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Conserved domains on  [gi|6754772|ref|NP_034981|]
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myeloid differentiation primary response protein MyD88 [Mus musculus]

Protein Classification

Death_MyD88 and TIR domain-containing protein( domain architecture ID 10169774)

Death_MyD88 and TIR domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
161-296 8.63e-32

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 115.11  E-value: 8.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772     161 FDAFICYCPNDIeFVQEMIRQLEQTDYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 240
Cdd:smart00255   2 YDVFISYSGKED-VRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754772     241 LSLSPGVQQKRLIPIKYKAMKKDFPSILRFITICDYTN----PCTKS-WFWTRLAKALSLP 296
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.43e-26

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: 99.60  E-value: 1.43e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6754772   29 VRRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRPDPTRSLLDAWQGRS-GASVGRLLELLALLDREDILKELK 106
Cdd:cd08312   1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
 
Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
161-296 8.63e-32

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 115.11  E-value: 8.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772     161 FDAFICYCPNDIeFVQEMIRQLEQTDYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 240
Cdd:smart00255   2 YDVFISYSGKED-VRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754772     241 LSLSPGVQQKRLIPIKYKAMKKDFPSILRFITICDYTN----PCTKS-WFWTRLAKALSLP 296
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.43e-26

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: 99.60  E-value: 1.43e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6754772   29 VRRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRPDPTRSLLDAWQGRS-GASVGRLLELLALLDREDILKELK 106
Cdd:cd08312   1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 161-294 2.12e-12

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 63.92  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772    161 FDAFICYCPNDIE--FVQEMIRQLEQtdYRLKLCVSDRDVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQ 236
Cdd:pfam01582   1 YDVFLSFRGSDTRewFVSHLLKELKQ--KGIKLFIDDRDLEPGE---AIAPELLSaiEKSRRSVVVLSPNYASSGWCLDE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772    237 TKFALSLSPGVQQKrLIPIKYKAMKKD-----------FPSILRFIT----------------ICDYTNPCTKSWFWTRL 289
Cdd:pfam01582  76 LVKILECALDLGQK-VIPIFYEVDPSDvrkqtgsfgkaFKKHKKVLTeekvlkwrgalnevanIWHSKSVSDESKFWKKI 154


                  ....*
gi 6754772    290 AKALS 294
Cdd:pfam01582 155 AYDIS 159
Death pfam00531
Death domain;
30-107 5.30e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 57.76  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772     30 RRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRP----DPTRSLLDAWQGRSG--ASVGRLLELLALLDREDILK 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESENprlrSQTYELLRLWEQREGknATVGTLLEALRKLGRRDAAE 80


                  ....
gi 6754772    104 ELKS 107
Cdd:pfam00531  81 KIQS 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 29-108 2.13e-06

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: 45.09  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772      29 VRRRLSLFLNPrtPVAADWTLLAEEMGFEYLEIRELETRP-----DPTRSLLDAWQGRSG--ASVGRLLELLALLDREDI 101
Cdd:smart00005   4 TRQKLAKLLDH--PLGLDWRELARKLGLSEADIDQIRTEAprdlaEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDA 81


                   ....*..
gi 6754772     102 LKELKSR 108
Cdd:smart00005  82 VELLRSE 88
 
Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
161-296 8.63e-32

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 115.11  E-value: 8.63e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772     161 FDAFICYCPNDIeFVQEMIRQLEQTDYRLKLCVSDRDVLPGTCVWSIASELIEKrCRRMVVVVSDDYLQSKECDFQTKFA 240
Cdd:smart00255   2 YDVFISYSGKED-VRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVAA 79

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754772     241 LSLSPGVQQKRLIPIKYKAMKKDFPSILRFITICDYTN----PCTKS-WFWTRLAKALSLP 296
Cdd:smart00255  80 LENALEEGGLRVIPIFYEVIPSDVRKQPGKFRKVFKKNylkwPEDEKeQFWKKALYAVPSK 140
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 29-106 1.43e-26

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: 99.60  E-value: 1.43e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6754772   29 VRRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRPDPTRSLLDAWQGRS-GASVGRLLELLALLDREDILKELK 106
Cdd:cd08312   1 VRKKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPpGATVGNLLEILEELERKDVLEDLQ 79
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 161-294 2.12e-12

TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular signalling domain found in MyD88, interleukin 1 receptor and the Toll receptor. It contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. TIR-like motifs are also found in plant proteins thought to be involved in resistance to disease. When activated, TIR domains recruit cytoplasmic adaptor proteins MyD88 and TOLLIP (Toll interacting protein). In turn, these associate with various kinases to set off signalling cascades.


Pssm-ID: 396246 [Multi-domain]  Cd Length: 165  Bit Score: 63.92  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772    161 FDAFICYCPNDIE--FVQEMIRQLEQtdYRLKLCVSDRDVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQ 236
Cdd:pfam01582   1 YDVFLSFRGSDTRewFVSHLLKELKQ--KGIKLFIDDRDLEPGE---AIAPELLSaiEKSRRSVVVLSPNYASSGWCLDE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772    237 TKFALSLSPGVQQKrLIPIKYKAMKKD-----------FPSILRFIT----------------ICDYTNPCTKSWFWTRL 289
Cdd:pfam01582  76 LVKILECALDLGQK-VIPIFYEVDPSDvrkqtgsfgkaFKKHKKVLTeekvlkwrgalnevanIWHSKSVSDESKFWKKI 154


                  ....*
gi 6754772    290 AKALS 294
Cdd:pfam01582 155 AYDIS 159
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 164-257 3.51e-11

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 59.25  E-value: 3.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772    164 FICYCPNDIEFVQEMIRQLEQTDYRlklCVSDR-DVLPGTcvwSIASELIE--KRCRRMVVVVSDDYLQSKECDFQTKFA 240
Cdd:pfam13676   2 FISYAGEDRAWAEWLADALEAAGYR---VWLDRwDIRPGD---DWVEEIEEaiENSDRVLVVLSPNYLESPWCRAEWEAA 75

                          90
                  ....*....|....*..
gi 6754772    241 LSLSPGvqQKRLIPIKY 257
Cdd:pfam13676  76 LADPEG--RKRLIPVRL 90
Death pfam00531
Death domain;
30-107 5.30e-11

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 57.76  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772     30 RRRLSLFLNPRTPVAADWTLLAEEMGFEYLEIRELETRP----DPTRSLLDAWQGRSG--ASVGRLLELLALLDREDILK 103
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESENprlrSQTYELLRLWEQREGknATVGTLLEALRKLGRRDAAE 80


                  ....
gi 6754772    104 ELKS 107
Cdd:pfam00531  81 KIQS 84
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 30-105 1.43e-07

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: 48.05  E-value: 1.43e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754772   30 RRRLSLFLNPRTPvAADWTLLAEEMGFEYLEIRELETRPDPTRSLLDAWQGRSGASVGRLLELLALLDREDILKEL 105
Cdd:cd08311   5 QEEVEKLLNAGRE-GSDWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGATLGVLLTALRKIGRDDIVEIL 79
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 29-108 2.13e-06

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: 45.09  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6754772      29 VRRRLSLFLNPrtPVAADWTLLAEEMGFEYLEIRELETRP-----DPTRSLLDAWQGRSG--ASVGRLLELLALLDREDI 101
Cdd:smart00005   4 TRQKLAKLLDH--PLGLDWRELARKLGLSEADIDQIRTEAprdlaEQSVQLLRLWEQREGknATLGTLLEALRKMGRDDA 81


                   ....*..
gi 6754772     102 LKELKSR 108
Cdd:smart00005  82 VELLRSE 88
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 25-81 1.21e-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: 39.95  E-value: 1.21e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6754772   25 LNVGVRRRLSLFLNPRTPVAADWTLLAEEMGFE-YleIRELETRPDPTRSLLDAWQGR 81
Cdd:cd08781   1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDrY--INYFATKPSPTEVILDLWEAR 56
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 28-100 1.26e-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: 36.94  E-value: 1.26e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6754772   28 GVRRRLSLFLNPRTPVAADWTLLAEEMGF-EYLEIREL--ETRPDPTRSLLDAWQGRSGASVGRLLELLALLDRED 100
Cdd:cd08782   1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLtDLVAKLDStsSPLPSPTDRLLQEWTARPPSTIGALLRKLRELGRRD 76
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 43-106 2.32e-03

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: 36.11  E-value: 2.32e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6754772   43 VAADWTLLAEEMGFEYLEIRELETR-----PDPTRSLLDAWQGRSG--ASVGRLLELLALLDREDILKELK 106
Cdd:cd01670   9 LGRDWKKLARKLGLSEGDIDQIEEDnrddlKEQAYQMLERWREREGdeATLGRLIQALREIGRRDLAEKLE 79
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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