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Conserved domains on  [gi|1958801381|ref|XP_038939100|]
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UNC5C-like protein isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
158-238 5.91e-28

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 cd08781:

Pssm-ID: 472698  Cd Length: 83  Bit Score: 102.35  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 158 LPPELFEQLQMLLEPSSVTGNDWRKLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTSMERLDCA 234
Cdd:cd08781     1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                  ....
gi 1958801381 235 SAIQ 238
Cdd:cd08781    80 TILE 83
UPA super family cl25437
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
5-105 3.36e-05

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


The actual alignment was detected with superfamily member pfam17217:

Pssm-ID: 465384  Cd Length: 140  Bit Score: 42.73  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381   5 PLAPGQTHLQLRVYFLNNTPCALQWAITNEQPHGGR-MRGPCQLFdFTGARADQCLKLKYISEG-WENVDDSSSQLVPHL 82
Cdd:pfam17217  12 PAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQlLEEPKTLH-FKDSTHNLRLSIHDIPPSlWKSKLFAKYQEIPFY 90
                          90       100
                  ....*....|....*....|....*
gi 1958801381  83 HIWHGKCPFRSFCF--RRKSANGNE 105
Cdd:pfam17217  91 HVWSGNQNPLHCTFtlERYSLATTE 115
 
Name Accession Description Interval E-value
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
158-238 5.91e-28

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: 102.35  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 158 LPPELFEQLQMLLEPSSVTGNDWRKLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTSMERLDCA 234
Cdd:cd08781     1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                  ....
gi 1958801381 235 SAIQ 238
Cdd:cd08781    80 TILE 83
Death pfam00531
Death domain;
164-241 3.33e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 77.02  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 164 EQLQMLLEPSSVTGNDWRKLASHLGLCGMKIRFLSCQ----RSPAAAILELFEEQ---NGSLQELHYLMTSMERLDCASA 236
Cdd:pfam00531   2 KQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWEQRegkNATVGTLLEALRKLGRRDAAEK 81

                  ....*
gi 1958801381 237 IQNYL 241
Cdd:pfam00531  82 IQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
164-238 1.82e-07

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: 47.79  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381  164 EQLQMLLEPssVTGNDWRKLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNG---SLQELHYLMTSMERLDCAS 235
Cdd:smart00005   6 QKLAKLLDH--PLGLDWRELARKLGLSEADIDQIRTEaprdlAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDDAVE 83

                   ...
gi 1958801381  236 AIQ 238
Cdd:smart00005  84 LLR 86
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
5-105 3.36e-05

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 465384  Cd Length: 140  Bit Score: 42.73  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381   5 PLAPGQTHLQLRVYFLNNTPCALQWAITNEQPHGGR-MRGPCQLFdFTGARADQCLKLKYISEG-WENVDDSSSQLVPHL 82
Cdd:pfam17217  12 PAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQlLEEPKTLH-FKDSTHNLRLSIHDIPPSlWKSKLFAKYQEIPFY 90
                          90       100
                  ....*....|....*....|....*
gi 1958801381  83 HIWHGKCPFRSFCF--RRKSANGNE 105
Cdd:pfam17217  91 HVWSGNQNPLHCTFtlERYSLATTE 115
 
Name Accession Description Interval E-value
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
158-238 5.91e-28

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: 102.35  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 158 LPPELFEQLQMLLEPSSVTGNDWRKLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTSMERLDCA 234
Cdd:cd08781     1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                  ....
gi 1958801381 235 SAIQ 238
Cdd:cd08781    80 TILE 83
Death pfam00531
Death domain;
164-241 3.33e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 77.02  E-value: 3.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 164 EQLQMLLEPSSVTGNDWRKLASHLGLCGMKIRFLSCQ----RSPAAAILELFEEQ---NGSLQELHYLMTSMERLDCASA 236
Cdd:pfam00531   2 KQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWEQRegkNATVGTLLEALRKLGRRDAAEK 81

                  ....*
gi 1958801381 237 IQNYL 241
Cdd:pfam00531  82 IQSIL 86
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
164-238 2.83e-10

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: 55.33  E-value: 2.83e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801381 164 EQLQMLLEPssvtGNDWRKLASHLGLCGMkIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTSMERLDCASAIQ 238
Cdd:cd08310     3 LRLCKLLDV----GKDWRELAELLGLGHL-VESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
164-238 1.82e-07

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: 47.79  E-value: 1.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381  164 EQLQMLLEPssVTGNDWRKLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNG---SLQELHYLMTSMERLDCAS 235
Cdd:smart00005   6 QKLAKLLDH--PLGLDWRELARKLGLSEADIDQIRTEaprdlAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDDAVE 83

                   ...
gi 1958801381  236 AIQ 238
Cdd:smart00005  84 LLR 86
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
164-232 1.47e-06

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: 44.90  E-value: 1.47e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801381 164 EQLQMLLEPSSVTGNDWRKLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGS--LQELHYLMTSMERLD 232
Cdd:cd08312     3 KKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPPGatVGNLLEILEELERKD 73
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
159-238 1.13e-05

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: 42.66  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 159 PPELFEQLQMLLEPSSvTGNDWRKLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGS-LQELHYLMTSMERLDCASAI 237
Cdd:cd08311     1 PPHKQEEVEKLLNAGR-EGSDWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGAtLGVLLTALRKIGRDDIVEIL 79

                  .
gi 1958801381 238 Q 238
Cdd:cd08311    80 Q 80
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
5-105 3.36e-05

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 465384  Cd Length: 140  Bit Score: 42.73  E-value: 3.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381   5 PLAPGQTHLQLRVYFLNNTPCALQWAITNEQPHGGR-MRGPCQLFdFTGARADQCLKLKYISEG-WENVDDSSSQLVPHL 82
Cdd:pfam17217  12 PAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQlLEEPKTLH-FKDSTHNLRLSIHDIPPSlWKSKLFAKYQEIPFY 90
                          90       100
                  ....*....|....*....|....*
gi 1958801381  83 HIWHGKCPFRSFCF--RRKSANGNE 105
Cdd:pfam17217  91 HVWSGNQNPLHCTFtlERYSLATTE 115
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
158-232 8.06e-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: 8.06e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801381 158 LPPELFEQLQMLLEPSSVTGNDWRKLASHLGLcGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTSMERLD 232
Cdd:cd08799     1 IPLSIRQKLCGSLDAPQTRGNDWRMLAHKLNL-DRYLNYFATKSSPTGVILDLWEAQHfpdGNLSRLAAVLEEMGRHE 77
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
177-238 3.79e-04

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: 38.42  E-value: 3.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801381 177 GNDWRKLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNGS---LQELHYLMTSMERLDCASAIQ 238
Cdd:cd01670    10 GRDWKKLARKLGLSEGDIDQIEEDnrddlKEQAYQMLERWREREGDeatLGRLIQALREIGRRDLAEKLE 79
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
170-234 3.79e-04

Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). UNC5A is part of the UNC-5 homolog family. It is a receptor for the secreted netrin-1 and plays a critical role in neuronal development and differentiation, as well as axon-guidance. It also plays a role in regulating apoptosis in non-neuronal cells as a downstream target of p53. 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: 260065  Cd Length: 84  Bit Score: 38.33  E-value: 3.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801381 170 LEPSSVTGNDWRKLASHLGLcGMKIRFLSCQRSPAAAILELFEEQ---NGSLQELHYLMTSMERLDCA 234
Cdd:cd08800    13 LDPPCPRGADWRTLAQKLNL-DSHLSFFASKSSPTAMILNLWEAQhfpNGNLSQLAAVVAEIGKQDAM 79
Death_NFkB2_p100 cd08798
Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the ...
167-228 7.92e-04

Death domain of the Nuclear Factor-KappaB2 precursor protein p100; Death Domain (DD) of the Nuclear Factor-KappaB2 (NF-kB2) precursor protein p100. 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). NF-kB2 (or p52) is produced from the processing of the precursor protein p100, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the non-canonical NF-kB pathway. The p100 precursor is cytosolic and interacts with RelB. Upon phosphorylation by IKKalpha, p100 is processed to its 52kDa active, DNA-binding form and the p52/RelB complex is translocated into the nucleus. The non-canonical pathway plays a role in adaptive immunity and lymphorganogenesis. 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: 176776  Cd Length: 76  Bit Score: 37.49  E-value: 7.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801381 167 QMLLEPSsvTGNDWRKLASHLGLCGMKIRFLSCQrSPAAAILELFEEQNGSLQELHYLMTSM 228
Cdd:cd08798     7 QLLNDTQ--TDVPWMELAERLGLQSLVDTYKPTQ-SPPGSLLRSYELAGGPLQGLIEALQDM 65
Death_NFkB1_p105 cd08797
Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the ...
164-238 1.23e-03

Death domain of the Nuclear Factor-KappaB1 precursor protein p105; Death Domain (DD) of the Nuclear Factor-KappaB1 (NF-kB1) precursor protein p105. 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). NF-kB1 (or p50) is produced from the processing of the precursor protein p105, which contains ANK repeats and a C-terminal DD in addition to the RHD. It is regulated by the classical (or canonical) NF-kB pathway. In the cytosol, p50 forms an inactive complex with RelA (or p65) and the Inhibitor of NF-kB (IkB). Activation is triggered by the phosphorylation and degradation of IkB, resulting in the active DNA-binding p50-RelA dimer to migrate to the nucleus. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. 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: 260063  Cd Length: 76  Bit Score: 36.81  E-value: 1.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801381 164 EQLQMLLEPSSVTGNdWRKLASHLGLCGMKIRF-LScqRSPAAAILELFEEQNGSLQELHYLMTSMERLDCASAIQ 238
Cdd:cd08797     3 QQLYKLLESPDPDKN-WATLAQKLGLGILNNAFrLS--PSPSKTLLDNYEVSGGTVRELLAALRQMGYTEAIEVIE 75
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
158-231 3.90e-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: 35.77  E-value: 3.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801381 158 LPPELFEQLQMLLEPSSVTGNDWRKLASHLGLcGMKIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTSMERL 231
Cdd:cd08802     1 IPLSIRQKICNSLDAPNSRGNDWRLLAQKLSM-DRYLNYFATKASPTGVILDLWEARHQDDGDLNSLASALEEM 73
 
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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