|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
623-1207 |
5.04e-78 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 263.31 E-value: 5.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 623 FSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQV 702
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 703 NCCHFTnkSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSIn 782
Cdd:COG2319 82 LSVAFS--PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 783 vkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqy 862
Cdd:COG2319 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 863 cvelwnidsrlkvadcRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdN 942
Cdd:COG2319 159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLW--------------------------------D 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 943 IRGLQLIagktgqidylpeaqvsccclsphleyvafgdedgaikiielpnnRVFSsgvGHKKAVRHIQFTADGKTLISSS 1022
Cdd:COG2319 191 LATGKLL--------------------------------------------RTLT---GHTGAVRSVAFSPDGKLLASGS 223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1023 EDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKF 1100
Cdd:COG2319 224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1101 SSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGW 1180
Cdd:COG2319 304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT---------LTGHTGA 374
|
570 580
....*....|....*....|....*....
gi 110347471 1181 VTDVCFSPDSKTLVSAG--GYLKWWNVAT 1207
Cdd:COG2319 375 VTSVAFSPDGRTLASGSadGTVRLWDLAT 403
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
453-587 |
4.24e-73 |
|
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: 238.86 E-value: 4.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 453 LQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHI 532
Cdd:pfam17908 1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110347471 533 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQE 587
Cdd:pfam17908 81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
607-910 |
5.89e-73 |
|
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: 244.94 E-value: 5.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 607 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDS 686
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 687 ATGKLVHTYDEHSEQVNCCHFTNksNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGT 766
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 767 LRLWDVRsanerkSINVKRFFLSSEDPpedveviVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEIhTGHHSTIQY 845
Cdd:cd00200 159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347471 846 CDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
129-374 |
8.06e-67 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 225.72 E-value: 8.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 129 RKKLVHAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCMRL 206
Cdd:pfam00931 1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 207 DQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPkHV 279
Cdd:pfam00931 79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 280 VPVESGLGREKGLEILSLFVNMK----KEDLPAEAHSIIKECKGSPLVVSLIGALL--RDFPNRWAYYLRQLQNKQfkri 353
Cdd:pfam00931 150 PHEVELLEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
|
250 260
....*....|....*....|.
gi 110347471 354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931 226 -KSNSYSLNSVRSILQLSYEN 245
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
3.23e-47 |
|
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: 163.45 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 7 NCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAAL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 110347471 87 LQSGLP 92
Cdd:cd08323 81 LHDGLP 86
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
9.51e-20 |
|
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: 84.92 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 6 RNCLLQHREALEKDIKT-SYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLhEGYKDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79
|
....*.
gi 110347471 85 ALLQSG 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
623-772 |
1.94e-11 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 68.57 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 623 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHT 694
Cdd:PLN00181 491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 695 YDEHSEQVNCCHFTNkSNHLLLATGSNDFFLKLWDLNQK-------------------------------------ECRN 737
Cdd:PLN00181 571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110347471 738 ------TMFGHTNSVNHCRFSpDDELLASCSADGTLRLWDV 772
Cdd:PLN00181 650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
732-771 |
3.96e-10 |
|
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: 56.17 E-value: 3.96e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110347471 732 QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 771
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
733-771 |
1.64e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 54.27 E-value: 1.64e-09
10 20 30
....*....|....*....|....*....|....*....
gi 110347471 733 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 771
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-377 |
3.73e-05 |
|
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: 47.99 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 119 VPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhsllegcFSGG---VHWVSigKQDKSG 194
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 195 LLMKLQNLCMRLdqeesfsqRLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 266
Cdd:NF040586 71 VRASLAELARRL--------GLPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 267 KSVTDSVmGPKHVVPVESglgREKGLEILSLFVnmkKEDLPAEAHSIIKECKGS-PLVVSLIGALLRDFPNRWAYYLRQL 345
Cdd:NF040586 143 RAWSEVA-AATLEVDVFS---REESVALLRRRV---PGLTSEEDADRLAEALGDlPLALEQAAAWLAETGMPVDEYLRLL 215
|
250 260 270
....*....|....*....|....*....|....
gi 110347471 346 QNKQFKRI-RKSSSYDYEALDEAM-SISVEMLRE 377
Cdd:NF040586 216 DEQATAALlLELKPPGYPTSVAATwRLSLDRLRE 249
|
|
| eIF2A |
pfam08662 |
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
796-931 |
1.79e-04 |
|
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.
Pssm-ID: 462552 [Multi-domain] Cd Length: 194 Bit Score: 43.80 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 796 DVEVIVKCCSWSADGDKIIVA---AKNKVLLFDiHTSGLLAEIHTGHHSTIQycdFSPYDHLAVIA----LSQYcVELWN 868
Cdd:pfam08662 57 DKEGPIHDVAWSPNGKEFAVIygyMPAKVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347471 869 IDSRLKVADCRGhlSWVHGVMFSPDGSSFLTASD------DQTIRVWETkkvckNSAIVLKQEIDVVFQ 931
Cdd:pfam08662 132 VVNKKKIATAEA--SNATLCEWSPDGRYFLTATTaprlrvDNGFKIWHY-----NGALVYKYDFDELYQ 193
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
150-185 |
2.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|....*.
gi 110347471 150 VTIYGMAGCGKSVLAAEAVRDhslLEGCFSGGVHWV 185
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
623-1207 |
5.04e-78 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 263.31 E-value: 5.04e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 623 FSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQV 702
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 703 NCCHFTnkSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSIn 782
Cdd:COG2319 82 LSVAFS--PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 783 vkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqy 862
Cdd:COG2319 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 863 cvelwnidsrlkvadcRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdN 942
Cdd:COG2319 159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLW--------------------------------D 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 943 IRGLQLIagktgqidylpeaqvsccclsphleyvafgdedgaikiielpnnRVFSsgvGHKKAVRHIQFTADGKTLISSS 1022
Cdd:COG2319 191 LATGKLL--------------------------------------------RTLT---GHTGAVRSVAFSPDGKLLASGS 223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1023 EDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKF 1100
Cdd:COG2319 224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1101 SSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGW 1180
Cdd:COG2319 304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT---------LTGHTGA 374
|
570 580
....*....|....*....|....*....
gi 110347471 1181 VTDVCFSPDSKTLVSAG--GYLKWWNVAT 1207
Cdd:COG2319 375 VTSVAFSPDGRTLASGSadGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
608-912 |
2.84e-76 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 258.30 E-value: 2.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSA 687
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 688 TGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTL 767
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 768 RLWDVRSANERKSInvkrfflssedppEDVEVIVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEiHTGHHSTIQYC 846
Cdd:COG2319 271 RLWDLATGELLRTL-------------TGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGAVRSV 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347471 847 DFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETK 912
Cdd:COG2319 337 AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
608-1034 |
1.90e-74 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 253.29 E-value: 1.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSA 687
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 688 TGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTL 767
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 768 RLWDVRSANERKSInvkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihTGHHSTIQYCD 847
Cdd:COG2319 229 RLWDLATGKLLRTL-------------------------------------------------------TGHSGSVRSVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 848 FSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeid 927
Cdd:COG2319 254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW------------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 928 vvfqenetmvlavdNIRGLQLIAGKTGQIDylpeaQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVR 1007
Cdd:COG2319 316 --------------DLATGKLLRTLTGHTG-----AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVT 376
|
410 420
....*....|....*....|....*..
gi 110347471 1008 HIQFTADGKTLISSSEDSVIQVWNWQT 1034
Cdd:COG2319 377 SVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
453-587 |
4.24e-73 |
|
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: 238.86 E-value: 4.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 453 LQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHI 532
Cdd:pfam17908 1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 110347471 533 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQE 587
Cdd:pfam17908 81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
607-910 |
5.89e-73 |
|
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: 244.94 E-value: 5.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 607 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDS 686
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 687 ATGKLVHTYDEHSEQVNCCHFTNksNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGT 766
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 767 LRLWDVRsanerkSINVKRFFLSSEDPpedveviVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEIhTGHHSTIQY 845
Cdd:cd00200 159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110347471 846 CDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
805-1235 |
4.32e-71 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 243.66 E-value: 4.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 805 SWSADGDKIIVAAKNKVLLFDIHTSGLLAEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSW 884
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 885 VHGVMFSPDGSSFLTASDDQTIRVWETKkvcknsaivlkqeidvvfqenetmvlavdnirglqliAGKTGQIDYLPEAQV 964
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLA-------------------------------------TGLLLRTLTGHTGAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 965 SCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAH 1043
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1044 QETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHE 1122
Cdd:COG2319 204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1123 LKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPisveegtatHGGWVTDVCFSPDSKTLVSAG--GYL 1200
Cdd:COG2319 284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG---------HTGAVRSVAFSPDGKTLASGSddGTV 354
|
410 420 430
....*....|....*....|....*....|....*
gi 110347471 1201 KWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:COG2319 355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
129-374 |
8.06e-67 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 225.72 E-value: 8.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 129 RKKLVHAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCMRL 206
Cdd:pfam00931 1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 207 DQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPkHV 279
Cdd:pfam00931 79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 280 VPVESGLGREKGLEILSLFVNMK----KEDLPAEAHSIIKECKGSPLVVSLIGALL--RDFPNRWAYYLRQLQNKQfkri 353
Cdd:pfam00931 150 PHEVELLEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
|
250 260
....*....|....*....|.
gi 110347471 354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931 226 -KSNSYSLNSVRSILQLSYEN 245
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
961-1235 |
1.14e-61 |
|
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: 212.58 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 961 EAQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF- 1039
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1040 LQAHQETVKDFRLLQDSRLLSWS-FDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLS 1118
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1119 PLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPisveegtatHGGWVTDVCFSPDSKTLVSAG- 1197
Cdd:cd00200 169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG---------HENGVNSVAFSPDGYLLASGSe 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 110347471 1198 -GYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
653-1071 |
3.94e-56 |
|
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: 196.79 E-value: 3.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 653 IKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQ 732
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT--YLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 733 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSInvkrfflssedppedvevivkccswsadgdk 812
Cdd:cd00200 83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 813 iivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqycvelwnidsrlkvadcRGHLSWVHGVMFSP 892
Cdd:cd00200 132 ------------------------------------------------------------------RGHTDWVNSVAFSP 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 893 DGSSFLTASDDQTIRVWEtkkvcknsaivlkqeidvvfqenetmvlaVDNIRGLQLIAGKTGqidylpeaQVSCCCLSPH 972
Cdd:cd00200 146 DGTFVASSSQDGTIKLWD-----------------------------LRTGKCVATLTGHTG--------EVNSVAFSPD 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 973 LEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETVKDFR 1051
Cdd:cd00200 189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQtLSGHTNSVTSLA 268
|
410 420
....*....|....*....|.
gi 110347471 1052 LLQD-SRLLSWSFDGTVKVWN 1071
Cdd:cd00200 269 WSPDgKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
879-1204 |
3.37e-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: 194.09 E-value: 3.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 879 RGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdNIRGLQLIAGKTGQIDy 958
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVW--------------------------------DLETGELLRTLKGHTG- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 959 lpeaQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYV 1038
Cdd:cd00200 53 ----PVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1039 F-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDL 1116
Cdd:cd00200 129 TtLRGHTDWVNSVAFSPDGTFVaSSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1117 LSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCapisveEGtatHGGWVTDVCFSPDSKTLVSA 1196
Cdd:cd00200 209 GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL------SG---HTNSVTSLAWSPDGKRLASG 279
|
330
....*....|
gi 110347471 1197 G--GYLKWWN 1204
Cdd:cd00200 280 SadGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
969-1247 |
8.36e-54 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 193.97 E-value: 8.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 969 LSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETV 1047
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRtLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1048 KDFRLLQD-SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGH 1126
Cdd:COG2319 124 RSVAFSPDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1127 NGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGWVTDVCFSPDSKTLVSAG--GYLKWWN 1204
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT---------LTGHSGSVRSVAFSPDGRLLASGSadGTVRLWD 274
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 110347471 1205 VATGDSSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQV 1247
Cdd:COG2319 275 LATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
3.23e-47 |
|
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: 163.45 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 7 NCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAAL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 110347471 87 LQSGLP 92
Cdd:cd08323 81 LHDGLP 86
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1001-1214 |
4.90e-47 |
|
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: 170.59 E-value: 4.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1001 GHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDS-RLLSWSFDGTVKVWNVITGRIE 1078
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGtYLASGSSDKTIRLWDLETGECV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1079 RDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSD 1158
Cdd:cd00200 87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 110347471 1159 GQLLHSCapisveegtATHGGWVTDVCFSPDSKTLVSAG--GYLKWWNVATGDSSQTF 1214
Cdd:cd00200 167 GKCVATL---------TGHTGEVNSVAFSPDGEKLLSSSsdGTIKLWDLSTGKCLGTL 215
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1079-1244 |
2.51e-21 |
|
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: 95.86 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1079 RDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSD 1158
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1159 GQLLHScapisveegTATHGGWVTDVCFSPDSKTLVSAG--GYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVTV 1236
Cdd:cd00200 83 GECVRT---------LTGHTSYVSSVAFSPDGRILSSSSrdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153
|
....*...
gi 110347471 1237 DNLGILYI 1244
Cdd:cd00200 154 SQDGTIKL 161
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
9.51e-20 |
|
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: 84.92 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 6 RNCLLQHREALEKDIKT-SYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLhEGYKDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79
|
....*.
gi 110347471 85 ALLQSG 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| CARD |
cd01671 |
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-87 |
7.59e-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: 7.59e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347471 9 LLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAALL 87
Cdd:cd01671 1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1119-1214 |
2.33e-12 |
|
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: 69.29 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1119 PLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCapisveegtATHGGWVTDVCFSPDSKTLVSAG- 1197
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL---------KGHTGPVRDVAASADGTYLASGSs 71
|
90
....*....|....*...
gi 110347471 1198 -GYLKWWNVATGDSSQTF 1214
Cdd:cd00200 72 dKTIRLWDLETGECVRTL 89
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
623-772 |
1.94e-11 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 68.57 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 623 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHT 694
Cdd:PLN00181 491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 695 YDEHSEQVNCCHFTNkSNHLLLATGSNDFFLKLWDLNQK-------------------------------------ECRN 737
Cdd:PLN00181 571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 110347471 738 ------TMFGHTNSVNHCRFSpDDELLASCSADGTLRLWDV 772
Cdd:PLN00181 650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
732-771 |
3.96e-10 |
|
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: 56.17 E-value: 3.96e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110347471 732 QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 771
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
646-685 |
1.45e-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: 54.24 E-value: 1.45e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110347471 646 TGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWD 685
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
733-771 |
1.64e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 54.27 E-value: 1.64e-09
10 20 30
....*....|....*....|....*....|....*....
gi 110347471 733 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 771
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
647-685 |
1.50e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 51.58 E-value: 1.50e-08
10 20 30
....*....|....*....|....*....|....*....
gi 110347471 647 GEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWD 685
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
869-1196 |
1.62e-08 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 58.94 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 869 IDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETKKVCKNSAivlkqeiDVVFQENEtmvlavdnirglql 948
Cdd:PLN00181 470 VKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGR-------DIHYPVVE-------------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 949 IAGKTgqidylpeaQVSCCCLSPHLE-YVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQF-TADGKTLISSSEDSV 1026
Cdd:PLN00181 529 LASRS---------KLSGICWNSYIKsQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGS 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1027 IQVWNWQTGDYVFLQAHQETVKDFRLLQDS-RLLSW-SFDGTVKVWNVITGRIER-DFTCHQGTVlSCAISSDATKFSST 1103
Cdd:PLN00181 600 VKLWSINQGVSIGTIKTKANICCVQFPSESgRSLAFgSADHKVYYYDLRNPKLPLcTMIGHSKTV-SYVRFVDSSTLVSS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1104 SADKTAKIWSFDLL------SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVS-----DGQLLHSCAPIS-VE 1171
Cdd:PLN00181 679 STDNTLKLWDLSMSisgineTPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAfpmpvLSYKFKTIDPVSgLE 758
|
330 340
....*....|....*....|....*
gi 110347471 1172 EGTATHggWVTDVCFSPDSKTLVSA 1196
Cdd:PLN00181 759 VDDASQ--FISSVCWRGQSSTLVAA 781
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
875-910 |
8.89e-07 |
|
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: 46.54 E-value: 8.89e-07
10 20 30
....*....|....*....|....*....|....*.
gi 110347471 875 VADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:smart00320 5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1118-1155 |
1.41e-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: 46.15 E-value: 1.41e-06
10 20 30
....*....|....*....|....*....|....*...
gi 110347471 1118 SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| CARD_CASP9 |
cd08326 |
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
6-88 |
1.85e-06 |
|
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: 47.04 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 6 RNCLLQHREALEKDIKTSYIMDHMISNGVLS--VIEEekVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDL 83
Cdd:cd08326 2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTpdMIEE--IQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDL 79
|
....*
gi 110347471 84 AALLQ 88
Cdd:cd08326 80 AELLR 84
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1118-1155 |
3.96e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 44.64 E-value: 3.96e-06
10 20 30
....*....|....*....|....*....|....*...
gi 110347471 1118 SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
1056-1227 |
5.85e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 50.86 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1056 SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISS-DATKFSSTSADKTAKIWSFDLLSPLHELKGH-NGCvrCS 1133
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1134 AFSLD-GILLATGDDNGEIRIWNVSDGQLlhscaPISVEEGtatHGGWVTDVCFSpDSKTLVSAG--GYLKWWNVATGDS 1210
Cdd:PLN00181 624 QFPSEsGRSLAFGSADHKVYYYDLRNPKL-----PLCTMIG---HSKTVSYVRFV-DSSTLVSSStdNTLKLWDLSMSIS 694
|
170 180
....*....|....*....|....*
gi 110347471 1211 --------SQTFYTNGTNLKKIHVS 1227
Cdd:PLN00181 695 ginetplhSFMGHTNVKNFVGLSVS 719
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
624-819 |
7.88e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 50.47 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 624 SQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDeVLCCAFSSDDSY-IATCSADKKVKIWDSATGKL-VHTYDEHSEQ 701
Cdd:PLN00181 585 SADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESGRsLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 702 VNCCHFTNKSNhllLATGSNDFFLKLWDLN------QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWdvrsa 775
Cdd:PLN00181 664 VSYVRFVDSST---LVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY----- 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 110347471 776 NERKSINVKRFFLSSEDPPEDVEV-----IVKCCSWSADGDKIIVAAKN 819
Cdd:PLN00181 736 HKAFPMPVLSYKFKTIDPVSGLEVddasqFISSVCWRGQSSTLVAANST 784
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
875-910 |
1.02e-05 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.49 E-value: 1.02e-05
10 20 30
....*....|....*....|....*....|....*.
gi 110347471 875 VADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
1110-1165 |
1.16e-05 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 44.96 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 110347471 1110 KIWSFDLlsplhelKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSC 1165
Cdd:pfam12894 28 RVWTLSP-------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
688-729 |
1.43e-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: 1.43e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 110347471 688 TGKLVHTYDEHSEQVNCCHFTNKSNHllLATGSNDFFLKLWD 729
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKY--LASGSDDGTIKLWD 40
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
119-377 |
3.73e-05 |
|
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: 47.99 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 119 VPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhsllegcFSGG---VHWVSigKQDKSG 194
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 195 LLMKLQNLCMRLdqeesfsqRLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 266
Cdd:NF040586 71 VRASLAELARRL--------GLPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 267 KSVTDSVmGPKHVVPVESglgREKGLEILSLFVnmkKEDLPAEAHSIIKECKGS-PLVVSLIGALLRDFPNRWAYYLRQL 345
Cdd:NF040586 143 RAWSEVA-AATLEVDVFS---REESVALLRRRV---PGLTSEEDADRLAEALGDlPLALEQAAAWLAETGMPVDEYLRLL 215
|
250 260 270
....*....|....*....|....*....|....
gi 110347471 346 QNKQFKRI-RKSSSYDYEALDEAM-SISVEMLRE 377
Cdd:NF040586 216 DEQATAALlLELKPPGYPTSVAATwRLSLDRLRE 249
|
|
| CARD_BIRC2_BIRC3 |
cd08329 |
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
11-75 |
4.43e-05 |
|
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: 43.59 E-value: 4.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110347471 11 QHREALEKDIKTSY-IMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNAL 75
Cdd:cd08329 13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
689-729 |
1.24e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.41 E-value: 1.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 110347471 689 GKLVHTYDEHSEQVNCCHFTnkSNHLLLATGSNDFFLKLWD 729
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFS--PDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
610-643 |
1.49e-04 |
|
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: 40.37 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....
gi 110347471 610 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVFK 643
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1074-1113 |
1.66e-04 |
|
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: 39.99 E-value: 1.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 110347471 1074 TGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1113
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| eIF2A |
pfam08662 |
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
796-931 |
1.79e-04 |
|
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.
Pssm-ID: 462552 [Multi-domain] Cd Length: 194 Bit Score: 43.80 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 796 DVEVIVKCCSWSADGDKIIVA---AKNKVLLFDiHTSGLLAEIHTGHHSTIQycdFSPYDHLAVIA----LSQYcVELWN 868
Cdd:pfam08662 57 DKEGPIHDVAWSPNGKEFAVIygyMPAKVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110347471 869 IDSRLKVADCRGhlSWVHGVMFSPDGSSFLTASD------DQTIRVWETkkvckNSAIVLKQEIDVVFQ 931
Cdd:pfam08662 132 VVNKKKIATAEA--SNATLCEWSPDGRYFLTATTaprlrvDNGFKIWHY-----NGALVYKYDFDELYQ 193
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1001-1031 |
3.35e-04 |
|
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: 39.22 E-value: 3.35e-04
10 20 30
....*....|....*....|....*....|.
gi 110347471 1001 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1031
Cdd:smart00320 10 GHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1001-1031 |
3.89e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 3.89e-04
10 20 30
....*....|....*....|....*....|.
gi 110347471 1001 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1031
Cdd:pfam00400 9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1075-1113 |
5.60e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.60e-04
10 20 30
....*....|....*....|....*....|....*....
gi 110347471 1075 GRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1113
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| Ge1_WD40 |
pfam16529 |
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
1044-1157 |
1.09e-03 |
|
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of Ge-1 or enhancer of mRNA-decapping proteins. WD40-repeat regions are involved in protein-protein interactions.
Pssm-ID: 465162 [Multi-domain] Cd Length: 328 Bit Score: 42.83 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 1044 QETVKDFRLLQDSRLLSWSFD--------GTVKVWNVITGRIERDftcHQGTVLSCAISSDATKFSSTSADKTAKIWS-- 1113
Cdd:pfam16529 140 DDESKLLVLLRGDKAEIWNVDmivsehgsGPLQPAALESGYIEIE---EHSLLVDAAFSPDGTALATASLDGEVKFFQiy 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 110347471 1114 -FDLLSP--LHELKGHNGCVRCSAFSLDGI-----------LLATGDDNGEIRIWNVS 1157
Cdd:pfam16529 217 lFDNRNPrcLHEWKPHDGKPLSSLFFLDNHkkppevqfwrfAITGADNNSELKLWSCE 274
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
630-734 |
1.09e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 42.96 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 630 IASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEH-SEQVNCCHFT 708
Cdd:PTZ00421 141 LASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHaSAKSQRCLWA 220
|
90 100
....*....|....*....|....*....
gi 110347471 709 NKSNhLLLATGSNDF---FLKLWDLNQKE 734
Cdd:PTZ00421 221 KRKD-LIITLGCSKSqqrQIMLWDTRKMA 248
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1177-1204 |
1.16e-03 |
|
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: 37.68 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|
gi 110347471 1177 HGGWVTDVCFSPDSKTLVSAG--GYLKWWN 1204
Cdd:smart00320 11 HTGPVTSVAFSPDGKYLASGSddGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
610-642 |
1.92e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|...
gi 110347471 610 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVF 642
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
150-185 |
2.93e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 2.93e-03
10 20 30
....*....|....*....|....*....|....*.
gi 110347471 150 VTIYGMAGCGKSVLAAEAVRDhslLEGCFSGGVHWV 185
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
632-690 |
3.18e-03 |
|
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.
Pssm-ID: 466575 [Multi-domain] Cd Length: 350 Bit Score: 41.21 E-value: 3.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110347471 632 SCGA-DKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGK 690
Cdd:pfam20426 98 SCGNwENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEVLRGR 157
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
659-708 |
5.71e-03 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 37.26 E-value: 5.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 110347471 659 EVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFT 708
Cdd:pfam12894 40 EVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| |
