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Conserved domains on  [gi|2023156764|ref|XP_040461299|]
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ankyrin-3 isoform X22 [Falco naumanni]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 453-582 8.01e-57

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 pfam17809:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 193.84  E-value: 8.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  453 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 532
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156764  533 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 582
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 127-231 8.84e-48

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 166.76  E-value: 8.84e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764   127 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 206
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156764   207 VEIPHFGSMRGKERELIVLRSENGE 231
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 3196-3279 2.42e-46

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. 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. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. 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: 176781  Cd Length: 84  Bit Score: 162.15  E-value: 2.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08803     81 TLLE 84
PTZ00121 super family cl31754
MAEBL; Provisional
 1719-2154 1.88e-03

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1719 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 1792
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1793 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 1869
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1870 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 1949
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1950 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2029
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 2030 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2105
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156764 2106 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2154
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 453-582 8.01e-57

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


Pssm-ID: 375346  Cd Length: 131  Bit Score: 193.84  E-value: 8.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  453 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 532
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156764  533 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 582
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 127-231 8.84e-48

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 166.76  E-value: 8.84e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764   127 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 206
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156764   207 VEIPHFGSMRGKERELIVLRSENGE 231
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 3196-3279 2.42e-46

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. 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. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. 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: 176781  Cd Length: 84  Bit Score: 162.15  E-value: 2.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 131-228 2.20e-41

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 148.44  E-value: 2.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  131 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 210
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156764  211 HFGSMRGKERELIVLRSE 228
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 3195-3281 2.03e-25

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: 102.49  E-value: 2.03e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  3195 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 3273
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156764  3274 IVTLLEGP 3281
Cdd:smart00005   81 AVELLRSE 88
Death pfam00531
Death domain;
3201-3279 6.86e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 6.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3201 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 3277
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156764 3278 LE 3279
Cdd:pfam00531   82 IQ 83
PTZ00121 PTZ00121
MAEBL; Provisional
 1719-2154 1.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1719 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 1792
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1793 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 1869
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1870 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 1949
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1950 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2029
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 2030 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2105
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156764 2106 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2154
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 453-582 8.01e-57

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


Pssm-ID: 375346  Cd Length: 131  Bit Score: 193.84  E-value: 8.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  453 VPYMAKFVIFAKMNDPVESNLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 532
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 2023156764  533 YAFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 582
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 127-231 8.84e-48

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 166.76  E-value: 8.84e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764   127 SSFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVI 206
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79

                            90       100
                    ....*....|....*....|....*
gi 2023156764   207 VEIPHFGSMRGKERELIVLRSENGE 231
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 3196-3279 2.42e-46

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. 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. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. 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: 176781  Cd Length: 84  Bit Score: 162.15  E-value: 2.42e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08803     81 TLLE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 131-228 2.20e-41

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 148.44  E-value: 2.20e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  131 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLASPPPMVEGEGLASRLVEMGPSGAQFLGPVIVEIP 210
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEVP 79

                           90
                   ....*....|....*...
gi 2023156764  211 HFGSMRGKERELIVLRSE 228
Cdd:pfam00791   80 HCASLRPEEWEIVLKRSD 97
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 3196-3279 3.81e-33

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: 124.30  E-value: 3.81e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08317     81 EKCE 84
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 3196-3279 7.32e-33

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. 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. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. 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: 260067  Cd Length: 84  Bit Score: 123.54  E-value: 7.32e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08805     81 NILE 84
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 3196-3279 1.16e-27

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. 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. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. 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: 260066  Cd Length: 84  Bit Score: 108.63  E-value: 1.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3196 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 3275
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 2023156764 3276 TLLE 3279
Cdd:cd08804     81 HLME 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 3195-3281 2.03e-25

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: 102.49  E-value: 2.03e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764  3195 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 3273
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 2023156764  3274 IVTLLEGP 3281
Cdd:smart00005   81 AVELLRSE 88
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 3205-3279 5.83e-20

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: 86.57  E-value: 5.83e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2023156764 3205 VADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLE 3279
Cdd:cd01670      5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Death pfam00531
Death domain;
3201-3279 6.86e-17

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 78.18  E-value: 6.86e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3201 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 3277
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 2023156764 3278 LE 3279
Cdd:pfam00531   82 IQ 83
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 3204-3280 1.73e-08

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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 they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 54.22  E-value: 1.73e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156764 3204 IVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEG 3280
Cdd:cd08306      7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDCQLNLVADLVEK 83
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 3198-3270 2.94e-08

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. 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, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260031  Cd Length: 83  Bit Score: 53.48  E-value: 2.94e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2023156764 3198 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 3270
Cdd:cd08319      1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 3212-3279 3.32e-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: 47.28  E-value: 3.32e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156764 3212 SWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDGknATTDALTSVLTKINRIDIVTLLE 3279
Cdd:cd08311     20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 3211-3270 6.30e-06

Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. 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: 260054  Cd Length: 80  Bit Score: 46.80  E-value: 6.30e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3211 LSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKIN 3270
Cdd:cd08784     12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
PTZ00121 PTZ00121
MAEBL; Provisional
 1719-2154 1.88e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1719 RVDRTVKEAEEKlTEVSQFFRDKTEKLNDELQSPEKKQH---KKNGKEIHSSQSSASSSPEKVLLSELPSSGDEWSK--- 1792
Cdd:PTZ00121  1330 KADAAKKKAEEA-KKAAEAAKAEAEAAADEAEAAEEKAEaaeKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkad 1408

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1793 -VKQYAHDGKcfpKVDE--RKASSLPSSPEKRifvQPAEDSKQTMEHKGSAQQtgvpevsqtgfqlkQSKLSSIRLKFEQ 1869
Cdd:PTZ00121  1409 eLKKAAAAKK---KADEakKKAEEKKKADEAK---KKAEEAKKADEAKKKAEE--------------AKKAEEAKKKAEE 1468

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1870 SISPRSKDVTQEEKKLDGQSKipvKKSQESKLPVYQFYSREKHAKQVEvidgstalqkEVKIQEDfvpgKAKAIEDFRAS 1949
Cdd:PTZ00121  1469 AKKADEAKKKAEEAKKADEAK---KKAEEAKKKADEAKKAAEAKKKAD----------EAKKAEE----AKKADEAKKAE 1531

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1950 DAQKRPEMSKGvvpeyfSEPQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKLSHVLVPDTVKENHVDHAETK 2029
Cdd:PTZ00121  1532 EAKKADEAKKA------EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 2030 TDKKSEFATVTEHKLAANGIH-SEEVK---ELTVKSPSKRVLYREFVVREGERNGEVADKISKRKEEIAVSHIPVRIVEE 2105
Cdd:PTZ00121  1606 KMKAEEAKKAEEAKIKAEELKkAEEEKkkvEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*....
gi 2023156764 2106 KrtmldgvyelsakvsqsaviKEKVERQIDYMEDEKIKCSEIRKVTKQQ 2154
Cdd:PTZ00121  1686 D--------------------EKKAAEALKKEAEEAKKAEELKKKEAEE 1714
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 3198-3274 2.02e-03

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. 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: 260030  Cd Length: 86  Bit Score: 39.81  E-value: 2.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2023156764 3198 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRvENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDI 3274
Cdd:cd08318      6 TSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
PTZ00121 PTZ00121
MAEBL; Provisional
 1701-2167 2.34e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1701 RFTEDRldRGREKLMYED-RVDRTVKEAEEKLTEVSQFFRDKTEKLNDELQSPEKKQHKKNGKEIHSSQSSASSSPEKVL 1779
Cdd:PTZ00121  1207 KAEEER--KAEEARKAEDaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK 1284

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1780 LSELPSSGDEWSK---------VKQYAHDGKcfpKVDERKASSLPSSPEKRIFVQPAEDSKQTMEHKGSAQQTGVPEVSQ 1850
Cdd:PTZ00121  1285 KAEEKKKADEAKKaeekkkadeAKKKAEEAK---KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1851 TGFQLKQSKLSSIRLKFEQSISPRSKDVTQEEKKLDGQSKIPVKKSQESKLPVYQFYSREKHAKQVEVIDGSTALQKEVK 1930
Cdd:PTZ00121  1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE 1441

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 1931 IQEDFVPGKAKAIEDFRASDAQKRPEMSKgvvpeyfsepQAKDLVYGSDSTAKGHWDKKIYRTWESPGTSNHQTQKEKls 2010
Cdd:PTZ00121  1442 EAKKADEAKKKAEEAKKAEEAKKKAEEAK----------KADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK-- 1509

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 2011 hvlvpdtVKENHVDHAETKTdKKSEFATVTEHKLAANGIHSEEVKELTVKSPSKRVLYREFVVREGERNGEVADK-ISKR 2089
Cdd:PTZ00121  1510 -------KKADEAKKAEEAK-KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKnMALR 1581

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2023156764 2090 KEEIAvshipvRIVEEKRT-MLDGVYELSAKVSQSAVIKEkverqidymEDEKIKCSEIRKVTKQQSSIGLTPPIEEME 2167
Cdd:PTZ00121  1582 KAEEA------KKAEEARIeEVMKLYEEEKKMKAEEAKKA---------EEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 3195-3278 5.99e-03

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: 38.35  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023156764 3195 CERTDIRMAIVADhlglsWTELARELNFSVDEINQI-RVENPnsliaqSFMLLKKWVTRDgKNATTDALTSVLTKINRID 3273
Cdd:cd08312      6 SLYLNPEKVVAND-----WRGLAELMGFDYLEIRNFeRQSSP------TERLLEDWETRP-PGATVGNLLEILEELERKD 73


                   ....*
gi 2023156764 3274 IVTLL 3278
Cdd:cd08312     74 VLEDL 78
 
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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