|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
612-1196 |
4.76e-78 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 263.31 E-value: 4.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 612 FSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQV 691
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 692 NCCHFTnkSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSIn 771
Cdd:COG2319 82 LSVAFS--PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 772 vkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqy 851
Cdd:COG2319 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 852 cvelwnidsrlkvadcRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdN 931
Cdd:COG2319 159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLW--------------------------------D 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 932 IRGLQLIagktgqidylpeaqvsccclsphleyvafgdedgaikiielpnnRVFSsgvGHKKAVRHIQFTADGKTLISSS 1011
Cdd:COG2319 191 LATGKLL--------------------------------------------RTLT---GHTGAVRSVAFSPDGKLLASGS 223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1012 EDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKF 1089
Cdd:COG2319 224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1090 SSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGW 1169
Cdd:COG2319 304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT---------LTGHTGA 374
|
570 580
....*....|....*....|....*....
gi 545479153 1170 VTDVCFSPDSKTLVSAG--GYLKWWNVAT 1196
Cdd:COG2319 375 VTSVAFSPDGRTLASGSadGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
596-899 |
4.89e-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: 4.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 596 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDS 675
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 676 ATGKLVHTYDEHSEQVNCCHFTNksNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGT 755
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 756 LRLWDVRsanerkSINVKRFFLSSEDPpedveviVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEIhTGHHSTIQY 834
Cdd:cd00200 159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545479153 835 CDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 899
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
442-576 |
5.61e-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: 238.48 E-value: 5.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 442 LQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHI 521
Cdd:pfam17908 1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 545479153 522 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQE 576
Cdd:pfam17908 81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
118-363 |
8.26e-67 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 225.72 E-value: 8.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 118 RKKLVHAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCMRL 195
Cdd:pfam00931 1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 196 DQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPkHV 268
Cdd:pfam00931 79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 269 VPVESGLGREKGLEILSLFVNMK----KEDLPAEAHSIIKECKGSPLVVSLIGALL--RDFPNRWAYYLRQLQNKQfkri 342
Cdd:pfam00931 150 PHEVELLEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
|
250 260
....*....|....*....|.
gi 545479153 343 rKSSSYDYEALDEAMSISVEM 363
Cdd:pfam00931 226 -KSNSYSLNSVRSILQLSYEN 245
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
4.21e-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: 163.06 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 7 NCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAAL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 545479153 87 LQSGLP 92
Cdd:cd08323 81 LHDGLP 86
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
1.12e-19 |
|
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: 84.53 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 6 RNCLLQHREALEKDIKT-SYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLhEGYKDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79
|
....*.
gi 545479153 85 ALLQSG 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
612-761 |
1.92e-11 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 68.57 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 612 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHT 683
Cdd:PLN00181 491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 684 YDEHSEQVNCCHFTNkSNHLLLATGSNDFFLKLWDLNQK-------------------------------------ECRN 726
Cdd:PLN00181 571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545479153 727 ------TMFGHTNSVNHCRFSpDDELLASCSADGTLRLWDV 761
Cdd:PLN00181 650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
721-760 |
3.81e-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: 3.81e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 545479153 721 QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 760
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
722-760 |
1.54e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 54.27 E-value: 1.54e-09
10 20 30
....*....|....*....|....*....|....*....
gi 545479153 722 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 760
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
108-366 |
3.69e-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: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 108 VPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhsllegcFSGG---VHWVSigKQDKSG 183
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 184 LLMKLQNLCMRLdqeesfsqRLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 255
Cdd:NF040586 71 VRASLAELARRL--------GLPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 256 KSVTDSVmGPKHVVPVESglgREKGLEILSLFVnmkKEDLPAEAHSIIKECKGS-PLVVSLIGALLRDFPNRWAYYLRQL 334
Cdd:NF040586 143 RAWSEVA-AATLEVDVFS---REESVALLRRRV---PGLTSEEDADRLAEALGDlPLALEQAAAWLAETGMPVDEYLRLL 215
|
250 260 270
....*....|....*....|....*....|....
gi 545479153 335 QNKQFKRI-RKSSSYDYEALDEAM-SISVEMLRE 366
Cdd:NF040586 216 DEQATAALlLELKPPGYPTSVAATwRLSLDRLRE 249
|
|
| eIF2A |
pfam08662 |
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
785-920 |
1.71e-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: 44.19 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 785 DVEVIVKCCSWSADGDKIIVA---AKNKVLLFDiHTSGLLAEIHTGHHSTIQycdFSPYDHLAVIA----LSQYcVELWN 857
Cdd:pfam08662 57 DKEGPIHDVAWSPNGKEFAVIygyMPAKVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545479153 858 IDSRLKVADCRGhlSWVHGVMFSPDGSSFLTASD------DQTIRVWETkkvckNSAIVLKQEIDVVFQ 920
Cdd:pfam08662 132 VVNKKKIATAEA--SNATLCEWSPDGRYFLTATTaprlrvDNGFKIWHY-----NGALVYKYDFDELYQ 193
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
139-174 |
2.90e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....*.
gi 545479153 139 VTIYGMAGCGKSVLAAEAVRDhslLEGCFSGGVHWV 174
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
612-1196 |
4.76e-78 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 263.31 E-value: 4.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 612 FSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQV 691
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 692 NCCHFTnkSNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSIn 771
Cdd:COG2319 82 LSVAFS--PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 772 vkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqy 851
Cdd:COG2319 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 852 cvelwnidsrlkvadcRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdN 931
Cdd:COG2319 159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLW--------------------------------D 190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 932 IRGLQLIagktgqidylpeaqvsccclsphleyvafgdedgaikiielpnnRVFSsgvGHKKAVRHIQFTADGKTLISSS 1011
Cdd:COG2319 191 LATGKLL--------------------------------------------RTLT---GHTGAVRSVAFSPDGKLLASGS 223
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1012 EDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKF 1089
Cdd:COG2319 224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1090 SSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGW 1169
Cdd:COG2319 304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT---------LTGHTGA 374
|
570 580
....*....|....*....|....*....
gi 545479153 1170 VTDVCFSPDSKTLVSAG--GYLKWWNVAT 1196
Cdd:COG2319 375 VTSVAFSPDGRTLASGSadGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
597-901 |
2.69e-76 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 258.30 E-value: 2.69e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 597 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSA 676
Cdd:COG2319 113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 677 TGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTL 756
Cdd:COG2319 193 TGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 757 RLWDVRSANERKSInvkrfflssedppEDVEVIVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEiHTGHHSTIQYC 835
Cdd:COG2319 271 RLWDLATGELLRTL-------------TGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGAVRSV 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545479153 836 DFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETK 901
Cdd:COG2319 337 AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
597-1023 |
1.81e-74 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 253.29 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 597 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSA 676
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 677 TGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTL 756
Cdd:COG2319 151 TGKLLRTLTGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 757 RLWDVRSANERKSInvkrfflssedppedvevivkccswsadgdkiivaaknkvllfdihtsgllaeihTGHHSTIQYCD 836
Cdd:COG2319 229 RLWDLATGKLLRTL-------------------------------------------------------TGHSGSVRSVA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 837 FSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeid 916
Cdd:COG2319 254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW------------------ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 917 vvfqenetmvlavdNIRGLQLIAGKTGQIDylpeaQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVR 996
Cdd:COG2319 316 --------------DLATGKLLRTLTGHTG-----AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVT 376
|
410 420
....*....|....*....|....*..
gi 545479153 997 HIQFTADGKTLISSSEDSVIQVWNWQT 1023
Cdd:COG2319 377 SVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
596-899 |
4.89e-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: 4.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 596 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDS 675
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 676 ATGKLVHTYDEHSEQVNCCHFTNksNHLLLATGSNDFFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDELLASCSADGT 755
Cdd:cd00200 81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 756 LRLWDVRsanerkSINVKRFFLSSEDPpedveviVKCCSWSADGDKIIVAAKNK-VLLFDIHTSGLLAEIhTGHHSTIQY 834
Cdd:cd00200 159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545479153 835 CDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 899
Cdd:cd00200 225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| APAF1_C |
pfam17908 |
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ... |
442-576 |
5.61e-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: 238.48 E-value: 5.61e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 442 LQDLHRKMVTQFQRYYQPHTLSPDQEDCMYWYNFLAYHMASANMHKELCALMFSLDWIKAKTELVGPAHLIHEFVAYRHI 521
Cdd:pfam17908 1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 545479153 522 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYRQAKLQAKQE 576
Cdd:pfam17908 81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
794-1224 |
4.15e-71 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 243.66 E-value: 4.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 794 SWSADGDKIIVAAKNKVLLFDIHTSGLLAEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRLKVADCRGHLSW 873
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 874 VHGVMFSPDGSSFLTASDDQTIRVWETKkvcknsaivlkqeidvvfqenetmvlavdnirglqliAGKTGQIDYLPEAQV 953
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLA-------------------------------------TGLLLRTLTGHTGAV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 954 SCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAH 1032
Cdd:COG2319 124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1033 QETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHE 1111
Cdd:COG2319 204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1112 LKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPisveegtatHGGWVTDVCFSPDSKTLVSAG--GYL 1189
Cdd:COG2319 284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG---------HTGAVRSVAFSPDGKTLASGSddGTV 354
|
410 420 430
....*....|....*....|....*....|....*
gi 545479153 1190 KWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVT 1224
Cdd:COG2319 355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
|
| NB-ARC |
pfam00931 |
NB-ARC domain; |
118-363 |
8.26e-67 |
|
NB-ARC domain;
Pssm-ID: 395745 [Multi-domain] Cd Length: 245 Bit Score: 225.72 E-value: 8.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 118 RKKLVHAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHSLLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCMRL 195
Cdd:pfam00931 1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 196 DQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPkHV 268
Cdd:pfam00931 79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 269 VPVESGLGREKGLEILSLFVNMK----KEDLPAEAHSIIKECKGSPLVVSLIGALL--RDFPNRWAYYLRQLQNKQfkri 342
Cdd:pfam00931 150 PHEVELLEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
|
250 260
....*....|....*....|.
gi 545479153 343 rKSSSYDYEALDEAMSISVEM 363
Cdd:pfam00931 226 -KSNSYSLNSVRSILQLSYEN 245
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
950-1224 |
9.14e-62 |
|
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: 212.97 E-value: 9.14e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 950 EAQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF- 1028
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1029 LQAHQETVKDFRLLQDSRLLSWS-FDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLS 1107
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1108 PLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCAPisveegtatHGGWVTDVCFSPDSKTLVSAG- 1186
Cdd:cd00200 169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG---------HENGVNSVAFSPDGYLLASGSe 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 545479153 1187 -GYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVT 1224
Cdd:cd00200 240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
642-1060 |
3.00e-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: 197.17 E-value: 3.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 642 IKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFTNKSNhlLLATGSNDFFLKLWDLNQ 721
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT--YLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 722 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWDVRSANERKSInvkrfflssedppedvevivkccswsadgdk 801
Cdd:cd00200 83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL------------------------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 802 iivaaknkvllfdihtsgllaeihtghhstiqycdfspydhlavialsqycvelwnidsrlkvadcRGHLSWVHGVMFSP 881
Cdd:cd00200 132 ------------------------------------------------------------------RGHTDWVNSVAFSP 145
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 882 DGSSFLTASDDQTIRVWEtkkvcknsaivlkqeidvvfqenetmvlaVDNIRGLQLIAGKTGqidylpeaQVSCCCLSPH 961
Cdd:cd00200 146 DGTFVASSSQDGTIKLWD-----------------------------LRTGKCVATLTGHTG--------EVNSVAFSPD 188
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 962 LEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETVKDFR 1040
Cdd:cd00200 189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQtLSGHTNSVTSLA 268
|
410 420
....*....|....*....|.
gi 545479153 1041 LLQD-SRLLSWSFDGTVKVWN 1060
Cdd:cd00200 269 WSPDgKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
868-1193 |
2.94e-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: 2.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 868 RGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetkkvcknsaivlkqeidvvfqenetmvlavdNIRGLQLIAGKTGQIDy 947
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVW--------------------------------DLETGELLRTLKGHTG- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 948 lpeaQVSCCCLSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYV 1027
Cdd:cd00200 53 ----PVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1028 F-LQAHQETVKDFRLLQDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDL 1105
Cdd:cd00200 129 TtLRGHTDWVNSVAFSPDGTFVaSSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1106 LSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCapisveEGtatHGGWVTDVCFSPDSKTLVSA 1185
Cdd:cd00200 209 GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL------SG---HTNSVTSLAWSPDGKRLASG 279
|
330
....*....|
gi 545479153 1186 G--GYLKWWN 1193
Cdd:cd00200 280 SadGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
958-1236 |
8.25e-54 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 193.97 E-value: 8.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 958 LSPHLEYVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETV 1036
Cdd:COG2319 44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRtLTGHTGAV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1037 KDFRLLQD-SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGH 1115
Cdd:COG2319 124 RSVAFSPDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1116 NGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHScapisveegTATHGGWVTDVCFSPDSKTLVSAG--GYLKWWN 1193
Cdd:COG2319 204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT---------LTGHSGSVRSVAFSPDGRLLASGSadGTVRLWD 274
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 545479153 1194 VATGDSSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQV 1236
Cdd:COG2319 275 LATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
|
|
| CARD_APAF1 |
cd08323 |
Caspase activation and recruitment domain similar to that found in Apoptotic ... |
7-92 |
4.21e-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: 163.06 E-value: 4.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 7 NCLLQHREALEKDIKTSYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDLAAL 86
Cdd:cd08323 1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80
|
....*.
gi 545479153 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 ... |
990-1203 |
4.24e-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: 4.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 990 GHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTGDYVF-LQAHQETVKDFRLLQDS-RLLSWSFDGTVKVWNVITGRIE 1067
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGtYLASGSSDKTIRLWDLETGECV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1068 RDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSD 1147
Cdd:cd00200 87 RTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 545479153 1148 GQLLHSCapisveegtATHGGWVTDVCFSPDSKTLVSAG--GYLKWWNVATGDSSQTF 1203
Cdd:cd00200 167 GKCVATL---------TGHTGEVNSVAFSPDGEKLLSSSsdGTIKLWDLSTGKCLGTL 215
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1068-1233 |
2.31e-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: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1068 RDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFDLLSPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSD 1147
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1148 GQLLHScapisveegTATHGGWVTDVCFSPDSKTLVSAG--GYLKWWNVATGDSSQTFYTNGTNLKKIHVSPDFRTYVTV 1225
Cdd:cd00200 83 GECVRT---------LTGHTSYVSSVAFSPDGRILSSSSrdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153
|
....*...
gi 545479153 1226 DNLGILYI 1233
Cdd:cd00200 154 SQDGTIKL 161
|
|
| CARD |
pfam00619 |
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
6-90 |
1.12e-19 |
|
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: 84.53 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 6 RNCLLQHREALEKDIKT-SYIMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNALLhEGYKDLA 84
Cdd:pfam00619 1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79
|
....*.
gi 545479153 85 ALLQSG 90
Cdd:pfam00619 80 SDLEGL 85
|
|
| CARD |
cd01671 |
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
9-87 |
8.29e-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: 8.29e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545479153 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 ... |
1108-1203 |
2.22e-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: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1108 PLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSCapisveegtATHGGWVTDVCFSPDSKTLVSAG- 1186
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL---------KGHTGPVRDVAASADGTYLASGSs 71
|
90
....*....|....*...
gi 545479153 1187 -GYLKWWNVATGDSSQTF 1203
Cdd:cd00200 72 dKTIRLWDLETGECVRTL 89
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
612-761 |
1.92e-11 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 68.57 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 612 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHT 683
Cdd:PLN00181 491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 684 YDEHSEQVNCCHFTNkSNHLLLATGSNDFFLKLWDLNQK-------------------------------------ECRN 726
Cdd:PLN00181 571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 545479153 727 ------TMFGHTNSVNHCRFSpDDELLASCSADGTLRLWDV 761
Cdd:PLN00181 650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
721-760 |
3.81e-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: 3.81e-10
10 20 30 40
....*....|....*....|....*....|....*....|
gi 545479153 721 QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 760
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
635-674 |
1.41e-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: 54.63 E-value: 1.41e-09
10 20 30 40
....*....|....*....|....*....|....*....|
gi 545479153 635 TGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWD 674
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
722-760 |
1.54e-09 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 54.27 E-value: 1.54e-09
10 20 30
....*....|....*....|....*....|....*....
gi 545479153 722 KECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWD 760
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
636-674 |
1.40e-08 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 51.58 E-value: 1.40e-08
10 20 30
....*....|....*....|....*....|....*....
gi 545479153 636 GEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWD 674
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
858-1185 |
1.60e-08 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 58.94 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 858 IDSRLKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETKKVCKNSAivlkqeiDVVFQENEtmvlavdnirglql 937
Cdd:PLN00181 470 VKADLKQGDLLNSSNLVCAIGFDRDGEFFATAGVNKKIKIFECESIIKDGR-------DIHYPVVE-------------- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 938 IAGKTgqidylpeaQVSCCCLSPHLE-YVAFGDEDGAIKIIELPNNRVFSSGVGHKKAVRHIQF-TADGKTLISSSEDSV 1015
Cdd:PLN00181 529 LASRS---------KLSGICWNSYIKsQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYsSADPTLLASGSDDGS 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1016 IQVWNWQTGDYVFLQAHQETVKDFRLLQDS-RLLSW-SFDGTVKVWNVITGRIER-DFTCHQGTVlSCAISSDATKFSST 1092
Cdd:PLN00181 600 VKLWSINQGVSIGTIKTKANICCVQFPSESgRSLAFgSADHKVYYYDLRNPKLPLcTMIGHSKTV-SYVRFVDSSTLVSS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1093 SADKTAKIWSFDLL------SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVS-----DGQLLHSCAPIS-VE 1160
Cdd:PLN00181 679 STDNTLKLWDLSMSisgineTPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYHKAfpmpvLSYKFKTIDPVSgLE 758
|
330 340
....*....|....*....|....*
gi 545479153 1161 EGTATHggWVTDVCFSPDSKTLVSA 1185
Cdd:PLN00181 759 VDDASQ--FISSVCWRGQSSTLVAA 781
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
864-899 |
8.72e-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: 8.72e-07
10 20 30
....*....|....*....|....*....|....*.
gi 545479153 864 VADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 899
Cdd:smart00320 5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1107-1144 |
1.37e-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: 1.37e-06
10 20 30
....*....|....*....|....*....|....*...
gi 545479153 1107 SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWN 1144
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| CARD_CASP9 |
cd08326 |
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ... |
6-88 |
1.86e-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: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 6 RNCLLQHREALEKDIKTSYIMDHMISNGVLS--VIEEekVKSQATQYQRAAALIKMILNKDNCAYISFYNALLHEGYKDL 83
Cdd:cd08326 2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTpdMIEE--IQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDL 79
|
....*
gi 545479153 84 AALLQ 88
Cdd:cd08326 80 AELLR 84
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1107-1144 |
3.74e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 44.64 E-value: 3.74e-06
10 20 30
....*....|....*....|....*....|....*...
gi 545479153 1107 SPLHELKGHNGCVRCSAFSLDGILLATGDDNGEIRIWN 1144
Cdd:pfam00400 2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
1045-1216 |
5.79e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 50.86 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1045 SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISS-DATKFSSTSADKTAKIWSFDLLSPLHELKGH-NGCvrCS 1122
Cdd:PLN00181 546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1123 AFSLD-GILLATGDDNGEIRIWNVSDGQLlhscaPISVEEGtatHGGWVTDVCFSpDSKTLVSAG--GYLKWWNVATGDS 1199
Cdd:PLN00181 624 QFPSEsGRSLAFGSADHKVYYYDLRNPKL-----PLCTMIG---HSKTVSYVRFV-DSSTLVSSStdNTLKLWDLSMSIS 694
|
170 180
....*....|....*....|....*
gi 545479153 1200 --------SQTFYTNGTNLKKIHVS 1216
Cdd:PLN00181 695 ginetplhSFMGHTNVKNFVGLSVS 719
|
|
| PLN00181 |
PLN00181 |
protein SPA1-RELATED; Provisional |
613-808 |
7.80e-06 |
|
protein SPA1-RELATED; Provisional
Pssm-ID: 177776 [Multi-domain] Cd Length: 793 Bit Score: 50.47 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 613 SQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDeVLCCAFSSDDSY-IATCSADKKVKIWDSATGKL-VHTYDEHSEQ 690
Cdd:PLN00181 585 SADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESGRsLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 691 VNCCHFTNKSNhllLATGSNDFFLKLWDLN------QKECRNTMFGHTNSVNHCRFSPDDELLASCSADGTLRLWdvrsa 764
Cdd:PLN00181 664 VSYVRFVDSST---LVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY----- 735
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 545479153 765 NERKSINVKRFFLSSEDPPEDVEV-----IVKCCSWSADGDKIIVAAKN 808
Cdd:PLN00181 736 HKAFPMPVLSYKFKTIDPVSGLEVddasqFISSVCWRGQSSTLVAANST 784
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
864-899 |
9.69e-06 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 43.49 E-value: 9.69e-06
10 20 30
....*....|....*....|....*....|....*.
gi 545479153 864 VADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 899
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
1099-1154 |
1.19e-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: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 545479153 1099 KIWSFDLlsplhelKGHNGCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHSC 1154
Cdd:pfam12894 28 RVWTLSP-------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
677-718 |
1.39e-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: 1.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 545479153 677 TGKLVHTYDEHSEQVNCCHFTNKSNHllLATGSNDFFLKLWD 718
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKY--LASGSDDGTIKLWD 40
|
|
| FxSxx_TPR |
NF040586 |
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ... |
108-366 |
3.69e-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: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 108 VPQRPVIFVTRKKLVHAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhsllegcFSGG---VHWVSigKQDKSG 183
Cdd:NF040586 1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 184 LLMKLQNLCMRLdqeesfsqRLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 255
Cdd:NF040586 71 VRASLAELARRL--------GLPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 256 KSVTDSVmGPKHVVPVESglgREKGLEILSLFVnmkKEDLPAEAHSIIKECKGS-PLVVSLIGALLRDFPNRWAYYLRQL 334
Cdd:NF040586 143 RAWSEVA-AATLEVDVFS---REESVALLRRRV---PGLTSEEDADRLAEALGDlPLALEQAAAWLAETGMPVDEYLRLL 215
|
250 260 270
....*....|....*....|....*....|....
gi 545479153 335 QNKQFKRI-RKSSSYDYEALDEAM-SISVEMLRE 366
Cdd:NF040586 216 DEQATAALlLELKPPGYPTSVAATwRLSLDRLRE 249
|
|
| CARD_BIRC2_BIRC3 |
cd08329 |
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
11-75 |
4.66e-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: 43.20 E-value: 4.66e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545479153 11 QHREALEKDIKTSY-IMDHMISNGVLSVIEEEKVKSQATQYQRAAALIKMILNKDNCAYISFYNAL 75
Cdd:cd08329 13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
678-718 |
1.15e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 40.41 E-value: 1.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 545479153 678 GKLVHTYDEHSEQVNCCHFTnkSNHLLLATGSNDFFLKLWD 718
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFS--PDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
599-632 |
1.48e-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: 1.48e-04
10 20 30
....*....|....*....|....*....|....
gi 545479153 599 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVFK 632
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1063-1102 |
1.62e-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: 1.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 545479153 1063 TGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1102
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| eIF2A |
pfam08662 |
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ... |
785-920 |
1.71e-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: 44.19 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 785 DVEVIVKCCSWSADGDKIIVA---AKNKVLLFDiHTSGLLAEIHTGHHSTIQycdFSPYDHLAVIA----LSQYcVELWN 857
Cdd:pfam08662 57 DKEGPIHDVAWSPNGKEFAVIygyMPAKVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWD 131
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545479153 858 IDSRLKVADCRGhlSWVHGVMFSPDGSSFLTASD------DQTIRVWETkkvckNSAIVLKQEIDVVFQ 920
Cdd:pfam08662 132 VVNKKKIATAEA--SNATLCEWSPDGRYFLTATTaprlrvDNGFKIWHY-----NGALVYKYDFDELYQ 193
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
990-1020 |
3.28e-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: 3.28e-04
10 20 30
....*....|....*....|....*....|.
gi 545479153 990 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1020
Cdd:smart00320 10 GHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
990-1020 |
3.71e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 3.71e-04
10 20 30
....*....|....*....|....*....|.
gi 545479153 990 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1020
Cdd:pfam00400 9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1064-1102 |
5.34e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 5.34e-04
10 20 30
....*....|....*....|....*....|....*....
gi 545479153 1064 GRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1102
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
619-723 |
1.07e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 42.96 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 619 IASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEH-SEQVNCCHFT 697
Cdd:PTZ00421 141 LASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHaSAKSQRCLWA 220
|
90 100
....*....|....*....|....*....
gi 545479153 698 NKSNhLLLATGSNDF---FLKLWDLNQKE 723
Cdd:PTZ00421 221 KRKD-LIITLGCSKSqqrQIMLWDTRKMA 248
|
|
| Ge1_WD40 |
pfam16529 |
WD40 region of Ge1, enhancer of mRNA-decapping protein; Ge1_WD40 is the N-terminal region of ... |
1033-1146 |
1.10e-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: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 1033 QETVKDFRLLQDSRLLSWSFD--------GTVKVWNVITGRIERDftcHQGTVLSCAISSDATKFSSTSADKTAKIWS-- 1102
Cdd:pfam16529 140 DDESKLLVLLRGDKAEIWNVDmivsehgsGPLQPAALESGYIEIE---EHSLLVDAAFSPDGTALATASLDGEVKFFQiy 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 545479153 1103 -FDLLSP--LHELKGHNGCVRCSAFSLDGI-----------LLATGDDNGEIRIWNVS 1146
Cdd:pfam16529 217 lFDNRNPrcLHEWKPHDGKPLSSLFFLDNHkkppevqfwrfAITGADNNSELKLWSCE 274
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1166-1193 |
1.13e-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: 1.13e-03
10 20 30
....*....|....*....|....*....|
gi 545479153 1166 HGGWVTDVCFSPDSKTLVSAG--GYLKWWN 1193
Cdd:smart00320 11 HTGPVTSVAFSPDGKYLASGSddGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
599-631 |
1.83e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.32 E-value: 1.83e-03
10 20 30
....*....|....*....|....*....|...
gi 545479153 599 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVF 631
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
139-174 |
2.90e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 2.90e-03
10 20 30
....*....|....*....|....*....|....*.
gi 545479153 139 VTIYGMAGCGKSVLAAEAVRDhslLEGCFSGGVHWV 174
Cdd:COG3903 179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
|
|
| NBCH_WD40 |
pfam20426 |
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ... |
621-679 |
3.14e-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: 3.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 545479153 621 SCGA-DKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSADKKVKIWDSATGK 679
Cdd:pfam20426 98 SCGNwENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWEVLRGR 157
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
648-697 |
5.72e-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: 5.72e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 545479153 648 EVLCCAFSSDDSYIATCSADKKVKIWDSATGKLVHTYDEHSEQVNCCHFT 697
Cdd:pfam12894 40 EVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
|
|
| |
