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Conserved domains on  [gi|767966149|ref|XP_011518514|]
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p53-induced death domain-containing protein 1 isoform X5 [Homo sapiens]

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];
1-149 7.73e-38

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 146.62  E-value: 7.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLAS 80
Cdd:COG4886  135 LTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSG 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149  81 NRLQSLPASLAGLRSLRLLVLHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPE--LLDAPFVRLQGNPL 149
Cdd:COG4886  215 NQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLanLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 666-751 1.92e-35

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: 128.97  E-value: 1.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 745
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966149 746 EVRAVL 751
Cdd:cd08779   81 ELRDKL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 275-307 1.21e-11

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: 59.47  E-value: 1.21e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966149  275 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 307
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.
 179-270 5.23e-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: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  179 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 255
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966149  256 PPQARRCREVVVRTR 270
Cdd:pfam00791  82 ASLRPEEWEIVLKRS 96
ZU5 super family cl02517
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 319-391 9.28e-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: 47.52  E-value: 9.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  319 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 391
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-149 7.73e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 146.62  E-value: 7.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLAS 80
Cdd:COG4886  135 LTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSG 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149  81 NRLQSLPASLAGLRSLRLLVLHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPE--LLDAPFVRLQGNPL 149
Cdd:COG4886  215 NQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLanLTNLKTLDLSNNQL 284
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 666-751 1.92e-35

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: 128.97  E-value: 1.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 745
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966149 746 EVRAVL 751
Cdd:cd08779   81 ELRDKL 86
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 1-129 3.10e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 76.81  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLL-DTLPPEIGGLGSLLELN 77
Cdd:PLN00113 211 MKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIFSLQKLISLD 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767966149  78 LASNRLQ-SLPASLAGLRSLRLLVLHSN-LLASVPADLARLPLLTRLDLRDNQL 129
Cdd:PLN00113 291 LSDNSLSgEIPELVIQLQNLEILHLFSNnFTGKIPVALTSLPRLQVLQLWSNKF 344
Death pfam00531
Death domain;
677-751 6.06e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 65.08  E-value: 6.06e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  677 LGLDWPAVALHLGVSYREVQRIRHEFRdDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 751
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 12-149 1.84e-12

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: 67.50  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  12 NCLSELpEALGALPALTFLTVTHNRLQTLPPaLGALSTLQRLDLSQNLLDTLppE-IGGLGSLLELNLASNRL---QSL- 86
Cdd:cd21340   34 NKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIENQRLppgEKLt 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966149  87 --PASLAGL-RSLRLLVLHSNLLASVpADLARLPLLTRLDLRDNQLRDLpPELLDA----PFVR---LQGNPL 149
Cdd:cd21340  110 fdPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDL-EELLDLlsswPSLReldLTGNPV 180
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 275-307 1.21e-11

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: 59.47  E-value: 1.21e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966149  275 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 307
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
LRR_8 pfam13855
Leucine rich repeat;
48-106 7.40e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.30  E-value: 7.40e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149   48 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 106
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 673-748 1.35e-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: 52.80  E-value: 1.35e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149   673 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 748
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 179-270 5.23e-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: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  179 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 255
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966149  256 PPQARRCREVVVRTR 270
Cdd:pfam00791  82 ASLRPEEWEIVLKRS 96
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 319-391 9.28e-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: 47.52  E-value: 9.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  319 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 391
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 329-391 3.88e-05

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 43.11  E-value: 3.88e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966149   329 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLQPVTVQLP 391
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 194-244 4.82e-03

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 37.33  E-value: 4.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767966149   194 GVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAF 244
Cdd:smart00218  22 GVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALF 74
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-149 7.73e-38

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 146.62  E-value: 7.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLAS 80
Cdd:COG4886  135 LTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSG 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149  81 NRLQSLPASLAGLRSLRLLVLHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPE--LLDAPFVRLQGNPL 149
Cdd:COG4886  215 NQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPLanLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-156 2.59e-36

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 141.99  E-value: 2.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   4 LGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRL 83
Cdd:COG4886  115 LESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQI 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149  84 QSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLpPELLDAP---FVRLQGNPLGEASPDA 156
Cdd:COG4886  195 TDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDL-PELGNLTnleELDLSNNQLTDLPPLA 269
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 666-751 1.92e-35

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: 128.97  E-value: 1.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 745
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966149 746 EVRAVL 751
Cdd:cd08779   81 ELRDKL 86
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-153 1.38e-32

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 131.21  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   7 LLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSL 86
Cdd:COG4886  164 LDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDL 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966149  87 PaSLAGLRSLRLLVLHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEAS 153
Cdd:COG4886  244 P-ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLL 308
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-136 1.15e-31

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 128.51  E-value: 1.15e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNclselpEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLAS 80
Cdd:COG4886   95 LTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSN 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149  81 NRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPEL 136
Cdd:COG4886  169 NQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPL 224
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 673-748 2.39e-18

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: 80.02  E-value: 2.39e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149 673 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 748
Cdd:cd01670    5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWRERE-GDEATLGRLIQALREIGRRDLAEKLE 79
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
14-154 5.12e-18

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 87.30  E-value: 5.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  14 LSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNlldtlpPEIGGLGSLLELNLASNRLQSLPASLAGL 93
Cdd:COG4886   62 LSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANL 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966149  94 RSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVR---LQGNPLGEASP 154
Cdd:COG4886  136 TNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKeldLSNNQITDLPE 199
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1-157 1.94e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 85.37  E-value: 1.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPpALGALSTLQRLDLSQNLLDTLPPEiGGLGSLLELNLAS 80
Cdd:COG4886  204 LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSN 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  81 NRLQSLP----ASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDA 156
Cdd:COG4886  282 NQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSL 361


                 .
gi 767966149 157 P 157
Cdd:COG4886  362 L 362
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 1-129 3.10e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 76.81  E-value: 3.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   1 MRGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLL-DTLPPEIGGLGSLLELN 77
Cdd:PLN00113 211 MKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLsGPIPPSIFSLQKLISLD 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 767966149  78 LASNRLQ-SLPASLAGLRSLRLLVLHSN-LLASVPADLARLPLLTRLDLRDNQL 129
Cdd:PLN00113 291 LSDNSLSgEIPELVIQLQNLEILHLFSNnFTGKIPVALTSLPRLQVLQLWSNKF 344
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
9-136 2.02e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.96  E-value: 2.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   9 LSHNCLSELPEALGAlpALTFLTVTHNRLQTLPPALGalSTLQRLDLSQNLLDTLPPEIGGlgSLLELNLASNRLQSLPA 88
Cdd:PRK15370 248 LSINRITELPERLPS--ALQSLDLFHNKISCLPENLP--EELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPE 321

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767966149  89 SLAglRSLRLLVLHSNLLASVPADLArlPLLTRLDLRDNQLRDLPPEL 136
Cdd:PRK15370 322 TLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETL 365
Death pfam00531
Death domain;
677-751 6.06e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 65.08  E-value: 6.06e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  677 LGLDWPAVALHLGVSYREVQRIRHEFRdDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 751
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 12-149 1.84e-12

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: 67.50  E-value: 1.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  12 NCLSELpEALGALPALTFLTVTHNRLQTLPPaLGALSTLQRLDLSQNLLDTLppE-IGGLGSLLELNLASNRL---QSL- 86
Cdd:cd21340   34 NKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRISVV--EgLENLTNLEELHIENQRLppgEKLt 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966149  87 --PASLAGL-RSLRLLVLHSNLLASVpADLARLPLLTRLDLRDNQLRDLpPELLDA----PFVR---LQGNPL 149
Cdd:cd21340  110 fdPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDL-EELLDLlsswPSLReldLTGNPV 180
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 8-129 5.57e-12

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 69.49  E-value: 5.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   8 LLSHNCLSELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQN-LLDTLPPEIGGLGSLLELNLASNRLQS 85
Cdd:PLN00113 315 LFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNnLTGEIPEGLCSSGNLFKLILFSNSLEG 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767966149  86 -LPASLAGLRSLRLLVLHSNLLA-SVPADLARLPLLTRLDLRDNQL 129
Cdd:PLN00113 395 eIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNL 440
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 275-307 1.21e-11

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: 59.47  E-value: 1.21e-11
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966149  275 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 307
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-149 4.89e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.73  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   4 LGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRl 83
Cdd:COG4886   29 LLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE- 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966149  84 qslpaSLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAP---FVRLQGNPL 149
Cdd:COG4886  108 -----ELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTnlkSLDLSNNQL 171
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 2-136 6.30e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 66.02  E-value: 6.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   2 RGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-------------------------TLPPALGAlSTLQRLDL 55
Cdd:PLN00113 404 RSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsrkwdmpslqmlslarnkffgGLPDSFGS-KRLENLDL 482

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  56 SQNLLD-TLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLRLLVL-HSNLLASVPADLARLPLLTRLDLRDNQLR-D 131
Cdd:PLN00113 483 SRNQFSgAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDLsHNQLSGQIPASFSEMPVLSQLDLSQNQLSgE 562


                 ....*
gi 767966149 132 LPPEL 136
Cdd:PLN00113 563 IPKNL 567
LRR_8 pfam13855
Leucine rich repeat;
48-106 7.40e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 58.30  E-value: 7.40e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149   48 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 106
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 666-743 1.18e-10

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: 58.43  E-value: 1.18e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQP-GAVglLVQALEQSDRQDV 743
Cdd:cd08317    3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKAtGNA--LESALKKIGRDDI 79
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-136 1.85e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.48  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   7 LLLSHNCLSElPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQN-LLDTLPPEIGGLGSLLELNLASNRLQ 84
Cdd:PLN00113 123 LNLSNNNFTG-SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNvLVGKIPNSLTNLTSLEFLTLASNQLV 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  85 -SLPASLAGLRSLRLLVL-HSNLLASVPADLARLPLLTRLDLRDNQLR-DLPPEL 136
Cdd:PLN00113 202 gQIPRELGQMKSLKWIYLgYNNLSGEIPYEIGGLTSLNHLDLVYNNLTgPIPSSL 256
LRR_8 pfam13855
Leucine rich repeat;
25-83 1.08e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.84  E-value: 1.08e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149   25 PALTFLTVTHNRLQTLPP-ALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRL 83
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 3-138 2.79e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 60.63  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   3 GLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQN-LLDTLPPEIGGLGSLLELNLA 79
Cdd:PLN00113 141 NLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNqLVGQIPRELGQMKSLKWIYLG 220

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966149  80 SNRLQ-SLPASLAGLRSLRLLVL-HSNLLASVPADLARLPLLTRLDLRDNQLRD-LPPELLD 138
Cdd:PLN00113 221 YNNLSgEIPYEIGGLTSLNHLDLvYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGpIPPSIFS 282
LRR_8 pfam13855
Leucine rich repeat;
72-129 1.30e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 51.76  E-value: 1.30e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   72 SLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLLASV-PADLARLPLLTRLDLRDNQL 129
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 673-748 1.35e-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: 52.80  E-value: 1.35e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149   673 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 748
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
3-116 2.46e-08

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 57.78  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   3 GLGALLLSHNCLSELPEALGalPALTFLTVTHNRLQTLPPALGalSTLQRLDLSQNLLDTLPPEIGglGSLLELNLASNR 82
Cdd:PRK15370 326 GLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNALTNLPENLP--AALQIMQASRNN 399

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 767966149  83 LQSLPASLAGLRS-----LRLLVLHSNLLASVPADLARL 116
Cdd:PRK15370 400 LVRLPESLPHFRGegpqpTRIIVEYNPFSERTIQNMQRL 438
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 666-739 3.12e-08

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: 51.56  E-value: 3.12e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSD 739
Cdd:cd08319    1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQ-GKKATVQSLIQSLKAVE 73
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 179-270 5.23e-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: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  179 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 255
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966149  256 PPQARRCREVVVRTR 270
Cdd:pfam00791  82 ASLRPEEWEIVLKRS 96
PLN03150 PLN03150
hypothetical protein; Provisional
 40-127 5.48e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.36  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  40 LPPALGALSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSNLLAS-VPADLARL 116
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGrVPAALGGR 513

                         90
                 ....*....|..
gi 767966149 117 PLL-TRLDLRDN 127
Cdd:PLN03150 514 LLHrASFNFTDN 525
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 666-743 9.65e-08

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: 50.12  E-value: 9.65e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966149 666 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEF-RDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDV 743
Cdd:cd08777    1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYeRDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDL 79
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 319-391 9.28e-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: 47.52  E-value: 9.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  319 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 391
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
PLN03150 PLN03150
hypothetical protein; Provisional
 17-93 1.43e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 51.74  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  17 LPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRLQS-LPASLAGL 93
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNGSIPEsLGQLTSLRILNLNGNSLSGrVPAALGGR 513
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 7-93 1.80e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.77  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   7 LLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRL 83
Cdd:PLN00113 504 LKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSEMPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHL 583

                         90
                 ....*....|.
gi 767966149  84 Q-SLPASLAGL 93
Cdd:PLN00113 584 HgSLPSTGAFL 594
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
3-197 8.54e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 49.39  E-value: 8.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   3 GLGALLLSHNCLSELPEALGAlpALTFLTVTHNRLQTLPPALGALSTLQrldLSQNLLDTLPPEIGGLgslLELNLASNR 82
Cdd:PRK15387 202 GNAVLNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLPALPPELRTLE---VSGNQLTSLPVLPPGL---LELSIFSNP 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  83 LQSLPASLAGLRSLRLLvlhSNLLASVPadlARLPLLTRLDLRDNQLRDLP--PELL------DAPFVRLQGNPLGEASP 154
Cdd:PRK15387 274 LTHLPALPSGLCKLWIF---GNQLTSLP---VLPPGLQELSVSDNQLASLPalPSELcklwayNNQLTSLPTLPSGLQEL 347

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 767966149 155 DAPSSPVAALiPEMP----RLFLTSD-LDSFPVTPQGCSVTLACGVRL 197
Cdd:PRK15387 348 SVSDNQLASL-PTLPselyKLWAYNNrLTSLPALPSGLKELIVSGNRL 394
PLN03150 PLN03150
hypothetical protein; Provisional
 1-70 2.62e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 47.89  E-value: 2.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966149   1 MRGLGALLLSHNCL-SELPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLLD-TLPPEIGGL 70
Cdd:PLN03150 441 LRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSgRVPAALGGR 513
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 684-752 3.19e-05

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: 43.05  E-value: 3.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966149 684 VALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVLE 752
Cdd:cd08316   23 FARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKH-GKKGAYRTLIKTLRKAGKRAKADKIQDIIK 90
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 665-747 3.32e-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: 42.89  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149 665 LTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEfRDDLDEQIRHMLFSWAERQAGQpGAVGLLVQALEQSDRQDVA 744
Cdd:cd08318    5 VTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESD-SEDMKMRAKQLLVTWQDREGAQ-ATPEILMTALNAAGLNEIA 82


                 ...
gi 767966149 745 EEV 747
Cdd:cd08318   83 ENL 85
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 329-391 3.88e-05

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 43.11  E-value: 3.88e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966149   329 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLQPVTVQLP 391
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-136 5.16e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 46.76  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   4 LGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQT-LPPALGALSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLAS 80
Cdd:PLN00113 358 LTVLDLSTNNLTgEIPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISN 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  81 NRLQ-------------------------SLPASLaGLRSLRLLVLHSNLLA-SVPADLARLPLLTRLDLRDNQLR-DLP 133
Cdd:PLN00113 438 NNLQgrinsrkwdmpslqmlslarnkffgGLPDSF-GSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSgEIP 516


                 ...
gi 767966149 134 PEL 136
Cdd:PLN00113 517 DEL 519
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
3-131 1.57e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 45.15  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   3 GLGALLLSHNCLSELPealgALPA-LTFLTVTHNRLQTLPpalGALSTLQRLDLSQNLLDTLP--PEigglgSLLELNLA 79
Cdd:PRK15387 343 GLQELSVSDNQLASLP----TLPSeLYKLWAYNNRLTSLP---ALPSGLKELIVSGNRLTSLPvlPS-----ELKELMVS 410

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767966149  80 SNRLQSLPASLAGLRSLRllvLHSNLLASVPADLARLPLLTRLDLRDNQLRD 131
Cdd:PRK15387 411 GNRLTSLPMLPSGLLSLS---VYRNQLTRLPESLIHLSSETTVNLEGNPLSE 459
PLN03150 PLN03150
hypothetical protein; Provisional
 57-129 1.90e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.81  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966149  57 QNLLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSNLL-ASVPADLARLPLLTRLDLRDNQL 129
Cdd:PLN03150 428 QGLRGFIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFnGSIPESLGQLTSLRILNLNGNSL 502
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 673-744 2.13e-04

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. 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. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. 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: 260067  Cd Length: 84  Bit Score: 40.73  E-value: 2.13e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966149 673 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVA 744
Cdd:cd08805   10 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDRE-GENAKMEPLYPALYSIDRLTIV 80
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
7-136 2.39e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   7 LLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSL 86
Cdd:COG4886    9 TLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLG 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966149  87 PASLAGLRSLRLLVLHSNllasvpADLARLPLLTRLDLRDNQLRDLPPEL 136
Cdd:COG4886   89 LTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEEL 132
LRR_8 pfam13855
Leucine rich repeat;
94-149 4.56e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 4.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966149   94 RSLRLLVLHSNLLASVPAD-LARLPLLTRLDLRDNQLRDLPPELLDAP----FVRLQGNPL 149
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLpslrYLDLSGNRL 61
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 673-751 5.48e-04

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: 39.59  E-value: 5.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966149 673 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 751
Cdd:cd08306    8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIK-KAEATVADLIKALRDCQLNLVADLVEKKL 85
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 7-172 8.59e-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: 42.47  E-value: 8.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149   7 LLLSHNC-----LSELPEALGALPALTFLTVTHNRL-----QTLPPALGALSTLQRLDLSQNLLD-----TLPPEIGGLG 71
Cdd:COG5238  241 LDLSNNQigdegVIALAEALKNNTTVETLYLSGNQIgaegaIALAKALQGNTTLTSLDLSVNRIGdegaiALAEGLQGNK 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966149  72 SLLELNLASNRL-----QSLPASLAGLRSLRLLVLHSNLLASVPAD-----LARLPLLTRLDLRDNQLRDLPPE-LLDA- 139
Cdd:COG5238  321 TLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDNQIGDEGAIalakyLEGNTTLRELNLGKNNIGKQGAEaLIDAl 400

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767966149 140 -----PFVRLQGNPLGEASPDApsspVAALIPEMPRLF 172
Cdd:COG5238  401 qtnrlHTLILDGNLIGAEAQQR----LEQLLERIKSVY 434
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 681-748 1.50e-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: 38.14  E-value: 1.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767966149 681 WPAVALHLGVSYREVQRIRHEFRDDLDEQIRhMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVR 748
Cdd:cd08313   14 WKEFVRRLGLSDNEIERVELDHRRCRDAQYQ-MLKVWKERGPRPYATLQHLLSVLRDMELVGCAEDIE 80
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 670-745 1.70e-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: 38.04  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966149 670 LLSvAGRLGLDWPAVALHLGvsYREvQRIRHeFRDDLDEqIRHMLFSWAERQAGqpgAVGLLVQALEQSDRQDVAE 745
Cdd:cd08311   11 LLN-AGREGSDWRALAGELG--YSA-EEIDS-FAREADP-CRALLTDWSAQDGA---TLGVLLTALRKIGRDDIVE 77
LRR_8 pfam13855
Leucine rich repeat;
1-37 4.02e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 36.35  E-value: 4.02e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 767966149    1 MRGLGALLLSHNCLSEL-PEALGALPALTFLTVTHNRL 37
Cdd:pfam13855  24 LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 194-244 4.82e-03

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 37.33  E-value: 4.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767966149   194 GVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAF 244
Cdd:smart00218  22 GVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALF 74
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 667-743 5.09e-03

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. 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. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066  Cd Length: 84  Bit Score: 36.60  E-value: 5.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966149 667 QSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDV 743
Cdd:cd08804    4 EERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERD-GKHATDTNLTQCLTKINRMDI 79
 
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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