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Conserved domains on  [gi|4502123|ref|NP_001151|]
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apoptotic protease-activating factor 1 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
612-1152 3.61e-76

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.92  E-value: 3.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   612 FSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQV 691
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   692 NCCHFtnSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSIn 771
Cdd:COG2319   82 LSVAF--SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   772 vkqfflnledpqedmevivkccswsadgarimvaaknkiflwntdsrskvadcRGHLSWVHGVMFSPDGSSFLTSSDDQT 851
Cdd:COG2319  159 -----------------------------------------------------TGHSGAVTSVAFSPDGKLLASGSDDGT 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   852 IRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGrtgqidylteaqvsccclsphlqyiafgdengai 931
Cdd:COG2319  186 VRLWD-----------------------------LATGKLLRTLTG---------------------------------- 202

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   932 eilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNSRLL-SWSF 1009
Cdd:COG2319  203 ----------------HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSA 266

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1010 DGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLA 1089
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4502123  1090 TGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWVTDLCFSPDGKMLISAG--GYIKWWNVVT 1152
Cdd:COG2319  347 SGSDDGTVRLWDLATGELLR---TLTG-----HTGAVTSVAFSPDGRTLASGSadGTVRLWDLAT 403
NB-ARC pfam00931
NB-ARC domain;
118-363 2.31e-73

NB-ARC domain;


:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 243.83  E-value: 2.31e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     118 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 195
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     196 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 268
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     269 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 342
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 4502123     343 rKSSSYDYEALDEAMSISVEM 363
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 442-576 6.52e-70

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


:

Pssm-ID: 465560  Cd Length: 135  Bit Score: 229.62  E-value: 6.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     442 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 521
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4502123     522 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 576
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 5.09e-52

Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260034  Cd Length: 86  Bit Score: 176.93  E-value: 5.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 4502123    87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1122-1194 7.38e-06

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 49.26  E-value: 7.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502123  1122 HGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTV--DNLGILYILQTLE 1194
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGssDKTIRLWDLETGE 84
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
612-1152 3.61e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.92  E-value: 3.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   612 FSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQV 691
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   692 NCCHFtnSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSIn 771
Cdd:COG2319   82 LSVAF--SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   772 vkqfflnledpqedmevivkccswsadgarimvaaknkiflwntdsrskvadcRGHLSWVHGVMFSPDGSSFLTSSDDQT 851
Cdd:COG2319  159 -----------------------------------------------------TGHSGAVTSVAFSPDGKLLASGSDDGT 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   852 IRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGrtgqidylteaqvsccclsphlqyiafgdengai 931
Cdd:COG2319  186 VRLWD-----------------------------LATGKLLRTLTG---------------------------------- 202

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   932 eilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNSRLL-SWSF 1009
Cdd:COG2319  203 ----------------HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSA 266

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1010 DGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLA 1089
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4502123  1090 TGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWVTDLCFSPDGKMLISAG--GYIKWWNVVT 1152
Cdd:COG2319  347 SGSDDGTVRLWDLATGELLR---TLTG-----HTGAVTSVAFSPDGRTLASGSadGTVRLWDLAT 403
NB-ARC pfam00931
NB-ARC domain;
118-363 2.31e-73

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 243.83  E-value: 2.31e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     118 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 195
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     196 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 268
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     269 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 342
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 4502123     343 rKSSSYDYEALDEAMSISVEM 363
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 596-859 2.77e-70

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: 236.85  E-value: 2.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   596 SRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNS 675
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   676 MTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGT 755
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGR--ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   756 LKLWDATSANERKSInvkqfflnledpqEDMEVIVKCCSWSADGARIMVAAKNK-IFLWNTDSRSKVADCRGHLSWVHGV 834
Cdd:cd00200  159 IKLWDLRTGKCVATL-------------TGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTLRGHENGVNSV 225

                        250       260
                 ....*....|....*....|....*
gi 4502123   835 MFSPDGSSFLTSSDDQTIRLWETKK 859
Cdd:cd00200  226 AFSPDGYLLASGSEDGTIRVWDLRT 250
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 442-576 6.52e-70

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


Pssm-ID: 465560  Cd Length: 135  Bit Score: 229.62  E-value: 6.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     442 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 521
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4502123     522 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 576
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 5.09e-52

Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260034  Cd Length: 86  Bit Score: 176.93  E-value: 5.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 4502123    87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-90 8.78e-19

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 81.84  E-value: 8.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123       6 RNCLLQHREALEKDIKT-SYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79


                   ....*.
gi 4502123      85 ALLHDG 90
Cdd:pfam00619   80 SDLEGL 85
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 618-775 9.99e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 9.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    618 RIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFST-DDRFIATCSVDKKVKIWNSMTGELVHTYDEHSeQVNCCHF 696
Cdd:PLN00181  547 QVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQF 625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    697 TNSSHHlLLATGSSDCFLKLWDL-NQKECRNTMFGHTNSVNHCRFSpDDKLLASCSADGTLKLWD----ATSANERK--- 768
Cdd:PLN00181  626 PSESGR-SLAFGSADHKVYYYDLrNPKLPLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmsISGINETPlhs 703

                         170
                  ....*....|
gi 4502123    769 ---SINVKQF 775
Cdd:PLN00181  704 fmgHTNVKNF 713
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 721-760 1.73e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.94  E-value: 1.73e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 4502123      721 QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 760
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
722-760 7.69e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 7.69e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4502123     722 KECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 760
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1122-1194 7.38e-06

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 49.26  E-value: 7.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502123  1122 HGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTV--DNLGILYILQTLE 1194
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGssDKTIRLWDLETGE 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
126-426 5.42e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 47.49  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   126 QQKLSKLKGEPGWVTIHGMAGCGKSV----LAAEAVRDHSLLEGCFPggvhwvsvgkqdksgLLMKLQNLCTRLDQDESF 201
Cdd:COG5635  170 LKRLELLEAKKKRLLILGEPGSGKTTllryLALELAERYLDAEDPIP---------------ILIELRDLAEEASLEDLL 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   202 SQRLPLNIEEAKDRLRilMLRKHPRSLLILDDvWD--------SWVLKAFD------SQCQILLTTRdksvtdsvmgpky 267
Cdd:COG5635  235 AEALEKRGGEPEDALE--RLLRNGRLLLLLDG-LDevpdeadrDEVLNQLRrfleryPKARVIITSR------------- 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   268 vvPVESSLGKEKGLEILSL----------FVNMKKADLPEQAHSIIKECK---------GSPLVVSLIGALLRD---FPN 325
Cdd:COG5635  299 --PEGYDSSELEGFEVLELaplsdeqieeFLKKWFEATERKAERLLEALEenpelrelaRNPLLLTLLALLLRErgeLPD 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   326 R----WEYYLKQL--QNKQFKRIRKSSSYDYEALDEAMS-ISVEMLREDikdyytDLSILQKDVKvptKVLCILWDMEtE 398
Cdd:COG5635  377 TraelYEQFVELLleRWDEQRGLTIYRELSREELRELLSeLALAMQENG------RTEFAREELE---EILREYLGRR-K 446

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 4502123   399 EVEDILQEFVNKSLLFCDRNG-------KSFRYYL 426
Cdd:COG5635  447 DAEALLDELLLRTGLLVERGEgrysfahRSFQEYL 481
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 108-255 2.66e-03

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


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 41.83  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    108 VPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAE-AVR---DHSLlegcfpggVHWVSVgkQDKSG 183
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHRfraDYDL--------VWWIPA--DQPEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    184 LLMKLQNLCTRLdqdesfsqRLPLNIEEAKDRLRIL--MLRK---HPRSLLILDDVWDSWVLKAF---DSQCQILLTTRD 255
Cdd:NF040586   71 VRASLAELARRL--------GLPLGPDDVDEAARAVldALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
612-1152 3.61e-76

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 257.92  E-value: 3.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   612 FSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQV 691
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   692 NCCHFtnSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDATSANERKSIn 771
Cdd:COG2319   82 LSVAF--SPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   772 vkqfflnledpqedmevivkccswsadgarimvaaknkiflwntdsrskvadcRGHLSWVHGVMFSPDGSSFLTSSDDQT 851
Cdd:COG2319  159 -----------------------------------------------------TGHSGAVTSVAFSPDGKLLASGSDDGT 185

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   852 IRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGrtgqidylteaqvsccclsphlqyiafgdengai 931
Cdd:COG2319  186 VRLWD-----------------------------LATGKLLRTLTG---------------------------------- 202

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   932 eilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNSRLL-SWSF 1009
Cdd:COG2319  203 ----------------HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRtLTGHSGSVRSVAFSPDGRLLaSGSA 266

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1010 DGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLA 1089
Cdd:COG2319  267 DGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLA 346

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4502123  1090 TGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWVTDLCFSPDGKMLISAG--GYIKWWNVVT 1152
Cdd:COG2319  347 SGSDDGTVRLWDLATGELLR---TLTG-----HTGAVTSVAFSPDGRTLASGSadGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
597-979 3.26e-75

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 255.22  E-value: 3.26e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   597 RLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSM 676
Cdd:COG2319   71 LATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   677 TGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTL 756
Cdd:COG2319  151 TGKLLRTLTGHSGAVTSVAFSPDGK--LLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTV 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   757 KLWDATSANERKSINVKQFFlnledpqedmeviVKCCSWSADGARIMVA-AKNKIFLWNTDSRSKVADCRGHLSWVHGVM 835
Cdd:COG2319  229 RLWDLATGKLLRTLTGHSGS-------------VRSVAFSPDGRLLASGsADGTVRLWDLATGELLRTLTGHSGGVNSVA 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   836 FSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGRTGqidylteaQVSCCCL 915
Cdd:COG2319  296 FSPDGKLLASGSDDGTVRLWD-----------------------------LATGKLLRTLTGHTG--------AVRSVAF 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4502123   916 SPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQ 979
Cdd:COG2319  339 SPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
NB-ARC pfam00931
NB-ARC domain;
118-363 2.31e-73

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 243.83  E-value: 2.31e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     118 RKKLVNAIQQKLSKlKGEPGWVTIHGMAGCGKSVLAAEAVRDHSLLEGCFPgGVHWVSVGKQDKSGLLMK--LQNLCTRL 195
Cdd:pfam00931    1 REDMVEKVIGKLSE-KDEPGIVGIHGMGGVGKTTLAAQIFNDFDEVEGHFD-SVAWVVVSKTFTISTLQQtiLQNLGLSE 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     196 DQDESFSQRlplnieEAKDRLRILMLRKhpRSLLILDDVWDS--W-----VLKAFDSQCQILLTTRDKSVTDSVMGPkYV 268
Cdd:pfam00931   79 DDWDNKEEG------ELARKIRRALLTK--RFLLVLDDVWDEedWdkigiPLPDRENGCRVLLTTRSEEVAGRVGGP-SD 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     269 VPVESSLGKEKGLEILSLFVNMKKAD----LPEQAHSIIKECKGSPLVVSLIGALL--RDFPNRWEYYLKQLQNKQfkri 342
Cdd:pfam00931  150 PHEVELLEPDEAWELFENKVFPKTLGecelLEDVAKEIVEKCRGLPLALKVLGGLLscKKTVEEWKHVYDVLQSEL---- 225

                          250       260
                   ....*....|....*....|.
gi 4502123     343 rKSSSYDYEALDEAMSISVEM 363
Cdd:pfam00931  226 -KSNSYSLNSVRSILQLSYEN 245
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 596-859 2.77e-70

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: 236.85  E-value: 2.77e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   596 SRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNS 675
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   676 MTGELVHTYDEHSEQVNCCHFTNSSHhlLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGT 755
Cdd:cd00200   81 ETGECVRTLTGHTSYVSSVAFSPDGR--ILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   756 LKLWDATSANERKSInvkqfflnledpqEDMEVIVKCCSWSADGARIMVAAKNK-IFLWNTDSRSKVADCRGHLSWVHGV 834
Cdd:cd00200  159 IKLWDLRTGKCVATL-------------TGHTGEVNSVAFSPDGEKLLSSSSDGtIKLWDLSTGKCLGTLRGHENGVNSV 225

                        250       260
                 ....*....|....*....|....*
gi 4502123   835 MFSPDGSSFLTSSDDQTIRLWETKK 859
Cdd:cd00200  226 AFSPDGYLLASGSEDGTIRVWDLRT 250
WD40 COG2319
WD40 repeat [General function prediction only];
592-1104 3.26e-70

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 240.97  E-value: 3.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   592 ITNLSRLVVRPHTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVK 671
Cdd:COG2319   24 ALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   672 IWNSMTGELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCS 751
Cdd:COG2319  104 LWDLATGLLLRTLTGHTGAVRSVAF--SPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGS 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   752 ADGTLKLWDATSANERKSInvkqfflnledpqedmevivkccswsadgarimvaaknkiflwntdsrskvadcRGHLSWV 831
Cdd:COG2319  182 DDGTVRLWDLATGKLLRTL------------------------------------------------------TGHTGAV 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   832 HGVMFSPDGSSFLTSSDDQTIRLWEtkkvcknsavmlkqevdvvfqenevmvlaVDHIRRLQLINGrtgqidylteaqvs 911
Cdd:COG2319  208 RSVAFSPDGKLLASGSADGTVRLWD-----------------------------LATGKLLRTLTG-------------- 244

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   912 ccclsphlqyiafgdengaieilelvnnrifqsrfqHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCI-FLRGHQ 990
Cdd:COG2319  245 ------------------------------------HSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLrTLTGHS 288

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   991 ETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHEL 1069
Cdd:COG2319  289 GGVNSVAFSPDGKLLaSGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 4502123  1070 RGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSN 1104
Cdd:COG2319  369 TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
APAF1_C pfam17908
APAF-1 helical domain; This domain represents the C-terminal alpha helical domain of the ...
 442-576 6.52e-70

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


Pssm-ID: 465560  Cd Length: 135  Bit Score: 229.62  E-value: 6.52e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     442 LQDLHKKIITQFQRYHQPHTLSPDQEDCMYWYNFLAYHMASAKMHKELCALMFSLDWIKAKTELVGPAHLIHEFVEYRHI 521
Cdd:pfam17908    1 LQDLHRKLVERYQRHCQPHTLSPDDEDDLYWYNYLGYHLASANMHEELCALLLDLDWIEAKVKLTGPSDLLHDYVKYRHI 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 4502123     522 LDEKDCAVSENFQEFLSLNGHLLGRQPFPNIVQLGLCEPETSEVYQQAKLQAKQE 576
Cdd:pfam17908   81 LDENDCAVLEDFEEFLSVNGHLLERDPFPDIIQLALCQPETSEVYQQAKLLARQR 135
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 907-1180 9.54e-57

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: 198.33  E-value: 9.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   907 EAQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF- 985
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRt 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   986 LRGHQETVKDFRLLKNSRLLSWS-FDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLL 1064
Cdd:cd00200   89 LTGHTSYVSSVAFSPDGRILSSSsRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1065 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCAPlseegaatHGGWVTDLCFSPDGKMLISAG-- 1142
Cdd:cd00200  169 CVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRG--------HENGVNSVAFSPDGYLLASGSed 240

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 4502123  1143 GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVT 1180
Cdd:cd00200  241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLAS 278
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 603-856 6.70e-54

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: 190.24  E-value: 6.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   603 HTDAVYHACFSEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVH 682
Cdd:cd00200   92 HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   683 TYDEHSEQVNCCHFTNSSHHLLlaTGSSDCFLKLWDLNQKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWDat 762
Cdd:cd00200  172 TLTGHTGEVNSVAFSPDGEKLL--SSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWD-- 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   763 sanerksinvkqfflnledpqedmevivkccswsadgarimvaaknkiflwnTDSRSKVADCRGHLSWVHGVMFSPDGSS 842
Cdd:cd00200  248 ----------------------------------------------------LRTGECVQTLSGHTNSVTSLAWSPDGKR 275

                        250
                 ....*....|....
gi 4502123   843 FLTSSDDQTIRLWE 856
Cdd:cd00200  276 LASGSADGTIRIWD 289
CARD_APAF1 cd08323
Caspase activation and recruitment domain similar to that found in Apoptotic ...
 7-92 5.09e-52

Caspase activation and recruitment domain similar to that found in Apoptotic Protease-Activating Factor 1; Caspase activation and recruitment domain (CARD) similar to that found in apoptotic protease-activating factor 1 (APAF-1), which is an activator of caspase-9. APAF-1 contains WD-40 repeats, a CARD, and an ATPase domain. Upon stimulation, APAF-1, together with caspase-9, forms the heptameric 'apoptosome', which leads to the processing and activation of caspase-9, starting a caspase cascade which leads to apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260034  Cd Length: 86  Bit Score: 176.93  E-value: 5.09e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     7 NCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAAL 86
Cdd:cd08323    1 SCLLQHRAALERDIKTSYIMDHMISDGVLTLSEEEKVRAQPTQQERAAALIKIILRKDNDAYISFYNALLHEGYKDLAAL 80


                 ....*.
gi 4502123    87 LHDGIP 92
Cdd:cd08323   81 LHDGLP 86
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 825-1149 1.00e-51

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 184.08  E-value: 1.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   825 RGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWETKkvcknsavmlkqevdvvfqenevmvlavdhirRLQLINGRTGQIDy 904
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLE--------------------------------TGELLRTLKGHTG- 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   905 lteaQVSCCCLSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCI 984
Cdd:cd00200   53 ----PVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   985 F-LRGHQETVKDFRLLKNSRLL-SWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDL 1062
Cdd:cd00200  129 TtLRGHTDWVNSVAFSPDGTFVaSSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLST 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1063 LLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLCaplseEGaatHGGWVTDLCFSPDGKMLISAG 1142
Cdd:cd00200  209 GKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL-----SG---HTNSVTSLAWSPDGKRLASGS 280


                 ....*....
gi 4502123  1143 --GYIKWWN 1149
Cdd:cd00200  281 adGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
915-1183 1.36e-49

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 181.65  E-value: 1.36e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   915 LSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETV 993
Cdd:COG2319   44 ASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRtLTGHTGAV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   994 KDFRLLKN-SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGH 1072
Cdd:COG2319  124 RSVAFSPDgKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGH 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1073 NGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLcaplseegAATHGGWVTDLCFSPDGKMLISAG--GYIKWWNV 1150
Cdd:COG2319  204 TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT--------LTGHSGSVRSVAFSPDGRLLASGSadGTVRLWDL 275

                        250       260       270
                 ....*....|....*....|....*....|...
gi 4502123  1151 VTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDN 1183
Cdd:COG2319  276 ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSD 308
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 948-1159 8.93e-46

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 166.74  E-value: 8.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   948 HKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETVKDFRLLKNS-RLLSWSFDGTVKVWNIITGNKEK 1025
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtLKGHTGPVRDVAASADGtYLASGSSDKTIRLWDLETGECVR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1026 DFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNG 1105
Cdd:cd00200   88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTG 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 4502123  1106 ELLHLCaplseegaATHGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTF 1159
Cdd:cd00200  168 KCVATL--------TGHTGEVNSVAFSPDGEKLLSSSsdGTIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
915-1189 3.11e-42

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 160.08  E-value: 3.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   915 LSPHLQYIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISSSDDAEIQVWNWQLDKCIF-LRGHQETV 993
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAtLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   994 KDFRLLKN-SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWSFDLLLPLHELRGH 1072
Cdd:COG2319   82 LSVAFSPDgRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1073 NGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaPLSEegaatHGGWVTDLCFSPDGKMLISAG--GYIKWWNV 1150
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLR---TLTG-----HTGAVRSVAFSPDGKLLASGSadGTVRLWDL 233

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 4502123  1151 VTGESSQTFYTNGTNLKKIHVSPDFKTYVTVDNLGILYI 1189
Cdd:COG2319  234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRL 272
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 6-90 8.78e-19

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 81.84  E-value: 8.78e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123       6 RNCLLQHREALEKDIKT-SYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLhEGYKDLA 84
Cdd:pfam00619    1 RKLLKKNRVALVERLGTlDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALK-EGDPDLA 79


                   ....*.
gi 4502123      85 ALLHDG 90
Cdd:pfam00619   80 SDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 9-87 1.32e-17

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 78.33  E-value: 1.32e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4502123     9 LLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAALL 87
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQPHLAELL 79
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1065-1159 2.38e-13

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 71.98  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123  1065 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHlcaplSEEGaatHGGWVTDLCFSPDGKMLISAG-- 1142
Cdd:cd00200    1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLR-----TLKG---HTGPVRDVAASADGTYLASGSsd 72

                         90
                 ....*....|....*..
gi 4502123  1143 GYIKWWNVVTGESSQTF 1159
Cdd:cd00200   73 KTIRLWDLETGECVRTL 89
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 618-775 9.99e-12

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 69.35  E-value: 9.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    618 RIASCGADKTLQVFKAETGEKLLEIKAHEDEVLCCAFST-DDRFIATCSVDKKVKIWNSMTGELVHTYDEHSeQVNCCHF 696
Cdd:PLN00181  547 QVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKA-NICCVQF 625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    697 TNSSHHlLLATGSSDCFLKLWDL-NQKECRNTMFGHTNSVNHCRFSpDDKLLASCSADGTLKLWD----ATSANERK--- 768
Cdd:PLN00181  626 PSESGR-SLAFGSADHKVYYYDLrNPKLPLCTMIGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWDlsmsISGINETPlhs 703

                         170
                  ....*....|
gi 4502123    769 ---SINVKQF 775
Cdd:PLN00181  704 fmgHTNVKNF 713
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 721-760 1.73e-10

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 56.94  E-value: 1.73e-10
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 4502123      721 QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 760
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
722-760 7.69e-10

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 55.04  E-value: 7.69e-10
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4502123     722 KECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWD 760
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 650-856 5.41e-09

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 60.49  E-value: 5.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    650 LCCA--FSTDDRFIATCSVDKKVKIW--NSMT--GELVH----TYDEHSEQVNCCHftNSSHHLLLATGSSDCFLKLWDL 719
Cdd:PLN00181  485 LVCAigFDRDGEFFATAGVNKKIKIFecESIIkdGRDIHypvvELASRSKLSGICW--NSYIKSQVASSNFEGVVQVWDV 562

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    720 NQKECRNTMFGHTNSVNHCRFSP-DDKLLASCSADGTLKLWdatSANERKSINVKQFFLNledpqedmeviVKCCSWSAD 798
Cdd:PLN00181  563 ARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLW---SINQGVSIGTIKTKAN-----------ICCVQFPSE 628

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4502123    799 GARIMV--AAKNKIFLWntDSRS-KVADCR--GHLSWVHGVMFSpDGSSFLTSSDDQTIRLWE 856
Cdd:PLN00181  629 SGRSLAfgSADHKVYYY--DLRNpKLPLCTmiGHSKTVSYVRFV-DSSTLVSSSTDNTLKLWD 688
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 635-674 7.86e-09

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 52.31  E-value: 7.86e-09
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 4502123      635 TGEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWN 674
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 902-1101 2.89e-08

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 58.17  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    902 IDYLTEAQVSCCCLSPHLQ-YIAFGDENGAIEILELVNNRIFQSRFQHKKTVWHIQFTADEKTLISS-SDDAEIQVWNWQ 979
Cdd:PLN00181  527 VELASRSKLSGICWNSYIKsQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSADPTLLASgSDDGSVKLWSIN 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    980 LDKCIFLRGHQETVKDFRLLKNS-RLLSW-SFDGTVKVWNIitgNKEKDFVC----HQGTVLSCDIShDATKFSSTSADK 1053
Cdd:PLN00181  607 QGVSIGTIKTKANICCVQFPSESgRSLAFgSADHKVYYYDL---RNPKLPLCtmigHSKTVSYVRFV-DSSTLVSSSTDN 682

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 4502123   1054 TAKIWSFDLLL------PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1101
Cdd:PLN00181  683 TLKLWDLSMSIsginetPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVYH 736
WD40 pfam00400
WD domain, G-beta repeat;
636-674 3.67e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 3.67e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4502123     636 GEKLLEIKAHEDEVLCCAFSTDDRFIATCSVDKKVKIWN 674
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 817-856 7.63e-07

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.54  E-value: 7.63e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 4502123      817 SRSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 856
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 677-718 1.02e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.15  E-value: 1.02e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 4502123      677 TGELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWD 718
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAF--SPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1065-1101 1.23e-06

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 46.15  E-value: 1.23e-06
                            10        20        30
                    ....*....|....*....|....*....|....*..
gi 4502123     1065 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1101
Cdd:smart00320    4 LLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
1065-1101 1.54e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 45.80  E-value: 1.54e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 4502123    1065 PLHELRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWN 1101
Cdd:pfam00400    3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 1122-1194 7.38e-06

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 49.26  E-value: 7.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4502123  1122 HGGWVTDLCFSPDGKMLISAG--GYIKWWNVVTGESSQTFYTNGTNLKKIHVSPDFKTYVTV--DNLGILYILQTLE 1194
Cdd:cd00200    8 HTGGVTCVAFSPDGKLLATGSgdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGssDKTIRLWDLETGE 84
WD40 pfam00400
WD domain, G-beta repeat;
818-856 7.75e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 7.75e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4502123     818 RSKVADCRGHLSWVHGVMFSPDGSSFLTSSDDQTIRLWE 856
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
678-718 1.37e-05

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.10  E-value: 1.37e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 4502123     678 GELVHTYDEHSEQVNCCHFtnSSHHLLLATGSSDCFLKLWD 718
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAF--SPDGKLLASGSDDGTVKVWD 39
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 613-808 1.46e-05

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 49.31  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    613 SEDGQRIASCGADKTLQVFKAETGEKLLEIKAHEDeVLCCAFSTDD-RFIATCSVDKKVKIWNSMTGEL-VHTYDEHSEQ 690
Cdd:PLN00181  585 SADPTLLASGSDDGSVKLWSINQGVSIGTIKTKAN-ICCVQFPSESgRSLAFGSADHKVYYYDLRNPKLpLCTMIGHSKT 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    691 VNCCHFTNSShhlLLATGSSDCFLKLWDLN------QKECRNTMFGHTNSVNHCRFSPDDKLLASCSADGTLKLWdatsa 764
Cdd:PLN00181  664 VSYVRFVDSS---TLVSSSTDNTLKLWDLSmsisgiNETPLHSFMGHTNVKNFVGLSVSDGYIATGSETNEVFVY----- 735

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 4502123    765 NERKSINVKQFFLNLEDPQEDMEV-----IVKCCSWSADGARIMVAAKN 808
Cdd:PLN00181  736 HKAFPMPVLSYKFKTIDPVSGLEVddasqFISSVCWRGQSSTLVAANST 784
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 1056-1111 4.16e-05

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


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 43.42  E-value: 4.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 4502123    1056 KIWSFDLllplhelRGHNGCVRCSAFSVDSTLLATGDDNGEIRIWNVSNGELLHLC 1111
Cdd:pfam12894   28 RVWTLSP-------DKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHF 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
126-426 5.42e-05

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 47.49  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   126 QQKLSKLKGEPGWVTIHGMAGCGKSV----LAAEAVRDHSLLEGCFPggvhwvsvgkqdksgLLMKLQNLCTRLDQDESF 201
Cdd:COG5635  170 LKRLELLEAKKKRLLILGEPGSGKTTllryLALELAERYLDAEDPIP---------------ILIELRDLAEEASLEDLL 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   202 SQRLPLNIEEAKDRLRilMLRKHPRSLLILDDvWD--------SWVLKAFD------SQCQILLTTRdksvtdsvmgpky 267
Cdd:COG5635  235 AEALEKRGGEPEDALE--RLLRNGRLLLLLDG-LDevpdeadrDEVLNQLRrfleryPKARVIITSR------------- 298

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   268 vvPVESSLGKEKGLEILSL----------FVNMKKADLPEQAHSIIKECK---------GSPLVVSLIGALLRD---FPN 325
Cdd:COG5635  299 --PEGYDSSELEGFEVLELaplsdeqieeFLKKWFEATERKAERLLEALEenpelrelaRNPLLLTLLALLLRErgeLPD 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   326 R----WEYYLKQL--QNKQFKRIRKSSSYDYEALDEAMS-ISVEMLREDikdyytDLSILQKDVKvptKVLCILWDMEtE 398
Cdd:COG5635  377 TraelYEQFVELLleRWDEQRGLTIYRELSREELRELLSeLALAMQENG------RTEFAREELE---EILREYLGRR-K 446

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 4502123   399 EVEDILQEFVNKSLLFCDRNG-------KSFRYYL 426
Cdd:COG5635  447 DAEALLDELLLRTGLLVERGEgrysfahRSFQEYL 481
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1122-1149 1.23e-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: 1.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 4502123     1122 HGGWVTDLCFSPDGKMLISAG--GYIKWWN 1149
Cdd:smart00320   11 HTGPVTSVAFSPDGKYLASGSddGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 599-632 1.72e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 39.99  E-value: 1.72e-04
                            10        20        30
                    ....*....|....*....|....*....|....
gi 4502123      599 VVRPHTDAVYHACFSEDGQRIASCGADKTLQVFK 632
Cdd:smart00320    7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
COG3903 COG3903
Predicted ATPase [General function prediction only];
139-174 2.08e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 45.78  E-value: 2.08e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 4502123   139 VTIHGMAGCGKSVLAAEAVRDhslLEGCFPGGVHWV 174
Cdd:COG3903  179 VTLTGPGGVGKTRLALEVAHR---LADRFPDGVWFV 211
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 1002-1167 2.29e-04

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 45.46  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   1002 SRLLSWSFDGTVKVWNIITGNKEKDFVCHQGTVLSCDISH-DATKFSSTSADKTAKIWSFDLLLPLHELRGH-NGCvrCS 1079
Cdd:PLN00181  546 SQVASSNFEGVVQVWDVARSQLVTEMKEHEKRVWSIDYSSaDPTLLASGSDDGSVKLWSINQGVSIGTIKTKaNIC--CV 623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123   1080 AFSVDS-TLLATGDDNGEIRIWNVSNGElLHLCAPLSEEGAATHGGWVtdlcfspDGKMLISAG--GYIKWWNV---VTG 1153
Cdd:PLN00181  624 QFPSESgRSLAFGSADHKVYYYDLRNPK-LPLCTMIGHSKTVSYVRFV-------DSSTLVSSStdNTLKLWDLsmsISG 695

                         170
                  ....*....|....*.
gi 4502123   1154 --ESSQTFYTNGTNLK 1167
Cdd:PLN00181  696 inETPLHSFMGHTNVK 711
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 11-75 3.88e-04

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


Pssm-ID: 260038  Cd Length: 94  Bit Score: 40.89  E-value: 3.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4502123    11 QHREALEKDIKTSY-IMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNAL 75
Cdd:cd08329   13 KNRMALFQHLTCVLpILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCL 78
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 1020-1059 5.18e-04

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 38.83  E-value: 5.18e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 4502123     1020 TGNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWS 1059
Cdd:smart00320    1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
CARD_CASP2 cd08332
Caspase activation and recruitment domain of Caspase-2; Caspase activation and recruitment ...
 1-87 1.74e-03

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


Pssm-ID: 260040  Cd Length: 87  Bit Score: 38.56  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     1 MDAKARNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGY 80
Cdd:cd08332    1 MQKRHREALKKNRVKLAKELVLDELLIHLLQKDILTDSMVESIMAKPTSFSQNVALLNLLPKRGPRAFSAFCEALRETSQ 80


                 ....*..
gi 4502123    81 KDLAALL 87
Cdd:cd08332   81 EHLADLL 87
WD40 pfam00400
WD domain, G-beta repeat;
1021-1059 1.94e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 4502123    1021 GNKEKDFVCHQGTVLSCDISHDATKFSSTSADKTAKIWS 1059
Cdd:pfam00400    1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
599-631 2.30e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 2.30e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 4502123     599 VVRPHTDAVYHACFSEDGQRIASCGADKTLQVF 631
Cdd:pfam00400    6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVW 38
FxSxx_TPR NF040586
FxSxx-COOH system tetratricopeptide repeat protein; Members of this family are typically about ...
 108-255 2.66e-03

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


Pssm-ID: 468560 [Multi-domain]  Cd Length: 836  Bit Score: 41.83  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    108 VPQRPVVFVTRKKLVNAIQQKLSKLKGEPGWVTIHGMAGCGKSVLAAE-AVR---DHSLlegcfpggVHWVSVgkQDKSG 183
Cdd:NF040586    1 VPPRNPNFTGREELLERLRDQLRSGGAAVVPQALHGLGGVGKTQLALEyAHRfraDYDL--------VWWIPA--DQPEL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    184 LLMKLQNLCTRLdqdesfsqRLPLNIEEAKDRLRIL--MLRK---HPRSLLILDDVWDSWVLKAF---DSQCQILLTTRD 255
Cdd:NF040586   71 VRASLAELARRL--------GLPLGPDDVDEAARAVldALRRgepYRRWLLVFDNADDPEDLRDLlptGGPGHVLITSRN 142
WD40 pfam00400
WD domain, G-beta repeat;
1122-1149 2.74e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.74e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 4502123    1122 HGGWVTDLCFSPDGKMLISAG--GYIKWWN 1149
Cdd:pfam00400   10 HTGSVTSLAFSPDGKLLASGSddGTVKVWD 39
PTZ00421 PTZ00421
coronin; Provisional
 960-1057 3.76e-03

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 41.42  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123    960 DEKTLISSSDDAEIQVWNWQ--------LDKCIFLRGHQETVK--DFRLLKNSRLLSWSFDGTVKVWNIITGNKEKDFVC 1029
Cdd:PTZ00421   87 DPQKLFTASEDGTIMGWGIPeegltqniSDPIVHLQGHTKKVGivSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKC 166

                          90       100
                  ....*....|....*....|....*...
gi 4502123   1030 HQGTVLSCDISHDATKFSSTSADKTAKI 1057
Cdd:PTZ00421  167 HSDQITSLEWNLDGSLLCTTSKDKKLNI 194
ANAPC4_WD40 pfam12894
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ...
 648-697 5.72e-03

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


Pssm-ID: 403945 [Multi-domain]  Cd Length: 91  Bit Score: 37.26  E-value: 5.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 4502123     648 EVLCCAFSTDDRFIATCSVDKKVKIWNSMTGELVHTYDEHSEQVNCCHFT 697
Cdd:pfam12894   40 EVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGSDLITCLGWG 89
CARD_CASP9 cd08326
Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment ...
 6-87 7.74e-03

Caspase activation and recruitment domain of Caspase-9; Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176740  Cd Length: 84  Bit Score: 36.63  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4502123     6 RNCLLQHREALEKDIKTSYIMDHMISDGFLTISEEEKVRNEPTQQQRAAMLIKMILKKDNDSYVSFYNALLHEGYKDLAA 85
Cdd:cd08326    2 RQILRRHRARLVEELQPKYLWDHLLSRGVFTPDMIEEIQAAGSRRDQARQLLIDLETRGKQAFPAFLSALRETGQTDLAE 81


                 ..
gi 4502123    86 LL 87
Cdd:cd08326   82 LL 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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