|
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 |
8.11e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 105.88 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 755512845 324 FDGRISVYS 332
Cdd:cd00200 281 ADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.23e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 755512845 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 ... |
533-727 |
1.67e-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: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 533 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 604
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 605 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 676
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512845 677 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 727
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
753-1034 |
2.99e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.88 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 753 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 831
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 832 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 911
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 912 QHGGPGA--PPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFM--PPVPITSPIMNPSGDPQSQGLQQQPSTPG 987
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755512845 988 PLSSHASFPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1034
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
730-994 |
4.80e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.94 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 730 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 807
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 808 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 883
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 884 qmytaqQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAyalPPGTTGPqngwndppalnrVPKKKKMPenfMPPVPI 963
Cdd:pfam03154 464 ------QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGP------------VPAAVSCP---LPPVQI 519
|
250 260 270
....*....|....*....|....*....|....*
gi 755512845 964 TSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 994
Cdd:pfam03154 520 KEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
533-727 |
3.17e-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: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 533 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 602
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 603 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 674
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755512845 675 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 727
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
855-987 |
3.12e-04 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 44.80 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 855 PQQPVAPPASNAYPNTPYIS--PVASYSGQPQMYTAQQAssptsssaasFPPPSsgasfqhgGPGAPPSSSAYALPPgtt 932
Cdd:TIGR01628 383 RQLPMGSPMGGAMGQPPYYGqgPQQQFNGQPLGWPRMSM----------MPTPM--------GPGGPLRPNGLAPMN--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 755512845 933 gpQNGWNDPPALNRVPKKKKMPENFMPpvpitspimNPSGDPQSQGLQQQPSTPG 987
Cdd:TIGR01628 442 --AVRAPSRNAQNAAQKPPMQPVMYPP---------NYQSLPLSQDLPQPQSTAS 485
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
962-1128 |
3.41e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 962 PITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQH 1041
Cdd:PRK10263 747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 1042 VQALPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIAR 1118
Cdd:PRK10263 824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892
|
170 180
....*....|....*....|.
gi 755512845 1119 SIETR-----------NYSEG 1128
Cdd:PRK10263 893 LVEARladfrikadvvNYSPG 913
|
|
|
|
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 |
8.11e-25 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 105.88 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 13 AWSPAQNhpiYLATGtsaqqldatfSTNASLEIFELD-------LSDPSLDMKSCATFSSSHRyhkliwgphkmdskgdv 85
Cdd:cd00200 16 AFSPDGK---LLATG----------SGDGTIKVWDLEtgellrtLKGHTGPVRDVAASADGTY----------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 86 sgvLIAGGENGNIILYDPSKiiagdKEVVIAQKDkHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGA 163
Cdd:cd00200 66 ---LASGSSDKTIRLWDLET-----GECVRTLTG-HTSYVSSVA---FSPDgrILSSSSRDKTIKVWDVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 164 KTQPpedISCIAWNrQVQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDrlpVIQM 243
Cdd:cd00200 134 HTDW---VNSVAFS-PDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNS--VAFSPD-GEKLLSSSSDG---TIKL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 244 WDLRfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaAS 323
Cdd:cd00200 204 WDLS-TGKCLGTLRGHENGVNSVAFS-PDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GS 280
|
....*....
gi 755512845 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 ... |
121-337 |
1.01e-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: 102.80 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 121 HTGPVRALDVNIfQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPPEDISCIAWNRQvqhiLASASPSGRATVWDLRK 200
Cdd:cd00200 8 HTGGVTCVAFSP-DGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTY----LASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 201 NEPIIKVSDHSNRMHCsgLAWHPDvaTQMVLASEDDRlpVIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:cd00200 83 GECVRTLTGHTSYVSS--VAFSPD--GRILSSSSRDK--TIKVWDVE-TGKCLTTLRGHTDWVNSVAFS-PDGTFVASSS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 755512845 281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSAASfDGRISVYSIMGGS 337
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGK 210
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
1.23e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTQPp 168
Cdd:COG2319 177 LASGSDDGTVRLWD----LATGKL--LRTLTGHTGAVRSVAFS-PDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGS- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 169 edISCIAWNRQVQHiLASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPDvATQMVLASEDDRlpvIQMWDLRf 248
Cdd:COG2319 249 --VRSVAFSPDGRL-LASGSADGTVRLWDLATGELLRTLTGHSGGVN--SVAFSPD-GKLLASGSDDGT---VRLWDLA- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 249 ASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRI 328
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFS-PDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTV 396
|
....*
gi 755512845 329 SVYSI 333
Cdd:COG2319 397 RLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-333 |
4.51e-22 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 99.99 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 89 LIAGGENGNIILYDpskiIAGDKEvvIAQKDKHTGPVRALDvniFQTN--LVASGANESEIYIWDLNNFATPMTPGAKTQ 166
Cdd:COG2319 135 LASGSADGTVRLWD----LATGKL--LRTLTGHSGAVTSVA---FSPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 167 PpedISCIAWNRQvQHILASASPSGRATVWDLRKNEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDL 246
Cdd:COG2319 206 A---VRSVAFSPD-GKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRS--VAFSPD-GRLLASGSADGT---VRLWDL 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 247 RfASSPLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDG 326
Cdd:COG2319 276 A-TGELLRTLTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLAS-GSDDG 352
|
....*..
gi 755512845 327 RISVYSI 333
Cdd:COG2319 353 TVRLWDL 359
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
121-338 |
6.31e-20 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 93.82 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 121 HTGPVRALDVNiFQTNLVASGANESEIYIWDLnnfATPMTPGAKTQPPEDISCIAWNRQvQHILASASPSGRATVWDLRK 200
Cdd:COG2319 77 HTAAVLSVAFS-PDGRLLASASADGTVRLWDL---ATGLLLRTLTGHTGAVRSVAFSPD-GKTLASGSADGTVRLWDLAT 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 201 NEPIIKVSDHSNRMHCsgLAWHPDvATQMVLASEDDRlpvIQMWDLRfASSPLRVLENHARGILAVAWSmADPELLLSCG 280
Cdd:COG2319 152 GKLLRTLTGHSGAVTS--VAFSPD-GKLLASGSDDGT---VRLWDLA-TGKLLRTLTGHTGAVRSVAFS-PDGKLLASGS 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755512845 281 KDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPrNPAVLSAASFDGRISVYSIMGGSI 338
Cdd:COG2319 224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGEL 280
|
|
| ACE1-Sec16-like |
cd09233 |
Ancestral coatomer element 1 (ACE1) of COPII coat complex assembly protein Sec16; COPII coat ... |
533-727 |
1.67e-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: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 533 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKyFAKSQSKIT---RLITAVVMKNWREIVESC---- 604
Cdd:cd09233 69 FRNLLLTGNRKEALELAL-DNGLwAHALLLASSLGKETWAEVVSR-FARSESKLNdplQTLYQLFSGNSPEAITELadnp 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 605 -----DLKNWREALAAVLTYAKPD-EFSALCdLLGTRLEREGDSLlrtQACLCYICAGnverlvacwtkAQDGSSPLS-- 676
Cdd:cd09233 147 aeaewALGNWREHLAIILSNRTSNlDLEALV-ELGDLLAQRGLVE---AAHICYLLAG-----------VPLGPYPSSps 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755512845 677 -----LQDLIEKVVILR--KAVQLT------QALDTNTVG--ALLAEKMsQYASLLAAQGSIAAAL 727
Cdd:cd09233 212 scllgGAVHNKSPRTFAtpEAIQLTeiyeyaLSLGNPQFGlpHLQPYKL-IHAARLAELGLVSEAL 276
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
753-1034 |
2.99e-09 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 61.88 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 753 PVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPhgenPPPPGFIMQGNVIPNPAAPLPTAPGH-MPSQLPPY 831
Cdd:PHA03247 2702 PPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP----AVPAGPATPGGPARPARPPTTAGPPApAPPAAPAA 2777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 832 PQPQPYQPAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASfPPPSSGASF 911
Cdd:PHA03247 2778 GPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPP-PSLPLGGSV 2856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 912 QHGGPGA--PPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFM--PPVPITSPIMNPSGDPQSQGLQQQPSTPG 987
Cdd:PHA03247 2857 APGGDVRrrPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPerPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 755512845 988 PLSSHASFPQQHLAG-GQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAP 1034
Cdd:PHA03247 2937 PRPQPPLAPTTDPAGaGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAP 2984
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
89-247 |
3.19e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 60.31 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 89 LIAGGENGNIILYDpskiIAGDKEVVIaqKDKHTGPVRALDVNiFQTNLVASGANESEIYIWDLNNFATPMTPGAKTqpp 168
Cdd:COG2319 261 LASGSADGTVRLWD----LATGELLRT--LTGHSGGVNSVAFS-PDGKLLASGSDDGTVRLWDLATGKLLRTLTGHT--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 169 EDISCIAWNRQVQhILASASPSGRATVWDLRKNEPIIKVSDHSNRMHcsGLAWHPD---VATqmvlASEDDRlpvIQMWD 245
Cdd:COG2319 331 GAVRSVAFSPDGK-TLASGSDDGTVRLWDLATGELLRTLTGHTGAVT--SVAFSPDgrtLAS----GSADGT---VRLWD 400
|
..
gi 755512845 246 LR 247
Cdd:COG2319 401 LA 402
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
730-994 |
4.80e-09 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 60.94 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 730 LPDNTNQPNIVQLRDRLCKAQGKPVSGQESSQSPYERQPLSKG--RPGPVAGHSQMPRVQTQQYYPHGENPPPpgFIMQG 807
Cdd:pfam03154 311 PGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPhiKPPPTTPIPQLPNPQSHKHPPHLSGPSP--FQMNS 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 808 NVIPNPA-APLPTAPGHMPSQLPPYPQPQPYQPAQQYSfgtggAAAYRP---QQPVAPPASNAYPNTPYISPVASYSGQP 883
Cdd:pfam03154 389 NLPPPPAlKPLSSLSTHHPPSAHPPPLQLMPQSQQLPP-----PPAQPPvltQSQSLPPPAASHPPTSGLHQVPSQSPFP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 884 qmytaqQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAyalPPGTTGPqngwndppalnrVPKKKKMPenfMPPVPI 963
Cdd:pfam03154 464 ------QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSA---SVSSSGP------------VPAAVSCP---LPPVQI 519
|
250 260 270
....*....|....*....|....*....|....*
gi 755512845 964 TSPIMNPSGDPQSQGLQQQPSTPGP----LSSHAS 994
Cdd:pfam03154 520 KEEALDEAEEPESPPPPPRSPSPEPtvvnTPSHAS 554
|
|
| Med15 |
pfam09606 |
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of ... |
749-1098 |
6.26e-09 |
|
ARC105 or Med15 subunit of Mediator complex non-fungal; The approx. 70 residue Med15 domain of the ARC-Mediator co-activator is a three-helix bundle with marked similarity to the KIX domain. The sterol regulatory element binding protein (SREBP) family of transcription activators use the ARC105 subunit to activate target genes in the regulation of cholesterol and fatty acid homeostasis. In addition, Med15 is a critical transducer of gene activation signals that control early metazoan development.
Pssm-ID: 312941 [Multi-domain] Cd Length: 732 Bit Score: 60.41 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 749 AQGKPVSGQESSQSPYERQPLSK----GRPGPVAGHSQMPrvqtQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTApghm 824
Cdd:pfam09606 181 GQGQAGGMNGGQQGPMGGQMPPQmgvpGMPGPADAGAQMG----QQAQANGGMNPQQMGGAPNQVAMQQQQPQQQG---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 825 psqlPPYPQPQPYQPAQQYSFGTGGAA-AYRPQQPVAPPasnayPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFP 903
Cdd:pfam09606 253 ----QQSQLGMGINQMQQMPQGVGGGAgQGGPGQPMGPP-----GQQPGAMPNVMSIGDQNNYQQQQTRQQQQQQGGNHP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 904 PPSSGASFQHGGPGAPPSSSAYALPPGTTGPQN--GWNDPPALNRVPKKKKMPEnfmpPVPITSPI-MNPsgdPQSQGLQ 980
Cdd:pfam09606 324 AAHQQQMNQSVGQGGQVVALGGLNHLETWNPGNfgGLGANPMQRGQPGMMSSPS----PVPGQQVRqVTP---NQFMRQS 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 981 QQPSTPGPLSSHASFPQQHLAGGQPF-HGVQQPLAQTG-MPPSFSKPNTEGaPGAPIGNTIQ---------HVQALPTEK 1049
Cdd:pfam09606 397 PQPSVPSPQGPGSQPPQSHPGGMIPSpALIPSPSPQMSqQPAQQRTIGQDS-PGGSLNTPGQsavnsplnpQEEQLYREK 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 755512845 1050 ---ITKKPIPEEHLILKTTfedliqrclssaTDPQTKRKLDDASKRLEFLYD 1098
Cdd:pfam09606 476 yrqLTKYIEPLKRMIAKME------------NDPGDIDKMNKMKRLLEILSN 515
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
767-1041 |
2.06e-07 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 55.54 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 767 QPLSKGRPGPvaghsQMPRVQTQQYYPHGENPPPPGFIMQGNVI---PNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQY 843
Cdd:pfam03154 250 QPMTQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGPSHmqhPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQR 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 844 SFGTGGAAAYRPQQPVA----PPASNAYPNT--PYISPVASY-SGQPQMYTAQQASSPTSSSAASFPPPS-----SGASF 911
Cdd:pfam03154 325 IHTPPSQSQLQSQQPPReqplPPAPLSMPHIkpPPTTPIPQLpNPQSHKHPPHLSGPSPFQMNSNLPPPPalkplSSLST 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 912 QHGGPGAPPS----------SSAYALPPGTTGPQN----GWNDPP--ALNRVPKKKKMPEN-FMP--PVPITSPIMNPSG 972
Cdd:pfam03154 405 HHPPSAHPPPlqlmpqsqqlPPPPAQPPVLTQSQSlpppAASHPPtsGLHQVPSQSPFPQHpFVPggPPPITPPSGPPTS 484
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755512845 973 DPQSQGLQQQPSTpGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQH 1041
Cdd:pfam03154 485 TSSAMPGIQPPSS-ASVSSSGPVPAAVSCPLPPVQIKEEALDEAEEPESPPPPPRSPSPEPTVVNTPSH 552
|
|
| Sec16_C |
pfam12931 |
Sec23-binding domain of Sec16; Sec16 is a multi-domain vesicle coat protein. The C-terminal ... |
533-727 |
3.17e-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: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 533 ITRALLTGNFESAVDLCLhDNRM-ADAIILAIAGGQELLAQTQKKY----FAKSQSKITRLItAVVMK----NWREIVE- 602
Cdd:pfam12931 1 IRALLLTGDREKALWLAL-DKKLwAHALLIASTLGKEKWKEVVQEFvrseFKGSNNKSGESL-AALYQvfagNSEEAVDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 603 --------SCDLKNWREALAAVLTYAKPDEFSALCDlLGTRLEREGdslLRTQACLCYICAgNVERLVACWTKAQDGSSP 674
Cdd:pfam12931 79 lvppsknaLWALDNWRETLALVLSNRSPGDVEALLA-LGDLLAQYG---RTEAAHICFLLA-GLPLSQTVLLGADHVRFP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755512845 675 LSLQDLIEkvvilrkAVQLTQ----ALDTNTVGA-------LLAEKMsQYASLLAAQGSIAAAL 727
Cdd:pfam12931 154 STFGNDLE-------SILLTEiyeyALSLSPPQPpfvglphLLPYKL-QHAAVLAEYGLVSEAQ 209
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
751-1060 |
2.39e-06 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 52.25 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 751 GKPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFimQGNVIPNPAAPL-----PTAPGHMP 825
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRP--RRRAARPTVGSLtsladPPPPPPTP 2708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 826 SQLPpypqpQPYQPAQQYSFGTGGAAAYRPQQPVApPASNAYPNTPYISPVASYSGQPQMyTAQQASSPTSSSAASFPPP 905
Cdd:PHA03247 2709 EPAP-----HALVSATPLPPGPAAARQASPALPAA-PAPPAVPAGPATPGGPARPARPPT-TAGPPAPAPPAAPAAGPPR 2781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 906 S----SGASFQHGGPGAPPSSSAYALPPGTTGPQNGWND--------PPALNRVPKKKKMPENFMPPVPITSPIMNPSGD 973
Cdd:PHA03247 2782 RltrpAVASLSESRESLPSPWDPADPPAAVLAPAAALPPaaspagplPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGD 2861
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 974 PQSQGLQQQPSTPGPLSSHAsfPQQHLAGGQPfhgVQQPLAQTGMPPSFSKPNTEGAPGAPIGNTIQHVQALPTEKITKK 1053
Cdd:PHA03247 2862 VRRRPPSRSPAAKPAAPARP--PVRRLARPAV---SRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPP 2936
|
....*..
gi 755512845 1054 PIPEEHL 1060
Cdd:PHA03247 2937 PRPQPPL 2943
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
252-336 |
2.40e-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: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 252 PLRVLENHARGILAVAWSmADPELLLSCGKDAKILCSNPNTGEVLYELPTNTQWCFDIQWCPRNPAVLSaASFDGRISVY 331
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFS-PDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLW 78
|
....*
gi 755512845 332 SIMGG 336
Cdd:cd00200 79 DLETG 83
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
780-1059 |
4.32e-06 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 51.31 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 780 HSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPYPqpqpyqpaqqysfgtggaaayrpQQPV 859
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQ-----------------------TQST 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 860 APPASnAYPNTPYISPVASYSGQPQMYTAQQassptsssaasfPPPSSGASFQhggpGAPPSSSAYALPPGTTGPQNGwn 939
Cdd:pfam03154 225 AAPHT-LIQQTPTLHPQRLPSPHPPLQPMTQ------------PPPPSQVSPQ----PLPQPSLHGQMPPMPHSLQTG-- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 940 dppalnrvpkkkkmPENFMPPVPiTSPIMNPSGDPQSQGlqqqPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQTGMP 1019
Cdd:pfam03154 286 --------------PSHMQHPVP-PQPFPLTPQSSQSQV----PPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLP 346
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 755512845 1020 PsfskpntegapgAPIgnTIQHVQALPTEKITKKPIPEEH 1059
Cdd:pfam03154 347 P------------APL--SMPHIKPPPTTPIPQLPNPQSH 372
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
750-1040 |
1.02e-05 |
|
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: 49.77 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 750 QGKPVSGQesSQSPYERQPlskgrPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPL-------PTAPG 822
Cdd:pfam03154 168 QTQPPVLQ--AQSGAASPP-----SPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHtliqqtpTLHPQ 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 823 HMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYRPQQPVAP------PASNAYPNTPYISPVASYSGQPQMYTAQQASSPTS 896
Cdd:pfam03154 241 RLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPhslqtgPSHMQHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 897 SSAASFPPPSSGASFQHGG------PGAPPSSSAYALPPGTTGPQ----NGWNDPPALNrVPKKKKMPENfMPPVPITSP 966
Cdd:pfam03154 321 SQQRIHTPPSQSQLQSQQPpreqplPPAPLSMPHIKPPPTTPIPQlpnpQSHKHPPHLS-GPSPFQMNSN-LPPPPALKP 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 967 IMN------PSGDP-------QSQGLQ----------QQPSTPGPLSSHASFPQQHLAGGQPfhgvqqPLAQ----TGMP 1019
Cdd:pfam03154 399 LSSlsthhpPSAHPpplqlmpQSQQLPpppaqppvltQSQSLPPPAASHPPTSGLHQVPSQS------PFPQhpfvPGGP 472
|
330 340
....*....|....*....|.
gi 755512845 1020 PSFSKPNTEGAPGAPIGNTIQ 1040
Cdd:pfam03154 473 PPITPPSGPPTSTSSAMPGIQ 493
|
|
| PAT1 |
pfam09770 |
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ... |
851-1015 |
8.49e-05 |
|
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.
Pssm-ID: 401645 [Multi-domain] Cd Length: 846 Bit Score: 46.95 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 851 AAYRPQQPVAPPAsnaypntpyisPVASYSGQPQMYTAQQASSPTSssaasFPPPSSGASFQHGGPGAPPSSSAYALPPG 930
Cdd:pfam09770 201 AAMRAQAKKPAQQ-----------PAPAPAQPPAAPPAQQAQQQQQ-----FPPQIQQQQQPQQQPQQPQQHPGQGHPVT 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 931 T-TGPQNGWNDPPALNRVPKKKKMPENfMPPVPI--TSPIMNPS--GDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQ- 1004
Cdd:pfam09770 265 IlQRPQSPQPDPAQPSIQPQAQQFHQQ-PPPVPVqpTQILQNPNrlSAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQa 343
|
170
....*....|.
gi 755512845 1005 PFHGVQQPLAQ 1015
Cdd:pfam09770 344 PIITHPQQLAQ 354
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
752-1031 |
1.79e-04 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 45.85 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 752 KPVSGQESSQSPYERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVIPNPAAPLPTAPGHMPSQLPPY 831
Cdd:PRK10263 355 QPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 832 PQPQPYQPaqqysfgTGGAAAYRPQQPVAPPASNAYPNTPYISPVAsysgQPQMYTAQQASSPTSSSAasfPPPssgaSF 911
Cdd:PRK10263 435 APAPEQPV-------AGNAWQAEEQQSTFAPQSTYQTEQTYQQPAA----QEPLYQQPQPVEQQPVVE---PEP----VV 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 912 QHGGPGAPPSSSAYALPPGTTGPQN---GWNDPpalnrVPKKKKMPENFMPPVPITSPIMNP------SGDPQSQGLQQQ 982
Cdd:PRK10263 497 EETKPARPPLYYFEEVEEKRAREREqlaAWYQP-----IPEPVKEPEPIKSSLKAPSVAAVPpveaaaAVSPLASGVKKA 571
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 755512845 983 PSTPGPLSSHASfPQQHLAGGqpfhGVQQPLAQTGMPPSFSKPNTEGAP 1031
Cdd:PRK10263 572 TLATGAAATVAA-PVFSLANS----GGPRPQVKEGIGPQLPRPKRIRVP 615
|
|
| PABP-1234 |
TIGR01628 |
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ... |
855-987 |
3.12e-04 |
|
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.
Pssm-ID: 130689 [Multi-domain] Cd Length: 562 Bit Score: 44.80 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 855 PQQPVAPPASNAYPNTPYIS--PVASYSGQPQMYTAQQAssptsssaasFPPPSsgasfqhgGPGAPPSSSAYALPPgtt 932
Cdd:TIGR01628 383 RQLPMGSPMGGAMGQPPYYGqgPQQQFNGQPLGWPRMSM----------MPTPM--------GPGGPLRPNGLAPMN--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 755512845 933 gpQNGWNDPPALNRVPKKKKMPENFMPpvpitspimNPSGDPQSQGLQQQPSTPG 987
Cdd:TIGR01628 442 --AVRAPSRNAQNAAQKPPMQPVMYPP---------NYQSLPLSQDLPQPQSTAS 485
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
798-1036 |
1.21e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.39 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 798 PPPPGfiMQGNVIPNPAAPLPTAPG-----HMPSQLppypqpqpyqpaqqysfgtggAAAYRPQQPVAPPASNAYPNTPY 872
Cdd:PHA03247 2559 APPAA--PDRSVPPPRPAPRPSEPAvtsraRRPDAP---------------------PQSARPRAPVDDRGDPRGPAPPS 2615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 873 ISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYAL--PPGTTGPQNGWNdPPALNrvPKK 950
Cdd:PHA03247 2616 PLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLgrAAQASSPPQRPR-RRAAR--PTV 2692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 951 KKMPENFMPPVPITSPimNPSGDPQSQGLqqqPSTPGPLSSHASFPQQHLAGGQPF--HGVQQPLAQT--GMPPSFSKPN 1026
Cdd:PHA03247 2693 GSLTSLADPPPPPPTP--EPAPHALVSAT---PLPPGPAAARQASPALPAAPAPPAvpAGPATPGGPArpARPPTTAGPP 2767
|
250
....*....|
gi 755512845 1027 TEGAPGAPIG 1036
Cdd:PHA03247 2768 APAPPAAPAA 2777
|
|
| PHA03378 |
PHA03378 |
EBNA-3B; Provisional |
768-1048 |
1.38e-03 |
|
EBNA-3B; Provisional
Pssm-ID: 223065 [Multi-domain] Cd Length: 991 Bit Score: 43.13 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 768 PLSKGRPGPVAGHSQMPRVQTQQYYPhGENPPPPGFIMQGNVIPNPAAPLPTAP--------GHMPSQLPPYPQPQPYQP 839
Cdd:PHA03378 590 PSYAQTPWPVPHPSQTPEPPTTQSHI-PETSAPRQWPMPLRPIPMRPLRMQPITfnvlvfptPHQPPQVEITPYKPTWTQ 668
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 840 AQQYSFG--TGGAAAYRPQQ--------------PVAPPASnayPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFP 903
Cdd:PHA03378 669 IGHIPYQpsPTGANTMLPIQwapgtmqpppraptPMRPPAA---PPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRAR 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 904 PPSSGASFQHGGPGAPPSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENfMPPVPITSPIMNPSGDPQSQGLQQQ- 982
Cdd:PHA03378 746 PPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQP-PPQAGPTSMQLMPRAAPGQQGPTKQi 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 983 -------------PSTPGPLS---SHASFPQQHLAGGQPFHGVQQPLAqtgMPPSFSKPNTEGAPGAPIGNTIQHVQALP 1046
Cdd:PHA03378 825 lrqlltggvkrgrPSLKKPAAlerQAAAGPTPSPGSGTSDKIVQAPVF---YPPVLQPIQVMRQLGSVRAAAASTVTQAP 901
|
..
gi 755512845 1047 TE 1048
Cdd:PHA03378 902 TE 903
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
749-1034 |
2.25e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 42.35 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 749 AQGKPVSGQESSQSPYERQPLSKGRPGPV-----AGH---------SQMPRVQTQQYYPH---GENPPPPGFIMQGNVIP 811
Cdd:PHA03379 468 AQLPPGPLQDLEPGDQLPGVVQDGRPACApvpapAGPivrpweaslSQVPGVAFAPVMPQpmpVEPVPVPTVALERPVCP 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 812 NPAAPLPTAPGHMPSQLPPYPQPQPYQ-------PAQQYSFGTGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSG--- 881
Cdd:PHA03379 548 APPLIAMQGPGETSGIVRVRERWRPAPwtpnpprSPSQMSVRDRLARLRAEAQPYQASVEVQPPQLTQVSPQQPMEYple 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 882 -QPQMYT----AQQASSPTSSSAASFPPPSSGASFQH----GGPGAPPSSSAYALPP-GTTGPQngWNDppalnrvpkkk 951
Cdd:PHA03379 628 pEQQMFPgspfSQVADVMRAGGVPAMQPQYFDLPLQQpisqGAPLAPLRASMGPVPPvPATQPQ--YFD----------- 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 952 kmpenfmppVPITSPImnPSGDPQSQGLQQQPSTPGPLSSHASFPqqhlaGGQPFHGVQQPLAQT---GMPpsFSKPNTE 1028
Cdd:PHA03379 695 ---------IPLTEPI--NQGASAAHFLPQQPMEGPLVPERWMFQ-----GATLSQSVRPGVAQSqyfDLP--LTQPINH 756
|
....*.
gi 755512845 1029 GAPGAP 1034
Cdd:PHA03379 757 GAPAAH 762
|
|
| DUF4813 |
pfam16072 |
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. ... |
847-943 |
2.98e-03 |
|
Domain of unknown function (DUF4813); This family of proteins is functionally uncharacterized. This family of proteins is found in eukaryotes. Proteins in this family are typically between 345 and 672 amino acids in length.
Pssm-ID: 435117 [Multi-domain] Cd Length: 288 Bit Score: 40.90 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 847 TGGAAAYRPQQPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPtsssaasfPPPSSGASFQHGGPGAPPSSSAYA 926
Cdd:pfam16072 163 AGGQQPAAPAAPAYPVAPAAYPAQAPAAAPAPAPGAPQTPLAPLNPVA--------AAPAAAAGAAAAPVVAAAAPAAAA 234
|
90
....*....|....*..
gi 755512845 927 LPPGTTGPQNGWNDPPA 943
Cdd:pfam16072 235 PPPPAPAAPPADAAPPA 251
|
|
| DUF3824 |
pfam12868 |
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ... |
755-871 |
3.18e-03 |
|
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.
Pssm-ID: 372351 [Multi-domain] Cd Length: 145 Bit Score: 39.34 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 755 SGQESSQSPYERQPLSKGRPGPVAGHsqmprvqtQQYYPHGEN-PPPPGFIMQGNVIPNPAAPL-PTAPGHMPSqlppyp 832
Cdd:pfam12868 47 DYRDYYEDPYSPSPYPPSPAGPYASQ--------GQYYPETNYfPPPPGSTPQPPVDPQPNAPPpPYNPADYPP------ 112
|
90 100 110
....*....|....*....|....*....|....*....
gi 755512845 833 qpqpyqpaqqysfGTGGAAAYRPQQPVAPPASNAYPNTP 871
Cdd:pfam12868 113 -------------PPGAAPPPQPYQYPPPPGPDPYAPRP 138
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
962-1128 |
3.41e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 41.61 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 962 PITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGVQQPLAQtgmPPSFSKPNTEGAPGAPIGNTIQH 1041
Cdd:PRK10263 747 PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAP---QPQYQQPQQPVAPQPQYQQPQQP 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 1042 VQALPTEKITKKPI---PEEHLILKTTFEDLIQRCLSSATDPQTKrklddaskrLEFLYDKLREqtLSPTIINGLHSIAR 1118
Cdd:PRK10263 824 VAPQPQYQQPQQPVapqPQDTLLHPLLMRNGDSRPLHKPTTPLPS---------LDLLTPPPSE--VEPVDTFALEQMAR 892
|
170 180
....*....|....*....|.
gi 755512845 1119 SIETR-----------NYSEG 1128
Cdd:PRK10263 893 LVEARladfrikadvvNYSPG 913
|
|
| PHA03379 |
PHA03379 |
EBNA-3A; Provisional |
759-1056 |
6.51e-03 |
|
EBNA-3A; Provisional
Pssm-ID: 223066 [Multi-domain] Cd Length: 935 Bit Score: 40.81 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 759 SSQSPyERQPLSKGRPGPVAGHSQMPRVQTQQYYPHGENPPPPGFIMQGNVI-PNPA-APLPTAPGHMpsqlppypqpqp 836
Cdd:PHA03379 439 SAQVP-EPPPVHDLEPGPLHDQHSMAPCPVAQLPPGPLQDLEPGDQLPGVVQdGRPAcAPVPAPAGPI------------ 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 837 yqpaqqysfgtggaaaYRPQQPvappasnAYPNTPYISPvASYSGQPqMYTAQQASSPTSSSAASFPPPSSGASfqhGGP 916
Cdd:PHA03379 506 ----------------VRPWEA-------SLSQVPGVAF-APVMPQP-MPVEPVPVPTVALERPVCPAPPLIAM---QGP 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 917 GAPPS----SSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMnpsgdpqSQGLQQQPSTpGPLSsh 992
Cdd:PHA03379 558 GETSGivrvRERWRPAPWTPNPPRSPSQMSVRDRLARLRAEAQPYQASVEVQPPQL-------TQVSPQQPME-YPLE-- 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755512845 993 asfPQQHLAGGQPFHGVQQPLAQTGM----PPSFS----KPNTEGAPGAPIGNTIQHVQALPTEKITKKPIP 1056
Cdd:PHA03379 628 ---PEQQMFPGSPFSQVADVMRAGGVpamqPQYFDlplqQPISQGAPLAPLRASMGPVPPVPATQPQYFDIP 696
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
775-1014 |
7.52e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.63 E-value: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 775 GPVAghSQMPRVQTQQYYPHGENPPPPgfimqgnVIPNPAAPLPTAPGHMPSQLPPYPQPQPYQPAQQYSFGTGGAAAYR 854
Cdd:PRK12323 380 APVA--QPAPAAAAPAAAAPAPAAPPA-------APAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAP 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 855 PQQPVAPPASNAYPNTPYISPVASYSGQPQmytAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPPGTTGP 934
Cdd:PRK12323 451 APAPAAAPAAAARPAAAGPRPVAAAAAAAP---ARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIP 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 935 QNGWNDPPAlNRVPKKKKMPENFMPPVPITSPIMNPSGDPQsqglQQQPSTPGplSSHASFPQqhLAGGQPFHGVQQPLA 1014
Cdd:PRK12323 528 DPATADPDD-AFETLAPAPAAAPAPRAAAATEPVVAPRPPR----ASASGLPD--MFDGDWPA--LAARLPVRGLAQQLA 598
|
|
| PRK10263 |
PRK10263 |
DNA translocase FtsK; Provisional |
915-1015 |
7.68e-03 |
|
DNA translocase FtsK; Provisional
Pssm-ID: 236669 [Multi-domain] Cd Length: 1355 Bit Score: 40.45 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 915 GPGAP---PSSSAYALPPGTTGPQNGWNDPPALNRVPKKKKMPENFMPPVPITSPIMNPSGDPQSQGLQQQPSTPGPLSS 991
Cdd:PRK10263 739 GPHEPlftPIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQ 818
|
90 100
....*....|....*....|....
gi 755512845 992 HasfPQQHLAGGQPFHGVQQPLAQ 1015
Cdd:PRK10263 819 Q---PQQPVAPQPQYQQPQQPVAP 839
|
|
| PRK12323 |
PRK12323 |
DNA polymerase III subunit gamma/tau; |
850-1034 |
9.30e-03 |
|
DNA polymerase III subunit gamma/tau;
Pssm-ID: 237057 [Multi-domain] Cd Length: 700 Bit Score: 40.24 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 850 AAAYRPqqPVAPPASNAYPNTPYISPVASYSGQPQMYTAQQASSPTSSSAASFPPPSSGASFQHGGPGAPPSSSAYALPP 929
Cdd:PRK12323 387 PAAAAP--AAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARP 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755512845 930 GTTGPQngwnDPPALNRVPKKkkmpenfmPPVPITSPIMNPSGDPQSQGLQQQPSTPGPLSSHASFPQQHLAGGQPFHGV 1009
Cdd:PRK12323 465 AAAGPR----PVAAAAAAAPA--------RAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATA 532
|
170 180
....*....|....*....|....*
gi 755512845 1010 QQPLAQTGMPPSFSKPNTEGAPGAP 1034
Cdd:PRK12323 533 DPDDAFETLAPAPAAAPAPRAAAAT 557
|
|
|