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Conserved domains on  [gi|1622861448|ref|XP_014968752|]
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p53-induced death domain-containing protein 1 isoform X1 [Macaca mulatta]

Protein Classification

leucine-rich repeat domain-containing protein; leucine-rich repeat and calponin homology domain-containing protein( domain architecture ID 11469511)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions| leucine-rich repeat and calponin homology (LRCH) domain-containing protein similar to human LRCH4 which is a Toll-like receptor (TLR) accessory protein that regulates signaling by multiple TLRs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-295 4.05e-44

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 165.49  E-value: 4.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 120 GLSGLAHLAHLDLSFNSLETLPACVLRMRGLGALLLSHNCLSELPEALGALPALTFLAVTHNRLQTLPPALGALSTLQRL 199
Cdd:COG4886   108 ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 200 DLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPAgLARLPLLTRLDLRDNQLRDLP 279
Cdd:COG4886   188 DLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP 266

                         170
                  ....*....|....*...
gi 1622861448 280 PE--LLDAPFVRLQGNPL 295
Cdd:COG4886   267 PLanLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 812-897 2.37e-34

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260049  Cd Length: 86  Bit Score: 126.28  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 891
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                  ....*.
gi 1622861448 892 EVRAVL 897
Cdd:cd08779    81 ELRDKL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 2.70e-10

Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex with RAIDD and procaspase-2 that is known as the 'PIDDosome'. The PIDDosome forms when DNA damage occurs and either activates NF-kappaB, leading to cell survival, or caspase-2, which leads to apoptosis.


:

Pssm-ID: 463098  Cd Length: 34  Bit Score: 56.00  E-value: 2.70e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622861448 421 WGDLETHLEEEAPQRL-WAHCQAPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
ZU5 super family cl02517
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-398 6.38e-08

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


The actual alignment was detected with superfamily member pfam00791:

Pssm-ID: 470600  Cd Length: 97  Bit Score: 51.37  E-value: 6.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622861448 325 SFPVTPRGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWL 398
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78
ZU5 super family cl02517
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 465-537 1.15e-06

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


The actual alignment was detected with superfamily member pfam00791:

Pssm-ID: 470600  Cd Length: 97  Bit Score: 47.52  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622861448 465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLRPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-295 4.05e-44

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 165.49  E-value: 4.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 120 GLSGLAHLAHLDLSFNSLETLPACVLRMRGLGALLLSHNCLSELPEALGALPALTFLAVTHNRLQTLPPALGALSTLQRL 199
Cdd:COG4886   108 ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 200 DLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPAgLARLPLLTRLDLRDNQLRDLP 279
Cdd:COG4886   188 DLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP 266

                         170
                  ....*....|....*...
gi 1622861448 280 PE--LLDAPFVRLQGNPL 295
Cdd:COG4886   267 PLanLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 812-897 2.37e-34

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 126.28  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 891
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                  ....*.
gi 1622861448 892 EVRAVL 897
Cdd:cd08779    81 ELRDKL 86
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 5.01e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 86.44  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLRMRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113  180 IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 194 STLQRLDLSQNLL-DTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSN-LLASVPAGLARLPLLTRLDL 270
Cdd:PLN00113  260 KNLQYLFLYQNKLsGPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNnFTGKIPVALTSLPRLQVLQL 339


                  ....*
gi 1622861448 271 RDNQL 275
Cdd:PLN00113  340 WSNKF 344
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-273 9.50e-14

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 71.36  E-value: 9.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 114 LTTLPaGLSGLAHLAHLDLSFNSLEtlpacvlRMRGLGALL------LSHNCLSELpEALGALPALTFLAVTHnrlQTLP 187
Cdd:cd21340    36 ITKIE-NLEFLTNLTHLYLQNNQIE-------KIENLENLVnlkklyLGGNRISVV-EGLENLTNLEELHIEN---QRLP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 188 PAlgalstlQRLDLSQNLLDTLppeiggLGSLLELNLASNRLQSLpASLAGLRSLRLLVLHSNLLASVPA---GLARLPL 264
Cdd:cd21340   104 PG-------EKLTFDPRSLAAL------SNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPS 169


                  ....*....
gi 1622861448 265 LTRLDLRDN 273
Cdd:cd21340   170 LRELDLTGN 178
Death pfam00531
Death domain;
823-897 3.13e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 65.85  E-value: 3.13e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622861448 823 LGPDWPTVALHLGVSYRELQRIRHEFRDDLDgQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 897
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENPRLRS-QTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
LRR_8 pfam13855
Leucine rich repeat;
194-252 2.06e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 2.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 194 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 252
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 2.70e-10

Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex with RAIDD and procaspase-2 that is known as the 'PIDDosome'. The PIDDosome forms when DNA damage occurs and either activates NF-kappaB, leading to cell survival, or caspase-2, which leads to apoptosis.


Pssm-ID: 463098  Cd Length: 34  Bit Score: 56.00  E-value: 2.70e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622861448 421 WGDLETHLEEEAPQRL-WAHCQAPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 819-894 5.52e-08

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 51.26  E-value: 5.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622861448  819 VAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 894
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-398 6.38e-08

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 51.37  E-value: 6.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622861448 325 SFPVTPRGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWL 398
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 465-537 1.15e-06

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 47.52  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622861448 465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLRPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 475-537 9.99e-06

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 45.03  E-value: 9.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622861448  475 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLRPVTVQLP 537
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 320-417 7.29e-04

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 40.03  E-value: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  320 TSDLDSFPVTPRGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGL 396
Cdd:smart00218   1 PSFLVSGTFDARGGRLRGPrTGVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVIL 80

                           90       100
                   ....*....|....*....|..
gi 1622861448  397 WL-LFTPPRARRCREVVVRTRN 417
Cdd:smart00218  81 EVpHCASLRPRDWEIVLLRSEN 102
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
120-295 4.05e-44

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 165.49  E-value: 4.05e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 120 GLSGLAHLAHLDLSFNSLETLPACVLRMRGLGALLLSHNCLSELPEALGALPALTFLAVTHNRLQTLPPALGALSTLQRL 199
Cdd:COG4886   108 ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 200 DLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPAgLARLPLLTRLDLRDNQLRDLP 279
Cdd:COG4886   188 DLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPE-LGNLTNLEELDLSNNQLTDLP 266

                         170
                  ....*....|....*...
gi 1622861448 280 PE--LLDAPFVRLQGNPL 295
Cdd:COG4886   267 PLanLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-296 3.21e-41

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 157.02  E-value: 3.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  87 QSLSCLRSLVLKGGQrrdtlgaclrgaLTTLPAGLSGLAHLAHLDLSFNSLETLPACVLRMRGLGALLLSHNCLSELPEA 166
Cdd:COG4886   110 SNLTNLESLDLSGNQ------------LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 167 LGALPALTFLAVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPaSLAGLRSLRLLV 246
Cdd:COG4886   178 LGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELD 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622861448 247 LHSNLLASVPAgLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLG 296
Cdd:COG4886   257 LSNNQLTDLPP-LANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLL 305
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 812-897 2.37e-34

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 126.28  E-value: 2.37e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 891
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                  ....*.
gi 1622861448 892 EVRAVL 897
Cdd:cd08779    81 ELRDKL 86
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
130-282 8.62e-31

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 126.20  E-value: 8.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 130 LDLSFNSLETLPACVLRMRGLGALLLSHNclselpEALGALPALTFLAVTHNRLQTLPPALGALSTLQRLDLSQNLLDTL 209
Cdd:COG4886    78 SLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDL 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622861448 210 PPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPAGLARLPLLTRLDLRDNQLRDLPPEL 282
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPL 224
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
49-301 1.14e-27

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 116.96  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  49 RLLHLCVQQPL-QLLQVEFLRLStheDPQL--LEATLAQLPQslscLRSLVLKGGQrrdtlgaclrgaLTTLPAGLSGLA 125
Cdd:COG4886    99 TELDLSGNEELsNLTNLESLDLS---GNQLtdLPEELANLTN----LKELDLSNNQ------------LTDLPEPLGNLT 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 126 HLAHLDLSFNSLETLPACVLRMRGLGALLLSHNCLSELPEALGALPALTFLAVTHNRLQTLPPALGALSTLQRLDLSQNL 205
Cdd:COG4886   160 NLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQ 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 206 LDTLP---------------------PEIGGLGSLLELNLASNRLQSLP----ASLAGLRSLRLLVLHSNLLASVPAGLA 260
Cdd:COG4886   240 LTDLPelgnltnleeldlsnnqltdlPPLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLL 319

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1622861448 261 RLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPD 301
Cdd:COG4886   320 LTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLS 360
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 819-894 1.29e-17

Death Domain: a protein-protein interaction domain; Death Domains (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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 78.09  E-value: 1.29e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622861448 819 VAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 894
Cdd:cd01670     5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWRERE-GDEATLGRLIQALREIGRRDLAEKLE 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
181-300 3.49e-17

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 84.99  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 181 NRLQTLPPALGALSTLQRLDLSQNlldtlpPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPAGLA 260
Cdd:COG4886    83 SLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLG 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622861448 261 RLPLLTRLDLRDNQLRDLPPELLDAPFVR---LQGNPLGEASP 300
Cdd:COG4886   157 NLTNLKSLDLSNNQLTDLPEELGNLTNLKeldLSNNQITDLPE 199
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 5.01e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 86.44  E-value: 5.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLRMRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113  180 IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 194 STLQRLDLSQNLL-DTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSN-LLASVPAGLARLPLLTRLDL 270
Cdd:PLN00113  260 KNLQYLFLYQNKLsGPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNnFTGKIPVALTSLPRLQVLQL 339


                  ....*
gi 1622861448 271 RDNQL 275
Cdd:PLN00113  340 WSNKF 344
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 7.35e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 85.67  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLRMRGLGAL-LLSHNCLSELPEALGALPALTFLAVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113  276 IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKH 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 194 STLQRLDLSQN-LLDTLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLRLLVLHSNLLA-SVPAGLARLPLLTRLDL 270
Cdd:PLN00113  356 NNLTVLDLSTNnLTGEIPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDI 435


                  ....*
gi 1622861448 271 RDNQL 275
Cdd:PLN00113  436 SNNNL 440
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-282 2.42e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 77.58  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 117 LPAGLSGLAHLAHLDLSFNSLE-----TLPACvlrmRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ------ 184
Cdd:PLN00113  372 IPEGLCSSGNLFKLILFSNSLEgeipkSLGAC----RSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsr 447

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 185 -------------------TLPPALGAlSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLR 243
Cdd:PLN00113  448 kwdmpslqmlslarnkffgGLPDSFGS-KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLV 526

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622861448 244 LLVL-HSNLLASVPAGLARLPLLTRLDLRDNQLR-DLPPEL 282
Cdd:PLN00113  527 SLDLsHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKNL 567
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
58-249 8.90e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.50  E-value: 8.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  58 PLQLLQVEFLRLSTHEDPQLLEATLAQLPQS---LSCLRSLVLKGGQRRDTLgaclRGALTTLPAGLSglAHLAHLDLSF 134
Cdd:PRK15370  240 PDTIQEMELSINRITELPERLPSALQSLDLFhnkISCLPENLPEELRYLSVY----DNSIRTLPAHLP--SGITHLNVQS 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 135 NSLETLPAcVLRMrGLGALLLSHNCLSELPEALGalPALTFLAVTHNRLQTLPPALGalSTLQRLDLSQNLLDTLPPEIG 214
Cdd:PRK15370  314 NSLTALPE-TLPP-GLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP 387

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622861448 215 glGSLLELNLASNRLQSLPASLAGLRS-----LRLLVLHS 249
Cdd:PRK15370  388 --AALQIMQASRNNLVRLPESLPHFRGegpqpTRIIVEYN 425
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-273 9.50e-14

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 71.36  E-value: 9.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 114 LTTLPaGLSGLAHLAHLDLSFNSLEtlpacvlRMRGLGALL------LSHNCLSELpEALGALPALTFLAVTHnrlQTLP 187
Cdd:cd21340    36 ITKIE-NLEFLTNLTHLYLQNNQIE-------KIENLENLVnlkklyLGGNRISVV-EGLENLTNLEELHIEN---QRLP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 188 PAlgalstlQRLDLSQNLLDTLppeiggLGSLLELNLASNRLQSLpASLAGLRSLRLLVLHSNLLASVPA---GLARLPL 264
Cdd:cd21340   104 PG-------EKLTFDPRSLAAL------SNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPS 169


                  ....*....
gi 1622861448 265 LTRLDLRDN 273
Cdd:cd21340   170 LRELDLTGN 178
Death pfam00531
Death domain;
823-897 3.13e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 65.85  E-value: 3.13e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622861448 823 LGPDWPTVALHLGVSYRELQRIRHEFRDDLDgQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 897
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENPRLRS-QTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 126-295 4.24e-13

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 69.43  E-value: 4.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 126 HLAHLDLSFNSLETLPACvlrmRGLGALLLSHNCLSELpEALGALPALTFLAVTHNRLQTLPPaLGALSTLQRLDLSQNL 205
Cdd:cd21340     6 HLYLNDKNITKIDNLSLC----KNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 206 LDTLppE-IGGLGSLLELNLASNRL---QSL---PASLAGL-RSLRLLVLHSNLLASVpAGLARLPLLTRLDLRDNQLRD 277
Cdd:cd21340    80 ISVV--EgLENLTNLEELHIENQRLppgEKLtfdPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISD 156

                         170       180
                  ....*....|....*....|....*
gi 1622861448 278 LpPELLDA----PFVR---LQGNPL 295
Cdd:cd21340   157 L-EELLDLlsswPSLReldLTGNPV 180
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
114-282 8.84e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.42  E-value: 8.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 114 LTTLPAGLSGlaHLAHLDLSFNSL----ETLPACVLRMRglgallLSHNCLSELPEALGAlpALTFLAVTHNRLQTLPPA 189
Cdd:PRK15370  211 LKSLPENLQG--NIKTLYANSNQLtsipATLPDTIQEME------LSINRITELPERLPS--ALQSLDLFHNKISCLPEN 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 190 LGalSTLQRLDLSQNLLDTLPPEIGGlgSLLELNLASNRLQSLPASLAglRSLRLLVLHSNLLASVPAGLA--------- 260
Cdd:PRK15370  281 LP--EELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLPpelqvldvs 354

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622861448 261 --RL--------PLLTRLDLRDNQLRDLPPEL 282
Cdd:PRK15370  355 knQItvlpetlpPTITTLDVSRNALTNLPENL 386
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 124-283 2.39e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 71.03  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 124 LAHLAHLDLSFNSLE-TLPACVLRMRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ-TLPPALGALSTLQRLD 200
Cdd:PLN00113  139 IPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 201 LS-QNLLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSNLLA-SVPAGLARLPLLTRLDLRDNQLRD 277
Cdd:PLN00113  219 LGyNNLSGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSG 298


                  ....*.
gi 1622861448 278 LPPELL 283
Cdd:PLN00113  299 EIPELV 304
LRR_8 pfam13855
Leucine rich repeat;
194-252 2.06e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 57.15  E-value: 2.06e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 194 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 252
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 123-282 2.19e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.87  E-value: 2.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 123 GLAHLAHLDLSFNSLE-TLPACVLRM-RGLGALLLSHNCLSElPEALGALPALTFLAVTHNRLQ-TLPPALGALSTLQRL 199
Cdd:PLN00113   91 RLPYIQTINLSNNQLSgPIPDDIFTTsSSLRYLNLSNNNFTG-SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 200 DLSQN-LLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVL-HSNLLASVPAGLARLPLLTRLDLRDNQLR 276
Cdd:PLN00113  170 DLGGNvLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLgYNNLSGEIPYEIGGLTSLNHLDLVYNNLT 249


                  ....*..
gi 1622861448 277 -DLPPEL 282
Cdd:PLN00113  250 gPIPSSL 256
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 2.70e-10

Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex with RAIDD and procaspase-2 that is known as the 'PIDDosome'. The PIDDosome forms when DNA damage occurs and either activates NF-kappaB, leading to cell survival, or caspase-2, which leads to apoptosis.


Pssm-ID: 463098  Cd Length: 34  Bit Score: 56.00  E-value: 2.70e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1622861448 421 WGDLETHLEEEAPQRL-WAHCQAPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
LRR_8 pfam13855
Leucine rich repeat;
171-229 4.40e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.30  E-value: 4.40e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 171 PALTFLAVTHNRLQTLPP-ALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRL 229
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 812-885 4.79e-09

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260031  Cd Length: 83  Bit Score: 53.87  E-value: 4.79e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQaGQPGAVGLLVQALEQSD 885
Cdd:cd08319     1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQ-GKKATVQSLIQSLKAVE 73
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 121-239 1.11e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 59.09  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 121 LSGLAHLAHLDLSFNSL-ETLPACVLRMRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ-TLPPALGALSTLQ 197
Cdd:PLN00113  471 SFGSKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLS 550

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622861448 198 RLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQ-SLPASLAGL 239
Cdd:PLN00113  551 QLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLPSTGAFL 594
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
114-306 1.46e-08

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 58.63  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 114 LTTLPAGLSGLAHLAHLDLSFNSLETLPAcvlrmrGLGALLLSHNCLSELPealgALPA-LTFLAVTHNRLQTLPPALGA 192
Cdd:PRK15387  274 LTHLPALPSGLCKLWIFGNQLTSLPVLPP------GLQELSVSDNQLASLP----ALPSeLCKLWAYNNQLTSLPTLPSG 343

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 193 LSTLQRLDLSQNLLDTLPPEIGGL--------------GSLLELNLASNRLQSLPASLAGLRSlrlLVLHSNLLASVPAg 258
Cdd:PRK15387  344 LQELSVSDNQLASLPTLPSELYKLwaynnrltslpalpSGLKELIVSGNRLTSLPVLPSELKE---LMVSGNRLTSLPM- 419

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622861448 259 larLPL-LTRLDLRDNQLRDLPPELL---DAPFVRLQGNPLGE----ASPDVPSSP 306
Cdd:PRK15387  420 ---LPSgLLSLSVYRNQLTRLPESLIhlsSETTVNLEGNPLSErtlqALREITSAP 472
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 812-889 1.86e-08

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 52.27  E-value: 1.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQAGQP-GAVglLVQALEQSDRQDV 889
Cdd:cd08317     3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKAtGNA--LESALKKIGRDDI 79
LRR_8 pfam13855
Leucine rich repeat;
218-275 4.31e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 4.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 218 SLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLLASV-PAGLARLPLLTRLDLRDNQL 275
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 819-894 5.52e-08

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 51.26  E-value: 5.52e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622861448  819 VAGRLGPDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 894
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-398 6.38e-08

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 51.37  E-value: 6.38e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622861448 325 SFPVTPRGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWL 398
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 29-252 7.05e-07

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 52.87  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  29 VRPFLGGNRLSLDLYPGGCQRLLHLCVQQPLQLLQVEFLRLSTHE-DPQLLEATLAQLPQSLScLRSLVLK----GGQRR 103
Cdd:COG5238   147 LKDPLGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQiGDEGIEELAEALTQNTT-VTTLWLKrnpiGDEGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 104 DTLGACLRG--ALTTL-----PAGLSGLAHLA----------HLDLSFNSL-----ETLPACVLRMRGLGALLLSHNCLS 161
Cdd:COG5238   226 EILAEALKGnkSLTTLdlsnnQIGDEGVIALAealknnttveTLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIG 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 162 E-----LPEALGALPALTFLAVTHNRLQT-----LPPALGALSTLQRLDLSQNLL-----DTLPPEIGGLGSLLELNLAS 226
Cdd:COG5238   306 DegaiaLAEGLQGNKTLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNQIgdegaIALAKYLEGNTTLRELNLGK 385

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1622861448 227 NRL-----QSLPASLAGLRsLRLLVLHSNLL 252
Cdd:COG5238   386 NNIgkqgaEALIDALQTNR-LHTLILDGNLI 415
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 116-245 9.37e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 52.93  E-value: 9.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 116 TLPAGLSGLAHLAHLDLSFNSL-----ETLPACvlrmRGLGALLLSHNCLS-ELPEALGALPALTFLAVTHNRLQ-TLPP 188
Cdd:PLN00113  490 AVPRKLGSLSELMQLKLSENKLsgeipDELSSC----KKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPK 565

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 189 ALGALSTLQRLDLSQNLLD-TLPPEigglGSLLELN---LASNRLQSLPASLAGLRSLRLL 245
Cdd:PLN00113  566 NLGNVESLVQVNISHNHLHgSLPST----GAFLAINasaVAGNIDLCGGDTTSGLPPCKRV 622
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 465-537 1.15e-06

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 47.52  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622861448 465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLRPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
142-343 2.27e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 51.70  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 142 ACVLRMR-----GLGALLLSHNCLSELPEALGAlpALTFLAVTHNRLQTLPPALGALSTLQrldLSQNLLDTLPPEIGGL 216
Cdd:PRK15387  190 AVVQKMRaclnnGNAVLNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLPALPPELRTLE---VSGNQLTSLPVLPPGL 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 217 gslLELNLASNRLQSLPASLAGLRSLRLLvlhSNLLASVPaglARLPLLTRLDLRDNQLRDLP--PELL------DAPFV 288
Cdd:PRK15387  265 ---LELSIFSNPLTHLPALPSGLCKLWIF---GNQLTSLP---VLPPGLQELSVSDNQLASLPalPSELcklwayNNQLT 335

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 289 RLQGNPLGEASPDVPSSPVAALiPEMP----RLFLTSD-LDSFPVTPRGCSVTLACGVRL 343
Cdd:PRK15387  336 SLPTLPSGLQELSVSDNQLASL-PTLPselyKLWAYNNrLTSLPALPSGLKELIVSGNRL 394
PLN03150 PLN03150
hypothetical protein; Provisional
 163-239 2.86e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.97  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 163 LPEALGALPALTFLAVTHNRLQ-TLPPALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRLQS-LPASLAGL 239
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNGSIPEsLGQLTSLRILNLNGNSLSGrVPAALGGR 513
PLN03150 PLN03150
hypothetical protein; Provisional
 110-216 3.60e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.97  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 110 LRGaltTLPAGLSGLAHLAHLDLSFNSLEtlpacvlrmrglgalllshnclSELPEALGALPALTFLAVTHNRLQ-TLPP 188
Cdd:PLN03150  430 LRG---FIPNDISKLRHLQSINLSGNSIR----------------------GNIPPSLGSITSLEVLDLSYNSFNgSIPE 484

                          90       100
                  ....*....|....*....|....*....
gi 1622861448 189 ALGALSTLQRLDLSQNLLD-TLPPEIGGL 216
Cdd:PLN03150  485 SLGQLTSLRILNLNGNSLSgRVPAALGGR 513
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 812-889 4.00e-06

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 45.89  E-value: 4.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622861448 812 TQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEF-RDDLDGQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDV 889
Cdd:cd08777     1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYeRDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDL 79
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 811-893 7.03e-06

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260030  Cd Length: 86  Bit Score: 45.20  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 811 LTQSNLLSVAGRLGPDWPTVALHLGVSYRELQRIRHEfRDDLDGQIRHMLFSWAERQAGQpGAVGLLVQALEQSDRQDVA 890
Cdd:cd08318     5 VTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESD-SEDMKMRAKQLLVTWQDREGAQ-ATPEILMTALNAAGLNEIA 82


                  ...
gi 1622861448 891 EEV 893
Cdd:cd08318    83 ENL 85
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 475-537 9.99e-06

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 45.03  E-value: 9.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622861448  475 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLRPVTVQLP 537
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
LRR_8 pfam13855
Leucine rich repeat;
126-183 1.31e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 1.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 126 HLAHLDLSFNSLETL-PACVLRMRGLGALLLSHNCLSEL-PEALGALPALTFLAVTHNRL 183
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 113-279 2.12e-05

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 47.74  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 113 ALTTLPAGLSGLAHLAHLDLSFNSL-----ETLPACvLRMRGLGALLLSHNCLSELPEAL--GAL----PALTFLAVTHN 181
Cdd:cd00116    69 GLQSLLQGLTKGCGLQELDLSDNALgpdgcGVLESL-LRSSSLQELKLNNNGLGDRGLRLlaKGLkdlpPALEKLVLGRN 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 182 RLQT-----LPPALGALSTLQRLDLSQNlldtlppEIGGLGsllelnlasnrLQSLPASLAGLRSLRLLVLHSNLL---- 252
Cdd:cd00116   148 RLEGasceaLAKALRANRDLKELNLANN-------GIGDAG-----------IRALAEGLKANCNLEVLDLNNNGLtdeg 209

                         170       180
                  ....*....|....*....|....*...
gi 1622861448 253 -ASVPAGLARLPLLTRLDLRDNQLRDLP 279
Cdd:cd00116   210 aSALAETLASLKSLEVLNLGDNNLTDAG 237
PLN03150 PLN03150
hypothetical protein; Provisional
 203-351 2.28e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.81  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 203 QNLLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVL-HSNLLASVPAGLARLPLLTRLDLRDNQLRDLPP 280
Cdd:PLN03150  428 QGLRGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLsYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVP 507

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 281 elldapfVRLQGNPLGEASPDVPSSPVAALIPEMprlfltsdldsfpvtpRGCSVTLACGVRLQFPAGATA 351
Cdd:PLN03150  508 -------AALGGRLLHRASFNFTDNAGLCGIPGL----------------RACGPHLSVGAKIGIAFGVSV 555
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-306 3.15e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 145 LRMRGLGALLLSHNCLSELPEALGALPALTFLAVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNL 224
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 225 ASNRLQSLPASLAGLRSLRLLVLHSNllasvpAGLARLPLLTRLDLRDNQLRDLPPELLDAPFVR---LQGNPLGEASPD 301
Cdd:COG4886    81 LLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKeldLSNNQLTDLPEP 154


                  ....*
gi 1622861448 302 VPSSP 306
Cdd:COG4886   155 LGNLT 159
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 320-417 7.29e-04

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 40.03  E-value: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448  320 TSDLDSFPVTPRGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGL 396
Cdd:smart00218   1 PSFLVSGTFDARGGRLRGPrTGVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVIL 80

                           90       100
                   ....*....|....*....|..
gi 1622861448  397 WL-LFTPPRARRCREVVVRTRN 417
Cdd:smart00218  81 EVpHCASLRPRDWEIVLLRSEN 102
LRR_8 pfam13855
Leucine rich repeat;
240-295 8.61e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 8.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622861448 240 RSLRLLVLHSNLLASVPAG-LARLPLLTRLDLRDNQLRDLPPELLDAP----FVRLQGNPL 295
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLpslrYLDLSGNRL 61
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 829-898 1.12e-03

Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260028  Cd Length: 94  Bit Score: 39.20  E-value: 1.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 829 TVALHLGVSYRELQRIRHEFRDDLDGQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVLE 898
Cdd:cd08316    22 KFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKH-GKKGAYRTLIKTLRKAGKRAKADKIQDIIK 90
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 825-894 1.31e-03

Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176729  Cd Length: 80  Bit Score: 38.52  E-value: 1.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622861448 825 PDWPTVALHLGVSYRELQRIRHEFRDDLDGQIRhMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVR 894
Cdd:cd08313    12 RRWKEFVRRLGLSDNEIERVELDHRRCRDAQYQ-MLKVWKERGPRPYATLQHLLSVLRDMELVGCAEDIE 80
 
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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