|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
806-1215 |
1.86e-68 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 236.35 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 806 STWSADGSQIICAARNTVFVFDVETSDLLLKLKTSRLSTIQFCHACPNSSLLAVALSHYTVELWNFESSKKKAECSGHLS 885
Cdd:COG2319 42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 886 WVHCVQFSPDGSLLLSSSDDQTIRLWETDrvhtssavalkrdtdvlsshsdatiiapdSSNRLQVLSGSTGAVvleseel 965
Cdd:COG2319 122 AVRSVAFSPDGKTLASGSADGTVRLWDLA-----------------------------TGKLLRTLTGHSGAV------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 966 ssriRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-V 1044
Cdd:COG2319 166 ----TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLrT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1045 LQGHMEPVRkfhllsssssphLFSWS----------FDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSAN 1114
Cdd:COG2319 242 LTGHSGSVR------------SVAFSpdgrllasgsADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1115 RTAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHF 1194
Cdd:COG2319 310 GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG---------HTGAVTSVAF 380
|
410 420
....*....|....*....|...
gi 18858279 1195 SPDNRVLVSTA--GYIKWWSVES 1215
Cdd:COG2319 381 SPDGRTLASGSadGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
567-1039 |
6.19e-63 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 220.55 E-value: 6.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 567 QLALSQPDRSEVYRQALMQAQKRASRGQIYLNWVNKNIEEGLSRLVMHPHQGAVYYACFSKDGSKIASCGASKALRVFKS 646
Cdd:COG2319 28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 647 TSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIREFEvEHEEQINHCQFTNTGRRvlLATCSNDK 726
Cdd:COG2319 108 ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKL--LASGSDDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 727 ftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFEVSSANEWKSIDVDSffpesdeeikAMVKCS 806
Cdd:COG2319 185 --TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS----------GSVRSV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 807 TWSADGsqiicaarntvfvfdvetsdlllklktsrlstiqfchacpnsSLLAVALSHYTVELWNFESSKKKAECSGHLSW 886
Cdd:COG2319 253 AFSPDG------------------------------------------RLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 887 VHCVQFSPDGSLLLSSSDDQTIRLWETdrvhtssavalkrdtdvlsshsdatiiapDSSNRLQVLSGSTGAVvleseels 966
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRLWDL-----------------------------ATGKLLRTLTGHTGAV-------- 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858279 967 sriRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRT 1039
Cdd:COG2319 334 ---RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
616-912 |
8.29e-59 |
|
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: 204.49 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 616 HQGAVYYACFSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIR 695
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 696 EFEvEHEEQINHCQFTNTGRrvLLATCSNDKftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLF 775
Cdd:cd00200 88 TLT-GHTSYVSSVAFSPDGR--ILSSSSRDK--TIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 776 EVSSANEwksidVDSFFPESDEeikamVKCSTWSADGSQII-CAARNTVFVFDVETSDlLLKLKTSRLSTIQFCHACPNS 854
Cdd:cd00200 163 DLRTGKC-----VATLTGHTGE-----VNSVAFSPDGEKLLsSSSDGTIKLWDLSTGK-CLGTLRGHENGVNSVAFSPDG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 18858279 855 SLLAVALSHYTVELWNFESSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
457-589 |
2.99e-56 |
|
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein.
Pssm-ID: 465560 Cd Length: 135 Bit Score: 191.10 E-value: 2.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 457 ELHKKMVRQYQRFYSKRPPDSADKDSLYWYQFIPYHMAKAGLSKELYSLMFSLDWVKEKARIMGSAHLINDYVEYGEILD 536
Cdd:pfam17908 3 DLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHILD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 18858279 537 KENSEVRVQFQEFLSLNGHHLEQRPFPDVVQLALSQPDRSEVYRQALMQAQKR 589
Cdd:pfam17908 83 ENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
877-1212 |
5.80e-55 |
|
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: 193.32 E-value: 5.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 877 KAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWETDRVHTssavalkrdtdvlsshsdatiiapdssnrLQVLSGSTG 956
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-----------------------------LRTLKGHTG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 957 AVVleseelssRIRCSCISRnaaFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWK 1036
Cdd:cd00200 53 PVR--------DVAASADGT---YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1037 WRTGEC-MVLQGHMEPVRKFHLLSSSSSPHLFswSFDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANR 1115
Cdd:cd00200 122 VETGKClTTLRGHTDWVNSVAFSPDGTFVASS--SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1116 TAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHFS 1195
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG---------HTNSVTSLAWS 270
|
330
....*....|....*....
gi 18858279 1196 PDNRVLVSTA--GYIKWWS 1212
Cdd:cd00200 271 PDGKRLASGSadGTIRIWD 289
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
6.99e-45 |
|
Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260034 Cd Length: 86 Bit Score: 156.51 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 7 SRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLASL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 18858279 87 LHSDLP 92
Cdd:cd08323 81 LHDGLP 86
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
145-370 |
2.28e-44 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 161.39 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 145 DTPGWVTVFGMAGSGKSVMAAEVVRDRSLIKECFpDGVHWLSVGQC--ERADLLVRMQSLCFRLEQCQSSDTSqrppstv 222
Cdd:pfam00931 16 DEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHF-DSVAWVVVSKTftISTLQQTILQNLGLSEDDWDNKEEG------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 223 eEAKERLRFLMLRRfpRSLLILDDVWDSSSLR-------SFDIQCRVLLTTRNRALTDSVSGvRYEVPVENGLDEEKALE 295
Cdd:pfam00931 88 -ELARKIRRALLTK--RFLLVLDDVWDEEDWDkigiplpDRENGCRVLLTTRSEEVAGRVGG-PSDPHEVELLEPDEAWE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 296 ILALYVN----GKMHKLPEQARSIVSECKGSPLVVSLIGALL--REFPDRWSYYLRQLQQKQfkrirKSSSYDYEALDQA 369
Cdd:pfam00931 164 LFENKVFpktlGECELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL-----KSNSYSLNSVRSI 238
|
.
gi 18858279 370 M 370
Cdd:pfam00931 239 L 239
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
2.31e-17 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.
Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 77.99 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 6 RSRLLRSKATLEQDIK-ASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALiRESYGDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEAL-KEGDPDLA 79
|
....*.
gi 18858279 85 SLLHSD 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-386 |
2.03e-10 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 65.33 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 119 VPQRPVVFVSRPPLLNLIREMLYQLRDTPGWVTVFGMAGSGKSVMAAEVV-RDRSLIkecfpDGVHWLSVGQCER----- 192
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEYAhRFRADY-----DLVWWIPADQPELvrasl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 193 ADLLVRMqslcfRLEqcqssdtsqRPPSTVEEAKERLRfLMLRR---FPRSLLILDDVWDSSSLRSF---DIQCRVLLTT 266
Cdd:NF040586 76 AELARRL-----GLP---------LGPDDVDEAARAVL-DALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 267 RNRALTDsVSGVRYEVPVengLDEEKALEILALYVNGKMhkLPEQARSIVSECKGSPLVVSLIGALLREFPDRWSYYLRQ 346
Cdd:NF040586 141 RNRAWSE-VAAATLEVDV---FSREESVALLRRRVPGLT--SEEDADRLAEALGDLPLALEQAAAWLAETGMPVDEYLRL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18858279 347 LQQKQFKRI-RKSSSYDYEALDQAM-DASLQVLEAEHQELYR 386
Cdd:NF040586 215 LDEQATAALlLELKPPGYPTSVAATwRLSLDRLRERSPAAAR 256
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
873-912 |
4.23e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 53.09 E-value: 4.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18858279 873 SSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
648-687 |
7.45e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 52.31 E-value: 7.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18858279 648 SGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWN 687
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
874-912 |
2.31e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 51.19 E-value: 2.31e-08
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 874 SKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
649-687 |
8.16e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 49.65 E-value: 8.16e-08
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 649 GEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWN 687
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
630-826 |
1.01e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 53.17 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 630 SKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSP-DDRHIATCASDRKVKLWNVERGVLIREFEVeheeQINHC 708
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKT----KANIC 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 709 --QFTNTGRRVLLATCSNDKFTNTRLWNPnkKTSQNTMFGHMEPVNHCCFSPNDLyLATSSSDGSLKLFEVS-SANEWKS 785
Cdd:PLN00181 622 cvQFPSESGRSLAFGSADHKVYYYDLRNP--KLPLCTMIGHSKTVSYVRFVDSST-LVSSSTDNTLKLWDLSmSISGINE 698
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18858279 786 IDVDSFFPESDeeIKAMVKCSTwsADGSQIICAARNTVFVF 826
Cdd:PLN00181 699 TPLHSFMGHTN--VKNFVGLSV--SDGYIATGSETNEVFVY 735
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
1070-1121 |
4.78e-05 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 47.77 E-value: 4.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 18858279 1070 SFDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSS-DGRLFATTSANRTAKVWS 1121
Cdd:PLN00181 552 NFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWS 604
|
|
| CARD |
smart00114 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-87 |
1.00e-04 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.
Pssm-ID: 128424 Cd Length: 88 Bit Score: 42.32 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1 MEERARSRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALiRESY 80
Cdd:smart00114 1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSL-QETD 79
|
....*..
gi 18858279 81 GDLASLL 87
Cdd:smart00114 80 QKLADFL 86
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
806-1215 |
1.86e-68 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 236.35 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 806 STWSADGSQIICAARNTVFVFDVETSDLLLKLKTSRLSTIQFCHACPNSSLLAVALSHYTVELWNFESSKKKAECSGHLS 885
Cdd:COG2319 42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 886 WVHCVQFSPDGSLLLSSSDDQTIRLWETDrvhtssavalkrdtdvlsshsdatiiapdSSNRLQVLSGSTGAVvleseel 965
Cdd:COG2319 122 AVRSVAFSPDGKTLASGSADGTVRLWDLA-----------------------------TGKLLRTLTGHSGAV------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 966 ssriRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-V 1044
Cdd:COG2319 166 ----TSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLrT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1045 LQGHMEPVRkfhllsssssphLFSWS----------FDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSAN 1114
Cdd:COG2319 242 LTGHSGSVR------------SVAFSpdgrllasgsADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1115 RTAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHF 1194
Cdd:COG2319 310 GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTG---------HTGAVTSVAF 380
|
410 420
....*....|....*....|...
gi 18858279 1195 SPDNRVLVSTA--GYIKWWSVES 1215
Cdd:COG2319 381 SPDGRTLASGSadGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
809-1243 |
7.34e-65 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 225.95 E-value: 7.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 809 SADGSQIICAARNTVFVFDVETSDLLLKLKTSRLSTIQFCHACPNSSLLAVALSHYTVELWNFESSKKKAECSGHLSWVH 888
Cdd:COG2319 3 SADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 889 CVQFSPDGSLLLSSSDDQTIRLWETDrvhtssavalkrdtdvlsshsdatiiapdssnrlqvlsgsTGAVVLESEELSSR 968
Cdd:COG2319 83 SVAFSPDGRLLASASADGTVRLWDLA----------------------------------------TGLLLRTLTGHTGA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 969 IRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-VLQG 1047
Cdd:COG2319 123 VRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLrTLTG 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1048 HMEPVRkfhllsssssphLFSWS----------FDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTA 1117
Cdd:COG2319 203 HTGAVR------------SVAFSpdgkllasgsADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1118 KVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHFSPD 1197
Cdd:COG2319 271 RLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG---------HTGAVRSVAFSPD 341
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 18858279 1198 NRVLVSTA--GYIKWWSVESGEALQTFYTMGGNLKKIHVSPDFSTFIT 1243
Cdd:COG2319 342 GKTLASGSddGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
666-1164 |
5.06e-63 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 220.55 E-value: 5.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 666 AFSPDDRHIATCASDRKVKLWNVERGVLIREFEVEHEEQINHCQFTNTGRRVLLATcsndkFTNTRLWNPNKKTSQNTMF 745
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAG-----DLTLLLLDAAAGALLATLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 746 GHMEPVNHCCFSPNDLYLATSSSDGSLKLFEVSSANEwksidvdsffPESDEEIKAMVKCSTWSADGSqiicaarntvfv 825
Cdd:COG2319 76 GHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLL----------LRTLTGHTGAVRSVAFSPDGK------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 826 fdvetsdlllklktsrlstiqfchacpnssLLAVALSHYTVELWNFESSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDD 905
Cdd:COG2319 134 ------------------------------TLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 906 QTIRLWETDrvhtssavalkrdtdvlsshsdatiiapdSSNRLQVLSGSTGAVvleseelssriRCSCISRNAAFVALGS 985
Cdd:COG2319 184 GTVRLWDLA-----------------------------TGKLLRTLTGHTGAV-----------RSVAFSPDGKLLASGS 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 986 EDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-VLQGHMEPVRkfhllsssssp 1064
Cdd:COG2319 224 ADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLrTLTGHSGGVN----------- 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1065 hLFSWS----------FDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWSSASWKMLFLLEGH 1134
Cdd:COG2319 293 -SVAFSpdgkllasgsDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGH 371
|
490 500 510
....*....|....*....|....*....|
gi 18858279 1135 KDCVRSCRFSWDNKRLATGDDNGEIRLWSM 1164
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
567-1039 |
6.19e-63 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 220.55 E-value: 6.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 567 QLALSQPDRSEVYRQALMQAQKRASRGQIYLNWVNKNIEEGLSRLVMHPHQGAVYYACFSKDGSKIASCGASKALRVFKS 646
Cdd:COG2319 28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 647 TSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIREFEvEHEEQINHCQFTNTGRRvlLATCSNDK 726
Cdd:COG2319 108 ATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKL--LASGSDDG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 727 ftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFEVSSANEWKSIDVDSffpesdeeikAMVKCS 806
Cdd:COG2319 185 --TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS----------GSVRSV 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 807 TWSADGsqiicaarntvfvfdvetsdlllklktsrlstiqfchacpnsSLLAVALSHYTVELWNFESSKKKAECSGHLSW 886
Cdd:COG2319 253 AFSPDG------------------------------------------RLLASGSADGTVRLWDLATGELLRTLTGHSGG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 887 VHCVQFSPDGSLLLSSSDDQTIRLWETdrvhtssavalkrdtdvlsshsdatiiapDSSNRLQVLSGSTGAVvleseels 966
Cdd:COG2319 291 VNSVAFSPDGKLLASGSDDGTVRLWDL-----------------------------ATGKLLRTLTGHTGAV-------- 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858279 967 sriRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRT 1039
Cdd:COG2319 334 ---RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
625-1124 |
1.71e-59 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 210.54 E-value: 1.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 625 FSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIREFEvEHEEQ 704
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 705 INHCQFTNTGRRvlLATCSNDKftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFEVSSANEWK 784
Cdd:COG2319 81 VLSVAFSPDGRL--LASASADG--TVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 785 SIDVDSffpesdeeikAMVKCSTWSADGSQIICAAR-NTVFVFDVETSDLLLKLKtsrlstiqfchacpnssllavalsh 863
Cdd:COG2319 157 TLTGHS----------GAVTSVAFSPDGKLLASGSDdGTVRLWDLATGKLLRTLT------------------------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 864 ytvelwnfesskkkaecsGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWETDrvhtssavalkrdtdvlsshsdatiiapd 943
Cdd:COG2319 202 ------------------GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA----------------------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 944 SSNRLQVLSGSTGAVvleseelssriRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEIL 1023
Cdd:COG2319 235 TGKLLRTLTGHSGSV-----------RSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1024 ITSSEDSTIRVWKWRTGECM-VLQGHMEPVRkfhllsssssphLFSWS----------FDGTVKVWDLTRGQMLQDLVCH 1092
Cdd:COG2319 304 ASGSDDGTVRLWDLATGKLLrTLTGHTGAVR------------SVAFSpdgktlasgsDDGTVRLWDLATGELLRTLTGH 371
|
490 500 510
....*....|....*....|....*....|..
gi 18858279 1093 EGAVLSCDVSSDGRLFATTSANRTAKVWSSAS 1124
Cdd:COG2319 372 TGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
616-912 |
8.29e-59 |
|
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: 204.49 E-value: 8.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 616 HQGAVYYACFSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIR 695
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 696 EFEvEHEEQINHCQFTNTGRrvLLATCSNDKftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLF 775
Cdd:cd00200 88 TLT-GHTSYVSSVAFSPDGR--ILSSSSRDK--TIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 776 EVSSANEwksidVDSFFPESDEeikamVKCSTWSADGSQII-CAARNTVFVFDVETSDlLLKLKTSRLSTIQFCHACPNS 854
Cdd:cd00200 163 DLRTGKC-----VATLTGHTGE-----VNSVAFSPDGEKLLsSSSDGTIKLWDLSTGK-CLGTLRGHENGVNSVAFSPDG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 18858279 855 SLLAVALSHYTVELWNFESSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
891-1252 |
3.32e-57 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 203.99 E-value: 3.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 891 QFSPDGSLLLSSSDDQTIRLW--ETDRVHTSSAVALKRDTDVLSSHSDATIIAPDSSNRLQVLSGSTGAVVLESEELSSR 968
Cdd:COG2319 1 ALSADGAALAAASADLALALLaaALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 969 IRCSCISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-VLQG 1047
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLrTLTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1048 HMEPVRkfhllsssssphLFSWS----------FDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTA 1117
Cdd:COG2319 161 HSGAVT------------SVAFSpdgkllasgsDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1118 KVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHFSPD 1197
Cdd:COG2319 229 RLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTG---------HSGGVNSVAFSPD 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 18858279 1198 NRVLVSTA--GYIKWWSVESGEALQTFYTMGGNLKKIHVSPDFSTFITVDSIGILYI 1252
Cdd:COG2319 300 GKLLASGSddGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
457-589 |
2.99e-56 |
|
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein.
Pssm-ID: 465560 Cd Length: 135 Bit Score: 191.10 E-value: 2.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 457 ELHKKMVRQYQRFYSKRPPDSADKDSLYWYQFIPYHMAKAGLSKELYSLMFSLDWVKEKARIMGSAHLINDYVEYGEILD 536
Cdd:pfam17908 3 DLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHILD 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 18858279 537 KENSEVRVQFQEFLSLNGHHLEQRPFPDVVQLALSQPDRSEVYRQALMQAQKR 589
Cdd:pfam17908 83 ENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
877-1212 |
5.80e-55 |
|
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: 193.32 E-value: 5.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 877 KAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWETDRVHTssavalkrdtdvlsshsdatiiapdssnrLQVLSGSTG 956
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL-----------------------------LRTLKGHTG 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 957 AVVleseelssRIRCSCISRnaaFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWK 1036
Cdd:cd00200 53 PVR--------DVAASADGT---YLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1037 WRTGEC-MVLQGHMEPVRKFHLLSSSSSPHLFswSFDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANR 1115
Cdd:cd00200 122 VETGKClTTLRGHTDWVNSVAFSPDGTFVASS--SQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1116 TAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWSMLDGALLKICPRdtkdsmnsyHAGWVTDLHFS 1195
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG---------HTNSVTSLAWS 270
|
330
....*....|....*....
gi 18858279 1196 PDNRVLVSTA--GYIKWWS 1212
Cdd:cd00200 271 PDGKRLASGSadGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
654-1121 |
1.51e-50 |
|
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: 180.61 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 654 ELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWNVERGVLIREFEVeHEEQINHCQFTNTGRRvlLATCSNDKFtnTRLW 733
Cdd:cd00200 4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTY--LASGSSDKT--IRLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 734 NPNKKTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKlfevssanewksidvdsffpesdeeikamvkcstwsadgs 813
Cdd:cd00200 79 DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIK---------------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 814 qiicaarntvfvfdvetsdlllklktsrlstiqfchacpnssllavalshytveLWNFESSKKKAECSGHLSWVHCVQFS 893
Cdd:cd00200 119 ------------------------------------------------------VWDVETGKCLTTLRGHTDWVNSVAFS 144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 894 PDGSLLLSSSDDQTIRLWEtdrvhtssavalkrdtdvlsshsdatiiaPDSSNRLQVLSGSTGAVvleseelssriRCSC 973
Cdd:cd00200 145 PDGTFVASSSQDGTIKLWD-----------------------------LRTGKCVATLTGHTGEV-----------NSVA 184
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 974 ISRNAAFVALGSEDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECMvlqghmepvr 1053
Cdd:cd00200 185 FSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECV---------- 254
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18858279 1054 kfhllsssssphlfswsfdgtvkvwdltrgqmlQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWS 1121
Cdd:cd00200 255 ---------------------------------QTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
746-1163 |
2.32e-48 |
|
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: 174.45 E-value: 2.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 746 GHMEPVNHCCFSPNDLYLATSSSDGSLKlfevssanewksidvdsffpesdeeikamvkcstwsadgsqiicaarntvfV 825
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATGSGDGTIK---------------------------------------------------V 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 826 FDVETSDLLLKLKTSRLStIQFCHACPNSSLLAVALSHYTVELWNFESSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDD 905
Cdd:cd00200 36 WDLETGELLRTLKGHTGP-VRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRD 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 906 QTIRLWETdrvhtssavalkrdtdvlsshsdatiiapDSSNRLQVLSGSTGAVvleseelssriRCSCISRNAAFVALGS 985
Cdd:cd00200 115 KTIKVWDV-----------------------------ETGKCLTTLRGHTDWV-----------NSVAFSPDGTFVASSS 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 986 EDGTVQVIEVPSSKASVKLSGHTKTVHHCQFTDDCEILITSSEDSTIrvwkwrtgecmvlqghmepvrkfhllsssssph 1065
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTI--------------------------------- 201
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1066 lfswsfdgtvKVWDLTRGQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWSSASWKMLFLLEGHKDCVRSCRFSW 1145
Cdd:cd00200 202 ----------KLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
|
410
....*....|....*...
gi 18858279 1146 DNKRLATGDDNGEIRLWS 1163
Cdd:cd00200 272 DGKRLASGSADGTIRIWD 289
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
6.99e-45 |
|
Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260034 Cd Length: 86 Bit Score: 156.51 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 7 SRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLASL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 18858279 87 LHSDLP 92
Cdd:cd08323 81 LHDGLP 86
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
145-370 |
2.28e-44 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 161.39 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 145 DTPGWVTVFGMAGSGKSVMAAEVVRDRSLIKECFpDGVHWLSVGQC--ERADLLVRMQSLCFRLEQCQSSDTSqrppstv 222
Cdd:pfam00931 16 DEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHF-DSVAWVVVSKTftISTLQQTILQNLGLSEDDWDNKEEG------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 223 eEAKERLRFLMLRRfpRSLLILDDVWDSSSLR-------SFDIQCRVLLTTRNRALTDSVSGvRYEVPVENGLDEEKALE 295
Cdd:pfam00931 88 -ELARKIRRALLTK--RFLLVLDDVWDEEDWDkigiplpDRENGCRVLLTTRSEEVAGRVGG-PSDPHEVELLEPDEAWE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 296 ILALYVN----GKMHKLPEQARSIVSECKGSPLVVSLIGALL--REFPDRWSYYLRQLQQKQfkrirKSSSYDYEALDQA 369
Cdd:pfam00931 164 LFENKVFpktlGECELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL-----KSNSYSLNSVRSI 238
|
.
gi 18858279 370 M 370
Cdd:pfam00931 239 L 239
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1004-1252 |
8.34e-43 |
|
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: 158.27 E-value: 8.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1004 LSGHTKTVHHCQFTDDCEILITSSEDSTIRVWKWRTGECM-VLQGHMEPVRKFHLLSSSSSPHLFswSFDGTVKVWDLTR 1082
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLrTLKGHTGPVRDVAASADGTYLASG--SSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1083 GQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWSSASWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLW 1162
Cdd:cd00200 83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1163 SMLDGALLKICPRdtkdsmnsyHAGWVTDLHFSPDNRVLVSTA--GYIKWWSVESGEALQTFYTMGGNLKKIHVSPDFST 1240
Cdd:cd00200 163 DLRTGKCVATLTG---------HTGEVNSVAFSPDGEKLLSSSsdGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYL 233
|
250
....*....|..
gi 18858279 1241 FITVDSIGILYI 1252
Cdd:cd00200 234 LASGSEDGTIRV 245
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
603-776 |
4.27e-28 |
|
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: 115.51 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 603 NIEEGLSRLVMHPHQGAVYYACFSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRK 682
Cdd:cd00200 121 DVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 683 VKLWNVERGVLIREFEVeHEEQINHCQFTNTGRrvLLATCSNDKftNTRLWNPNKKTSQNTMFGHMEPVNHCCFSPNDLY 762
Cdd:cd00200 201 IKLWDLSTGKCLGTLRG-HENGVNSVAFSPDGY--LLASGSEDG--TIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKR 275
|
170
....*....|....
gi 18858279 763 LATSSSDGSLKLFE 776
Cdd:cd00200 276 LASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
593-734 |
1.79e-20 |
|
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: 93.17 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 593 GQIYLnWvnkNIEEGLSRLVMHPHQGAVYYACFSKDGSKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSPDDR 672
Cdd:cd00200 157 GTIKL-W---DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGY 232
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18858279 673 HIATCASDRKVKLWNVERGVLIREFEvEHEEQINHCQFTNTGRRvlLATCSNDKftNTRLWN 734
Cdd:cd00200 233 LLASGSEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKR--LASGSADG--TIRIWD 289
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
2.31e-17 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.
Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 77.99 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 6 RSRLLRSKATLEQDIK-ASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALiRESYGDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEAL-KEGDPDLA 79
|
....*.
gi 18858279 85 SLLHSD 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| CARD |
cd01671 |
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-87 |
7.97e-16 |
|
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 73.32 E-value: 7.97e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18858279 9 LLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLASLL 87
Cdd:cd01671 1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
47-590 |
1.31e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 72.74 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 47 ATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLASLLHSDLPLLSPEGEKSFADGVSPSVQAILSVGGVPQRPVVF 126
Cdd:COG3903 76 LLLLLAARLLARLAAAAAAALARAAAAALALLLRLRLAARRLLLARALAAAALAAAAAAAAAAAAAPAPPPPAPPPPAPL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 127 VSRPPLLNLIREMLYQLRDTPGWVTVFGMAGSGKSVMAAEVVRDRSlikECFPDGVHWLSVGQCERADLLVRM--QSLCF 204
Cdd:COG3903 156 AALARRAAALAAAARALLSAARLVTLTGPGGVGKTRLALEVAHRLA---DRFPDGVWFVDLAGVTDPALVLAAvaRALGV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 205 RleqcqssDTSQRPPStveeakERLR-FLMLRrfpRSLLILD---DVWDSSS-----LRSFDIQCRVLLTTRnRALTdsV 275
Cdd:COG3903 233 R-------DAPGRDPA------ARLRaALADR---RLLLVLDnceHVVDAAAalvrpLLPAAPGLRVLATSR-EPLG--L 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 276 SG-VRYEVPV------ENGLDEEKALEILALYVNGKMHKL------PEQARSIVSECKGSPLVVSLIGALLREFP----- 337
Cdd:COG3903 294 PGeRVLPLPPlavpppGAEALASEAVALFVERAGAARPGFaldaaeAAAVAEICRRLDGLPLAIELAAARLRTLSlaela 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 338 DRWSYYLRQLQqkqfkRIRKSSSYDYEALDQAMDASLQVLEAEHQELYRDLSVMQKDIKVPAkVLSVLWGLELEEVEDVL 417
Cdd:COG3903 374 ARLDDRLRLLT-----GGRRDAPPRHRTLRAALDWSYDLLSPAERRLLRRLSVFPGGFTLEA-AEAVCGGDGPADVLDLL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 418 QEFVNKSLLFRDCNQRPYRYYLHDLQLDFLAEQ--NRDQIAELHKKMVRQYQRFYSKRPPDSADKDSLYWYqfipyhmak 495
Cdd:COG3903 448 AALVDKSLLEVEGGGGGPRYRLLETVREYAAERlaEAGERAAARRRHADYYLALAERAAAELRGPDQLAWL--------- 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 496 AGLSKELYSLMFSLDWVKEKARIMGSAHLINDYVEYGEILDkENSEVRVQFQEFLSLNGHHLEQRPFPDVVQLALSQPDR 575
Cdd:COG3903 519 ARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRG-LLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARA 597
|
570
....*....|....*
gi 18858279 576 SEVYRQALMQAQKRA 590
Cdd:COG3903 598 AAAAAAAAAAAAAAA 612
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-386 |
2.03e-10 |
|
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.
Pssm-ID: 468560 [Multi-domain] Cd Length: 836 Bit Score: 65.33 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 119 VPQRPVVFVSRPPLLNLIREMLYQLRDTPGWVTVFGMAGSGKSVMAAEVV-RDRSLIkecfpDGVHWLSVGQCER----- 192
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEYAhRFRADY-----DLVWWIPADQPELvrasl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 193 ADLLVRMqslcfRLEqcqssdtsqRPPSTVEEAKERLRfLMLRR---FPRSLLILDDVWDSSSLRSF---DIQCRVLLTT 266
Cdd:NF040586 76 AELARRL-----GLP---------LGPDDVDEAARAVL-DALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 267 RNRALTDsVSGVRYEVPVengLDEEKALEILALYVNGKMhkLPEQARSIVSECKGSPLVVSLIGALLREFPDRWSYYLRQ 346
Cdd:NF040586 141 RNRAWSE-VAAATLEVDV---FSREESVALLRRRVPGLT--SEEDADRLAEALGDLPLALEQAAAWLAETGMPVDEYLRL 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 18858279 347 LQQKQFKRI-RKSSSYDYEALDQAM-DASLQVLEAEHQELYR 386
Cdd:NF040586 215 LDEQATAALlLELKPPGYPTSVAATwRLSLDRLRERSPAAAR 256
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
873-912 |
4.23e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 53.09 E-value: 4.23e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18858279 873 SSKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
648-687 |
7.45e-09 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 52.31 E-value: 7.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18858279 648 SGEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWN 687
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| CARD_CASP2 |
cd08332 |
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ... |
1-87 |
2.21e-08 |
|
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260040 Cd Length: 87 Bit Score: 52.43 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1 MEERARSRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESY 80
Cdd:cd08332 1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80
|
....*..
gi 18858279 81 GDLASLL 87
Cdd:cd08332 81 EHLADLL 87
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
874-912 |
2.31e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 51.19 E-value: 2.31e-08
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 874 SKKKAECSGHLSWVHCVQFSPDGSLLLSSSDDQTIRLWE 912
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| CARD_CASP9 |
cd08326 |
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
6-87 |
2.58e-08 |
|
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 176740 Cd Length: 84 Bit Score: 52.43 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 6 RSRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALIRESYGDLAS 85
Cdd:cd08326 2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAE 81
|
..
gi 18858279 86 LL 87
Cdd:cd08326 82 LL 83
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
649-687 |
8.16e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 49.65 E-value: 8.16e-08
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 649 GEKLLELQAHEEDVLCCAFSPDDRHIATCASDRKVKLWN 687
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
630-826 |
1.01e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 53.17 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 630 SKIASCGASKALRVFKSTSGEKLLELQAHEEDVLCCAFSP-DDRHIATCASDRKVKLWNVERGVLIREFEVeheeQINHC 708
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKT----KANIC 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 709 --QFTNTGRRVLLATCSNDKFTNTRLWNPnkKTSQNTMFGHMEPVNHCCFSPNDLyLATSSSDGSLKLFEVS-SANEWKS 785
Cdd:PLN00181 622 cvQFPSESGRSLAFGSADHKVYYYDLRNP--KLPLCTMIGHSKTVSYVRFVDSST-LVSSSTDNTLKLWDLSmSISGINE 698
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18858279 786 IDVDSFFPESDeeIKAMVKCSTwsADGSQIICAARNTVFVF 826
Cdd:PLN00181 699 TPLHSFMGHTN--VKNFVGLSV--SDGYIATGSETNEVFVY 735
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1124-1163 |
2.19e-06 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 45.38 E-value: 2.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 18858279 1124 SWKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWS 1163
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
742-776 |
8.40e-06 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.84 E-value: 8.40e-06
10 20 30
....*....|....*....|....*....|....*
gi 18858279 742 NTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFE 776
Cdd:smart00320 6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1125-1163 |
1.31e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.10 E-value: 1.31e-05
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 1125 WKMLFLLEGHKDCVRSCRFSWDNKRLATGDDNGEIRLWS 1163
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1004-1036 |
1.33e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 43.07 E-value: 1.33e-05
10 20 30
....*....|....*....|....*....|...
gi 18858279 1004 LSGHTKTVHHCQFTDDCEILITSSEDSTIRVWK 1036
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1083-1121 |
3.26e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 42.30 E-value: 3.26e-05
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 1083 GQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWS 1121
Cdd:smart00320 2 GELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1003-1035 |
3.33e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.95 E-value: 3.33e-05
10 20 30
....*....|....*....|....*....|...
gi 18858279 1003 KLSGHTKTVHHCQFTDDCEILITSSEDSTIRVW 1035
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
1070-1121 |
4.78e-05 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 47.77 E-value: 4.78e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 18858279 1070 SFDGTVKVWDLTRGQMLQDLVCHEGAVLSCDVSS-DGRLFATTSANRTAKVWS 1121
Cdd:PLN00181 552 NFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWS 604
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1083-1121 |
5.24e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.56 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 1083 GQMLQDLVCHEGAVLSCDVSSDGRLFATTSANRTAKVWS 1121
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
738-776 |
7.53e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 41.18 E-value: 7.53e-05
10 20 30
....*....|....*....|....*....|....*....
gi 18858279 738 KTSQNTMFGHMEPVNHCCFSPNDLYLATSSSDGSLKLFE 776
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
940-1164 |
8.64e-05 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 46.87 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 940 IAPDSSNRLqvlsgstgavvLESEELSSRIRCSC-ISRNAAFVALGSE---DGTVQVIEVPSSKAS---VKLSGHTKTVH 1012
Cdd:PTZ00420 10 LYPDPSNNL-----------FDDLRICSRVIDSCgIACSSGFVAVPWEvegGGLIGAIRLENQMRKppvIKLKGHTSSIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1013 HCQFtDDC--EILITSSEDSTIRVWKWRTGE----------CmVLQGHMEPVRKFHLLSSSSSPHLFSwSFDGTVKVWDL 1080
Cdd:PTZ00420 79 DLQF-NPCfsEILASGSEDLTIRVWEIPHNDesvkeikdpqC-ILKGHKKKISIIDWNPMNYYIMCSS-GFDSFVNIWDI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1081 -TRGQMLQDLVCHEGAVLSCDVSsdGRLFATTSAN--------RTAKVWSS-------ASWKMLFL--LEGHKDCVRSCR 1142
Cdd:PTZ00420 156 eNEKRAFQINMPKKLSSLKWNIK--GNLLSGTCVGkhmhiidpRKQEIASSfhihdggKNTKNIWIdgLGGDDNYILSTG 233
|
250 260
....*....|....*....|..
gi 18858279 1143 FSWDNKRlatgddngEIRLWSM 1164
Cdd:PTZ00420 234 FSKNNMR--------EMKLWDL 247
|
|
| CARD |
smart00114 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
1-87 |
1.00e-04 |
|
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.
Pssm-ID: 128424 Cd Length: 88 Bit Score: 42.32 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1 MEERARSRLLRSKATLEQDIKASYLMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNALiRESY 80
Cdd:smart00114 1 MAERDKRLLRRNRVRLGEELGVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSL-QETD 79
|
....*..
gi 18858279 81 GDLASLL 87
Cdd:smart00114 80 QKLADFL 86
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
897-1035 |
1.75e-04 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 45.85 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 897 SLLLSSSDDQTIRLWETDRVH--TSSAVALKRDTDVLSSHSDATIIAPDSSNRLQVLSGSTGAVVLESEELSSRIRCSCI 974
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQlvTEMKEHEKRVWSIDYSSADPTLLASGSDDGSVKLWSINQGVSIGTIKTKANICCVQF 625
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18858279 975 -SRNAAFVALGSEDGTVQVIEVPSSKASV-KLSGHTKTVHHCQFTDDcEILITSSEDSTIRVW 1035
Cdd:PLN00181 626 pSESGRSLAFGSADHKVYYYDLRNPKLPLcTMIGHSKTVSYVRFVDS-STLVSSSTDNTLKLW 687
|
|
| CARD_BIRC2_BIRC3 |
cd08329 |
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
11-75 |
9.50e-04 |
|
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Pssm-ID: 260038 Cd Length: 94 Bit Score: 39.74 E-value: 9.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18858279 11 RSKATLEQDIKASY-LMDHMISDGVLTNDEEAKVLSKATRKEQAVALLETLLRKDNRAYISFYNAL 75
Cdd:cd08329 13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
1019-1145 |
5.21e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 41.03 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18858279 1019 DCEILITSSEDSTIRVW-------KWRTGECMV-LQGHMEPVrKFHLLSSSSSPHLFSWSFDGTVKVWDLTRGQMLQDLV 1090
Cdd:PTZ00421 87 DPQKLFTASEDGTIMGWgipeeglTQNISDPIVhLQGHTKKV-GIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIK 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 18858279 1091 CHEGAVLSCDVSSDGRLFATTSANRTAKVWSSASWKMLFLLEGHKDcVRSCRFSW 1145
Cdd:PTZ00421 166 CHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHAS-AKSQRCLW 219
|
|
| |
