|
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 |
8.57e-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: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1318663222 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.31e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1318663222 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
792-1088 |
5.97e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 792 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 870
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 871 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 950
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 951 QHGGPGA--PPSSSAYALPpgTTGTPPAASELPASQRTGPQNGWNDPPalnrvPKKKKMPENFMPPVPITSPIMNPSGDP 1028
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKP--AAPARPPVRRLARPAVSRSTESFALPP-----DQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318663222 1029 QSQgLQQQPSTPGPLSshasfPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1088
Cdd:PHA03247 2930 QPP-PPPPPRPQPPLA-----PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
572-766 |
1.76e-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: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318663222 716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
769-1048 |
2.50e-08 |
|
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: 58.63 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 846
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 847 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 922
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 923 QMytaqqassptsssaasfpppssgaSFQHGGPGA--PPSSSAYALPPGTTGTPPAASELPASQRTGPqngwndppalnr 1000
Cdd:pfam03154 464 QH------------------------PFVPGGPPPitPPSGPPTSTSSAMPGIQPPSSASVSSSGPVP------------ 507
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1318663222 1001 vpkkkKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 1048
Cdd:pfam03154 508 -----AAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
572-766 |
3.56e-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: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663222 714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| KREPA2 |
cd23959 |
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ... |
885-989 |
4.97e-03 |
|
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.
Pssm-ID: 467780 [Multi-domain] Cd Length: 424 Bit Score: 41.01 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 885 GTGGAAAYRPQQPVAP-PASNAYPNTPY-------ISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPG 956
Cdd:cd23959 123 SSTQRETHKTAQVAPPkAEPQTAPVTPFgqlpmfgQHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDT 202
|
90 100 110
....*....|....*....|....*....|....*...
gi 1318663222 957 APPSSSAYALP-----PGTTGTPPAASELPASQRTGPQ 989
Cdd:cd23959 203 APSSGAPDGFPaeasaPSPFAAPASAASFPAAPVANGE 240
|
|
|
|
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 |
8.57e-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: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 1318663222 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.31e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 1318663222 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.79e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.99 E-value: 4.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 247 RfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319 276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352
|
....*..
gi 1318663222 327 RISVYSI 333
Cdd:COG2319 353 TVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-338 |
6.70e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.82 E-value: 6.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1318663222 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 |
1.09e-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: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 171 ISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMhcSGLAWHPDvATQMVLASEDDrlpVIQMWDLRfAS 250
Cdd:cd00200 12 VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPV--RDVAASAD-GTYLASGSSDK---TIRLWDLE-TG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 251 SPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISV 330
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFS-PDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP-DGTFVASSSQDGTIKL 161
|
....*..
gi 1318663222 331 YSIMGGS 337
Cdd:cd00200 162 WDLRTGK 168
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
792-1088 |
5.97e-10 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 64.19 E-value: 5.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 792 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 870
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 871 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 950
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 951 QHGGPGA--PPSSSAYALPpgTTGTPPAASELPASQRTGPQNGWNDPPalnrvPKKKKMPENFMPPVPITSPIMNPSGDP 1028
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKP--AAPARPPVRRLARPAVSRSTESFALPP-----DQPERPPQPQAPPPPQPQPQPPPPPQP 2929
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1318663222 1029 QSQgLQQQPSTPGPLSshasfPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1088
Cdd:PHA03247 2930 QPP-PPPPPRPQPPLA-----PTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
572-766 |
1.76e-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: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 643
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 644 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 715
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1318663222 716 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 766
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
3.37e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.31 E-value: 3.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 1318663222 246 LR 247
Cdd:COG2319 401 LA 402
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
769-1048 |
2.50e-08 |
|
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: 58.63 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 769 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 846
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 847 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 922
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 923 QMytaqqassptsssaasfpppssgaSFQHGGPGA--PPSSSAYALPPGTTGTPPAASELPASQRTGPqngwndppalnr 1000
Cdd:pfam03154 464 QH------------------------PFVPGGPPPitPPSGPPTSTSSAMPGIQPPSSASVSSSGPVP------------ 507
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1318663222 1001 vpkkkKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 1048
Cdd:pfam03154 508 -----AAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
806-1095 |
3.17e-08 |
|
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: 58.24 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 806 QPLSKGRPGPvaghsQMPRVQTQQYYPHGENPPPPGFIMQGNVI---PNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQY 882
Cdd:pfam03154 250 QPMTQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGPSHmqhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 883 SFGTGGAAAYRPQQPVA----PPASNAYPNT--PYISPVASY-SGQPQMYTAQQASSPTSSSAASFPPPS-----SGASF 950
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPReqplPPAPLSMPHIkpPPTTPIPQLpNPQSHKHPPHLSGPSPFQMNSNLPPPPalkplSSLST 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 951 QHGGPGAPPS----SSAYALPPgttgtPPAASELPASQRTGPQNGWNDPP--ALNRVPKKKKMPEN-FMP--PVPITSPI 1021
Cdd:pfam03154 405 HHPPSAHPPPlqlmPQSQQLPP-----PPAQPPVLTQSQSLPPPAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITPPS 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663222 1022 MNPSGDPQSQGLQQQPSTpGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQH 1095
Cdd:pfam03154 480 GPPTSTSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
819-1094 |
1.56e-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: 55.93 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 819 HSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPL----PTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGG-AAAYR 893
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSvppqGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRlPSPHP 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 894 PQQPVAPPA-SNAYPNTPYISPVASYSGQPQMYTAQQ--------------ASSPTSSSAASFPPPSSGASFQ-HGGPGA 957
Cdd:pfam03154 248 PLQPMTQPPpPSQVSPQPLPQPSLHGQMPPMPHSLQTgpshmqhpvppqpfPLTPQSSQSQVPPGPSPAAPGQsQQRIHT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 958 PPSSSAYA--LPPGTTGTPPAASEL---------PASQRTGPQNgwNDPPALNRVPKKKKMPENfMPPVPITSPIMN--- 1023
Cdd:pfam03154 328 PPSQSQLQsqQPPREQPLPPAPLSMphikpppttPIPQLPNPQS--HKHPPHLSGPSPFQMNSN-LPPPPALKPLSSlst 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1024 ---PSGDP-------QSQGLQ----------QQPSTPGPLSSHASFPQQHLAGGQPfhgvqqPLAQ----TGMPPSFSKP 1079
Cdd:pfam03154 405 hhpPSAHPpplqlmpQSQQLPpppaqppvltQSQSLPPPAASHPPTSGLHQVPSQS------PFPQhpfvPGGPPPITPP 478
|
330
....*....|....*
gi 1318663222 1080 NTEGAPGAPIGNTIQ 1094
Cdd:pfam03154 479 SGPPTSTSSAMPGIQ 493
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
773-1152 |
1.66e-07 |
|
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: 55.78 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 773 TNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKGRP----GPVAGHSQMPRVQTQQyyPHGENPPP-------PG 841
Cdd:pfam09606 90 AGQGTRPQMMGPMGPGPGGPMGQQMGGPGTASNLLASLGRPqmpmGGAGFPSQMSRVGRMQ--PGGQAGGMmqpssgqPG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 842 FIMQGNVIPNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGT--GGAAAYRPQQPVAPPASN----AYPNTPYispv 915
Cdd:pfam09606 168 SGTPNQMGPNGGPGQGQAGGMNGGQQGPMGGQMPPQMGVPGMPGPadAGAQMGQQAQANGGMNPQqmggAPNQVAM---- 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 916 asySGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPG---APPSSSAYALPP-GTTGTPPAASELPASQRTGPQNG 991
Cdd:pfam09606 244 ---QQQQPQQQGQQSQLGMGINQMQQMPQGVGGGAGQGGPGqpmGPPGQQPGAMPNvMSIGDQNNYQQQQTRQQQQQQGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 992 wNDPPALNRVP------------------KKKKMPENF----MPPVPITSPIMNPSGDP----------QSQGLQQ--QP 1037
Cdd:pfam09606 321 -NHPAAHQQQMnqsvgqggqvvalgglnhLETWNPGNFgglgANPMQRGQPGMMSSPSPvpgqqvrqvtPNQFMRQspQP 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1038 STPGPLSSHASFPQQHLAGGQPF-HGVQQPLAQTG-MPPSFSKPNTEGaPGAPIGNTIQ---------HVQALPTEK--- 1103
Cdd:pfam09606 400 SVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSqQPAQQRTIGQDS-PGGSLNTPGQsavnsplnpQEEQLYREKyrq 478
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1318663222 1104 ITKKPIPEEHLILKTTfedliqrclssaTDPQTKRKLDDASKRLEFLYD 1152
Cdd:pfam09606 479 LTKYIEPLKRMIAKME------------NDPGDIDKMNKMKRLLEILSN 515
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
790-1090 |
1.75e-07 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 56.10 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 790 GKPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFimqgnviPNPAAPLPTA--------PG 861
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP-------RRRAARPTVGsltsladpPP 2703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 862 HMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYRPQQPVAP--------PASNAYPNTPYI-------SPVASYSGQPQMYT 926
Cdd:PHA03247 2704 PPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPavpagpatPGGPARPARPPTtagppapAPPAAPAAGPPRRL 2783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 927 AQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTGP------QNGWNDP--PAL 998
Cdd:PHA03247 2784 TRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPpppslpLGGSVAPggDVR 2863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 999 NRVPKKKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQ-QHLAGGQPFHGVQQPLAQTGMPPSFS 1077
Cdd:PHA03247 2864 RRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPpQPQPQPPPPPQPQPPPPPPPRPQPPL 2943
|
330
....*....|....
gi 1318663222 1078 KPNTEGAP-GAPIG 1090
Cdd:PHA03247 2944 APTTDPAGaGEPSG 2957
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
919-1113 |
2.43e-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: 55.16 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 919 SGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSS-SAYALPPGTTGTPPAASELPASQRTGPQNGWNDPPa 997
Cdd:pfam03154 161 SAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSApSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHP- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 998 lNRVPK--------KKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPS--------TPGPLSSHASFPQ-----QHLAG 1056
Cdd:pfam03154 240 -QRLPSphpplqpmTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPShmqhpvppQPFPLTPQSSQSQvppgpSPAAP 318
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1318663222 1057 GQPFHGVQQPLAQTgMPPSFSKPNTEGAPGAPIgnTIQHVQALPTEKITKKPIPEEH 1113
Cdd:pfam03154 319 GQSQQRIHTPPSQS-QLQSQQPPREQPLPPAPL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
572-766 |
3.56e-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: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 572 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 641
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 642 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 713
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1318663222 714 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 766
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
852-1044 |
1.56e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 53.02 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 852 PAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYRP--QQPVAPPASNAYPntpyisPVASYSgQPQMYTAQQ 929
Cdd:PHA03247 2824 PAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPpsRSPAAKPAAPARP------PVRRLA-RPAVSRSTE 2896
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 930 ASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTTGTPPAASELPASQRTGPQNGWNDPPALNRVPKKKKMPE 1009
Cdd:PHA03247 2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1318663222 1010 NFM----PPVPITSPIMNPSGDPQSQGLQQQPS--------TPGPLS 1044
Cdd:PHA03247 2977 FRVpqpaPSREAPASSTPPLTGHSLSRVSSWASslalheetDPPPVS 3023
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
2.53e-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: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 252 PLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 1318663222 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
886-982 |
1.92e-04 |
|
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: 44.75 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 886 TGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPtsssaasfPPPSSGASFQHGGPGAPPSSSAYA 965
Cdd:pfam16072 163 AGGQQPAAPAAPAYPVAPAAYPAQAPAAAPAPAPGAPQTPLAPLNPVA--------AAPAAAAGAAAAPVVAAAAPAAAA 234
|
90
....*....|....*..
gi 1318663222 966 LPPGTTGTPPAASELPA 982
Cdd:pfam16072 235 PPPPAPAAPPADAAPPA 251
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
894-1088 |
1.98e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 894 PQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGttGT 973
Cdd:PHA03247 2564 PDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPD--PH 2641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 974 PPAASELPASQRTGPQNGWNDPP----ALNRVPKKKKMPENFMPPV--PITSPIMNpSGDPQSQGLQQQPStPGPLSSHA 1047
Cdd:PHA03247 2642 PPPTVPPPERPRDDPAPGRVSRPrrarRLGRAAQASSPPQRPRRRAarPTVGSLTS-LADPPPPPPTPEPA-PHALVSAT 2719
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1318663222 1048 SFPQQHLAGGQPFhgvQQPLAQTGMPPSFSKPNTEGAPGAP 1088
Cdd:PHA03247 2720 PLPPGPAAARQAS---PALPAAPAPPAVPAGPATPGGPARP 2757
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
891-1088 |
3.73e-04 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 44.82 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 891 AYRPQQPVAPPASNAYPNTPYIS--PVASYSGQPQMYTAQQASSPTSSSAasfPPPSSGASFQHGGPGA-PPSSSAYALP 967
Cdd:PRK14086 92 AGEPAPPPPHARRTSEPELPRPGrrPYEGYGGPRADDRPPGLPRQDQLPT---ARPAYPAYQQRPEPGAwPRAADDYGWQ 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 968 PGTTGTPPAASELPASQRTGPQNGWNDPPALNRvpkkkkmPENFMPPVPITSPimNPSGDPQSQGLQQQPStPGPLSSHA 1047
Cdd:PRK14086 169 QQRLGFPPRAPYASPASYAPEQERDREPYDAGR-------PEYDQRRRDYDHP--RPDWDRPRRDRTDRPE-PPPGAGHV 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1318663222 1048 sfpqqHLAGGQPFHGVQQPL--AQTGMPPSFSK-PNTEGAPGAP 1088
Cdd:PRK14086 239 -----HRGGPGPPERDDAPVvpIRPSAPGPLAAqPAPAPGPGEP 277
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
837-1090 |
5.43e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.54 E-value: 5.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 837 PPPPGfiMQGNVIPNPAAPLPTAPghmpsqlppypqpqpyqpaqqysfgtggAAAYRPQQPVAPPASNAyPNTPyISPVA 916
Cdd:PHA03247 2559 APPAA--PDRSVPPPRPAPRPSEP----------------------------AVTSRARRPDAPPQSAR-PRAP-VDDRG 2606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 917 SYSGQPQMYTAQQASSPTSssaasfPPPSSGAS--FQHGGPG---APPSSSAYALPPGTTGTPP--AASELPASQRTGPQ 989
Cdd:PHA03247 2607 DPRGPAPPSPLPPDTHAPD------PPPPSPSPaaNEPDPHPpptVPPPERPRDDPAPGRVSRPrrARRLGRAAQASSPP 2680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 990 NGWNdPPALNrvPKKKKMPENFMPPVPITSPimNPSGDPQSQGLqqqPSTPGPLSSHASFPQQHLAGGQPF--HGVQQPL 1067
Cdd:PHA03247 2681 QRPR-RRAAR--PTVGSLTSLADPPPPPPTP--EPAPHALVSAT---PLPPGPAAARQASPALPAAPAPPAvpAGPATPG 2752
|
250 260
....*....|....*....|....*
gi 1318663222 1068 AQT--GMPPSFSKPNTEGAPGAPIG 1090
Cdd:PHA03247 2753 GPArpARPPTTAGPPAPAPPAAPAA 2777
|
|
| PRK14959 |
PRK14959 |
DNA polymerase III subunits gamma and tau; Provisional |
944-1059 |
5.77e-04 |
|
DNA polymerase III subunits gamma and tau; Provisional
Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 44.29 E-value: 5.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 944 PSSGASFQHGGPGAP-PSSSAYAL--PPGTTGTPPAAselPASQRTgPQNGWNDPPALNRVPkKKKMPENFMPPVPITSP 1020
Cdd:PRK14959 373 PSGGGASAPSGSAAEgPASGGAATipTPGTQGPQGTA---PAAGMT-PSSAAPATPAPSAAP-SPRVPWDDAPPAPPRSG 447
|
90 100 110
....*....|....*....|....*....|....*....
gi 1318663222 1021 IMnPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQP 1059
Cdd:PRK14959 448 IP-PRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDT 485
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
898-1069 |
6.10e-04 |
|
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: 44.26 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 898 VAPPASNAYPNTPYISPVASYSGQP------------QMyTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYA 965
Cdd:pfam09770 165 VAPKKAAAPAPAPQPAAQPASLPAPsrkmmsleeveaAM-RAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 966 LPPGTTGTPP---AASELPASQRTGPQNGWNDPPALNRVPKKKKMPENfMPPVPI--TSPIMNPS--GDPQSQGLQQQPS 1038
Cdd:pfam09770 244 QQPQQQPQQPqqhPGQGHPVTILQRPQSPQPDPAQPSIQPQAQQFHQQ-PPPVPVqpTQILQNPNrlSAARVGYPQNPQP 322
|
170 180 190
....*....|....*....|....*....|..
gi 1318663222 1039 TPGPLSSHASFPQQHLAGGQ-PFHGVQQPLAQ 1069
Cdd:pfam09770 323 GVQPAPAHQAHRQQGSFGRQaPIITHPQQLAQ 354
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
813-1111 |
7.74e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 813 PGP-VAGHSQMPRVQTQQYYPHGENPPPPGFimQGNVIPNPAAPLPTAPGHMPSQLppypqpqpyqPAQQYSFGTGGAAA 891
Cdd:PHA03247 2578 SEPaVTSRARRPDAPPQSARPRAPVDDRGDP--RGPAPPSPLPPDTHAPDPPPPSP----------SPAANEPDPHPPPT 2645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 892 Y-----------------------------------RPQQPVAPPA---------SNAYPNTPYISPVASYSGQP-QMYT 926
Cdd:PHA03247 2646 VppperprddpapgrvsrprrarrlgraaqassppqRPRRRAARPTvgsltsladPPPPPPTPEPAPHALVSATPlPPGP 2725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 927 AQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTtgTPPAASELPASQRTGPQNGWNDPPALNRVPKKKK 1006
Cdd:PHA03247 2726 AAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAP--APPAAPAAGPPRRLTRPAVASLSESRESLPSPWD 2803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1007 ---MPENFMPPVPITSPIMNPSG--DPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNT 1081
Cdd:PHA03247 2804 padPPAAVLAPAAALPPAASPAGplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPV 2883
|
330 340 350
....*....|....*....|....*....|
gi 1318663222 1082 EGAPGAPIGNTIQHvQALPTEKITKKPIPE 1111
Cdd:PHA03247 2884 RRLARPAVSRSTES-FALPPDQPERPPQPQ 2912
|
|
| PRK07764 |
PRK07764 |
DNA polymerase III subunits gamma and tau; Validated |
885-1090 |
1.06e-03 |
|
DNA polymerase III subunits gamma and tau; Validated
Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 43.44 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 885 GTGGAAAyRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAY 964
Cdd:PRK07764 589 GPAPGAA-GGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGD 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 965 ALPPGTTGTPPAAsELPASQRTGPQNGWNDPPALNRV-PKKKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGPl 1043
Cdd:PRK07764 668 GWPAKAGGAAPAA-PPPAPAPAAPAAPAGAAPAQPAPaPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEP- 745
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1318663222 1044 sSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIG 1090
Cdd:PRK07764 746 -DDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAP 791
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
947-1182 |
1.21e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 43.15 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 947 GASFQHGGPgappsssAYALPPGTTGTPPAASELPASQR---TGPQNGWNDPPALNRV---PKKKKMPENFMPPV--PIT 1018
Cdd:PRK10263 677 GEQYQHDVP-------VNAEDADAAAEAELARQFAQTQQqrySGEQPAGANPFSLDDFefsPMKALLDDGPHEPLftPIV 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1019 SPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQHVQA 1098
Cdd:PRK10263 750 EPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQPVAP 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1099 LPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIARSIE 1175
Cdd:PRK10263 827 QPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMARLVE 895
|
250
....*....|....*...
gi 1318663222 1176 TR-----------NYSEG 1182
Cdd:PRK10263 896 ARladfrikadvvNYSPG 913
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
814-1016 |
1.70e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 42.56 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 814 GPVAghSQMPRVQTQQYYPHGENPPPPgfimqgnVIPNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYR 893
Cdd:PRK12323 380 APVA--QPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 894 PQQPVAPPASNAYPNTPYISPVASYSGQPQmytAQQASSPTSSSAASFPPPSSGAsfqhggPGAPPSSSAYALPPGTTGT 973
Cdd:PRK12323 451 APAPAAAPAAAARPAAAGPRPVAAAAAAAP---ARAAPAAAPAPADDDPPPWEEL------PPEFASPAPAQPDAAPAGW 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1318663222 974 PPAASELPA-SQRTGPQNGWNDPPALNRVPKKKKMPENFMPPVP 1016
Cdd:PRK12323 522 VAESIPDPAtADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRP 565
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
792-988 |
3.04e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 41.73 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 792 PVSGQESSQSP----YERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPP--PPGFimqgnvipnPAAPLPTAPGHMPS 865
Cdd:PRK14086 90 PSAGEPAPPPPharrTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQLPtaRPAY---------PAYQQRPEPGAWPR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 866 QLPPYPQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSssaasfPPPS 945
Cdd:PRK14086 161 AADDYGWQQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQRRRDYDHPRPDWDRPRRDRTDRPE------PPPG 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1318663222 946 SGASfQHGGPGAPPSSSAYALPPGTT-GTPPAASELPASQRTGP 988
Cdd:PRK14086 235 AGHV-HRGGPGPPERDDAPVVPIRPSaPGPLAAQPAPAPGPGEP 277
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
885-1081 |
3.84e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 41.40 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 885 GTGGAAAYRP--QQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGA-------SFQHGGP 955
Cdd:PRK12323 367 QSGGGAGPATaaAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAlaaarqaSARGPGG 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 956 GAPPSSSAYALPPGTTGTPPAASELPASQRTGPQNGWNDP----PALNRVPKKKKMPENFMPPVPITspiMNPSGDPQSQ 1031
Cdd:PRK12323 447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAaapaPADDDPPPWEELPPEFASPAPAQ---PDAAPAGWVA 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1032 GLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNT 1081
Cdd:PRK12323 524 ESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGL 573
|
|
| DUF3824 |
pfam12868 |
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ... |
794-910 |
4.49e-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: 38.95 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 794 SGQESSQSPYERQPLSKGRPGPVAGHsqmprvqtQQYYPHGEN-PPPPGFIMQGNVIPNPAAPL-PTAPGHMPSqlppyp 871
Cdd:pfam12868 47 DYRDYYEDPYSPSPYPPSPAGPYASQ--------GQYYPETNYfPPPPGSTPQPPVDPQPNAPPpPYNPADYPP------ 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 1318663222 872 qpqpyqpaqqysfGTGGAAAYRPQQPVAPPASNAYPNTP 910
Cdd:pfam12868 113 -------------PPGAAPPPQPYQYPPPPGPDPYAPRP 138
|
|
| KREPA2 |
cd23959 |
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of ... |
885-989 |
4.97e-03 |
|
Kinetoplastid RNA Editing Protein A2 (KREPA2); The KREPA2 (TbMP63) protein is a component of the parasitic protozoan's KREPA RNA editing catalytic complex (RECC). Kinetoplastid RNA editing (KRE) proteins occur as pairs or sets of related proteins in multiple complexes. KREPA complex is composed of six components (KREPA1-6), which share a conserved C-terminal region containing an oligonucleotide-binding (OB)-fold-like domain. KREPAs are responsible for the site-specific insertion and deletion of U nucleotides in the kinetoplastid mitochondria pre-messenger RNA. Apart from the conserved C-terminal OB-fold domain, KREPA1, KREPA2, and KREPA3 contain two conserved C2H2 zinc-finger domains. KREPA2 and kinetoplastid RNA editing ligase 1 (KREL1) are specific for ligation post-U-deletion and are paralogous to KREL2 and KREPA1 that are specific for ligation post-U-insertion. KREPA2, is critical for RECC stability and KREL1 integration into the complex.
Pssm-ID: 467780 [Multi-domain] Cd Length: 424 Bit Score: 41.01 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 885 GTGGAAAYRPQQPVAP-PASNAYPNTPY-------ISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPG 956
Cdd:cd23959 123 SSTQRETHKTAQVAPPkAEPQTAPVTPFgqlpmfgQHPPPAKPLPAAAAAQQSSASPGEVASPFASGTVSASPFATATDT 202
|
90 100 110
....*....|....*....|....*....|....*...
gi 1318663222 957 APPSSSAYALP-----PGTTGTPPAASELPASQRTGPQ 989
Cdd:cd23959 203 APSSGAPDGFPaeasaPSPFAAPASAASFPAAPVANGE 240
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
788-1088 |
5.36e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 41.20 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 788 AQGKPVSGQESSQSPYERQPLSKGRPGPV-----AGH---------SQMPRVQTQQYYPH---GENPPPPGFIMQGNVIP 850
Cdd:PHA03379 468 AQLPPGPLQDLEPGDQLPGVVQDGRPACApvpapAGPivrpweaslSQVPGVAFAPVMPQpmpVEPVPVPTVALERPVCP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 851 NPAAPLPTAPGHMPSQLPPYPQPQPYQ-------PAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGqPQ 923
Cdd:PHA03379 548 APPLIAMQGPGETSGIVRVRERWRPAPwtpnpprSPSQMSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQQPMEY-PL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 924 MYTAQQASSPtsssaasfPPPSSGASFQHGG-PGAPPSSSAYALP-PGTTGTPPAaselPASQRTGPqngwndppalnRV 1001
Cdd:PHA03379 627 EPEQQMFPGS--------PFSQVADVMRAGGvPAMQPQYFDLPLQqPISQGAPLA----PLRASMGP-----------VP 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1318663222 1002 PKKKKMPENFmpPVPITSPImnPSGDPQSQGLQQQPSTPGPLSSHASFPqqhlaGGQPFHGVQQPLAQT---GMPpsFSK 1078
Cdd:PHA03379 684 PVPATQPQYF--DIPLTEPI--NQGASAAHFLPQQPMEGPLVPERWMFQ-----GATLSQSVRPGVAQSqyfDLP--LTQ 752
|
330
....*....|
gi 1318663222 1079 PNTEGAPGAP 1088
Cdd:PHA03379 753 PINHGAPAAH 762
|
|
|