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Conserved domains on  [gi|932085553|gb|ALG40990|]
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MyD88 protein [Anthopleura buddemeieri]

Protein Classification

toll-like receptor( domain architecture ID 10327514)

toll-like receptor (TLR) is involved in the recognition of microbial pathogens by the innate immune system, which recognize different pathogen-associated molecular patterns

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
142-258 6.86e-17

Toll - interleukin 1 - resistance;


:

Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 75.44  E-value: 6.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553   142 KYDAFICYaRENIEFAKKILKELEAPPYHLRLCIDYRDILPGGADLSTLAHVIEErCRKVVVVLSEHFNNDETADFQAKI 221
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 932085553   222 ALSLSPGCRDKRLIPIKYEPVK--IPTIYRFITHIDYTN 258
Cdd:smart00255  79 ALENALEEGGLRVIPIFYEVIPsdVRKQPGKFRKVFKKN 117
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
 32-104 4.19e-11

Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer.


The actual alignment was detected with superfamily member cd08312:

Pssm-ID: 472698  Cd Length: 79  Bit Score: 57.61  E-value: 4.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085553  32 RMSELLRPHHALGNDWTALAGQLGLTFEEITNLKEERDPVQVMFNKHEFL--DLTISRLKSCLRAIDRLDAVKDL 104
Cdd:cd08312    4 KLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRppGATVGNLLEILEELERKDVLEDL 78
 
Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
142-258 6.86e-17

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 75.44  E-value: 6.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553   142 KYDAFICYaRENIEFAKKILKELEAPPYHLRLCIDYRDILPGGADLSTLAHVIEErCRKVVVVLSEHFNNDETADFQAKI 221
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 932085553   222 ALSLSPGCRDKRLIPIKYEPVK--IPTIYRFITHIDYTN 258
Cdd:smart00255  79 ALENALEEGGLRVIPIFYEVIPsdVRKQPGKFRKVFKKN 117
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 146-263 2.66e-16

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 73.12  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553  146 FICYARENIEFAKKILKELEAPPYhlRLCIDYRDILPGGADLSTLAHVIeERCRKVVVVLSEHFNNDETADFQAKIALSL 225
Cdd:pfam13676   2 FISYAGEDRAWAEWLADALEAAGY--RVWLDRWDIRPGDDWVEEIEEAI-ENSDRVLVVLSPNYLESPWCRAEWEAALAD 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 932085553  226 SPGcrDKRLIPIKYEPVKIPTIYRFITHIDYTNENARE 263
Cdd:pfam13676  79 PEG--RKRLIPVRLECDLELPGLAGLQYIDLRDGDEFD 114
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 32-104 4.19e-11

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: 57.61  E-value: 4.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085553  32 RMSELLRPHHALGNDWTALAGQLGLTFEEITNLKEERDPVQVMFNKHEFL--DLTISRLKSCLRAIDRLDAVKDL 104
Cdd:cd08312    4 KLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRppGATVGNLLEILEELERKDVLEDL 78
Death pfam00531
Death domain;
32-107 4.44e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 46.97  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553   32 RMSELLRPHHALGNDWTALAGQLGLTFEEITNLKEE----RDPVQVMFNK---HEFLDLTISRLKSCLRAIDRLDAVKDL 104
Cdd:pfam00531   3 QLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLweqREGKNATVGTLLEALRKLGRRDAAEKI 82


                  ...
gi 932085553  105 EKF 107
Cdd:pfam00531  83 QSI 85
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 41-106 1.10e-05

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: 42.78  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085553    41 HALGNDWTALAGQLGLTFEEIT-----NLKEERDPVQVMFNK---HEFLDLTISRLKSCLRAIDRLDAVKDLEK 106
Cdd:smart00005  14 HPLGLDWRELARKLGLSEADIDqirteAPRDLAEQSVQLLRLweqREGKNATLGTLLEALRKMGRDDAVELLRS 87
 
Name Accession Description Interval E-value
TIR smart00255
Toll - interleukin 1 - resistance;
142-258 6.86e-17

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 75.44  E-value: 6.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553   142 KYDAFICYaRENIEFAKKILKELEAPPYHLRLCIDYRDILPGGADLSTLAHVIEErCRKVVVVLSEHFNNDETADFQAKI 221
Cdd:smart00255   1 EYDVFISY-SGKEDVRNEFLSHLLEKLRGYGLCVFIDDFEPGGGDLEEIDEAIEK-SRIAIVVLSPNYAESEWCLDELVA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 932085553   222 ALSLSPGCRDKRLIPIKYEPVK--IPTIYRFITHIDYTN 258
Cdd:smart00255  79 ALENALEEGGLRVIPIFYEVIPsdVRKQPGKFRKVFKKN 117
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 146-263 2.66e-16

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 73.12  E-value: 2.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553  146 FICYARENIEFAKKILKELEAPPYhlRLCIDYRDILPGGADLSTLAHVIeERCRKVVVVLSEHFNNDETADFQAKIALSL 225
Cdd:pfam13676   2 FISYAGEDRAWAEWLADALEAAGY--RVWLDRWDIRPGDDWVEEIEEAI-ENSDRVLVVLSPNYLESPWCRAEWEAALAD 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 932085553  226 SPGcrDKRLIPIKYEPVKIPTIYRFITHIDYTNENARE 263
Cdd:pfam13676  79 PEG--RKRLIPVRLECDLELPGLAGLQYIDLRDGDEFD 114
TIR pfam01582
TIR domain; The Toll/interleukin-1 receptor (TIR) homology domain is an intracellular ...
 143-243 5.47e-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: 62.77  E-value: 5.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553  143 YDAFICYARENIE--FAKKILKELEAPPYhlRLCIDYRDILPGGADLSTLAHVIEErCRKVVVVLSEHFNNDETADFQAK 220
Cdd:pfam01582   1 YDVFLSFRGSDTRewFVSHLLKELKQKGI--KLFIDDRDLEPGEAIAPELLSAIEK-SRRSVVVLSPNYASSGWCLDELV 77

                          90       100
                  ....*....|....*....|....*.
gi 932085553  221 IALslspGCRDKR---LIPIKYEPVK 243
Cdd:pfam01582  78 KIL----ECALDLgqkVIPIFYEVDP 99
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 32-104 4.19e-11

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: 57.61  E-value: 4.19e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 932085553  32 RMSELLRPHHALGNDWTALAGQLGLTFEEITNLKEERDPVQVMFNKHEFL--DLTISRLKSCLRAIDRLDAVKDL 104
Cdd:cd08312    4 KLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRppGATVGNLLEILEELERKDVLEDL 78
Death pfam00531
Death domain;
32-107 4.44e-07

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 46.97  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 932085553   32 RMSELLRPHHALGNDWTALAGQLGLTFEEITNLKEE----RDPVQVMFNK---HEFLDLTISRLKSCLRAIDRLDAVKDL 104
Cdd:pfam00531   3 QLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLweqREGKNATVGTLLEALRKLGRRDAAEKI 82


                  ...
gi 932085553  105 EKF 107
Cdd:pfam00531  83 QSI 85
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 41-105 1.22e-06

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: 45.35  E-value: 1.22e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 932085553  41 HALGNDWTALAGQLGLTFEEITNLKEERDPVQVMFN----KHeflDLTISRLKSCLRAIDRLDAVKDLE 105
Cdd:cd08311   15 GREGSDWRALAGELGYSAEEIDSFAREADPCRALLTdwsaQD---GATLGVLLTALRKIGRDDIVEILQ 80
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 32-105 2.61e-06

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: 44.16  E-value: 2.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085553  32 RMSELLRPhhalGNDWTALAGQLGLTFEeITNLKEERDPVQVMFNKHEFLDLTISRLKSCLRAIDRLDAVKDLE 105
Cdd:cd08310    4 RLCKLLDV----GKDWRELAELLGLGHL-VESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 43-105 5.50e-06

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: 43.42  E-value: 5.50e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085553  43 LGNDWTALAGQLGLTFEEITNLKEE-----RDPVQVMFNKH---EFLDLTISRLKSCLRAIDRLDAVKDLE 105
Cdd:cd01670    9 LGRDWKKLARKLGLSEGDIDQIEEDnrddlKEQAYQMLERWrerEGDEATLGRLIQALREIGRRDLAEKLE 79
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 41-106 1.10e-05

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: 42.78  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 932085553    41 HALGNDWTALAGQLGLTFEEIT-----NLKEERDPVQVMFNK---HEFLDLTISRLKSCLRAIDRLDAVKDLEK 106
Cdd:smart00005  14 HPLGLDWRELARKLGLSEADIDqirteAPRDLAEQSVQLLRLweqREGKNATLGTLLEALRKMGRDDAVELLRS 87
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 32-101 1.50e-05

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: 42.33  E-value: 1.50e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 932085553  32 RMSELLRPHHALGNDWTALAGQLGLT---FEEITNLKEERDPV----QVMFNKHeflDLTISRLKSCLRAIDRLDAV 101
Cdd:cd08782    5 KLARLLDPPDPMGRDWCLLAVNLGLTdlvAKLDSTSSPLPSPTdrllQEWTARP---PSTIGALLRKLRELGRRDAA 78
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 43-105 2.85e-04

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: 38.78  E-value: 2.85e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 932085553  43 LGNDWTALAGQLGLTFEEITNLKEE--RDPVQ---VMFN---KHEFLDLTISRLKSCLRAIDRLDAVKDLE 105
Cdd:cd08317   14 LGSDWPELARELGVSEEDIDLIRSEnpNSLAQqamAMLRlwlEREGEKATGNALESALKKIGRDDIVEKCE 84
 
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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