NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767966144|ref|XP_011518512|]
View 

p53-induced death domain-containing protein 1 isoform X4 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-296 1.23e-41

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  87 QSLSCLRSLVLKGGQrrdtlgaclrgaLTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEA 166
Cdd:COG4886  110 SNLTNLESLDLSGNQ------------LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 167 LGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPaSLAGLRSLRLLV 246
Cdd:COG4886  178 LGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELD 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966144 247 LHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLG 296
Cdd:COG4886  257 LSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLL 305
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 788-873 4.39e-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: 128.20  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 867
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966144 868 EVRAVL 873
Cdd:cd08779   81 ELRDKL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 7.16e-12

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: 60.62  E-value: 7.16e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966144  421 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
ZU5 super family cl02517
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-416 5.58e-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: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  325 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 401
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966144  402 PPQARRCREVVVRTR 416
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.
 465-537 9.07e-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: 47.91  E-value: 9.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144  465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-296 1.23e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  87 QSLSCLRSLVLKGGQrrdtlgaclrgaLTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEA 166
Cdd:COG4886  110 SNLTNLESLDLSGNQ------------LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 167 LGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPaSLAGLRSLRLLV 246
Cdd:COG4886  178 LGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELD 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966144 247 LHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLG 296
Cdd:COG4886  257 LSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLL 305
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 788-873 4.39e-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: 128.20  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 867
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966144 868 EVRAVL 873
Cdd:cd08779   81 ELRDKL 86
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 1.84e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 87.60  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLQMRGLGAL-LLSHNCLSELPEALGALPALTFLTVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113 276 IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKH 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 194 STLQRLDLSQN-LLDTLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLRLLVLHSNLLA-SVPADLARLPLLTRLDL 270
Cdd:PLN00113 356 NNLTVLDLSTNnLTGEIPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDI 435


                 ....*
gi 767966144 271 RDNQL 275
Cdd:PLN00113 436 SNNNL 440
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-273 5.47e-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: 72.13  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 114 LTNLPaGLSGLAHLAHLDLSFNSLETlpacvlqMRGLGALL------LSHNCLSELpEALGALPALTFLTVTHnrlQTLP 187
Cdd:cd21340   36 ITKIE-NLEFLTNLTHLYLQNNQIEK-------IENLENLVnlkklyLGGNRISVV-EGLENLTNLEELHIEN---QRLP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 188 PAlgalstlQRLDLSQNLLDTLppeiggLGSLLELNLASNRLQSLpASLAGLRSLRLLVLHSNLLASVPA---DLARLPL 264
Cdd:cd21340  104 PG-------EKLTFDPRSLAAL------SNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPS 169


                 ....*....
gi 767966144 265 LTRLDLRDN 273
Cdd:cd21340  170 LRELDLTGN 178
Death pfam00531
Death domain;
799-873 1.12e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 64.31  E-value: 1.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144  799 LGLDWPAVALHLGVSYREVQRIRHEFRdDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 873
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 7.16e-12

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: 60.62  E-value: 7.16e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966144  421 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
LRR_8 pfam13855
Leucine rich repeat;
194-252 2.28e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 2.28e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966144  194 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 252
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 795-870 2.39e-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: 52.03  E-value: 2.39e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966144   795 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 870
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-416 5.58e-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: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  325 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 401
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966144  402 PPQARRCREVVVRTR 416
Cdd:pfam00791  82 ASLRPEEWEIVLKRS 96
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 465-537 9.07e-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: 47.91  E-value: 9.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144  465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 475-537 3.87e-05

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 43.49  E-value: 3.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966144   475 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLQPVTVQLP 537
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 340-390 4.72e-03

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 37.72  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767966144   340 GVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAF 390
Cdd:smart00218  22 GVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALF 74
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
87-296 1.23e-41

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 158.17  E-value: 1.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  87 QSLSCLRSLVLKGGQrrdtlgaclrgaLTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEA 166
Cdd:COG4886  110 SNLTNLESLDLSGNQ------------LTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 167 LGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPaSLAGLRSLRLLV 246
Cdd:COG4886  178 LGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELD 256

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966144 247 LHSNLLASVPaDLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLG 296
Cdd:COG4886  257 LSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLL 305
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
104-302 1.23e-37

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 146.23  E-value: 1.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 104 DTLGACLRGALTNLPAGLSGLAHLAHLDLSFNSLetlpacVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRL 183
Cdd:COG4886   75 LLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEE------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 184 QTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLP 263
Cdd:COG4886  149 TDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLT 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767966144 264 LLTRLDLRDNQLRDLpPELLDAP---FVRLQGNPLGEASPDA 302
Cdd:COG4886  229 NLETLDLSNNQLTDL-PELGNLTnleELDLSNNQLTDLPPLA 269
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 788-873 4.39e-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: 128.20  E-value: 4.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAE 867
Cdd:cd08779    1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80


                 ....*.
gi 767966144 868 EVRAVL 873
Cdd:cd08779   81 ELRDKL 86
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
78-303 2.81e-27

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 115.80  E-value: 2.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  78 LEATLAQLPQslscLRSLVLKGGQrrdtlgaclrgaLTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSH 157
Cdd:COG4886  151 LPEPLGNLTN----LKSLDLSNNQ------------LTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSG 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 158 NCLSELPEALGALPALTFLTVTHNRLQTLPpALGALSTLQRLDLSQNLLDTLPPEiGGLGSLLELNLASNRLQSLP---- 233
Cdd:COG4886  215 NQLTDLPEPLANLTNLETLDLSNNQLTDLP-ELGNLTNLEELDLSNNQLTDLPPL-ANLTNLKTLDLSNNQLTDLKlkel 292

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 234 ASLAGLRSLRLLVLHSNLLASVPADLARLPLLTRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDAP 303
Cdd:COG4886  293 ELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLL 362
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 795-870 3.97e-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: 79.63  E-value: 3.97e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966144 795 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 870
Cdd:cd01670    5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWRERE-GDEATLGRLIQALREIGRRDLAEKLE 79
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 1.84e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 87.60  E-value: 1.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLQMRGLGAL-LLSHNCLSELPEALGALPALTFLTVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113 276 IPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILhLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKH 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 194 STLQRLDLSQN-LLDTLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLRLLVLHSNLLA-SVPADLARLPLLTRLDL 270
Cdd:PLN00113 356 NNLTVLDLSTNnLTGEIPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDI 435


                 ....*
gi 767966144 271 RDNQL 275
Cdd:PLN00113 436 SNNNL 440
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
110-300 2.69e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 85.37  E-value: 2.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 110 LRGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQT---- 185
Cdd:COG4886    8 LTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSllll 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 186 LPPALGALSTLQRLDLSQNlldtlpPEIGGLGSLLELNLASNRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLL 265
Cdd:COG4886   88 GLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNL 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 767966144 266 TRLDLRDNQLRDLPPELLDAPFVR---LQGNPLGEASP 300
Cdd:COG4886  162 KSLDLSNNQLTDLPEELGNLTNLKeldLSNNQITDLPE 199
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-275 1.20e-16

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 84.90  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 117 LPAGLSGLAHLAHLDLSFNSLE-TLPACVLQMRGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGAL 193
Cdd:PLN00113 180 IPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTgPIPSSLGNL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 194 STLQRLDLSQNLL-DTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSN-LLASVPADLARLPLLTRLDL 270
Cdd:PLN00113 260 KNLQYLFLYQNKLsGPIPPSIFSLQKLISLDLSDNSLSgEIPELVIQLQNLEILHLFSNnFTGKIPVALTSLPRLQVLQL 339


                 ....*
gi 767966144 271 RDNQL 275
Cdd:PLN00113 340 WSNKF 344
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 117-282 4.56e-14

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 76.81  E-value: 4.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 117 LPAGLSGLAHLAHLDLSFNSLET-LPACVLQMRGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ---------- 184
Cdd:PLN00113 372 IPEGLCSSGNLFKLILFSNSLEGeIPKSLGACRSLRRVRLQDNSFSgELPSEFTKLPLVYFLDISNNNLQgrinsrkwdm 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 185 ---------------TLPPALGAlSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQS-LPASLAGLRSLRLLVL 247
Cdd:PLN00113 452 pslqmlslarnkffgGLPDSFGS-KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDL 530

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 767966144 248 -HSNLLASVPADLARLPLLTRLDLRDNQLR-DLPPEL 282
Cdd:PLN00113 531 sHNQLSGQIPASFSEMPVLSQLDLSQNQLSgEIPKNL 567
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 114-273 5.47e-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: 72.13  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 114 LTNLPaGLSGLAHLAHLDLSFNSLETlpacvlqMRGLGALL------LSHNCLSELpEALGALPALTFLTVTHnrlQTLP 187
Cdd:cd21340   36 ITKIE-NLEFLTNLTHLYLQNNQIEK-------IENLENLVnlkklyLGGNRISVV-EGLENLTNLEELHIEN---QRLP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 188 PAlgalstlQRLDLSQNLLDTLppeiggLGSLLELNLASNRLQSLpASLAGLRSLRLLVLHSNLLASVPA---DLARLPL 264
Cdd:cd21340  104 PG-------EKLTFDPRSLAAL------SNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPS 169


                 ....*....
gi 767966144 265 LTRLDLRDN 273
Cdd:cd21340  170 LRELDLTGN 178
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
49-262 1.22e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.12  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  49 QLLHLCVQQPLQLLQVEFLRLSTHEDPQLLEATLAQLPQS---LSCLRSLVLKGGQRRDTLgaclRGALTNLPAGLSglA 125
Cdd:PRK15370 231 QLTSIPATLPDTIQEMELSINRITELPERLPSALQSLDLFhnkISCLPENLPEELRYLSVY----DNSIRTLPAHLP--S 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 126 HLAHLDLSFNSLETLPAcVLQMrGLGALLLSHNCLSELPEALGalPALTFLTVTHNRLQTLPPALGalSTLQRLDLSQNL 205
Cdd:PRK15370 305 GITHLNVQSNSLTALPE-TLPP-GLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLP--PTITTLDVSRNA 378

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966144 206 LDTLPPEIGglGSLLELNLASNRLQSLPASLAGLRS-----LRLLVLHSNLLASVPADLARL 262
Cdd:PRK15370 379 LTNLPENLP--AALQIMQASRNNLVRLPESLPHFRGegpqpTRIIVEYNPFSERTIQNMQRL 438
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 126-295 3.28e-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: 69.81  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 126 HLAHLDLSFNSLETLPACvlqmRGLGALLLSHNCLSELpEALGALPALTFLTVTHNRLQTLPPaLGALSTLQRLDLSQNL 205
Cdd:cd21340    6 HLYLNDKNITKIDNLSLC----KNLKVLYLYDNKITKI-ENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 206 LDTLppE-IGGLGSLLELNLASNRL---QSL---PASLAGL-RSLRLLVLHSNLLASVpADLARLPLLTRLDLRDNQLRD 277
Cdd:cd21340   80 ISVV--EgLENLTNLEELHIENQRLppgEKLtfdPRSLAALsNSLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISD 156

                        170       180
                 ....*....|....*....|....*
gi 767966144 278 LpPELLDA----PFVR---LQGNPL 295
Cdd:cd21340  157 L-EELLDLlsswPSLReldLTGNPV 180
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
114-282 5.31e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 73.19  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 114 LTNLPAGLSGlaHLAHLDLSFNSL----ETLPACVLQMRglgallLSHNCLSELPEALGAlpALTFLTVTHNRLQTLPPA 189
Cdd:PRK15370 211 LKSLPENLQG--NIKTLYANSNQLtsipATLPDTIQEME------LSINRITELPERLPS--ALQSLDLFHNKISCLPEN 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 190 LGalSTLQRLDLSQNLLDTLPPEIGGlgSLLELNLASNRLQSLPASLAglRSLRLLVLHSNLLASVPADLA--------- 260
Cdd:PRK15370 281 LP--EELRYLSVYDNSIRTLPAHLPS--GITHLNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLPpelqvldvs 354

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767966144 261 --RL--------PLLTRLDLRDNQLRDLPPEL 282
Cdd:PRK15370 355 knQItvlpetlpPTITTLDVSRNALTNLPENL 386
Death pfam00531
Death domain;
799-873 1.12e-12

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 64.31  E-value: 1.12e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144  799 LGLDWPAVALHLGVSYREVQRIRHEFRdDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 873
Cdd:pfam00531  14 LGKDWRELARKLGLSENEIDEIESENP-RLRSQTYELLRLWEQRE-GKNATVGTLLEALRKLGRRDAAEKIQSIL 86
Peptidase_S68 pfam10461
Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex ...
 421-453 7.16e-12

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: 60.62  E-value: 7.16e-12
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767966144  421 WGDLETYLEEEAPQRL-WAHCQVPHFSWFLVVSR 453
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 123-282 6.91e-11

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 66.41  E-value: 6.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 123 GLAHLAHLDLSFNSLE-TLPACVLQM-RGLGALLLSHNCLSElPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRL 199
Cdd:PLN00113  91 RLPYIQTINLSNNQLSgPIPDDIFTTsSSLRYLNLSNNNFTG-SIPRGSIPNLETLDLSNNMLSgEIPNDIGSFSSLKVL 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 200 DLSQN-LLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVL-HSNLLASVPADLARLPLLTRLDLRDNQLR 276
Cdd:PLN00113 170 DLGGNvLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKSLKWIYLgYNNLSGEIPYEIGGLTSLNHLDLVYNNLT 249


                 ....*..
gi 767966144 277 -DLPPEL 282
Cdd:PLN00113 250 gPIPSSL 256
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
114-302 1.78e-10

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 64.80  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 114 LTNLPAGLSGLAHLAHLDLSFNSLETLPAcvlqmrGLGALLLSHNCLSELPealgALPA-LTFLTVTHNRLQTLPPalgA 192
Cdd:PRK15387 274 LTHLPALPSGLCKLWIFGNQLTSLPVLPP------GLQELSVSDNQLASLP----ALPSeLCKLWAYNNQLTSLPT---L 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 193 LSTLQRLDLSQNLLDTLPPEIGGLGSLLELNlasNRLQSLPASLAGLRSlrlLVLHSNLLASVPA-------------DL 259
Cdd:PRK15387 341 PSGLQELSVSDNQLASLPTLPSELYKLWAYN---NRLTSLPALPSGLKE---LIVSGNRLTSLPVlpselkelmvsgnRL 414

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 767966144 260 ARLPLLT----RLDLRDNQLRDLPPELL---DAPFVRLQGNPLGEASPDA 302
Cdd:PRK15387 415 TSLPMLPsgllSLSVYRNQLTRLPESLIhlsSETTVNLEGNPLSERTLQA 464
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 788-865 1.79e-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: 58.04  E-value: 1.79e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQAGQP-GAVglLVQALEQSDRQDV 865
Cdd:cd08317    3 ADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKAtGNA--LESALKKIGRDDI 79
LRR_8 pfam13855
Leucine rich repeat;
194-252 2.28e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 56.76  E-value: 2.28e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966144  194 STLQRLDLSQNLLDTLPPEI-GGLGSLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLL 252
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAfKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
171-229 3.16e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 53.68  E-value: 3.16e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966144  171 PALTFLTVTHNRLQTLPP-ALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRL 229
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgAFKGLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 116-239 5.18e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 60.25  E-value: 5.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 116 NLPaGLSGLAHLAHLDLSFNSL-ETLPACVLQMRGLGALLLSHNCLS-ELPEALGALPALTFLTVTHNRLQ-TLPPALGA 192
Cdd:PLN00113 467 GLP-DSFGSKRLENLDLSRNQFsGAVPRKLGSLSELMQLKLSENKLSgEIPDELSSCKKLVSLDLSHNQLSgQIPASFSE 545

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 767966144 193 LSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQ-SLPASLAGL 239
Cdd:PLN00113 546 MPVLSQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHgSLPSTGAFL 594
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 795-870 2.39e-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: 52.03  E-value: 2.39e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966144   795 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVR 870
Cdd:smart00005  12 LDHPLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQRE-GKNATLGTLLEALRKMGRDDAVELLR 86
LRR_8 pfam13855
Leucine rich repeat;
218-275 3.84e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 50.60  E-value: 3.84e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  218 SLLELNLASNRLQSL-PASLAGLRSLRLLVLHSNLLASV-PADLARLPLLTRLDLRDNQL 275
Cdd:pfam13855   2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 325-416 5.58e-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: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  325 SFPVTPQGCSVTLA-CGVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAFQQDVGLWLLFT 401
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGtrIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHC 81

                          90
                  ....*....|....*
gi 767966144  402 PPQARRCREVVVRTR 416
Cdd:pfam00791  82 ASLRPEEWEIVLKRS 96
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 788-861 5.85e-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: 50.79  E-value: 5.85e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSD 861
Cdd:cd08319    1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQ-GKKATVQSLIQSLKAVE 73
PLN03150 PLN03150
hypothetical protein; Provisional
 186-273 6.60e-08

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 56.36  E-value: 6.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 186 LPPALGALSTLQRLDLSQNLLD-TLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSNLLAS-VPADLARL 262
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSGrVPAALGGR 513

                         90
                 ....*....|..
gi 767966144 263 PLL-TRLDLRDN 273
Cdd:PLN03150 514 LLHrASFNFTDN 525
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 788-865 1.17e-07

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: 1.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966144 788 TQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEF-RDDLDEQIRHMLFSWAERQAGQPGAVGLLVQALEQSDRQDV 865
Cdd:cd08777    1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYeRDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDL 79
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 465-537 9.07e-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: 47.91  E-value: 9.07e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144  465 GTLLCSsgHPGVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLsqsGPP--SFLQPVTVQLP 537
Cdd:pfam00791  10 GRLVLP--NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVEC---GPPglKFLKPVILEVP 79
PLN03150 PLN03150
hypothetical protein; Provisional
 163-239 1.73e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 51.74  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 163 LPEALGALPALTFLTVTHNRLQ-TLPPALGALSTLQRLDLSQNLLDTLPPE-IGGLGSLLELNLASNRLQS-LPASLAGL 239
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNGSIPEsLGQLTSLRILNLNGNSLSGrVPAALGGR 513
LRR_8 pfam13855
Leucine rich repeat;
126-183 2.62e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.59  E-value: 2.62e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  126 HLAHLDLSFNSLETLPACVLQ-MRGLGALLLSHNCLSEL-PEALGALPALTFLTVTHNRL 183
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
 110-216 2.82e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.97  E-value: 2.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 110 LRGALtnlPAGLSGLAHLAHLDLSFNSLEtlpacvlqmrglgalllshnclSELPEALGALPALTFLTVTHNRLQ-TLPP 188
Cdd:PLN03150 430 LRGFI---PNDISKLRHLQSINLSGNSIR----------------------GNIPPSLGSITSLEVLDLSYNSFNgSIPE 484

                         90       100
                 ....*....|....*....|....*....
gi 767966144 189 ALGALSTLQRLDLSQNLLD-TLPPEIGGL 216
Cdd:PLN03150 485 SLGQLTSLRILNLNGNSLSgRVPAALGGR 513
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
142-343 6.21e-06

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 50.16  E-value: 6.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 142 ACVLQMR-----GLGALLLSHNCLSELPEALGAlpALTFLTVTHNRLQTLPPALGALSTLQrldLSQNLLDTLPPEIGGL 216
Cdd:PRK15387 190 AVVQKMRaclnnGNAVLNVGESGLTTLPDCLPA--HITTLVIPDNNLTSLPALPPELRTLE---VSGNQLTSLPVLPPGL 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 217 gslLELNLASNRLQSLPASLAGLRSLRLLvlhSNLLASVPadlARLPLLTRLDLRDNQLRDLP--PELL------DAPFV 288
Cdd:PRK15387 265 ---LELSIFSNPLTHLPALPSGLCKLWIF---GNQLTSLP---VLPPGLQELSVSDNQLASLPalPSELcklwayNNQLT 335

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 289 RLQGNPLGEASPDAPSSPVAALiPEMP----RLFLTSD-LDSFPVTPQGCSVTLACGVRL 343
Cdd:PRK15387 336 SLPTLPSGLQELSVSDNQLASL-PTLPselyKLWAYNNrLTSLPALPSGLKELIVSGNRL 394
Death_FAS_TNFRSF6 cd08316
Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the ...
 806-874 3.72e-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: 3.72e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966144 806 VALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVLE 874
Cdd:cd08316   23 FARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKH-GKKGAYRTLIKTLRKAGKRAKADKIQDIIK 90
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 787-869 3.86e-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: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 787 LTQSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEfRDDLDEQIRHMLFSWAERQAGQpGAVGLLVQALEQSDRQDVA 866
Cdd:cd08318    5 VTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESD-SEDMKMRAKQLLVTWQDREGAQ-ATPEILMTALNAAGLNEIA 82


                 ...
gi 767966144 867 EEV 869
Cdd:cd08318   83 ENL 85
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 475-537 3.87e-05

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 43.49  E-value: 3.87e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767966144   475 GVKVIFPPGATEEPRRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSGpPSFLQPVTVQLP 537
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 33-318 4.48e-05

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: 47.09  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144  33 LGGNRLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHE-DPQLLEATLAQLPQSLScLRSLVLKggqrRDTLGAclR 111
Cdd:COG5238  151 LGGNAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQiGDEGIEELAEALTQNTT-VTTLWLK----RNPIGD--E 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 112 GAlTNLPAGLSGLAHLAHLDLSFNSLETlpacvlqmRGLGALLlshnclselpEALGALPALTFLTVTHNRL-----QTL 186
Cdd:COG5238  224 GA-EILAEALKGNKSLTTLDLSNNQIGD--------EGVIALA----------EALKNNTTVETLYLSGNQIgaegaIAL 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 187 PPALGALSTLQRLDLSQNLLD-----TLPPEIGGLGSLLELNLASNRL-----QSLPASLAGLRSLRLLVLHSNLLASVP 256
Cdd:COG5238  285 AKALQGNTTLTSLDLSVNRIGdegaiALAEGLQGNKTLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDNQIGDEG 364

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767966144 257 AD-----LARLPLLTRLDLRDNQLRDLPPE-LLDA------PFVRLQGNPLGEASPDApsspVAALIPEMPRLF 318
Cdd:COG5238  365 AIalakyLEGNTTLRELNLGKNNIGKQGAEaLIDAlqtnrlHTLILDGNLIGAEAQQR----LEQLLERIKSVY 434
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 117-279 6.71e-05

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 45.81  E-value: 6.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 117 LPAGLSGLAHLAHLDLSFNSL-----ETLPACvLQMRGLGALLLSHNCLSELPEAL--GAL----PALTFLTVTHNRLQT 185
Cdd:cd00116   73 LLQGLTKGCGLQELDLSDNALgpdgcGVLESL-LRSSSLQELKLNNNGLGDRGLRLlaKGLkdlpPALEKLVLGRNRLEG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 186 -----LPPALGALSTLQRLDLSQNlldtlppEIGGLGsllelnlasnrLQSLPASLAGLRSLRLLVLHSN--------LL 252
Cdd:cd00116  152 asceaLAKALRANRDLKELNLANN-------GIGDAG-----------IRALAEGLKANCNLEVLDLNNNgltdegasAL 213

                        170       180
                 ....*....|....*....|....*..
gi 767966144 253 ASVPADLARLpllTRLDLRDNQLRDLP 279
Cdd:cd00116  214 AETLASLKSL---EVLNLGDNNLTDAG 237
PLN03150 PLN03150
hypothetical protein; Provisional
 203-275 2.23e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.81  E-value: 2.23e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767966144 203 QNLLDTLPPEIGGLGSLLELNLASNRLQ-SLPASLAGLRSLRLLVLHSNLL-ASVPADLARLPLLTRLDLRDNQL 275
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 ...
 795-866 2.52e-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: 2.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767966144 795 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVA 866
Cdd:cd08805   10 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDRE-GENAKMEPLYPALYSIDRLTIV 80
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
145-282 5.27e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.38  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767966144 145 LQMRGLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLPPALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNL 224
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767966144 225 ASNRLQSLPASLAGLRSLRLLVLHSNllasvpADLARLPLLTRLDLRDNQLRDLPPEL 282
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEEL 132
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 795-873 6.43e-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: 6.43e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767966144 795 VAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDVAEEVRAVL 873
Cdd:cd08306    8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIK-KAEATVADLIKALRDCQLNLVADLVEKKL 85
LRR_8 pfam13855
Leucine rich repeat;
240-295 1.09e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 1.09e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767966144  240 RSLRLLVLHSNLLASVPAD-LARLPLLTRLDLRDNQLRDLPPELLDAP----FVRLQGNPL 295
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGaFKGLSNLKVLDLSNNLLTTLSPGAFSGLpslrYLDLSGNRL 61
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 803-870 1.82e-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: 1.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767966144 803 WPAVALHLGVSYREVQRIRHEFRDDLDEQIRhMLFSWAERQAGQPGAVGLLVQALEQSDRQDVAEEVR 870
Cdd:cd08313   14 WKEFVRRLGLSDNEIERVELDHRRCRDAQYQ-MLKVWKERGPRPYATLQHLLSVLRDMELVGCAEDIE 80
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 792-867 2.54e-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: 37.65  E-value: 2.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767966144 792 LLSvAGRLGLDWPAVALHLGvsYREvQRIRHeFRDDLDEqIRHMLFSWAERQAGqpgAVGLLVQALEQSDRQDVAE 867
Cdd:cd08311   11 LLN-AGREGSDWRALAGELG--YSA-EEIDS-FAREADP-CRALLTDWSAQDGA---TLGVLLTALRKIGRDDIVE 77
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 340-390 4.72e-03

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 37.72  E-value: 4.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767966144   340 GVRLQFPAGATATP--ITIRYRLLLPEPGLVPLGPHDALLSHVLELQPHGVAF 390
Cdd:smart00218  22 GVRLIIPPGAIPQGtrYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALF 74
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 789-865 6.09e-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: 6.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767966144 789 QSNLLSVAGRLGLDWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFSWAERQaGQPGAVGLLVQALEQSDRQDV 865
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH