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Conserved domains on  [gi|115333988|gb|AAI22557|]
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UNC5A protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 278-415 5.40e-87

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: 264.22  E-value: 5.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988  278 AAKRLKLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKL 357
Cdd:pfam17217   1 AIKRLRLAVFAPAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSLWKSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988  358 LVSYQEIPFYHIWNGTQRYLHCTFTLERVSPSTSDLACKLWVWQVEGDGQSFSINFNI 415
Cdd:pfam17217  81 FAKYQEIPFYHVWSGNQNPLHCTFTLERYSLATTELSCKICVRQVEGEGQIFQLYTTL 138
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
 444-527 3.05e-54

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: 177.39  E-value: 3.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDAGL 523
Cdd:cd08800    1 IPFLIRQKIISSLDPPCPRGADWRTLAQKLNLDSHLSFFASKSSPTAMILNLWEAQHFPNGNLSQLAAVVAEIGKQDAML 80


                 ....
gi 115333988 524 FTVS 527
Cdd:cd08800   81 FLVS 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 128-231 1.63e-49

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.60  E-value: 1.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988   128 TSNMTYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPIVSCGPPGVLLTRPVIL 207
Cdd:smart00218   1 PSFLVSGTFDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVIL 80

                           90       100
                   ....*....|....*....|....
gi 115333988   208 AMDHCGEPSPDSWSLRLKKQSCEG 231
Cdd:smart00218  81 EVPHCASLRPRDWEIVLLRSENGG 104
 
Name Accession Description Interval E-value
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 278-415 5.40e-87

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: 264.22  E-value: 5.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988  278 AAKRLKLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKL 357
Cdd:pfam17217   1 AIKRLRLAVFAPAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSLWKSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988  358 LVSYQEIPFYHIWNGTQRYLHCTFTLERVSPSTSDLACKLWVWQVEGDGQSFSINFNI 415
Cdd:pfam17217  81 FAKYQEIPFYHVWSGNQNPLHCTFTLERYSLATTELSCKICVRQVEGEGQIFQLYTTL 138
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
 444-527 3.05e-54

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: 177.39  E-value: 3.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDAGL 523
Cdd:cd08800    1 IPFLIRQKIISSLDPPCPRGADWRTLAQKLNLDSHLSFFASKSSPTAMILNLWEAQHFPNGNLSQLAAVVAEIGKQDAML 80


                 ....
gi 115333988 524 FTVS 527
Cdd:cd08800   81 FLVS 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 128-231 1.63e-49

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.60  E-value: 1.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988   128 TSNMTYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPIVSCGPPGVLLTRPVIL 207
Cdd:smart00218   1 PSFLVSGTFDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVIL 80

                           90       100
                   ....*....|....*....|....
gi 115333988   208 AMDHCGEPSPDSWSLRLKKQSCEG 231
Cdd:smart00218  81 EVPHCASLRPRDWEIVLLRSENGG 104
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 132-228 5.23e-38

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 134.58  E-value: 5.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988  132 TYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPIVSCGPPGVLLTRPVILAMDH 211
Cdd:pfam00791   1 VSGLVDSRGGRLVLPNSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80

                          90
                  ....*....|....*..
gi 115333988  212 CGEPSPDSWSLRLKKQS 228
Cdd:pfam00791  81 CASLRPEEWEIVLKRSD 97
Death pfam00531
Death domain;
449-521 3.50e-15

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 70.86  E-value: 3.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988  449 RQKIISSLDPPCRRGADWRTLAQKLHLDSH-LSFFASKP----SPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDA 521
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENeIDEIESENprlrSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 445-521 2.99e-13

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: 65.51  E-value: 2.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988   445 PFLIRQKIISSLDPPcrRGADWRTLAQKLHL-DSHLSFFASKP-----SPTAMILNLWEARHFPNGNLSQLAAAVAGLGQ 518
Cdd:smart00005   1 PELTRQKLAKLLDHP--LGLDWRELARKLGLsEADIDQIRTEAprdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78


                   ...
gi 115333988   519 PDA 521
Cdd:smart00005  79 DDA 81
 
Name Accession Description Interval E-value
UPA pfam17217
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 278-415 5.40e-87

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: 264.22  E-value: 5.40e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988  278 AAKRLKLLLFAPVACTSLEYNIRVYCLHDTHDALKEVVQLEKQLGGQLIQEPRVLHFKDSYHNLRLSIHDVPSSLWKSKL 357
Cdd:pfam17217   1 AIKRLRLAVFAPAACTSLEYSLRVYCLDDTPDALKEVVQLEKQLGGQLLEEPKTLHFKDSTHNLRLSIHDIPPSLWKSKL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988  358 LVSYQEIPFYHIWNGTQRYLHCTFTLERVSPSTSDLACKLWVWQVEGDGQSFSINFNI 415
Cdd:pfam17217  81 FAKYQEIPFYHVWSGNQNPLHCTFTLERYSLATTELSCKICVRQVEGEGQIFQLYTTL 138
Death_UNC5A cd08800
Death domain found in Uncoordinated-5A; Death Domain (DD) found in Uncoordinated-5A (UNC5A). ...
 444-527 3.05e-54

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: 177.39  E-value: 3.05e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDAGL 523
Cdd:cd08800    1 IPFLIRQKIISSLDPPCPRGADWRTLAQKLNLDSHLSFFASKSSPTAMILNLWEAQHFPNGNLSQLAAVVAEIGKQDAML 80


                 ....
gi 115333988 524 FTVS 527
Cdd:cd08800   81 FLVS 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 128-231 1.63e-49

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 165.60  E-value: 1.63e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988   128 TSNMTYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPIVSCGPPGVLLTRPVIL 207
Cdd:smart00218   1 PSFLVSGTFDARGGRLRGPRTGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVIL 80

                           90       100
                   ....*....|....*....|....
gi 115333988   208 AMDHCGEPSPDSWSLRLKKQSCEG 231
Cdd:smart00218  81 EVPHCASLRPRDWEIVLLRSENGG 104
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 132-228 5.23e-38

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 134.58  E-value: 5.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988  132 TYGTFNFLGGRLMIPNTGISLLIPPDAIPRGKIYEIYLTLHKPEDVRLPLAGCQTLLSPIVSCGPPGVLLTRPVILAMDH 211
Cdd:pfam00791   1 VSGLVDSRGGRLVLPNSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVPH 80

                          90
                  ....*....|....*..
gi 115333988  212 CGEPSPDSWSLRLKKQS 228
Cdd:pfam00791  81 CASLRPEEWEIVLKRSD 97
Death_UNC5-like cd08781
Death domain found in Uncoordinated-5 homolog family; Death Domain (DD) found in ...
 444-521 1.30e-32

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: 119.69  E-value: 1.30e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDA 521
Cdd:cd08781    1 LPYSIRQKLCSLLDPPNARGNDWRLLAQKLSVDRYINYFATKPSPTEVILDLWEARNRDDGALNSLAAILREMGRHDA 78
Death_UNC5C cd08799
Death domain found in Uncoordinated-5C; Death Domain (DD) found in Uncoordinated-5C (UNC5C). ...
 444-521 7.10e-28

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: 106.63  E-value: 7.10e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDA 521
Cdd:cd08799    1 IPLSIRQKLCGSLDAPQTRGNDWRMLAHKLNLDRYLNYFATKSSPTGVILDLWEAQHFPDGNLSRLAAVLEEMGRHET 78
Death_UNC5B cd08802
Death domain found in Uncoordinated-5B; Death Domain (DD) found in Uncoordinated-5B (UNC5B). ...
 444-520 1.35e-26

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: 103.18  E-value: 1.35e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPD 520
Cdd:cd08802    1 IPLSIRQKICNSLDAPNSRGNDWRLLAQKLSMDRYLNYFATKASPTGVILDLWEARHQDDGDLNSLASALEEMGKSE 77
Death_UNC5D cd08801
Death domain found in Uncoordinated-5D; Death Domain (DD) found in Uncoordinated-5D (UNC5D). ...
 444-530 4.11e-25

Death domain found in Uncoordinated-5D; Death Domain (DD) found in Uncoordinated-5D (UNC5D). UNC5D 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. 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: 176779  Cd Length: 98  Bit Score: 99.36  E-value: 4.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988 444 IPFLIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDAGL 523
Cdd:cd08801    1 IPYSIRQRICATFDTPNAKGKDWQMLAQKNSIDRNLSYFATQSSPSAVILSLWEARHQHDGDLDSLACALEEIGRTHSKQ 80


                 ....*..
gi 115333988 524 FTVSEAE 530
Cdd:cd08801   81 STIAETL 87
Death pfam00531
Death domain;
449-521 3.50e-15

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 70.86  E-value: 3.50e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115333988  449 RQKIISSLDPPCRRGADWRTLAQKLHLDSH-LSFFASKP----SPTAMILNLWEARHFPNGNLSQLAAAVAGLGQPDA 521
Cdd:pfam00531   1 RKQLDRLLDPPPPLGKDWRELARKLGLSENeIDEIESENprlrSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDA 78
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 445-521 2.99e-13

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: 65.51  E-value: 2.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115333988   445 PFLIRQKIISSLDPPcrRGADWRTLAQKLHL-DSHLSFFASKP-----SPTAMILNLWEARHFPNGNLSQLAAAVAGLGQ 518
Cdd:smart00005   1 PELTRQKLAKLLDHP--LGLDWRELARKLGLsEADIDQIRTEAprdlaEQSVQLLRLWEQREGKNATLGTLLEALRKMGR 78


                   ...
gi 115333988   519 PDA 521
Cdd:smart00005  79 DDA 81
Death_NFkB-like cd08310
Death domain of Nuclear Factor-KappaB precursor proteins; Death Domain (DD) of Nuclear ...
 448-521 4.59e-08

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: 49.93  E-value: 4.59e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115333988 448 IRQKIISSLDPPCrrgaDWRTLAQKLHLDSHLSFFASKPSPTAMILNLWEARhfpNGNLSQLAAAVAGLGQPDA 521
Cdd:cd08310    1 TRLRLCKLLDVGK----DWRELAELLGLGHLVESIEQSSSPTKLLLDYYEAQ---GGTLEKLREALRALGETDA 67
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 449-509 1.10e-07

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: 49.14  E-value: 1.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115333988 449 RQKIISSLDPPCRRGADWRTLAQKLHLDS-HLSFFASKPSPTAMILNLWEARHfPNGNLSQL 509
Cdd:cd08312    2 RKKLSLYLNPEKVVANDWRGLAELMGFDYlEIRNFERQSSPTERLLEDWETRP-PGATVGNL 62
Death_DAPK1 cd08782
Death domain found in death-associated protein kinase 1; Death domain (DD) found in ...
 447-521 6.63e-07

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: 46.95  E-value: 6.63e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115333988 447 LIRQKIISSLDPPCRRGADWRTLAQKLHLDSHLSFFAS----KPSPTAMILNLWEARhfPNGNLSQLAAAVAGLGQPDA 521
Cdd:cd08782    1 LTRRKLARLLDPPDPMGRDWCLLAVNLGLTDLVAKLDStsspLPSPTDRLLQEWTAR--PPSTIGALLRKLRELGRRDA 77
 
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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