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Conserved domains on  [gi|1478051056|ref|NP_001352805|]
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myeloid differentiation primary response protein MyD88 isoform 6 [Homo sapiens]

Protein Classification

TIR domain-containing protein; toll/interleukin-1 receptor domain-containing protein( domain architecture ID 10871043)

TIR (Toll/interleukin-1 receptor) domain-containing protein| toll/interleukin-1 receptor (TIR) domain-containing protein with leucine-rich repeats; the TIR domain is responsible for signal transduction in all toll-like receptors (TLR)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.85e-33

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 115.78  E-value: 1.85e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478051056  29 VRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRP-GASVGRLLELLTKLGRDDVLLELG 106
Cdd:cd08312     1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
SEFIR super family cl23749
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 160-207 4.11e-08

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


The actual alignment was detected with superfamily member smart00255:

Pssm-ID: 474043 [Multi-domain]  Cd Length: 140  Bit Score: 50.78  E-value: 4.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1478051056  160 RFDAFICYcPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSI 207
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEE 47
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.85e-33

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 115.78  E-value: 1.85e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478051056  29 VRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRP-GASVGRLLELLTKLGRDDVLLELG 106
Cdd:cd08312     1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
Death pfam00531
Death domain;
30-105 1.74e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 63.92  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  30 RRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQ----ADPTGRLLDAW--QGRPGASVGRLLELLTKLGRDDVLL 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWeqREGKNATVGTLLEALRKLGRRDAAE 80


                  ..
gi 1478051056 104 EL 105
Cdd:pfam00531  81 KI 82
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 27-105 6.80e-11

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: 57.04  E-value: 6.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056   27 MRVRRRLSLFLNVRTQvaADWTALAEEMDFEYLEIRQLETQA-----DPTGRLLDAWQGRPG--ASVGRLLELLTKLGRD 99
Cdd:smart00005   2 ELTRQKLAKLLDHPLG--LDWRELARKLGLSEADIDQIRTEAprdlaEQSVQLLRLWEQREGknATLGTLLEALRKMGRD 79


                   ....*.
gi 1478051056  100 DVLLEL 105
Cdd:smart00005  80 DAVELL 85
TIR smart00255
Toll - interleukin 1 - resistance;
160-207 4.11e-08

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.78  E-value: 4.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1478051056  160 RFDAFICYcPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSI 207
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEE 47
 
Name Accession Description Interval E-value
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.85e-33

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 115.78  E-value: 1.85e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1478051056  29 VRRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRP-GASVGRLLELLTKLGRDDVLLELG 106
Cdd:cd08312     1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
Death pfam00531
Death domain;
30-105 1.74e-13

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 63.92  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  30 RRRLSLFLNVRTQVAADWTALAEEMDFEYLEIRQLETQ----ADPTGRLLDAW--QGRPGASVGRLLELLTKLGRDDVLL 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWeqREGKNATVGTLLEALRKLGRRDAAE 80


                  ..
gi 1478051056 104 EL 105
Cdd:pfam00531  81 KI 82
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 27-105 6.80e-11

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: 57.04  E-value: 6.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056   27 MRVRRRLSLFLNVRTQvaADWTALAEEMDFEYLEIRQLETQA-----DPTGRLLDAWQGRPG--ASVGRLLELLTKLGRD 99
Cdd:smart00005   2 ELTRQKLAKLLDHPLG--LDWRELARKLGLSEADIDQIRTEAprdlaEQSVQLLRLWEQREGknATLGTLLEALRKMGRD 79


                   ....*.
gi 1478051056  100 DVLLEL 105
Cdd:smart00005  80 DAVELL 85
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 30-101 1.82e-09

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: 53.06  E-value: 1.82e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478051056  30 RRRLSLFLNvRTQVAADWTALAEEMDFEYLEIRQLETQADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDV 101
Cdd:cd08311     5 QEEVEKLLN-AGREGSDWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGATLGVLLTALRKIGRDDI 75
TIR smart00255
Toll - interleukin 1 - resistance;
160-207 4.11e-08

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 50.78  E-value: 4.11e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1478051056  160 RFDAFICYcPSDIQFVQEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSI 207
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEE 47
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 36-105 2.76e-07

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: 46.89  E-value: 2.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051056  36 FLNVRTQVAADWTALAEEMDFEYLEIRQLETQA-----DPTGRLLDAWQGRPG--ASVGRLLELLTKLGRDDVLLEL 105
Cdd:cd01670     2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNrddlkEQAYQMLERWREREGdeATLGRLIQALREIGRRDLAEKL 78
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
 27-105 7.31e-05

Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). UNC5C is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5C plays a critical role in the development of spinal accessory motor neurons. Methylation of the UNC5C gene is associated with early stages of colorectal carcinogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 260064  Cd Length: 83  Bit Score: 40.38  E-value: 7.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  27 MRVRRRLSLFLNVRTQVAADWTALAEEMDFE-YLEIrqLETQADPTGRLLDAWQGR--PGASVGRLLELLTKLGRDDVLL 103
Cdd:cd08799     3 LSIRQKLCGSLDAPQTRGNDWRMLAHKLNLDrYLNY--FATKSSPTGVILDLWEAQhfPDGNLSRLAAVLEEMGRHETVV 80


                  ..
gi 1478051056 104 EL 105
Cdd:cd08799    81 SL 82
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 29-100 1.22e-04

Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear Factor-KappaB (NF-kB) precursor proteins. The NF-kB family of transcription factors play a central role in cardiovascular growth, stress response, and inflammation by controlling the expression of a network of different genes. There are five NF-kB proteins, all containing an N-terminal REL Homology Domain (RHD). Two of these, NF-kB1 and NF-kB2 are produced from the processing of the precursor proteins p105 and p100, respectively. In addition to RHD, p105 and p100 contain ANK repeats and a C-terminal DD. NF-kBs are regulated by the Inhibitor of NF-kB (IkB) Kinase (IKK) complex through classical and non-canonical pathways, which differ in the IKK subunits involved and downstream targets. IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. The precursor proteins p105 and p100 function as IkBs and as NF-kB proteins after being processed by the proteasome. 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: 260024  Cd Length: 72  Bit Score: 39.53  E-value: 1.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1478051056  29 VRRRLSLFLNVrtqvAADWTALAEEMDFEYLeIRQLETQADPTGRLLDAWQGRPGaSVGRLLELLTKLGRDD 100
Cdd:cd08310     1 TRLRLCKLLDV----GKDWRELAELLGLGHL-VESIEQSSSPTKLLLDYYEAQGG-TLEKLREALRALGETD 66
Death_IRAK cd08309
Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in ...
 25-97 1.94e-04

Death domain of Interleukin-1 Receptor-Associated Kinases; Death Domains (DDs) found in Interleukin-1 (IL-1) Receptor-Associated Kinases (IRAK1-4) and similar proteins. IRAKs are essential components of innate immunity and inflammation in mammals and other vertebrates. All four types are involved in signal transduction involving IL-1 and IL-18 receptors, Toll-like receptors, nuclear factor-kappaB, and mitogen-activated protein kinase pathways. IRAK1 and IRAK4 are active kinases while IRAK2 and IRAK-M (also called IRAK3) are inactive. In general, IRAKs are expressed ubiquitously, except for IRAK-M which is detected only in macrophages. The insect homologs, Pelle and Tube, are important components of the Toll pathway, which functions in establishing dorsoventral polarity in embryos and also in the innate immune response. Most members have an N-terminal DD followed by a kinase domain. 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: 260023  Cd Length: 88  Bit Score: 39.25  E-value: 1.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051056  25 LNMRVRRRLSLFLNvrTQVAADWTALAEEMDFEYLEIRQLETQAD----PTGRLLDAWQGRpGASVGRLLELLTKLG 97
Cdd:cd08309     6 LPPWVLKRLCKVLD--ALELAGWRQLASLIPYDQTDVRQIESMKQrgqsPTRELLWDWGTQ-NATVQDLVQLLTQLG 79
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 41-101 2.32e-04

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: 39.04  E-value: 2.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1478051056  41 TQVAADWTALAEEMDFEYLEIRQLETQADPTG----RLLDAWQGRPG--ASVGRLLELLTKLGRDDV 101
Cdd:cd08318    15 NKLGEQWKTLAPYLEMKDKDIRQIESDSEDMKmrakQLLVTWQDREGaqATPEILMTALNAAGLNEI 81
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 25-103 5.73e-04

Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in Uncoordinated-5 (UNC-5) homolog family, which includes Unc5A, B, C and D in vertebrates. UNC5 proteins are receptors for secreted netrins (netrin-1, -3 and -4) that are involved in diverse processes like axonal guidance, neuronal migration, blood vessel patterning, and apoptosis. They are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 260051  Cd Length: 83  Bit Score: 37.64  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  25 LNMRVRRRLSLFLNVRTQVAADWTALAEEMDFE-YleIRQLETQADPTGRLLDAW--QGRPGASVGRLLELLTKLGRDDV 101
Cdd:cd08781     1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDrY--INYFATKPSPTEVILDLWeaRNRDDGALNSLAAILREMGRHDA 78


                  ..
gi 1478051056 102 LL 103
Cdd:cd08781    79 AT 80
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 29-101 2.91e-03

Death domain found in death-associated protein kinase 1; Death domain (DD) found in death-associated protein kinase 1 (DAPK1). DAPK1 is composed of several functional domains, including a kinase domain, a CaM regulatory domain, ankyrin repeats, a cytoskeletal-binding domain and a C-terminal DD. It plays important roles in a diverse range of signal transduction pathways including apoptosis, growth factor signalling, and autophagy. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. 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: 260052  Cd Length: 82  Bit Score: 35.78  E-value: 2.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478051056  29 VRRRLSLFLNVRTQVAADWTALAeeMDFEYLE-IRQLET----QADPTGRLLDAWQGRPGASVGRLLELLTKLGRDDV 101
Cdd:cd08782     2 TRRKLARLLDPPDPMGRDWCLLA--VNLGLTDlVAKLDStsspLPSPTDRLLQEWTARPPSTIGALLRKLRELGRRDA 77
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
 25-103 3.75e-03

Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). UNC5B is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a role in axonal guidance, angiogenesis, and apoptosis. UNC5B signaling is involved in the netrin-1-induced proliferation and migration of renal proximal tubular cells. It is also required for vascular patterning during embryonic development, and its activation inhibits sprouting angiogenesis. UNC5 proteins are transmembrane proteins with an extracellular domain consisting of two immunoglobulin repeats, two thrombospondin type-I modules and an intracellular region containing a ZU-5 domain, UPA domain and a DD. 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: 176780  Cd Length: 84  Bit Score: 35.38  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  25 LNMRVRRRLSLFLNVRTQVAADWTALAEEMDFE-YLEIrqLETQADPTGRLLDAWQGR--PGASVGRLLELLTKLGRDDV 101
Cdd:cd08802     1 IPLSIRQKICNSLDAPNSRGNDWRLLAQKLSMDrYLNY--FATKASPTGVILDLWEARhqDDGDLNSLASALEEMGKSEM 78


                  ..
gi 1478051056 102 LL 103
Cdd:cd08802    79 LV 80
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 28-102 4.33e-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: 35.44  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478051056  28 RVRRRLSLflnVRTQVAADWTALAEEMDFEYLEIRQLETQ-----ADPTGRLLDAWQGRPG--ASVGRLLELLTKLGRDD 100
Cdd:cd08804     2 RTEERLAH---IADHLGFSWTELARELDFTEEQIHQIRIEnpnslQDQSHALLKYWLERDGkhATDTNLTQCLTKINRMD 78


                  ..
gi 1478051056 101 VL 102
Cdd:cd08804    79 IV 80
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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