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Conserved domains on  [gi|301500656|ref|NP_775832|]
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UNC5C-like protein [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 12010081)

protein kinase family protein, may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
108-193 3.89e-29

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


:

Pssm-ID: 459941  Cd Length: 97  Bit Score: 110.31  E-value: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  108 VDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAEQ 187
Cdd:pfam00791   5 VDSRGGRLVLPNSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHCASL 84

                  ....*.
gi 301500656  188 PSHART 193
Cdd:pfam00791  85 RPEEWE 90
DD super family cl14633
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ...
408-488 7.36e-29

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: 109.29  E-value: 7.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656 408 LPPELFEQLRMLLEPNSITGNDWRRLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTVMERLDCA 484
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                 ....
gi 301500656 485 SAIQ 488
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 ...
243-346 3.83e-07

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: 49.28  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  243 ARKWLQLAVFcSPLVPGQSHLQLRIYFLNNTPCALQWALTNEQPHGGRLRGPCQLFDFNGARGDQCLKLTYISEG-WENV 321
Cdd:pfam17217   1 AIKRLRLAVF-APAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSlWKSK 79
                          90       100
                  ....*....|....*....|....*
gi 301500656  322 DDSSCQLVPHLHIWHGKCPFRSFCF 346
Cdd:pfam17217  80 LFAKYQEIPFYHVWSGNQNPLHCTF 104
 
Name Accession Description Interval E-value
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
108-193 3.89e-29

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 110.31  E-value: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  108 VDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAEQ 187
Cdd:pfam00791   5 VDSRGGRLVLPNSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHCASL 84

                  ....*.
gi 301500656  188 PSHART 193
Cdd:pfam00791  85 RPEEWE 90
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
408-488 7.36e-29

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: 109.29  E-value: 7.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656 408 LPPELFEQLRMLLEPNSITGNDWRRLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTVMERLDCA 484
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                 ....
gi 301500656 485 SAIQ 488
Cdd:cd08781   80 TILE 83
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
108-186 3.17e-21

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 88.56  E-value: 3.17e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500656   108 VDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAE 186
Cdd:smart00218   9 FDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVILEVPHCAS 87
Death pfam00531
Death domain;
414-491 5.72e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 75.86  E-value: 5.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  414 EQLRMLLEPNSITGNDWRRLASHLGLCGMKIRFLSCQ----RSPAAAILELFEEQ---NGSLQELHYLMTVMERLDCASA 486
Cdd:pfam00531   2 KQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWEQRegkNATVGTLLEALRKLGRRDAAEK 81

                  ....*
gi 301500656  487 IQNYL 491
Cdd:pfam00531  82 IQSIL 86
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
243-346 3.83e-07

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: 49.28  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  243 ARKWLQLAVFcSPLVPGQSHLQLRIYFLNNTPCALQWALTNEQPHGGRLRGPCQLFDFNGARGDQCLKLTYISEG-WENV 321
Cdd:pfam17217   1 AIKRLRLAVF-APAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSlWKSK 79
                          90       100
                  ....*....|....*....|....*
gi 301500656  322 DDSSCQLVPHLHIWHGKCPFRSFCF 346
Cdd:pfam17217  80 LFAKYQEIPFYHVWSGNQNPLHCTF 104
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
414-488 4.67e-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: 44.71  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656   414 EQLRMLLEPNsiTGNDWRRLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNG---SLQELHYLMTVMERLDCAS 485
Cdd:smart00005   6 QKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEaprdlAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDDAVE 83

                   ...
gi 301500656   486 AIQ 488
Cdd:smart00005  84 LLR 86
 
Name Accession Description Interval E-value
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
108-193 3.89e-29

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 459941  Cd Length: 97  Bit Score: 110.31  E-value: 3.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  108 VDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAEQ 187
Cdd:pfam00791   5 VDSRGGRLVLPNSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPHCASL 84

                  ....*.
gi 301500656  188 PSHART 193
Cdd:pfam00791  85 RPEEWE 90
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
408-488 7.36e-29

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: 109.29  E-value: 7.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656 408 LPPELFEQLRMLLEPNSITGNDWRRLASHLgLCGMKIRFLSCQRSPAAAILELFEEQN---GSLQELHYLMTVMERLDCA 484
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKL-SVDRYINYFATKPSPTEVILDLWEARNrddGALNSLAAILREMGRHDAA 79

                 ....
gi 301500656 485 SAIQ 488
Cdd:cd08781   80 TILE 83
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
108-186 3.17e-21

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 88.56  E-value: 3.17e-21
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 301500656   108 VDHRGGCLMLQDTGISLLIPPGAVAVGRQERVSLILVWDLSDAPSLSQAQGLVSPVVACGPHGASFLKPCTLTFKHCAE 186
Cdd:smart00218   9 FDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVILEVPHCAS 87
Death pfam00531
Death domain;
414-491 5.72e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 75.86  E-value: 5.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  414 EQLRMLLEPNSITGNDWRRLASHLGLCGMKIRFLSCQ----RSPAAAILELFEEQ---NGSLQELHYLMTVMERLDCASA 486
Cdd:pfam00531   2 KQLDRLLDPPPPLGKDWRELARKLGLSENEIDEIESEnprlRSQTYELLRLWEQRegkNATVGTLLEALRKLGRRDAAEK 81

                  ....*
gi 301500656  487 IQNYL 491
Cdd:pfam00531  82 IQSIL 86
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
414-488 6.48e-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: 6.48e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 301500656 414 EQLRMLLEPnsitGNDWRRLASHLGLCGMkIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTVMERLDCASAIQ 488
Cdd:cd08310    3 LRLCKLLDV----GKDWRELAELLGLGHL-VESIEQSSSPTKLLLDYYEAQGGTLEKLREALRALGETDAVELID 72
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
243-346 3.83e-07

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: 49.28  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656  243 ARKWLQLAVFcSPLVPGQSHLQLRIYFLNNTPCALQWALTNEQPHGGRLRGPCQLFDFNGARGDQCLKLTYISEG-WENV 321
Cdd:pfam17217   1 AIKRLRLAVF-APAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSlWKSK 79
                          90       100
                  ....*....|....*....|....*
gi 301500656  322 DDSSCQLVPHLHIWHGKCPFRSFCF 346
Cdd:pfam17217  80 LFAKYQEIPFYHVWSGNQNPLHCTF 104
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
414-482 3.16e-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: 3.16e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 301500656 414 EQLRMLLEPNSITGNDWRRLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGS--LQELHYLMTVMERLD 482
Cdd:cd08312    3 KKLSLYLNPEKVVANDWRGLAELMGFDYLEIRNFERQSSPTERLLEDWETRPPGatVGNLLEILEELERKD 73
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
414-488 4.67e-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: 44.71  E-value: 4.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656   414 EQLRMLLEPNsiTGNDWRRLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNG---SLQELHYLMTVMERLDCAS 485
Cdd:smart00005   6 QKLAKLLDHP--LGLDWRELARKLGLSEADIDQIRTEaprdlAEQSVQLLRLWEQREGknaTLGTLLEALRKMGRDDAVE 83

                   ...
gi 301500656   486 AIQ 488
Cdd:smart00005  84 LLR 86
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
409-488 4.06e-04

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: 39.19  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656 409 PPELFEQLRMLLEPNSiTGNDWRRLASHLGLCGMKIRFLSCQRSPAAAILELFEEQNGS-LQELHYLMTVMERLDCASAI 487
Cdd:cd08311    1 PPHKQEEVEKLLNAGR-EGSDWRALAGELGYSAEEIDSFAREADPCRALLTDWSAQDGAtLGVLLTALRKIGRDDIVEIL 79

                 .
gi 301500656 488 Q 488
Cdd:cd08311   80 Q 80
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
408-481 7.44e-04

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: 38.45  E-value: 7.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 301500656 408 LPPELFEQLRMLLEPNSITGNDWRRLASHLGLcGMKIRFLSCQRSPAAAILELFEEQNGSLQELHYLMTVMERL 481
Cdd:cd08799    1 IPLSIRQKLCGSLDAPQTRGNDWRMLAHKLNL-DRYLNYFATKSSPTGVILDLWEAQHFPDGNLSRLAAVLEEM 73
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
420-471 2.82e-03

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: 36.79  E-value: 2.82e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 301500656 420 LEPNSITGNDWRRLASHLGLcGMKIRFLSCQRSPAAAILELFEEQ---NGSLQEL 471
Cdd:cd08800   13 LDPPCPRGADWRTLAQKLNL-DSHLSFFASKSSPTAMILNLWEAQhfpNGNLSQL 66
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
427-488 3.79e-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: 36.49  E-value: 3.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301500656 427 GNDWRRLASHLGLCGMKIRFLSCQ-----RSPAAAILELFEEQNGS---LQELHYLMTVMERLDCASAIQ 488
Cdd:cd01670   10 GRDWKKLARKLGLSEGDIDQIEEDnrddlKEQAYQMLERWREREGDeatLGRLIQALREIGRRDLAEKLE 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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