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Conserved domains on  [gi|32483359|ref|NP_863651|]
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apoptotic protease-activating factor 1 isoform c [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
604-912 9.35e-76

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  604 TNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKI 683
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  684 WNSMTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSA 763
Cdd:COG2319  189 WDLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  764 DGTLKLWDATSANERKSinvkqfflnLEDPQEDmeviVKCCSWSADGARIMVAAKNK-IFLFDIHTSGLLGEiHTGHHST 842
Cdd:COG2319  267 DGTVRLWDLATGELLRT---------LTGHSGG----VNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGA 332
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  843 IQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETK 912
Cdd:COG2319  333 VRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
NB-ARC pfam00931
NB-ARC domain;
129-374 1.38e-73

NB-ARC domain;


:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 244.98  E-value: 1.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    129 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    207 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    280 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 353
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
                          250       260
                   ....*....|....*....|.
gi 32483359    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
453-587 1.21e-69

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: 229.23  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    453 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 32483359    533 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
805-1234 9.82e-65

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 225.56  E-value: 9.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  805 SWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  885 VHGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGRTGQidylteaqV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWD-----------------------------LATGLLLRTLTGHTGA--------V 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  965 SCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1044 QETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1123 LRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaplseeGAATHGGWVTDLCFSPDGKMLISAG--GYIK 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--------TLTGHTGAVRSVAFSPDGKTLASGSddGTVR 355
                        410       420       430
                 ....*....|....*....|....*....|....
gi 32483359 1201 WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1234
Cdd:COG2319  356 LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
7-92 5.34e-52

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: 176.93  E-value: 5.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80

                 ....*.
gi 32483359   87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
604-912 9.35e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  604 TNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKI 683
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  684 WNSMTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSA 763
Cdd:COG2319  189 WDLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  764 DGTLKLWDATSANERKSinvkqfflnLEDPQEDmeviVKCCSWSADGARIMVAAKNK-IFLFDIHTSGLLGEiHTGHHST 842
Cdd:COG2319  267 DGTVRLWDLATGELLRT---------LTGHSGG----VNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGA 332
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  843 IQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETK 912
Cdd:COG2319  333 VRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
607-910 3.93e-75

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: 251.10  E-value: 3.93e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  607 SRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNS 686
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  687 MTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGT 766
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGR--ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  767 LKLWDATSANERKSInvkqfflnledpqEDMEVIVKCCSWSADGARIMVAAKNK-IFLFDIHTSGLLGEIhTGHHSTIQY 845
Cdd:cd00200  159 IKLWDLRTGKCVATL-------------TGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32483359  846 CDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 910
Cdd:cd00200  225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
NB-ARC pfam00931
NB-ARC domain;
129-374 1.38e-73

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 244.98  E-value: 1.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    129 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    207 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    280 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 353
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
                          250       260
                   ....*....|....*....|.
gi 32483359    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
453-587 1.21e-69

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: 229.23  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    453 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 32483359    533 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
805-1234 9.82e-65

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 225.56  E-value: 9.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  805 SWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  885 VHGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGRTGQidylteaqV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWD-----------------------------LATGLLLRTLTGHTGA--------V 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  965 SCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1044 QETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1123 LRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaplseeGAATHGGWVTDLCFSPDGKMLISAG--GYIK 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--------TLTGHTGAVRSVAFSPDGKTLASGSddGTVR 355
                        410       420       430
                 ....*....|....*....|....*....|....
gi 32483359 1201 WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1234
Cdd:COG2319  356 LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
961-1234 1.62e-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: 197.94  E-value: 1.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  961 EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF- 1039
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1040 LRGHQETVKDFRLLKNSRLLSWS-FDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLL 1118
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPlseegaatHGGWVTDLCFSPDGKMLISAG-- 1196
Cdd:cd00200  169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG--------HENGVNSVAFSPDGYLLASGSed 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 32483359 1197 GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1234
Cdd:cd00200  241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
7-92 5.34e-52

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: 176.93  E-value: 5.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80

                 ....*.
gi 32483359   87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
6-90 7.27e-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: 82.22  E-value: 7.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359      6 RNCLLQHREALEKDIKT-SYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79

                   ....*.
gi 32483359     85 ALLHDG 90
Cdd:pfam00619   80 SDLEGL 85
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
629-786 1.06e-11

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   629 RIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFST-DDRFIATCSVDKKVKIWNSMTGELVHTYDEHSeQVNCCHF 707
Cdd:PLN00181  547 QVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQF 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   708 TNSSHHlLLATGSSDCFLKLWDL-NQKECRNTMFGHTNSVNHCRFSpDDKLLASCSADGTLKLWD----ATSANERK--- 779
Cdd:PLN00181  626 PSESGR-SLAFGSADHKVYYYDLrNPKLPLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmsISGINETPlhs 703
                         170
                  ....*....|
gi 32483359   780 ---SINVKQF 786
Cdd:PLN00181  704 fmgHTNVKNF 713
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
732-771 2.20e-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: 56.94  E-value: 2.20e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 32483359     732 QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 771
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
733-771 9.40e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 9.40e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 32483359    733 KECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 771
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1119-1155 1.49e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.77  E-value: 1.49e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 32483359    1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1155
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1119-1155 1.77e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 32483359   1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1155
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
28-437 2.95e-05

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 48.65  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   28 HMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGIT 107
Cdd:COG5635   60 ALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  108 SYVRTVLCEGGVPQRPVVFV-TRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSV----LAAEAVRDHSLLEGCFPggv 182
Cdd:COG5635  140 LLILLLDADGLLVSLDDLYVpLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTllryLALELAERYLDAEDPIP--- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  183 hwvsvgkqdksgLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRilMLRKHPRSLLILDDvWD--------SWVLKAF 254
Cdd:COG5635  217 ------------ILIELRDLAEEASLEDLLAEALEKRGGEPEDALE--RLLRNGRLLLLLDG-LDevpdeadrDEVLNQL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  255 D------SQCQILLTTRdksvtdsvmgpkyvvPVESSLGKEKGLEILSL----------FVNMKKADLPEQAHSIIKECK 318
Cdd:COG5635  282 RrfleryPKARVIITSR---------------PEGYDSSELEGFEVLELaplsdeqieeFLKKWFEATERKAERLLEALE 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  319 ---------GSPLVVSLIGALLRD---FPNR----WEYYLKQL--QNKQFKRIRKSSSYDYEALDEAMS-ISVEMLREDi 379
Cdd:COG5635  347 enpelrelaRNPLLLTLLALLLRErgeLPDTraelYEQFVELLleRWDEQRGLTIYRELSREELRELLSeLALAMQENG- 425
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32483359  380 kdyytDLSILQKDVKvptKVLCILWDMEtEEVEDILQEFVNKSLLFCDRNG-------KSFRYYL 437
Cdd:COG5635  426 -----RTEFAREELE---EILREYLGRR-KDAEALLDELLLRTGLLVERGEgrysfahRSFQEYL 481
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
1056-1221 2.41e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.46  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  1056 SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISH-DATKFSSTSADKTAKIWSFDLLLPLHELRGH-NGCvrCS 1133
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  1134 AFSVDS-TLLATGDDNGEIRIWNVSNGElLHLCAPLSEEGAATHGGWVtdlcfspDGKMLISAG--GYIKWWNV---VTG 1207
Cdd:PLN00181  624 QFPSESgRSLAFGSADHKVYYYDLRNPK-LPLCTMIGHSKTVSYVRFV-------DSSTLVSSStdNTLKLWDLsmsISG 695
                         170
                  ....*....|....*.
gi 32483359  1208 --ESSQTFYTNGTNLK 1221
Cdd:PLN00181  696 inETPLHSFMGHTNVK 711
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
119-266 2.80e-03

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: 41.83  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   119 VPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAE-AVR---DHSLlegcfpggVHWVSVgkQDKSG 194
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHRfraDYDL--------VWWIPA--DQPEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   195 LLMKLQNLCTRLdqdesfsqRLPLNIEEAKDRLRIL--MLRK---HPRSLLILDDVWDSWVLKAF---DSQCQILLTTRD 266
Cdd:NF040586   71 VRASLAELARRL--------GLPLGPDDVDEAARAVldALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
604-912 9.35e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.35e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  604 TNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKI 683
Cdd:COG2319  109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRL 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  684 WNSMTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSA 763
Cdd:COG2319  189 WDLATGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSA 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  764 DGTLKLWDATSANERKSinvkqfflnLEDPQEDmeviVKCCSWSADGARIMVAAKNK-IFLFDIHTSGLLGEiHTGHHST 842
Cdd:COG2319  267 DGTVRLWDLATGELLRT---------LTGHSGG----VNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGA 332
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  843 IQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETK 912
Cdd:COG2319  333 VRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
607-910 3.93e-75

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: 251.10  E-value: 3.93e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  607 SRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNS 686
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  687 MTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGT 766
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGR--ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  767 LKLWDATSANERKSInvkqfflnledpqEDMEVIVKCCSWSADGARIMVAAKNK-IFLFDIHTSGLLGEIhTGHHSTIQY 845
Cdd:cd00200  159 IKLWDLRTGKCVATL-------------TGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTL-RGHENGVNS 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32483359  846 CDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 910
Cdd:cd00200  225 VAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
NB-ARC pfam00931
NB-ARC domain;
129-374 1.38e-73

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 244.98  E-value: 1.38e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    129 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    207 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    280 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 353
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225
                          250       260
                   ....*....|....*....|.
gi 32483359    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
WD40 COG2319
WD40 repeat [General function prediction only];
608-1033 1.17e-70

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 242.51  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  608 RLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSM 687
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  688 TGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTL 767
Cdd:COG2319  151 TGKLLRTLTGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  768 KLWDATSANERKSInvkqfflnledpqedmevivkccswsadgarimvaaknkiflfdihtsgllgeihTGHHSTIQYCD 847
Cdd:COG2319  229 RLWDLATGKLLRTL-------------------------------------------------------TGHSGSVRSVA 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  848 FSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevd 927
Cdd:COG2319  254 FSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWD----------------- 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  928 vvfqenevmvlaVDHIRRLQLINGRTGqidylteaQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVW 1007
Cdd:COG2319  317 ------------LATGKLLRTLTGHTG--------AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVT 376
                        410       420
                 ....*....|....*....|....*.
gi 32483359 1008 HIQFTADEKTLISSSDDAEIQVWNWQ 1033
Cdd:COG2319  377 SVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
623-1206 3.28e-70

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 241.35  E-value: 3.28e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  623 FSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQV 702
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  703 NCCHFtnSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSIn 782
Cdd:COG2319   82 LSVAF--SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  783 vkqfflnledpqedmevivkccswsadgarimvaaknkiflfdihtsgllgeihtghhstiqycdfspqnhlavvalsqy 862
Cdd:COG2319      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  863 cvelwntdsrskvadcRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDH 942
Cdd:COG2319  159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLWD-----------------------------LAT 193
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  943 IRRLQLINGrtgqidylteaqvsccclsphlqyiafgdengaieilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSS 1022
Cdd:COG2319  194 GKLLRTLTG--------------------------------------------------HTGAVRSVAFSPDGKLLASGS 223
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1023 DDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKF 1100
Cdd:COG2319  224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1101 SSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWV 1180
Cdd:COG2319  304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLR---TLTG-----HTGAV 375
                        570       580
                 ....*....|....*....|....*...
gi 32483359 1181 TDLCFSPDGKMLISAG--GYIKWWNVVT 1206
Cdd:COG2319  376 TSVAFSPDGRTLASGSadGTVRLWDLAT 403
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
453-587 1.21e-69

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: 229.23  E-value: 1.21e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    453 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 32483359    533 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
805-1234 9.82e-65

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 225.56  E-value: 9.82e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  805 SWSADGARIMVAAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLAVVALSQYCVELWNTDSRSKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  885 VHGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGRTGQidylteaqV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWD-----------------------------LATGLLLRTLTGHTGA--------V 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  965 SCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1044 QETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1123 LRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaplseeGAATHGGWVTDLCFSPDGKMLISAG--GYIK 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR--------TLTGHTGAVRSVAFSPDGKTLASGSddGTVR 355
                        410       420       430
                 ....*....|....*....|....*....|....
gi 32483359 1201 WWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1234
Cdd:COG2319  356 LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
961-1234 1.62e-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: 197.94  E-value: 1.62e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  961 EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF- 1039
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1040 LRGHQETVKDFRLLKNSRLLSWS-FDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLL 1118
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPlseegaatHGGWVTDLCFSPDGKMLISAG-- 1196
Cdd:cd00200  169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG--------HENGVNSVAFSPDGYLLASGSed 240
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 32483359 1197 GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1234
Cdd:cd00200  241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
7-92 5.34e-52

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: 176.93  E-value: 5.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80

                 ....*.
gi 32483359   87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
879-1203 1.87e-51

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: 183.31  E-value: 1.87e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  879 RGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKkvcknsavmlkqevdvvfqenevmvlavdhirRLQLINGRTGQIDy 958
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE--------------------------------TGELLRTLKGHTG- 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  959 lteaQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCI 1038
Cdd:cd00200   53 ----PVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1039 F-LRGHQETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDL 1116
Cdd:cd00200  129 TtLRGHTDWVNSVAFSPDGTFVaSSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1117 LLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCaplseEGaatHGGWVTDLCFSPDGKMLISAG 1196
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL-----SG---HTNSVTSLAWSPDGKRLASGS 280

                 ....*....
gi 32483359 1197 --GYIKWWN 1203
Cdd:cd00200  281 adGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
969-1237 1.44e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.65  E-value: 1.44e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  969 LSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETV 1047
Cdd:COG2319   44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRtLTGHTGAV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1048 KDFRLLKN-SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGH 1126
Cdd:COG2319  124 RSVAFSPDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1127 NGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLcaplseegAATHGGWVTDLCFSPDGKMLISAG--GYIKWWNV 1204
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT--------LTGHSGSVRSVAFSPDGRLLASGSadGTVRLWDL 275
                        250       260       270
                 ....*....|....*....|....*....|...
gi 32483359 1205 VTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDN 1237
Cdd:COG2319  276 ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
652-1113 8.43e-49

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: 175.60  E-value: 8.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  652 EIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWDLN 731
Cdd:cd00200    4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAA--SADGTYLASGSSDKTIRLWDLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  732 QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSInvkqfflnledpqedmevivkccswsadga 811
Cdd:cd00200   82 TGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL------------------------------ 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  812 rimvaaknkiflfdihtsgllgeihtghhstiqycdfspqnhlavvalsqycvelwntdsrskvadcRGHLSWVHGVMFS 891
Cdd:cd00200  132 -------------------------------------------------------------------RGHTDWVNSVAFS 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  892 PDGSSFLTSSDDQTIRLWETKKvcknsavmlkqevdvvfqenevmvlavdhIRRLQLINGrtgqidylteaqvsccclsp 971
Cdd:cd00200  145 PDGTFVASSSQDGTIKLWDLRT-----------------------------GKCVATLTG-------------------- 175
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  972 hlqyiafgdengaieilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCI-FLRGHQETVKDF 1050
Cdd:cd00200  176 ------------------------------HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLgTLRGHENGVNSV 225
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32483359 1051 RLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWS 1113
Cdd:cd00200  226 AFSPDGYLLaSGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
604-774 1.66e-46

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 172.79  E-value: 1.66e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  604 TNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKI 683
Cdd:COG2319  235 TGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRL 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  684 WNSMTGELVHTYDEHSEQVNCCHFTNSSHHLllATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSA 763
Cdd:COG2319  315 WDLATGKLLRTLTGHTGAVRSVAFSPDGKTL--ASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSA 392
                        170
                 ....*....|.
gi 32483359  764 DGTLKLWDATS 774
Cdd:COG2319  393 DGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1002-1213 1.37e-45

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: 166.36  E-value: 1.37e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1002 HKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNS-RLLSWSFDGTVKVWNIITGNKEK 1079
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGtYLASGSSDKTIRLWDLETGECVR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1080 DFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNG 1159
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 32483359 1160 ELLHLCaplseegaATHGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTF 1213
Cdd:cd00200  168 KCVATL--------TGHTGEVNSVAFSPDGEKLLSSSsdGTIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
969-1243 3.31e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.08  E-value: 3.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  969 LSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETV 1047
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAtLLGHTAAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1048 KDFRLLKN-SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGH 1126
Cdd:COG2319   82 LSVAFSPDgRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1127 NGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWVTDLCFSPDGKMLISAG--GYIKWWNV 1204
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---TLTG-----HTGAVRSVAFSPDGKLLASGSadGTVRLWDL 233
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 32483359 1205 VTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYI 1243
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRL 272
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
6-90 7.27e-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: 82.22  E-value: 7.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359      6 RNCLLQHREALEKDIKT-SYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79

                   ....*.
gi 32483359     85 ALLHDG 90
Cdd:pfam00619   80 SDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
9-87 1.22e-17

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: 78.71  E-value: 1.22e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32483359    9 LLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALL 87
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1119-1213 3.00e-13

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: 71.60  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359 1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaplSEEGaatHGGWVTDLCFSPDGKMLISAG-- 1196
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR-----TLKG---HTGPVRDVAASADGTYLASGSsd 72
                         90
                 ....*....|....*..
gi 32483359 1197 GYIKWWNVVTGESSQTF 1213
Cdd:cd00200   73 KTIRLWDLETGECVRTL 89
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
629-786 1.06e-11

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   629 RIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFST-DDRFIATCSVDKKVKIWNSMTGELVHTYDEHSeQVNCCHF 707
Cdd:PLN00181  547 QVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQF 625
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   708 TNSSHHlLLATGSSDCFLKLWDL-NQKECRNTMFGHTNSVNHCRFSpDDKLLASCSADGTLKLWD----ATSANERK--- 779
Cdd:PLN00181  626 PSESGR-SLAFGSADHKVYYYDLrNPKLPLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmsISGINETPlhs 703
                         170
                  ....*....|
gi 32483359   780 ---SINVKQF 786
Cdd:PLN00181  704 fmgHTNVKNF 713
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
732-771 2.20e-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: 56.94  E-value: 2.20e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 32483359     732 QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 771
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
733-771 9.40e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 9.40e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 32483359    733 KECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 771
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
646-685 9.61e-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: 51.93  E-value: 9.61e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 32483359     646 TGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWN 685
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
661-868 2.67e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.56  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   661 LCCA--FSTDDRFIATCSVDKKVKIW--NSMT--GELVH----TYDEHSEQVNCCHftNSSHHLLLATGSSDCFLKLWDL 730
Cdd:PLN00181  485 LVCAigFDRDGEFFATAGVNKKIKIFecESIIkdGRDIHypvvELASRSKLSGICW--NSYIKSQVASSNFEGVVQVWDV 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   731 NQKECRNTMFGHTNSVNHCRFSP-DDKLLASCSADGTLKLWdatSANERKSINVKQFFLNledpqedmeviVKCCSWSAD 809
Cdd:PLN00181  563 ARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLW---SINQGVSIGTIKTKAN-----------ICCVQFPSE 628
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32483359   810 GARIMV--AAKNKIFLFDIHTSGLLGEIHTGHHSTIQYCDFSPQNHLaVVALSQYCVELWN 868
Cdd:PLN00181  629 SGRSLAfgSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTL-VSSSTDNTLKLWD 688
WD40 pfam00400
WD domain, G-beta repeat;
647-685 4.45e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.04  E-value: 4.45e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 32483359    647 GEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWN 685
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
871-910 9.32e-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: 9.32e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 32483359     871 SRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 910
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
688-729 1.28e-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: 1.28e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 32483359     688 TGELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWD 729
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAF--SPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1119-1155 1.49e-06

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 45.77  E-value: 1.49e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 32483359    1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1155
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1119-1155 1.77e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 32483359   1119 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1155
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
1176-1248 8.49e-06

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 49.26  E-value: 8.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32483359 1176 HGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTV--DNLGILYILQTLE 1248
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGssDKTIRLWDLETGE 84
WD40 pfam00400
WD domain, G-beta repeat;
872-910 8.94e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 8.94e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 32483359    872 RSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 910
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
624-819 1.54e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   624 SEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDeVLCCAFSTDD-RFIATCSVDKKVKIWNSMTGEL-VHTYDEHSEQ 701
Cdd:PLN00181  585 SADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   702 VNCCHFTNSShhlLLATGSSDCFLKLWDLN------QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWdatsa 775
Cdd:PLN00181  664 VSYVRFVDSS---TLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY----- 735
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 32483359   776 NERKSINVKQFFLNLEDPQEDMEV-----IVKCCSWSADGARIMVAAKN 819
Cdd:PLN00181  736 HKAFPMPVLSYKFKTIDPVSGLEVddasqFISSVCWRGQSSTLVAANST 784
WD40 pfam00400
WD domain, G-beta repeat;
689-729 1.66e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 1.66e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 32483359    689 GELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWD 729
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAF--SPDGKLLASGSDDGTVKVWD 39
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
28-437 2.95e-05

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 48.65  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   28 HMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALLHDGIPVVSSSSGKDSVSGIT 107
Cdd:COG5635   60 ALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  108 SYVRTVLCEGGVPQRPVVFV-TRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSV----LAAEAVRDHSLLEGCFPggv 182
Cdd:COG5635  140 LLILLLDADGLLVSLDDLYVpLNLLERIESLKRLELLEAKKKRLLILGEPGSGKTTllryLALELAERYLDAEDPIP--- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  183 hwvsvgkqdksgLLMKLQNLCTRLDQDESFSQRLPLNIEEAKDRLRilMLRKHPRSLLILDDvWD--------SWVLKAF 254
Cdd:COG5635  217 ------------ILIELRDLAEEASLEDLLAEALEKRGGEPEDALE--RLLRNGRLLLLLDG-LDevpdeadrDEVLNQL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  255 D------SQCQILLTTRdksvtdsvmgpkyvvPVESSLGKEKGLEILSL----------FVNMKKADLPEQAHSIIKECK 318
Cdd:COG5635  282 RrfleryPKARVIITSR---------------PEGYDSSELEGFEVLELaplsdeqieeFLKKWFEATERKAERLLEALE 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  319 ---------GSPLVVSLIGALLRD---FPNR----WEYYLKQL--QNKQFKRIRKSSSYDYEALDEAMS-ISVEMLREDi 379
Cdd:COG5635  347 enpelrelaRNPLLLTLLALLLRErgeLPDTraelYEQFVELLleRWDEQRGLTIYRELSREELRELLSeLALAMQENG- 425
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32483359  380 kdyytDLSILQKDVKvptKVLCILWDMEtEEVEDILQEFVNKSLLFCDRNG-------KSFRYYL 437
Cdd:COG5635  426 -----RTEFAREELE---EILREYLGRR-KDAEALLDELLLRTGLLVERGEgrysfahRSFQEYL 481
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
1110-1165 4.15e-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: 43.42  E-value: 4.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 32483359   1110 KIWSFDLllplhelRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLC 1165
Cdd:pfam12894   28 RVWTLSP-------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1176-1203 1.51e-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: 1.51e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 32483359    1176 HGGWVTDLCFSPDGKMLISAG--GYIKWWN 1203
Cdd:smart00320   11 HTGPVTSVAFSPDGKYLASGSddGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
610-643 2.06e-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: 2.06e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 32483359     610 VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFK 643
Cdd:smart00320    7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG3903 COG3903
Predicted ATPase [General function prediction only];
150-185 2.19e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.78  E-value: 2.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 32483359  150 VTIHGMAGCGKSVLAAEAVRDhslLEGCFPGGVHWV 185
Cdd:COG3903  179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
1056-1221 2.41e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.46  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  1056 SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISH-DATKFSSTSADKTAKIWSFDLLLPLHELRGH-NGCvrCS 1133
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  1134 AFSVDS-TLLATGDDNGEIRIWNVSNGElLHLCAPLSEEGAATHGGWVtdlcfspDGKMLISAG--GYIKWWNV---VTG 1207
Cdd:PLN00181  624 QFPSESgRSLAFGSADHKVYYYDLRNPK-LPLCTMIGHSKTVSYVRFV-------DSSTLVSSStdNTLKLWDLsmsISG 695
                         170
                  ....*....|....*.
gi 32483359  1208 --ESSQTFYTNGTNLK 1221
Cdd:PLN00181  696 inETPLHSFMGHTNVK 711
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
11-75 3.90e-04

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 40.89  E-value: 3.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32483359   11 QHREALEKDIKTSY-IMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNAL 75
Cdd:cd08329   13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
1074-1113 6.09e-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: 38.45  E-value: 6.09e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 32483359    1074 TGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWS 1113
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
1-87 1.80e-03

Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment domain (CARD) similar to that found in caspase-2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Caspase-2 (also known as ICH1, NEDD2, or CASP2) is one of the most evolutionarily conserved caspases, and plays a role in apoptosis, DNA damage response, cell cycle regulation, and tumor suppression. It is localized in the nucleus and exhibits properties of both an initiator and an effector caspase. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260040  Cd Length: 87  Bit Score: 38.56  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    1 MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY 80
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80

                 ....*..
gi 32483359   81 KDLAALL 87
Cdd:cd08332   81 EHLADLL 87
WD40 pfam00400
WD domain, G-beta repeat;
1075-1113 2.29e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 2.29e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 32483359   1075 GNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWS 1113
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
610-642 2.65e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.65e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 32483359    610 VVRPHTDAVYHACFSEDGQRIASCGADKTLQVF 642
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
119-266 2.80e-03

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: 41.83  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   119 VPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAE-AVR---DHSLlegcfpggVHWVSVgkQDKSG 194
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHRfraDYDL--------VWWIPA--DQPEL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359   195 LLMKLQNLCTRLdqdesfsqRLPLNIEEAKDRLRIL--MLRK---HPRSLLILDDVWDSWVLKAF---DSQCQILLTTRD 266
Cdd:NF040586   71 VRASLAELARRL--------GLPLGPDDVDEAARAVldALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
WD40 pfam00400
WD domain, G-beta repeat;
1176-1203 3.17e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 3.17e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 32483359   1176 HGGWVTDLCFSPDGKMLISAG--GYIKWWN 1203
Cdd:pfam00400   10 HTGSVTSLAFSPDGKLLASGSddGTVKVWD 39
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
796-901 3.24e-03

Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation initiation factors.


Pssm-ID: 462552 [Multi-domain]  Cd Length: 194  Bit Score: 40.33  E-value: 3.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    796 DMEVIVKCCSWSADGARIMVA---AKNKIFLFDiHTSGLLGEIHTGHHSTIQycdFSPQNHLAVVA----LSQYcVELWN 868
Cdd:pfam08662   57 DKEGPIHDVAWSPNGKEFAVIygyMPAKVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWD 131
                           90       100       110
                   ....*....|....*....|....*....|...
gi 32483359    869 TDSRSKVADCRGhlSWVHGVMFSPDGSSFLTSS 901
Cdd:pfam08662  132 VVNKKKIATAEA--SNATLCEWSPDGRYFLTAT 162
PTZ00421 PTZ00421
coronin; Provisional
1014-1111 3.95e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.42  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359  1014 DEKTLISSSDDAEIQVWNWQ--------LDKCIFLRGHQETVK--DFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVC 1083
Cdd:PTZ00421   87 DPQKLFTASEDGTIMGWGIPeegltqniSDPIVHLQGHTKKVGivSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKC 166
                          90       100
                  ....*....|....*....|....*...
gi 32483359  1084 HQGTVLSCDISHDATKFSSTSADKTAKI 1111
Cdd:PTZ00421  167 HSDQITSLEWNLDGSLLCTTSKDKKLNI 194
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
659-708 5.76e-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: 5.76e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 32483359    659 EVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFT 708
Cdd:pfam12894   40 EVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
6-87 7.13e-03

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: 37.02  E-value: 7.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32483359    6 RNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAA 85
Cdd:cd08326    2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAE 81

                 ..
gi 32483359   86 LL 87
Cdd:cd08326   82 LL 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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