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Conserved domains on  [gi|282165682|ref|NP_001099788|]
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p53-induced death domain-containing protein 1 [Rattus norvegicus]

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];
128-300 1.37e-41

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 128 DLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSLSTLQRLDLS 207
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 208 ENLLDTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLLTSVPpGLAHLPLITRLDLRDNQLRDLP--A 285
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPplA 269

                        170
                 ....*....|....*
gi 282165682 286 ELLDAPFVRLQGNPL 300
Cdd:COG4886  270 NLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 795-880 4.68e-32

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: 119.73  E-value: 4.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 874
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 282165682 875 EVRAIL 880
Cdd:cd08779   81 ELRDKL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 428-460 1.23e-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: 57.15  E-value: 1.23e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 282165682  428 WNDLETHLEEEAPKRR-WARCQVPHFSWFLVVLR 460
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.
 330-403 2.70e-07

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: 49.45  E-value: 2.70e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165682  330 SFLVTPHGCSVTLA-CGVRLQFPAGATTTPITIHYRLWLP--EPGLVSLGPHDFLLSGVLELQPHGVAFQQNVSLWL 403
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.
 471-544 1.82e-05

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: 44.06  E-value: 1.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682  471 EGALLCSSgHPGVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLsqsGPP--SFLQPVTVQLP 544
Cdd:pfam00791   8 RGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
128-300 1.37e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 128 DLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSLSTLQRLDLS 207
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 208 ENLLDTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLLTSVPpGLAHLPLITRLDLRDNQLRDLP--A 285
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPplA 269

                        170
                 ....*....|....*
gi 282165682 286 ELLDAPFVRLQGNPL 300
Cdd:COG4886  270 NLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 795-880 4.68e-32

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: 119.73  E-value: 4.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 874
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 282165682 875 EVRAIL 880
Cdd:cd08779   81 ELRDKL 86
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 129-288 1.03e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 78.74  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 129 LACLAHLDLSFNRLE-TLPTCVLELHSLDALLLSHNCLS-ELPEALGALPTLTFLTVTHN-LLERLPPTLGSLSTLQRLD 205
Cdd:PLN00113 139 IPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIY 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 206 LS-ENLLDTIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVLHSNLLT-SVPPGLAHLPLITRLDLRDNQLRD 282
Cdd:PLN00113 219 LGyNNLSGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSG 298


                 ....*.
gi 282165682 283 LPAELL 288
Cdd:PLN00113 299 EIPELV 304
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 134-300 3.41e-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: 72.51  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 134 HLDLS---FNRLETLPTCvlelHSLDALLLSHNCLSELpEALGALPTLTFLTVTHNLLERLPPtLGSLSTLQRLDLSENL 210
Cdd:cd21340    6 HLYLNdknITKIDNLSLC----KNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 211 LDTIpSEIGDLSSLRELNLASNRLQH------LPASLAGL-RSLRLLVLHSNLLTSVPPgLAHLPLITRLDLRDNQLRDL 283
Cdd:cd21340   80 ISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSLEP-LAPLRNLEQLDASNNQISDL 157

                        170       180
                 ....*....|....*....|....
gi 282165682 284 pAELLDA----PFVR---LQGNPL 300
Cdd:cd21340  158 -EELLDLlsswPSLReldLTGNPV 180
Death pfam00531
Death domain;
799-880 3.89e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 68.55  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682  799 LLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDgQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVRA 878
Cdd:pfam00531   7 LLDPPPPLGKDWRELARKLGLSENEIDEIESENPRLRS-QTYELLRLW-EQREGKNATVGTLLEALRKLGRRDAAEKIQS 84


                  ..
gi 282165682  879 IL 880
Cdd:pfam00531  85 IL 86
LRR_8 pfam13855
Leucine rich repeat;
222-280 8.22e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.30  E-value: 8.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165682  222 SSLRELNLASNRLQHL-PASLAGLRSLRLLVLHSNLLTSVPPG-LAHLPLITRLDLRDNQL 280
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 428-460 1.23e-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: 57.15  E-value: 1.23e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 282165682  428 WNDLETHLEEEAPKRR-WARCQVPHFSWFLVVLR 460
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 806-877 5.80e-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: 50.87  E-value: 5.80e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165682   806 LGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVR 877
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLW-EQREGKNATLGTLLEALRKMGRDDAVELLR 86
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 330-403 2.70e-07

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 49.45  E-value: 2.70e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165682  330 SFLVTPHGCSVTLA-CGVRLQFPAGATTTPITIHYRLWLP--EPGLVSLGPHDFLLSGVLELQPHGVAFQQNVSLWL 403
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGTRIECYLAVNrdESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 471-544 1.82e-05

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 44.06  E-value: 1.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682  471 EGALLCSSgHPGVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLsqsGPP--SFLQPVTVQLP 544
Cdd:pfam00791   8 RGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 482-544 1.42e-04

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 41.95  E-value: 1.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165682   482 GVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLSQSGpPSFLQPVTVQLP 544
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
128-300 1.37e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 128 DLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSLSTLQRLDLS 207
Cdd:COG4886  111 NLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLS 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 208 ENLLDTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLLTSVPpGLAHLPLITRLDLRDNQLRDLP--A 285
Cdd:COG4886  191 NNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPplA 269

                        170
                 ....*....|....*
gi 282165682 286 ELLDAPFVRLQGNPL 300
Cdd:COG4886  270 NLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-301 8.85e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 155.48  E-value: 8.85e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 119 LTTLPASMRDLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSL 198
Cdd:COG4886  125 LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNL 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 199 STLQRLDLSENLLDTIPSEIGDLSSLRELNLASNRLQHLPaSLAGLRSLRLLVLHSNLLTSVPPgLAHLPLITRLDLRDN 278
Cdd:COG4886  205 TNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPP-LANLTNLKTLDLSNN 282

                        170       180
                 ....*....|....*....|...
gi 282165682 279 QLRDLPAELLDAPFVRLQGNPLG 301
Cdd:COG4886  283 QLTDLKLKELELLLGLNSLLLLL 305
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
118-284 1.31e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 143.54  E-value: 1.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 118 TLTTLPASMRDLACLAHLDLSFNRLetlptcVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGS 197
Cdd:COG4886   84 LLLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGN 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 198 LSTLQRLDLSENLLDTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLLTSVPPGLAHLPLITRLDLRD 277
Cdd:COG4886  158 LTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSN 237


                 ....*..
gi 282165682 278 NQLRDLP 284
Cdd:COG4886  238 NQLTDLP 244
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 795-880 4.68e-32

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: 119.73  E-value: 4.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 874
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 282165682 875 EVRAIL 880
Cdd:cd08779   81 ELRDKL 86
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
132-287 2.64e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 106.56  E-value: 2.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 132 LAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNllerlpPTLGSLSTLQRLDLSENLL 211
Cdd:COG4886   52 LLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQL 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682 212 DTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLLTSVPPGLAHLPLITRLDLRDNQLRDLPAEL 287
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPL 201
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-289 2.54e-23

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.86  E-value: 2.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 119 LTTLPASMRDLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSL 198
Cdd:COG4886  148 LTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANL 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 199 STLQRLDLSENLLDTIP---------------------SEIGDLSSLRELNLASNRLQHLP----ASLAGLRSLRLLVLH 253
Cdd:COG4886  228 TNLETLDLSNNQLTDLPelgnltnleeldlsnnqltdlPPLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLL 307

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 282165682 254 SNLLTSVPPGLAHLPLITRLDLRDNQLRDLPAELLD 289
Cdd:COG4886  308 LNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALS 343
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 802-877 2.17e-16

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: 74.63  E-value: 2.17e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682 802 VASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAEsQTGQPGAVGHLVQALEQSDRQDVAEEVR 877
Cdd:cd01670    5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWRE-REGDEATLGRLIQALREIGRRDLAEKLE 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
119-271 5.83e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 78.05  E-value: 5.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 119 LTTLPASMRDLACLAHLDLSFNRLETLPTCVLELHSLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLP------ 192
Cdd:COG4886  171 LTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPelgnlt 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 193 ---------------PTLGSLSTLQRLDLSENLLDTIPSEIGDLSSLRELNLASNRLQHLPASLAGLRSLRLLVLHSNLL 257
Cdd:COG4886  251 nleeldlsnnqltdlPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330

                        170
                 ....*....|....
gi 282165682 258 TSVPPGLAHLPLIT 271
Cdd:COG4886  331 KGLLVTLTTLALSL 344
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 129-288 1.03e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 78.74  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 129 LACLAHLDLSFNRLE-TLPTCVLELHSLDALLLSHNCLS-ELPEALGALPTLTFLTVTHN-LLERLPPTLGSLSTLQRLD 205
Cdd:PLN00113 139 IPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIY 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 206 LS-ENLLDTIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVLHSNLLT-SVPPGLAHLPLITRLDLRDNQLRD 282
Cdd:PLN00113 219 LGyNNLSGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSG 298


                 ....*.
gi 282165682 283 LPAELL 288
Cdd:PLN00113 299 EIPELV 304
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 134-300 3.41e-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: 72.51  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 134 HLDLS---FNRLETLPTCvlelHSLDALLLSHNCLSELpEALGALPTLTFLTVTHNLLERLPPtLGSLSTLQRLDLSENL 210
Cdd:cd21340    6 HLYLNdknITKIDNLSLC----KNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 211 LDTIpSEIGDLSSLRELNLASNRLQH------LPASLAGL-RSLRLLVLHSNLLTSVPPgLAHLPLITRLDLRDNQLRDL 283
Cdd:cd21340   80 ISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSLEP-LAPLRNLEQLDASNNQISDL 157

                        170       180
                 ....*....|....*....|....
gi 282165682 284 pAELLDA----PFVR---LQGNPL 300
Cdd:cd21340  158 -EELLDLlsswPSLReldLTGNPV 180
Death pfam00531
Death domain;
799-880 3.89e-14

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 68.55  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682  799 LLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDgQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVRA 878
Cdd:pfam00531   7 LLDPPPPLGKDWRELARKLGLSENEIDEIESENPRLRS-QTYELLRLW-EQREGKNATVGTLLEALRKLGRRDAAEKIQS 84


                  ..
gi 282165682  879 IL 880
Cdd:pfam00531  85 IL 86
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 129-261 5.30e-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: 69.04  E-value: 5.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 129 LACLAHLDLSFNRLETLptCVLE-LHSLDALLLSHNCLSELpEALGALPTLTFLTVTHNlleRLPP---------TLGSL 198
Cdd:cd21340   45 LTNLTHLYLQNNQIEKI--ENLEnLVNLKKLYLGGNRISVV-EGLENLTNLEELHIENQ---RLPPgekltfdprSLAAL 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165682 199 S-TLQRLDLSENLLDTIpSEIGDLSSLRELNLASNRLQHLPA---SLAGLRSLRLLVLHSNLLTSVP 261
Cdd:cd21340  119 SnSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCKKP 184
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
119-287 7.01e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.81  E-value: 7.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 119 LTTLPASMRDlaCLAHLDLSFNRLETLPTCVLElhSLDALLLSHNCLSELPEalgALPtltfltvthnllerlpptlgsl 198
Cdd:PRK15370 232 LTSIPATLPD--TIQEMELSINRITELPERLPS--ALQSLDLFHNKISCLPE---NLP---------------------- 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 199 STLQRLDLSENLLDTIPSEIGdlSSLRELNLASNRLQHLPASLAglRSLRLLVLHSNLLTSVPPGLAhlPLITRLDLRDN 278
Cdd:PRK15370 283 EELRYLSVYDNSIRTLPAHLP--SGITHLNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKN 356


                 ....*....
gi 282165682 279 QLRDLPAEL 287
Cdd:PRK15370 357 QITVLPETL 365
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 122-287 3.30e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 67.57  E-value: 3.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 122 LPASMRDLACLAHLDLSFNRLET-LPTCVLELHSLDALLLSHNCLS-ELPEALGALPTLTFLTVTHNLLE---------- 189
Cdd:PLN00113 372 IPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsrkwdm 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 190 ---------------RLPPTLGSlSTLQRLDLSENLLD-TIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVL 252
Cdd:PLN00113 452 pslqmlslarnkffgGLPDSFGS-KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDL 530

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 282165682 253 -HSNLLTSVPPGLAHLPLITRLDLRDNQLR-DLPAEL 287
Cdd:PLN00113 531 sHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKNL 567
LRR_8 pfam13855
Leucine rich repeat;
222-280 8.22e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.30  E-value: 8.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165682  222 SSLRELNLASNRLQHL-PASLAGLRSLRLLVLHSNLLTSVPPG-LAHLPLITRLDLRDNQL 280
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 428-460 1.23e-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: 57.15  E-value: 1.23e-10
                          10        20        30
                  ....*....|....*....|....*....|....
gi 282165682  428 WNDLETHLEEEAPKRR-WARCQVPHFSWFLVVLR 460
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
LRR_8 pfam13855
Leucine rich repeat;
199-257 3.97e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.38  E-value: 3.97e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165682  199 STLQRLDLSENLLDTIPSEI-GDLSSLRELNLASNRLQHL-PASLAGLRSLRLLVLHSNLL 257
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 122-300 4.67e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.71  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 122 LPASMRDLACLAHLDLSFNRLE-TLPTCVLELHSLDALLLSHNCLS-ELPEALGALPTLTFLTVTHNLLE-RLPPTLGSL 198
Cdd:PLN00113 228 IPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 199 STLQRLDL-SENLLDTIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVLHSNLLTS-VPPGLAHLPLITRLDL 275
Cdd:PLN00113 308 QNLEILHLfSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNNLTGeIPEGLCSSGNLFKLIL 387

                        170       180
                 ....*....|....*....|....*....
gi 282165682 276 RDNQLRD-LPAELLDAPF---VRLQGNPL 300
Cdd:PLN00113 388 FSNSLEGeIPKSLGACRSlrrVRLQDNSF 416
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 160-262 6.45e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 63.33  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 160 LSHNCLS-ELPEALGALP-TLTFLTVTHNLLERLPPTlGSLSTLQRLDLSENLLD-TIPSEIGDLSSLRELNLASNRLQ- 235
Cdd:PLN00113 100 LSNNQLSgPIPDDIFTTSsSLRYLNLSNNNFTGSIPR-GSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVg 178

                         90       100
                 ....*....|....*....|....*..
gi 282165682 236 HLPASLAGLRSLRLLVLHSNLLTSVPP 262
Cdd:PLN00113 179 KIPNSLTNLTSLEFLTLASNQLVGQIP 205
LRR_8 pfam13855
Leucine rich repeat;
176-234 2.31e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 2.31e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165682  176 PTLTFLTVTHNLLERLPP-TLGSLSTLQRLDLSENLLDTI-PSEIGDLSSLRELNLASNRL 234
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 155-244 7.17e-09

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 59.44  E-value: 7.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 155 LDALLLSHNCL-SELPEALGALPTLTFLTVTHNLLE-RLPPTLGSLSTLQRLDLSENLLD-TIPSEIGDLSSLRELNLAS 231
Cdd:PLN03150 420 IDGLGLDNQGLrGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNG 499

                         90
                 ....*....|....
gi 282165682 232 NRLQ-HLPASLAGL 244
Cdd:PLN03150 500 NSLSgRVPAALGGR 513
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 795-872 5.67e-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: 50.73  E-value: 5.67e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAEsQTGQPGAVGHLVQALEQSDRQDV 872
Cdd:cd08317    3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLE-REGEKATGNALESALKKIGRDDI 79
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 806-877 5.80e-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: 50.87  E-value: 5.80e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165682   806 LGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVR 877
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLW-EQREGKNATLGTLLEALRKMGRDDAVELLR 86
PLN03150 PLN03150
hypothetical protein; Provisional
 191-278 8.63e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 55.98  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 191 LPPTLGSLSTLQRLDLSENLLD-TIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVLHSNLLTS-VPPGLAHL 267
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGrVPAALGGR 513

                         90
                 ....*....|..
gi 282165682 268 PLI-TRLDLRDN 278
Cdd:PLN03150 514 LLHrASFNFTDN 525
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 795-868 1.41e-07

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: 49.63  E-value: 1.41e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSD 868
Cdd:cd08319    1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQ-GKKATVQSLIQSLKAVE 73
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 330-403 2.70e-07

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 49.45  E-value: 2.70e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 282165682  330 SFLVTPHGCSVTLA-CGVRLQFPAGATTTPITIHYRLWLP--EPGLVSLGPHDFLLSGVLELQPHGVAFQQNVSLWL 403
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGTRIECYLAVNrdESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
118-291 5.03e-07

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 53.63  E-value: 5.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 118 TLTTLPASMRDLAclahldLSFNRLETLPTCVLELHSLDALllsHNCLSELPealgALPT-LTFLTVTHNLLERLPptlg 196
Cdd:PRK15387 336 SLPTLPSGLQELS------VSDNQLASLPTLPSELYKLWAY---NNRLTSLP----ALPSgLKELIVSGNRLTSLP---- 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 197 slstlqrldlsenlldTIPSEigdlssLRELNLASNRLQHLPASLAGLRSLRllvLHSNLLTSVPPGLAHLPLITRLDLR 276
Cdd:PRK15387 399 ----------------VLPSE------LKELMVSGNRLTSLPMLPSGLLSLS---VYRNQLTRLPESLIHLSSETTVNLE 453

                        170
                 ....*....|....*....
gi 282165682 277 DNQL--RDLPA--ELLDAP 291
Cdd:PRK15387 454 GNPLseRTLQAlrEITSAP 472
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 132-295 7.47e-07

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: 51.97  E-value: 7.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 132 LAHLDLSFNRLETLPT----CVLE--LHSLDALLLSHNCLS-----ELPEALGALPTLTFLTVTHN-----LLERLPPTL 195
Cdd:cd00116  110 LQELKLNNNGLGDRGLrllaKGLKdlPPALEKLVLGRNRLEgasceALAKALRANRDLKELNLANNgigdaGIRALAEGL 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 196 GSLSTLQRLDLSENLLDtiPSEIGDLS-------SLRELNLASNRL-----QHL-PASLAGLRSLRLLVLHSNLLT---- 258
Cdd:cd00116  190 KANCNLEVLDLNNNGLT--DEGASALAetlaslkSLEVLNLGDNNLtdagaAALaSALLSPNISLLTLSLSCNDITddga 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 282165682 259 -SVPPGLAHLPLITRLDLRDNQL----RDLPAELLDAPFVRL 295
Cdd:cd00116  268 kDLAEVLAEKESLLELDLRGNKFgeegAQLLAESLLEPGNEL 309
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 812-881 1.37e-06

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: 47.29  E-value: 1.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 812 TVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSDRQDVAEEVRAILE 881
Cdd:cd08316   22 KFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKH-GKKGAYRTLIKTLRKAGKRAKADKIQDIIK 90
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 110-290 4.49e-06

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: 49.66  E-value: 4.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 110 ALGACLHGtlttlpasMRDLACLAHLDLSFNRL-----ETLPTCvLELHSLDALLLSHNCLSELPEAL--GAL----PTL 178
Cdd:cd00116   69 GLQSLLQG--------LTKGCGLQELDLSDNALgpdgcGVLESL-LRSSSLQELKLNNNGLGDRGLRLlaKGLkdlpPAL 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 179 TFLTVTHNLLERlpptlgslstlqrlDLSENLLDTIPSeigdLSSLRELNLASNRL-----QHLPASLAGLRSLRLLVLH 253
Cdd:cd00116  140 EKLVLGRNRLEG--------------ASCEALAKALRA----NRDLKELNLANNGIgdagiRALAEGLKANCNLEVLDLN 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 282165682 254 SNLLTS-----VPPGLAHLPLITRLDLRDNQLRDLP-AELLDA 290
Cdd:cd00116  202 NNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAGaAALASA 244
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
118-292 8.02e-06

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 49.70  E-value: 8.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 118 TLTTLPASMRdlACLAHLDLSFNRLETLPTCVL-ELHSLDallLSHNCLSELPEALGalPTLTFLTVTHNLLERLPPTLG 196
Cdd:PRK15370 315 SLTALPETLP--PGLKTLEAGENALTSLPASLPpELQVLD---VSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 197 slSTLQRLDLSENLLDTIPSEIGDLSS--------LRELNLASNR----LQHLPASLA--GLRSLRLLVLHSNLLTSVPP 262
Cdd:PRK15370 388 --AALQIMQASRNNLVRLPESLPHFRGegpqptriIVEYNPFSERtiqnMQRLMSSVGyqGPRVLFAMGDFSIVRVTRPL 465

                        170       180       190
                 ....*....|....*....|....*....|.
gi 282165682 263 GLAHLPLITRLDLRD-NQLRDLPAELLDAPF 292
Cdd:PRK15370 466 HQAVQGWLTNLEEEDvNQWRAFETEVNAAAF 496
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 121-216 1.19e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 49.46  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 121 TLPASMRDLACLAHLDLSFNRL-----ETLPTCVlELHSLDallLSHNCLS-ELPEALGALPTLTFLTVTHNLLE-RLPP 193
Cdd:PLN00113 490 AVPRKLGSLSELMQLKLSENKLsgeipDELSSCK-KLVSLD---LSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPK 565

                         90       100
                 ....*....|....*....|....
gi 282165682 194 TLGSLSTLQRLDLSENLLD-TIPS 216
Cdd:PLN00113 566 NLGNVESLVQVNISHNHLHgSLPS 589
LRR_8 pfam13855
Leucine rich repeat;
132-188 1.23e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 1.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 282165682  132 LAHLDLSFNRLETLPTCVLE-LHSLDALLLSHNCLSEL-PEALGALPTLTFLTVTHNLL 188
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 471-544 1.82e-05

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 44.06  E-value: 1.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682  471 EGALLCSSgHPGVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLsqsGPP--SFLQPVTVQLP 544
Cdd:pfam00791   8 RGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
165-285 3.31e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 47.85  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 165 LSELPEALGAlpTLTFLTVTHNLLERLPPTLGSLSTLQrldLSENLLDTIPSEIgdlSSLRELNLASNRLQHLPASLAGL 244
Cdd:PRK15387 213 LTTLPDCLPA--HITTLVIPDNNLTSLPALPPELRTLE---VSGNQLTSLPVLP---PGLLELSIFSNPLTHLPALPSGL 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 282165682 245 RSLRLLVLHSNLLTSVPPGLahlpliTRLDLRDNQLRDLPA 285
Cdd:PRK15387 285 CKLWIFGNQLTSLPVLPPGL------QELSVSDNQLASLPA 319
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 794-876 3.53e-05

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: 43.28  E-value: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 794 LTQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEfRDDLDGQIRHMLFSWAEsQTGQPGAVGHLVQALEQSDRQDVA 873
Cdd:cd08318    5 VTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESD-SEDMKMRAKQLLVTWQD-REGAQATPEILMTALNAAGLNEIA 82


                 ...
gi 282165682 874 EEV 876
Cdd:cd08318   83 ENL 85
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
119-302 4.27e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 47.46  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 119 LTTLPASMRDLACLahlDLSFNRLETLPtcVLELHSLDALLLShNCLSELPEALGALPTLTFLTVTHNLLERLPPTLgsl 198
Cdd:PRK15387 234 LTSLPALPPELRTL---EVSGNQLTSLP--VLPPGLLELSIFS-NPLTHLPALPSGLCKLWIFGNQLTSLPVLPPGL--- 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 199 stlQRLDLSENLLDTIPSEIGDL-----------------SSLRELNLASNRLQHLP----------------ASLAGLR 245
Cdd:PRK15387 305 ---QELSVSDNQLASLPALPSELcklwaynnqltslptlpSGLQELSVSDNQLASLPtlpselyklwaynnrlTSLPALP 381

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165682 246 S-LRLLVLHSNLLTSVP--PG-----------LAHLPLIT----RLDLRDNQLRDLPAELL---DAPFVRLQGNPLGE 302
Cdd:PRK15387 382 SgLKELIVSGNRLTSLPvlPSelkelmvsgnrLTSLPMLPsgllSLSVYRNQLTRLPESLIhlsSETTVNLEGNPLSE 459
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 123-186 6.64e-05

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: 45.16  E-value: 6.64e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 282165682 123 PASMRDLA-CLAHLDLSFNRLETLpTCVLELHSLDALLLSHNCLS---ELPEALGALPTLTFLTVTHN 186
Cdd:cd21340  112 PRSLAALSnSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISdleELLDLLSSWPSLRELDLTGN 178
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 482-544 1.42e-04

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 41.95  E-value: 1.42e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 282165682   482 GVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLSQSGpPSFLQPVTVQLP 544
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 795-872 1.49e-04

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: 41.26  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282165682 795 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEF-RDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDV 872
Cdd:cd08777    1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYeRDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDL 79
PLN03150 PLN03150
hypothetical protein; Provisional
 208-287 1.64e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 45.58  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 208 ENLLDTIPSEIGDLSSLRELNLASNRLQ-HLPASLAGLRSLRLLVLHSNLLT-SVPPGLAHLPLITRLDLRDNQLR-DLP 284
Cdd:PLN03150 428 QGLRGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVP 507


                 ...
gi 282165682 285 AEL 287
Cdd:PLN03150 508 AAL 510
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 151-300 2.30e-04

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: 44.78  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 151 ELHSLDALLLSHNCLS-----ELPEALGALPTLTFLTVTHNLL-----ERLPPTLGSLSTLQRLDLSENlldtipsEIGD 220
Cdd:COG5238  234 GNKSLTTLDLSNNQIGdegviALAEALKNNTTVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVN-------RIGD 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 221 ------------LSSLRELNLASNRL-----QHLPASLAGLRSLRLLVLHSNLLT-SVPPGLAHL----PLITRLDLRDN 278
Cdd:COG5238  307 egaialaeglqgNKTLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDNQIGdEGAIALAKYlegnTTLRELNLGKN 386

                        170       180
                 ....*....|....*....|...
gi 282165682 279 QLRDLPAE-LLDApfvrLQGNPL 300
Cdd:COG5238  387 NIGKQGAEaLIDA----LQTNRL 405
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
154-287 8.41e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 154 SLDALLLSHNCLSELPEALGALPTLTFLTVTHNLLERLPPTLGSLSTLQRLDLSENLLDTIPSEIGDLSSLRELNLASNR 233
Cdd:COG4886    5 LLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSL 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 282165682 234 LQHLPASLAGLRSLRLLVLHSNlltsvpPGLAHLPLITRLDLRDNQLRDLPAEL 287
Cdd:COG4886   85 LLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEEL 132
PLN03150 PLN03150
hypothetical protein; Provisional
 122-176 9.39e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.88  E-value: 9.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 282165682 122 LPASMRDLACLAHLDLSFNRLE-TLPTCVLELHSLDALLLSHNCLS-ELPEALGALP 176
Cdd:PLN03150 458 IPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGGRL 514
LRR_8 pfam13855
Leucine rich repeat;
245-300 1.84e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.50  E-value: 1.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 282165682  245 RSLRLLVLHSNLLTSVPPG-LAHLPLITRLDLRDNQLRDLPAELLDAP----FVRLQGNPL 300
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLpslrYLDLSGNRL 61
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 132-258 3.93e-03

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: 40.54  E-value: 3.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682 132 LAHLDLSFNRL-----ETLPTCVLELHSLDALLLSHNCLSE-----LPEALGALPTLTFLTVTHNLL-----ERLPPTLG 196
Cdd:COG5238  266 VETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIGDegaiaLAEGLQGNKTLHTLNLAYNGIgaqgaIALAKALQ 345

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 282165682 197 SLSTLQRLDLSENlldtipsEIGDLS------------SLRELNLASNRL-----QHLPASLAGLRsLRLLVLHSNLLT 258
Cdd:COG5238  346 ENTTLHSLDLSDN-------QIGDEGaialakylegntTLRELNLGKNNIgkqgaEALIDALQTNR-LHTLILDGNLIG 416
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 132-194 5.05e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.60  E-value: 5.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682 132 LAHLDLSFNRLE-TLPTCVLELHSLDALLLSHNCLS-ELPEALGALPTLTFLTVTHNLLE-RLPPT 194
Cdd:PLN00113 525 LVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLPST 590
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 799-874 5.62e-03

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. 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: 260025  Cd Length: 80  Bit Score: 36.50  E-value: 5.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 282165682 799 LLSvASRLGSDWPTVALHLGmpYRKlQRIRHeFRDDLDgQIRHMLFSWAESQTGqpgAVGHLVQALEQSDRQDVAE 874
Cdd:cd08311   11 LLN-AGREGSDWRALAGELG--YSA-EEIDS-FAREAD-PCRALLTDWSAQDGA---TLGVLLTALRKIGRDDIVE 77
PLN03210 PLN03210
Resistant to P. syringae 6; Provisional
 118-240 6.31e-03

Resistant to P. syringae 6; Provisional


Pssm-ID: 215633 [Multi-domain]  Cd Length: 1153  Bit Score: 40.63  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 282165682  118 TLTTLPASMRDLACLAHLDLSFNR-LETLPTCVlELHSLDALLLSH---------------------NCLSELPEALGAL 175
Cdd:PLN03210  790 SLVELPSSIQNLHKLEHLEIENCInLETLPTGI-NLESLESLDLSGcsrlrtfpdistnisdlnlsrTGIEEVPWWIEKF 868

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 282165682  176 PTLTFLTVTH-NLLERLPPTLGSLSTLQRLD------LSENLLDTIPSEIGdlsslrelNLASNRLQHLPAS 240
Cdd:PLN03210  869 SNLSFLDMNGcNNLQRVSLNISKLKHLETVDfsdcgaLTEASWNGSPSEVA--------MATDNIHSKLPST 932
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 806-880 7.87e-03

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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 they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 36.50  E-value: 7.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 282165682 806 LGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSDRQDVAEEVRAIL 880
Cdd:cd08306   12 LGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIK-KAEATVADLIKALRDCQLNLVADLVEKKL 85
 
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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