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Conserved domains on  [gi|20137192|sp|Q9EPV5|]
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RecName: Full=Apoptotic protease-activating factor 1; Short=APAF-1

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];
608-912 9.49e-76

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSG 687
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  688 TGKLVHTYEEHSEQVNCCHFTNKSNhlLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTL 767
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  768 KLWDVRSANEKKSInvkrfflssedppEDVEVIVKCCSWSADGDRIIVAAKNK-VLLLDIHTSGLLTEiHTGHHSTIQYC 846
Cdd:COG2319  271 RLWDLATGELLRTL-------------TGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGAVRSV 336

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137192  847 DFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETR 912
Cdd:COG2319  337 AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 453-587 1.44e-73

APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein.


:

Pssm-ID: 465560  Cd Length: 135  Bit Score: 240.40  E-value: 1.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    453 LQDLHRKMVTQFQRYHQPHTLSPGQEDCMYWYNFLAYHMASAGMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20137192    533 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
805-1235 9.94e-69

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 237.12  E-value: 9.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  805 SWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  885 VHGVMFSPDGSSFLTASDDQTIRVWETRkvcknsaivlkqeidvvfqenemmvlavdnirglqliAGKTGQIDYLPEAQV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLA-------------------------------------TGLLLRTLTGHTGAV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  965 SCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF-LQAH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1044 QETVKDFRLLRDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1123 LKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHlcapisieeGTATHGGWVTDVCFSPDRKMLVSAG--GYL 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---------TLTGHTGAVRSVAFSPDGKTLASGSddGTV 354

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 20137192 1201 KWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:COG2319  355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
NB-ARC super family cl26397
NB-ARC domain;
129-374 2.09e-66

NB-ARC domain;


The actual alignment was detected with superfamily member pfam00931:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 224.57  E-value: 2.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    129 RKKLVSAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHALLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    207 GQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPKYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGPSDP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    280 IPVESgLGKEKGLEILSLFVNMK----KEDLPVEAHSIIKECKGSPLVVSLVGALL--RDFPNRWAYYLRQLQNKQfkri 353
Cdd:pfam00931  151 HEVEL-LEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 20137192    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 2.89e-48

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: 166.14  E-value: 2.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    7 NCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 20137192   87 LHSGLP 92
Cdd:cd08323   81 LHDGLP 86
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
608-912 9.49e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSG 687
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  688 TGKLVHTYEEHSEQVNCCHFTNKSNhlLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTL 767
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  768 KLWDVRSANEKKSInvkrfflssedppEDVEVIVKCCSWSADGDRIIVAAKNK-VLLLDIHTSGLLTEiHTGHHSTIQYC 846
Cdd:COG2319  271 RLWDLATGELLRTL-------------TGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGAVRSV 336

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137192  847 DFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETR 912
Cdd:COG2319  337 AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-910 1.62e-74

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: 249.17  E-value: 1.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  607 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDS 686
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  687 GTGKLVHTYEEHSEQVNCCHFTNksNHLLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGT 766
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  767 LKLWDVRsanekkSINVKRFFLSSEDPpedveviVKCCSWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYC 846
Cdd:cd00200  159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSV 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137192  847 DFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:cd00200  226 AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 453-587 1.44e-73

APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein.


Pssm-ID: 465560  Cd Length: 135  Bit Score: 240.40  E-value: 1.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    453 LQDLHRKMVTQFQRYHQPHTLSPGQEDCMYWYNFLAYHMASAGMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20137192    533 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
805-1235 9.94e-69

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 237.12  E-value: 9.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  805 SWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  885 VHGVMFSPDGSSFLTASDDQTIRVWETRkvcknsaivlkqeidvvfqenemmvlavdnirglqliAGKTGQIDYLPEAQV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLA-------------------------------------TGLLLRTLTGHTGAV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  965 SCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF-LQAH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1044 QETVKDFRLLRDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1123 LKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHlcapisieeGTATHGGWVTDVCFSPDRKMLVSAG--GYL 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---------TLTGHTGAVRSVAFSPDGKTLASGSddGTV 354

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 20137192 1201 KWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:COG2319  355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
NB-ARC pfam00931
NB-ARC domain;
129-374 2.09e-66

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 224.57  E-value: 2.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    129 RKKLVSAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHALLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    207 GQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPKYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGPSDP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    280 IPVESgLGKEKGLEILSLFVNMK----KEDLPVEAHSIIKECKGSPLVVSLVGALL--RDFPNRWAYYLRQLQNKQfkri 353
Cdd:pfam00931  151 HEVEL-LEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 20137192    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 961-1235 1.95e-60

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: 209.11  E-value: 1.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  961 EAQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF- 1039
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1040 LQAHQETVKDFRLLRDSRLLSWS-FDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPS 1118
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1119 PLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLCAPisieegtatHGGWVTDVCFSPDRKMLVSAG- 1197
Cdd:cd00200  169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG---------HENGVNSVAFSPDGYLLASGSe 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 20137192 1198 -GYLKWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:cd00200  240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 2.89e-48

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: 166.14  E-value: 2.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    7 NCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 20137192   87 LHSGLP 92
Cdd:cd08323   81 LHDGLP 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-90 1.16e-18

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: 81.84  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192      6 RNCLLQHKEALEKDIKT-SYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79


                   ....*.
gi 20137192     85 GLLHSG 90
Cdd:pfam00619   80 SDLEGL 85
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 623-772 3.94e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 70.89  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   623 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHT 694
Cdd:PLN00181  491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   695 YEEHSEQVNCCHFTNkSNHLLLATGSNDSFLKLWDLNQK-------------------------------------ECRN 737
Cdd:PLN00181  571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 20137192   738 ------TMFGHTNSVTHCRFSpDDELLASCSADGTLKLWDV 772
Cdd:PLN00181  650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 732-771 2.79e-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: 56.55  E-value: 2.79e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 20137192     732 QKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWD 771
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
733-771 1.10e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 1.10e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 20137192    733 KECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWD 771
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1118-1155 1.62e-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: 1.62e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 20137192    1118 SPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1118-1155 3.77e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 3.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 20137192   1118 SPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 1056-1222 1.14e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.70  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  1056 SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISS-DATKFSSTSADKTAKIWSFELPSPLHELKGH-NSCvrCS 1133
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  1134 AFSLD-GILLATGDDNGEIRIWNVSDGQlLHLCAPISieegtatHGGWVTDVCFSpDRKMLVSAG--GYLKWWNV---VT 1207
Cdd:PLN00181  624 QFPSEsGRSLAFGSADHKVYYYDLRNPK-LPLCTMIG-------HSKTVSYVRFV-DSSTLVSSStdNTLKLWDLsmsIS 694

                         170
                  ....*....|....*..
gi 20137192  1208 G--ESSQTFYTNGTNLK 1222
Cdd:PLN00181  695 GinETPLHSFMGHTNVK 711
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 119-266 6.70e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.22  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   119 VPQRPVIFVTRKKLVSAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhallegcFSGG---VHWVSigKQDKSG 194
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   195 LLMKLQNLCTRLGqeesfsqrLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 266
Cdd:NF040586   71 VRASLAELARRLG--------LPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
COG3903 COG3903
Predicted ATPase [General function prediction only];
150-185 1.25e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.08  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20137192  150 VTIYGMAGCGKSVLAAEAVRDHAlleGCFSGGVHWV 185
Cdd:COG3903  179 VTLTGPGGVGKTRLALEVAHRLA---DRFPDGVWFV 211
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
608-912 9.49e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.15  E-value: 9.49e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSG 687
Cdd:COG2319  113 LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  688 TGKLVHTYEEHSEQVNCCHFTNKSNhlLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTL 767
Cdd:COG2319  193 TGKLLRTLTGHTGAVRSVAFSPDGK--LLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTV 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  768 KLWDVRSANEKKSInvkrfflssedppEDVEVIVKCCSWSADGDRIIVAAKNK-VLLLDIHTSGLLTEiHTGHHSTIQYC 846
Cdd:COG2319  271 RLWDLATGELLRTL-------------TGHSGGVNSVAFSPDGKLLASGSDDGtVRLWDLATGKLLRT-LTGHTGAVRSV 336

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137192  847 DFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETR 912
Cdd:COG2319  337 AFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
623-1207 2.53e-75

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 255.61  E-value: 2.53e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  623 FSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHTYEEHSEQV 702
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  703 NCCHFTnkSNHLLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWDVRSANEKKSIn 782
Cdd:COG2319   82 LSVAFS--PDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  783 vkrfflssedppedvevivkccswsadgdriivaaknkvllldihtsgllteihtghhstiqycdfspydhlavialsqy 862
Cdd:COG2319      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  863 cvelwnidsrvkvadcRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWETRkvcknsaivlkqeidvvfqenemmvlavdn 942
Cdd:COG2319  159 ----------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLA------------------------------ 192

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  943 irglqliagkTGQidylpeaqvsccclsphleyvafgdeegaiKIIELPnnrvfssgiGHKKAVRHIQFTADGKTLISSS 1022
Cdd:COG2319  193 ----------TGK------------------------------LLRTLT---------GHTGAVRSVAFSPDGKLLASGS 223

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1023 EDSVIQVWNWQTEEYVF-LQAHQETVKDFRLLRDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKF 1100
Cdd:COG2319  224 ADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLL 303

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1101 SSTSADKTAKIWSFELPSPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLcapisieegTATHGGW 1180
Cdd:COG2319  304 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRT---------LTGHTGA 374

                        570       580
                 ....*....|....*....|....*....
gi 20137192 1181 VTDVCFSPDRKMLVSAG--GYLKWWNVVT 1207
Cdd:COG2319  375 VTSVAFSPDGRTLASGSadGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 607-910 1.62e-74

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: 249.17  E-value: 1.62e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  607 SRLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDS 686
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  687 GTGKLVHTYEEHSEQVNCCHFTNksNHLLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGT 766
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  767 LKLWDVRsanekkSINVKRFFLSSEDPpedveviVKCCSWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYC 846
Cdd:cd00200  159 IKLWDLR------TGKCVATLTGHTGE-------VNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSV 225

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20137192  847 DFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:cd00200  226 AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 453-587 1.44e-73

APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the apoptotic Apaf-1 protein.


Pssm-ID: 465560  Cd Length: 135  Bit Score: 240.40  E-value: 1.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    453 LQDLHRKMVTQFQRYHQPHTLSPGQEDCMYWYNFLAYHMASAGMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 532
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20137192    533 LDEKDCAVCENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 587
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 COG2319
WD40 repeat [General function prediction only];
608-1034 1.91e-72

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 247.52  E-value: 1.91e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  608 RLVVRPHTDAVYHACFSQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSG 687
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  688 TGKLVHTYEEHSEQVNCCHFTNKSNhlLLATGSNDSFLKLWDLNQKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTL 767
Cdd:COG2319  151 TGKLLRTLTGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  768 KLWDVRSANEKKSINVKRFFlssedppedveviVKCCSWSADGDRIIVAAKNKVllldihtsgllteihtghhstiqycd 847
Cdd:COG2319  229 RLWDLATGKLLRTLTGHSGS-------------VRSVAFSPDGRLLASGSADGT-------------------------- 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  848 fspydhlavialsqycVELWNIDSRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetrkvcknsaivlkqeid 927
Cdd:COG2319  270 ----------------VRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW------------------ 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  928 vvfqenemmvlavdNIRGLQLIAGKTGQIDylpeaQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVR 1007
Cdd:COG2319  316 --------------DLATGKLLRTLTGHTG-----AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVT 376

                        410       420
                 ....*....|....*....|....*..
gi 20137192 1008 HIQFTADGKTLISSSEDSVIQVWNWQT 1034
Cdd:COG2319  377 SVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
805-1235 9.94e-69

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 237.12  E-value: 9.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  805 SWSADGDRIIVAAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLAVIALSQYCVELWNIDSRVKVADCRGHLSW 884
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  885 VHGVMFSPDGSSFLTASDDQTIRVWETRkvcknsaivlkqeidvvfqenemmvlavdnirglqliAGKTGQIDYLPEAQV 964
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLA-------------------------------------TGLLLRTLTGHTGAV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  965 SCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF-LQAH 1043
Cdd:COG2319  124 RSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRtLTGH 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1044 QETVKDFRLLRDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHE 1122
Cdd:COG2319  204 TGAVRSVAFSPDGKLLaSGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1123 LKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHlcapisieeGTATHGGWVTDVCFSPDRKMLVSAG--GYL 1200
Cdd:COG2319  284 LTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---------TLTGHTGAVRSVAFSPDGKTLASGSddGTV 354

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 20137192 1201 KWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:COG2319  355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
NB-ARC pfam00931
NB-ARC domain;
129-374 2.09e-66

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 224.57  E-value: 2.09e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    129 RKKLVSAIQQKLWKlNGEPGWVTIYGMAGCGKSVLAAEAVRDHALLEGCFSgGVHWVSIGKQDKSGLLMK--LQNLCTRL 206
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    207 GQEESFSQRlplnieEAKDRLRVLMLRKhpRSLLILDDVWD--PW-----VLKAFDNQCQILLTTRDKSVTDSVMGPKYV 279
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDeeDWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGPSDP 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    280 IPVESgLGKEKGLEILSLFVNMK----KEDLPVEAHSIIKECKGSPLVVSLVGALL--RDFPNRWAYYLRQLQNKQfkri 353
Cdd:pfam00931  151 HEVEL-LEPDEAWELFENKVFPKtlgeCELLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 20137192    354 rKSSSYDYEALDEAMSISVEM 374
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 961-1235 1.95e-60

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: 209.11  E-value: 1.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  961 EAQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF- 1039
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1040 LQAHQETVKDFRLLRDSRLLSWS-FDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPS 1118
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1119 PLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLCAPisieegtatHGGWVTDVCFSPDRKMLVSAG- 1197
Cdd:cd00200  169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG---------HENGVNSVAFSPDGYLLASGSe 239

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 20137192 1198 -GYLKWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:cd00200  240 dGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 653-1071 4.46e-55

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 193.71  E-value: 4.46e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  653 IKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHTYEEHSEQVNCCHFTNKSNhlLLATGSNDSFLKLWDLNQ 732
Cdd:cd00200    5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGT--YLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  733 KECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWDVRSANEKKSInvkrfflssedppedvevivkccswsadgdr 812
Cdd:cd00200   83 GECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTL------------------------------- 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  813 iivaaknkvllldihtsgllteihtghhstiqycdfspydhlavialsqycvelwnidsrvkvadcRGHLSWVHGVMFSP 892
Cdd:cd00200  132 ------------------------------------------------------------------RGHTDWVNSVAFSP 145

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  893 DGSSFLTASDDQTIRVWETRkvcknsaivlkqeidvvfqenemmvlavdNIRGLQLIAGKTGqidylpeaQVSCCCLSPH 972
Cdd:cd00200  146 DGTFVASSSQDGTIKLWDLR-----------------------------TGKCVATLTGHTG--------EVNSVAFSPD 188

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  973 LEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYVF-LQAHQETVKDFR 1051
Cdd:cd00200  189 GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQtLSGHTNSVTSLA 268

                        410       420
                 ....*....|....*....|.
gi 20137192 1052 LLRD-SRLLSWSFDGTVKVWN 1071
Cdd:cd00200  269 WSPDgKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
969-1247 1.42e-52

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 190.51  E-value: 1.42e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  969 LSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQT-EEYVFLQAHQETV 1047
Cdd:COG2319   44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATgLLLRTLTGHTGAV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1048 KDFRLLRD-SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHELKGH 1126
Cdd:COG2319  124 RSVAFSPDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1127 NSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLcapisieegTATHGGWVTDVCFSPDRKMLVSAG--GYLKWWN 1204
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT---------LTGHSGSVRSVAFSPDGRLLASGSadGTVRLWD 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 20137192 1205 VVTGESSQTFYTNGTNLKKIHVSPDFRTYVTVDNLGILYILQV 1247
Cdd:COG2319  275 LATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 879-1204 3.13e-52

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: 185.62  E-value: 3.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  879 RGHLSWVHGVMFSPDGSSFLTASDDQTIRVWetrkvcknsaivlkqeidvvfqenemmvlavdNIRGLQLIAGKTGQIDy 958
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVW--------------------------------DLETGELLRTLKGHTG- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  959 lpeaQVSCCCLSPHLEYVAFGDEEGAIKIIELPNNRVFSSGIGHKKAVRHIQFTADGKTLISSSEDSVIQVWNWQTEEYV 1038
Cdd:cd00200   53 ----PVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1039 F-LQAHQETVKDFRLLRDSRLL-SWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFEL 1116
Cdd:cd00200  129 TtLRGHTDWVNSVAFSPDGTFVaSSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1117 PSPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHlcapiSIEEgtatHGGWVTDVCFSPDRKMLVSA 1196
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQ-----TLSG----HTNSVTSLAWSPDGKRLASG 279

                        330
                 ....*....|
gi 20137192 1197 G--GYLKWWN 1204
Cdd:cd00200  280 SadGTIRIWD 289
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 2.89e-48

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: 166.14  E-value: 2.89e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    7 NCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 20137192   87 LHSGLP 92
Cdd:cd08323   81 LHDGLP 86
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1079-1244 3.04e-22

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: 98.56  E-value: 3.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1079 RDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWSFELPSPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSD 1158
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1159 GQLLHlcapisieegT-ATHGGWVTDVCFSPDRKMLVSAG--GYLKWWNVVTGESSQTFYTNGTNLKKIHVSPDFRTYVT 1235
Cdd:cd00200   83 GECVR----------TlTGHTSYVSSVAFSPDGRILSSSSrdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVAS 152


                 ....*....
gi 20137192 1236 VDNLGILYI 1244
Cdd:cd00200  153 SSQDGTIKL 161
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-90 1.16e-18

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: 81.84  E-value: 1.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192      6 RNCLLQHKEALEKDIKT-SYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79


                   ....*.
gi 20137192     85 GLLHSG 90
Cdd:pfam00619   80 SDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 9-87 6.67e-15

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: 70.62  E-value: 6.67e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20137192    9 LLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAGLL 87
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 623-772 3.94e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 70.89  E-value: 3.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   623 FSQDGQRIASCGADKTLQVFKAETGEK--------LLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHT 694
Cdd:PLN00181  491 FDRDGEFFATAGVNKKIKIFECESIIKdgrdihypVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTE 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   695 YEEHSEQVNCCHFTNkSNHLLLATGSNDSFLKLWDLNQK-------------------------------------ECRN 737
Cdd:PLN00181  571 MKEHEKRVWSIDYSS-ADPTLLASGSDDGSVKLWSINQGvsigtiktkaniccvqfpsesgrslafgsadhkvyyyDLRN 649

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 20137192   738 ------TMFGHTNSVTHCRFSpDDELLASCSADGTLKLWDV 772
Cdd:PLN00181  650 pklplcTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDL 689
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1119-1214 1.04e-11

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: 66.97  E-value: 1.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192 1119 PLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLCapisieegtATHGGWVTDVCFSPDRKMLVSAG- 1197
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL---------KGHTGPVRDVAASADGTYLASGSs 71

                         90
                 ....*....|....*...
gi 20137192 1198 -GYLKWWNVVTGESSQTF 1214
Cdd:cd00200   72 dKTIRLWDLETGECVRTL 89
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 732-771 2.79e-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: 56.55  E-value: 2.79e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 20137192     732 QKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWD 771
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
733-771 1.10e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 54.66  E-value: 1.10e-09
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 20137192    733 KECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWD 771
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 646-685 2.42e-09

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 53.86  E-value: 2.42e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 20137192     646 TGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWD 685
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
647-685 1.75e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.19  E-value: 1.75e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 20137192    647 GEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWD 685
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 661-869 2.02e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 55.48  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   661 LCCA--FSSDDSYIATCSVDKKVKIWDSGT----GKLVH----TYEEHSEQVNCCHftNKSNHLLLATGSNDSFLKLWDL 730
Cdd:PLN00181  485 LVCAigFDRDGEFFATAGVNKKIKIFECESiikdGRDIHypvvELASRSKLSGICW--NSYIKSQVASSNFEGVVQVWDV 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   731 NQKECRNTMFGHTNSVTHCRFSP-DDELLASCSADGTLKLWDVRSANEKKSINVKrfflssedppedveVIVKCCSWSAD 809
Cdd:PLN00181  563 ARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTK--------------ANICCVQFPSE 628

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137192   810 GDRIIV--AAKNKVLLLDIHTSGLLTEIHTGHHSTIQYCDFSPYDHLaVIALSQYCVELWNI 869
Cdd:PLN00181  629 SGRSLAfgSADHKVYYYDLRNPKLPLCTMIGHSKTVSYVRFVDSSTL-VSSSTDNTLKLWDL 689
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 871-910 5.08e-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: 47.31  E-value: 5.08e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 20137192     871 SRVKVADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1118-1155 1.62e-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: 1.62e-06
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 20137192    1118 SPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:smart00320    3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 688-729 3.15e-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: 45.00  E-value: 3.15e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 20137192     688 TGKLVHTYEEHSEQVNCCHFTNKSNHllLATGSNDSFLKLWD 729
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKY--LASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1118-1155 3.77e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 44.64  E-value: 3.77e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 20137192   1118 SPLHELKGHNSCVRCSAFSLDGILLATGDDNGEIRIWN 1155
Cdd:pfam00400    2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
875-910 8.44e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 8.44e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 20137192    875 VADCRGHLSWVHGVMFSPDGSSFLTASDDQTIRVWE 910
Cdd:pfam00400    4 LKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 1056-1222 1.14e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.70  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  1056 SRLLSWSFDGTVKVWNVITGRIERDFTCHQGTVLSCAISS-DATKFSSTSADKTAKIWSFELPSPLHELKGH-NSCvrCS 1133
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  1134 AFSLD-GILLATGDDNGEIRIWNVSDGQlLHLCAPISieegtatHGGWVTDVCFSpDRKMLVSAG--GYLKWWNV---VT 1207
Cdd:PLN00181  624 QFPSEsGRSLAFGSADHKVYYYDLRNPK-LPLCTMIG-------HSKTVSYVRFV-DSSTLVSSStdNTLKLWDLsmsIS 694

                         170
                  ....*....|....*..
gi 20137192  1208 G--ESSQTFYTNGTNLK 1222
Cdd:PLN00181  695 GinETPLHSFMGHTNVK 711
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 6-87 1.56e-05

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: 44.34  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    6 RNCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGYKDLAG 85
Cdd:cd08326    2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAE 81


                 ..
gi 20137192   86 LL 87
Cdd:cd08326   82 LL 83
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 1110-1165 2.50e-05

Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 44.19  E-value: 2.50e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 20137192   1110 KIWSFELPsplhelkGHNSCVRCSAFSLDGILLATGDDNGEIRIWNVSDGQLLHLC 1165
Cdd:pfam12894   28 RVWTLSPD-------KEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76
WD40 pfam00400
WD domain, G-beta repeat;
689-729 3.14e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.33  E-value: 3.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 20137192    689 GKLVHTYEEHSEQVNCCHFTnkSNHLLLATGSNDSFLKLWD 729
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFS--PDGKLLASGSDDGTVKVWD 39
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 119-266 6.70e-05

FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about 850 amino acids long, or 1300 long because of an additional N-terminal domain. Proteins have a P-loop motif, GxGGxGKT, near the N-terminus of the region covered by this HMM, and a region over 400 residues long of tetratricopeptide repeat sequence. The family is found regularly next to other components of FxSxx-COOH systems, which feature an FxsB family radical SAM protein and a protein modified by it, FxsA. Members of this FxsA family typically have an FxSxx motif as the final five amino acids.


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 47.22  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   119 VPQRPVIFVTRKKLVSAIQQKLWKLNGEPGWVTIYGMAGCGKSVLAAE-AVRdhallegcFSGG---VHWVSigKQDKSG 194
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHR--------FRADydlVWWIP--ADQPEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   195 LLMKLQNLCTRLGqeesfsqrLPLNIEEAKDRLR-VL-MLRK---HPRSLLILDDVWDPWVLKAF---DNQCQILLTTRD 266
Cdd:NF040586   71 VRASLAELARRLG--------LPLGPDDVDEAARaVLdALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 624-819 9.26e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 47.00  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   624 SQDGQRIASCGADKTLQVFKAETGEKLLDIKAHEDeVLCCAFSSDDSY-IATCSVDKKVKIWDSGTGKL-VHTYEEHSEQ 701
Cdd:PLN00181  585 SADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESGRsLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   702 VNCCHFTNKSNhllLATGSNDSFLKLWDLN------QKECRNTMFGHTNSVTHCRFSPDDELLASCSADGTLKLWdvrsa 775
Cdd:PLN00181  664 VSYVRFVDSST---LVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY----- 735

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 20137192   776 NEKKSINVKRFFLSSEDPPEDVEV-----IVKCCSWSADGDRIIVAAKN 819
Cdd:PLN00181  736 HKAFPMPVLSYKFKTIDPVSGLEVddasqFISSVCWRGQSSTLVAANST 784
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 11-75 1.14e-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: 42.43  E-value: 1.14e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137192   11 QHKEALEKDIKTSY-IMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNAL 75
Cdd:cd08329   13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 610-643 1.26e-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: 1.26e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 20137192     610 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVFK 643
Cdd:smart00320    7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00421 PTZ00421
coronin; Provisional
 630-734 1.29e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 46.04  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   630 IASCGADKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWDSGTGKLVHTYEEH-SEQVNCCHFT 708
Cdd:PTZ00421  141 LASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRDGTIVSSVEAHaSAKSQRCLWA 220

                          90       100
                  ....*....|....*....|....*....
gi 20137192   709 NKSNhLLLATGSNDS---FLKLWDLNQKE 734
Cdd:PTZ00421  221 KRKD-LIITLGCSKSqqrQIMLWDTRKMA 248
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1074-1113 1.48e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 40.37  E-value: 1.48e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 20137192    1074 TGRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1113
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1001-1031 2.94e-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: 39.60  E-value: 2.94e-04
                            10        20        30
                    ....*....|....*....|....*....|.
gi 20137192    1001 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1031
Cdd:smart00320   10 GHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1001-1031 3.29e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 39.25  E-value: 3.29e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 20137192   1001 GHKKAVRHIQFTADGKTLISSSEDSVIQVWN 1031
Cdd:pfam00400    9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
1075-1113 4.74e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.87  E-value: 4.74e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 20137192   1075 GRIERDFTCHQGTVLSCAISSDATKFSSTSADKTAKIWS 1113
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1177-1204 1.12e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 37.68  E-value: 1.12e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 20137192    1177 HGGWVTDVCFSPDRKMLVSAG--GYLKWWN 1204
Cdd:smart00320   11 HTGPVTSVAFSPDGKYLASGSddGTIKLWD 40
COG3903 COG3903
Predicted ATPase [General function prediction only];
150-185 1.25e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 43.08  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 20137192  150 VTIYGMAGCGKSVLAAEAVRDHAlleGCFSGGVHWV 185
Cdd:COG3903  179 VTLTGPGGVGKTRLALEVAHRLA---DRFPDGVWFV 211
WD40 pfam00400
WD domain, G-beta repeat;
610-642 1.62e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 37.32  E-value: 1.62e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 20137192    610 VVRPHTDAVYHACFSQDGQRIASCGADKTLQVF 642
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
PTZ00421 PTZ00421
coronin; Provisional
 1014-1111 3.06e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.80  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192  1014 DGKTLISSSEDSVIQVWNWQTE--------EYVFLQAHQETVK--DFRLLRDSRLLSWSFDGTVKVWNVITGRIERDFTC 1083
Cdd:PTZ00421   87 DPQKLFTASEDGTIMGWGIPEEgltqnisdPIVHLQGHTKKVGivSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKC 166

                          90       100
                  ....*....|....*....|....*...
gi 20137192  1084 HQGTVLSCAISSDATKFSSTSADKTAKI 1111
Cdd:PTZ00421  167 HSDQITSLEWNLDGSLLCTTSKDKKLNI 194
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 632-685 3.20e-03

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 41.21  E-value: 3.20e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20137192    632 SCGA-DKTLQVFKAETGEKLLDIKAHEDEVLCCAFSSDDSYIATCSVDKKVKIWD 685
Cdd:pfam20426   98 SCGNwENSFQVISLNDGRMVQSIRQHKDVVSCVAVTSDGSILATGSYDTTVMVWE 152
eIF2A pfam08662
Eukaryotic translation initiation factor eIF2A; This is a family of eukaryotic translation ...
 751-931 4.32e-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: 39.95  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    751 FSPDD-ELLASCSADGTLKLWDVRSANEKKSI--NVKRFFLSSEDPPEDV-----EVIVKCCSWSADGDRIIVA---AKN 819
Cdd:pfam08662    4 FKADKvQLKWNKNGTYLLVLTDTDVDKTGKSYygETNLYLIGETGGPDCVveldkEGPIHDVAWSPNGKEFAVIygyMPA 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    820 KVLLLDiHTSGLLTEIHTGHHSTIQycdFSPYDHLAVIA----LSQYcVELWNIDSRVKVADCRGhlSWVHGVMFSPDGS 895
Cdd:pfam08662   84 KVSFFD-LKGNVIHSFGEQPRNTIF---WSPFGRLVLLAgfgnLAGD-IEFWDVVNKKKIATAEA--SNATLCEWSPDGR 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 20137192    896 SFLTASD------DQTIRVWETrkvckNSAIVLKQEIDVVFQ 931
Cdd:pfam08662  157 YFLTATTaprlrvDNGFKIWHY-----NGALVYKYDFDELYQ 193
PTZ00421 PTZ00421
coronin; Provisional
 668-774 5.24e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.03  E-value: 5.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192   668 DDSYIATCSVDKKVKIWD--------SGTGKLVHtYEEHSEQVNCCHFTNKSNHLLLATGSnDSFLKLWDLNQKECRNTM 739
Cdd:PTZ00421   87 DPQKLFTASEDGTIMGWGipeegltqNISDPIVH-LQGHTKKVGIVSFHPSAMNVLASAGA-DMVVNVWDVERGKAVEVI 164

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 20137192   740 FGHTNSVTHCRFSPDDELLASCSADGTLKLWDVRS 774
Cdd:PTZ00421  165 KCHSDQITSLEWNLDGSLLCTTSKDKKLNIIDPRD 199
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 606-796 5.40e-03

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 40.91  E-value: 5.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    606 LSRLVVRPHTDAVYHACFSQDGQRIASCGadktLQVFKAETGEKLLDikAHEDEVL----CCAFSSDDSYIATCSVDKKV 681
Cdd:pfam11715  173 LLKLTRSSDGGAWKESTFEPASWLQSLSG----LLGWLADPTIRYSG--SSVALSLsaapAVTTVGGQNFLFTLSLDHTL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    682 KIWDSGTGKLVHTYEehseqvncchftnksnhLLLATGSNDSFLKLwdlnqkecrnTMfGHTNSVTHCRFSPDDELLA-- 759
Cdd:pfam11715  247 RVWDLLTGKCLATID-----------------LLDLELPQDSSSWL----------TL-DPAPSSLIRVSGSFRAYLVlt 298

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 20137192    760 -SCSADGTLKLWDVRSANEkKSINVKRFFLSSEDPPED 796
Cdd:pfam11715  299 ySPSSNGQFKFWKVKSNDT-SELSLVDLFTDQTIRPAD 335
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 1-87 8.97e-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: 36.63  E-value: 8.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    1 MDAKARNCLLQHKEALEKDIKTSYIMDHMISNGVLTVVEEEKVKSQATQYQRAAALIKMILNKDNYAYISFYNALLHEGY 80
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80


                 ....*..
gi 20137192   81 KDLAGLL 87
Cdd:cd08332   81 EHLADLL 87
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 126-245 9.16e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 38.64  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    126 FVTRKKLVSAIQQKLWKLN-GEPGWVTIYGMAGCGKSVLAAEAVRD------HALLEGCFSGGVHWVSIGKQDKSGLLMK 198
Cdd:pfam13191    2 LVGREEELEQLLDALDRVRsGRPPSVLLTGEAGTGKTTLLRELLRAlerdggYFLRGKCDENLPYSPLLEALTREGLLRQ 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137192    199 L-------------QNLCTRLGQEESFSQRLPLNIEEAKDRLRVLMLRKHPRSLLILDDV 245
Cdd:pfam13191   82 LldelesslleawrAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVLVLDDL 141
 
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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