGEPSG 2957
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
534-728 |
5.70e-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: 52.56 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 534 ITQALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLARTQKKY----FAKSQSKITRLItAVVMK----NWKEIVE- 603
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 604 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLENEGdslLQTQACLCYICAG---NVEKLVACWTKAQDG 672
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLAGlplSQTVLLGADHVRFPS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 673 SHPLSLQDLI--EkvvILRKAVQLTqAMDTSTVGV--LLAAKMsQYANLLAAQGSIAAAL 728
Cdd:pfam12931 155 TFGNDLESILltE---IYEYALSLS-PPQPPFVGLphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
3.59e-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: 50.03 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 252 PLRVLENHARGILAIAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 1622939775 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
854-1051 |
5.62e-05 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 854 RPQQPVAPPTSnAYPNTPyissassysgqsqlyaaqhqassptSSPATSFPPPPSSGASFQHGGPGA--PPSSSAYALPp 931
Cdd:PHA03247 2823 SPAGPLPPPTS-AQPTAP-------------------------PPPPGPPPPSLPLGGSVAPGGDVRrrPPSRSPAAKP- 2875
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 932 gTTGTLPAASELPASQRTGPQNGWNDPPAlnrVPKKKKTPENFMPPVPITSPIMNPLGDPQSQMlQQQPSAPIPlssqss 1011
Cdd:PHA03247 2876 -AAPARPPVRRLARPAVSRSTESFALPPD---QPERPPQPQAPPPPQPQPQPPPPPQPQPPPPP-PPRPQPPLA------ 2944
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622939775 1012 fPQPHLSG-GQPFHGIQQPLGQTGMPPSFSKPNIEGAPGAP 1051
Cdd:PHA03247 2945 -PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
754-1075 |
1.85e-04 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 45.91 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 754 PVAGHESPKIPYEKQQLPKGRPGPVGHHQMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPpypq 833
Cdd:pfam03154 201 PSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMP---- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 834 pqpyqpAQPYPFGTGGSAMYRP--QQPVAPPTSNAY---PNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPs 908
Cdd:pfam03154 277 ------PMPHSLQTGPSHMQHPvpPQPFPLTPQSSQsqvPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAP- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 909 sgASFQHGGPgaPPSSSAYALPPGTTGTLPAASELPASQRTgPQNgWNDPPALNRV--------PKKKKTPENFMPPV-P 979
Cdd:pfam03154 350 --LSMPHIKP--PPTTPIPQLPNPQSHKHPPHLSGPSPFQM-NSN-LPPPPALKPLsslsthhpPSAHPPPLQLMPQSqQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 980 ITSPIMNPLGDPQSQML------QQQPSAPIPLSSQSSFPQ-PHLSGGQPfhGIQQPLG-QTGMPPSFSKPNIEGAPGAP 1051
Cdd:pfam03154 424 LPPPPAQPPVLTQSQSLpppaasHPPTSGLHQVPSQSPFPQhPFVPGGPP--PITPPSGpPTSTSSAMPGIQPPSSASVS 501
|
330 340
....*....|....*....|....*.
gi 1622939775 1052 IGNTFQHVQS--LPTKKITKKPiPDE 1075
Cdd:pfam03154 502 SSGPVPAAVScpLPPVQIKEEA-LDE 526
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
203-333 |
3.93e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 44.69 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 203 PIIKVSdhsNRMHCSGLAWHPDIATQMVLASEDDrlpVIQMWDLrfASSPLRV-LENHARGILAIAWSMADPELLLSCGK 281
Cdd:PLN00181 525 PVVELA---SRSKLSGICWNSYIKSQVASSNFEG---VVQVWDV--ARSQLVTeMKEHEKRVWSIDYSSADPTLLASGSD 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1622939775 282 DAKILCSNPNTGEVLYELPTNTQWCFdIQWCPRNPAVLSAASFDGRISVYSI 333
Cdd:PLN00181 597 DGSVKLWSINQGVSIGTIKTKANICC-VQFPSESGRSLAFGSADHKVYYYDL 647
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
753-1077 |
8.47e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.77 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 753 EPVAGHESPKIPYEKqqlPKGRPGPvGHHQMPRVQTQQYYPHGENPPPPGF---IMHGNVNPNAAGQLPTSPGHmhTQVP 829
Cdd:PHA03247 2637 EPDPHPPPTVPPPER---PRDDPAP-GRVSRPRRARRLGRAAQASSPPQRPrrrAARPTVGSLTSLADPPPPPP--TPEP 2710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 830 PYPQPQPYQPAQPYPFGTGGSAMYRPQQPVAPPTsnayPNTPYISSASSYSGQSQLYAAqhqassPTSSPATSFP---PP 906
Cdd:PHA03247 2711 APHALVSATPLPPGPAAARQASPALPAAPAPPAV----PAGPATPGGPARPARPPTTAG------PPAPAPPAAPaagPP 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 907 PSSGASfqhggPGAPPSSSAYALP------PGTTGTLPAASELPASQRTGPqngwNDPPALNRVPKKKKTPENFMPPVPI 980
Cdd:PHA03247 2781 RRLTRP-----AVASLSESRESLPspwdpaDPPAAVLAPAAALPPAASPAG----PLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 981 TSPIMNPLGD----PQSQMLQQQPSAPiPLSSQSSFPQPHLSggQPFHGIQQPlgqtgmPPSFSKPNIEGAPGAPIGNTF 1056
Cdd:PHA03247 2852 LGGSVAPGGDvrrrPPSRSPAAKPAAP-ARPPVRRLARPAVS--RSTESFALP------PDQPERPPQPQAPPPPQPQPQ 2922
|
330 340
....*....|....*....|.
gi 1622939775 1057 QHVQSLPTKKITKKPIPDEHL 1077
Cdd:PHA03247 2923 PPPPPQPQPPPPPPPRPQPPL 2943
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
854-1053 |
1.70e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 854 RPQQPVAPPTSNAyPNTPyissassySGQSQLYAAQHQASSPTSSPATSFPPPPS-SGASFQHGGPG---APPSSSAYAL 929
Cdd:PHA03247 2585 RARRPDAPPQSAR-PRAP--------VDDRGDPRGPAPPSPLPPDTHAPDPPPPSpSPAANEPDPHPpptVPPPERPRDD 2655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 930 PPGTTGTLP--AASELPASQRTGPQNGWNDPPA---------LNRVPKKKKTPENfmPPVPITSPIMNPLGdPQSQMlQQ 998
Cdd:PHA03247 2656 PAPGRVSRPrrARRLGRAAQASSPPQRPRRRAArptvgsltsLADPPPPPPTPEP--APHALVSATPLPPG-PAAAR-QA 2731
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622939775 999 QPSAPIPLSSQSSFPQPHLSGGQpfhgiqqplGQTGMPPSFSKPNIEGAPGAPIG 1053
Cdd:PHA03247 2732 SPALPAAPAPPAVPAGPATPGGP---------ARPARPPTTAGPPAPAPPAAPAA 2777
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
782-1015 |
1.77e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 42.45 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 782 QMPRVQTQQYYPHGENPPPPGFIMHGNVNPNAAGQLPTSPGHMHTQVPPYPQPQPYQPAQPYPFGTG--GSAMYRPQQPV 859
Cdd:pfam03154 170 QPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTlhPQRLPSPHPPL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 860 APPTSNAYPNTPYISSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTLPA 939
Cdd:pfam03154 250 QPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPP 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622939775 940 ASELPASQRtgPQNGWNDPPALNRVPKKKKTPENFMPPVPitspimnplgDPQSQMLQQQPSAPIPLSSQSSFPQP 1015
Cdd:pfam03154 330 SQSQLQSQQ--PPREQPLPPAPLSMPHIKPPPTTPIPQLP----------NPQSHKHPPHLSGPSPFQMNSNLPPP 393
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
711-1115 |
2.40e-03 |
|
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: 41.92 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 711 MSQYANLLAAQGSIAAALAFLPDNTNQPNIVQLrdrlcrAQGEPVAGHESPKIPYEKQQLPKgRPGPVGHHQMPrvQTQQ 790
Cdd:pfam09606 117 PGTASNLLASLGRPQMPMGGAGFPSQMSRVGRM------QPGGQAGGMMQPSSGQPGSGTPN-QMGPNGGPGQG--QAGG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 791 YYPHGENPPppgfimhGNVNPNAAGQlPTSPGHMHTQVPPYPQPQPYQPAQPYPfgTGGSAMYRPQQPvAPPTSNAYPNt 870
Cdd:pfam09606 188 MNGGQQGPM-------GGQMPPQMGV-PGMPGPADAGAQMGQQAQANGGMNPQQ--MGGAPNQVAMQQ-QQPQQQGQQS- 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 871 pyiSSASSYSGQSQLYAAQHQASSPTSSPATSFPPPPSSGASFQHGGPGAPPSSSAYALPP---GTTGTLPAASELPASQ 947
Cdd:pfam09606 256 ---QLGMGINQMQQMPQGVGGGAGQGGPGQPMGPPGQQPGAMPNVMSIGDQNNYQQQQTRQqqqQQGGNHPAAHQQQMNQ 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 948 ------RTGPQNGWNDPPALNRV--------PKKKKTPENFMPPVPITSPIMNPLGDPQSQMLQQQPSAPIPLSSQSSFP 1013
Cdd:pfam09606 333 svgqggQVVALGGLNHLETWNPGnfgglganPMQRGQPGMMSSPSPVPGQQVRQVTPNQFMRQSPQPSVPSPQGPGSQPP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622939775 1014 QPHLSGGQPF-HGIQQPLGQTGMPPSFSKPNIEGAPGAPIGNTFQHVQSLPTKKITKKPIPDEHLILKTTFEDLIQRCLS 1092
Cdd:pfam09606 413 QSHPGGMIPSpALIPSPSPQMSQQPAQQRTIGQDSPGGSLNTPGQSAVNSPLNPQEEQLYREKYRQLTKYIEPLKRMIAK 492
|
410 420
....*....|....*....|...
gi 1622939775 1093 SATDPQTKRKLDDASKRLEFLYD 1115
Cdd:pfam09606 493 MENDPGDIDKMNKMKRLLEILSN 515
|
|
|