2YQF,4D8O


Conserved Protein Domain Family
Death_ank

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cd08317: Death_ank 
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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.
Statistics
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PSSM-Id: 260029
Aligned: 26 rows
Threshold Bit Score: 92.3273
Created: 24-Feb-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
2YQF_A         15 EQAEMKMAVISEHL----GLSWAELARELqfSVEDINRIRVENPNsllEQSVALLNLWVIREgq-nANMENLYTALQSID 89   human
4D8O_A        495 ERIEERLAYIADHL----GFSWTELARELdfTEEQIHQIRIENPNslqDQSHALLKYWLERDgk-hATDTNLVECLTKIN 569  human
CAF93693     2799 PRPHLPPSQHPAHVlrvsRLLFSELARQLdfGDDKINLIRNENPNslqDQSHALLKLWAETEge-hGTEAALIKRLTKIN 2877 Tetraodon nig...
XP_002112080  513 NDDQSNIASVAAVI----GNDWPQLARELqlKESDIKAIDAECSPnstAAAQNILHTWAVRSgr-dATGVKLESALVGIG 587  Trichoplax ad...
CAF93751     1975 LSTFTTFSTFYTLSt---FSFSSELARELhfGVDDINRIRVENPNsllDQSAALLGLWAGREgr-rAKMESLCTALKNID 2050 Tetraodon nig...
AAC98956      134 EPDDLPLAHVARLT----GADWHRLARALevPDADIRQVRHQLVG---LEAIAILRIWIFLKke-qATPAALRSRLQRIG 205  Onchocerca oc...
EKC24774     1713 SKAKINLSEVADTL----KGDWVILATQLdiSGDEIHKINSDYRTv-nDQALAMLSLWKEKKgd-qATGNELERALKSIK 1786 Pacific oyster
GAA49432     1472 GRLELDLSNVANSV----GSDWPRLATALgiTAEEQKMISSSYRTd-sERAYAALIIWQDRAgiesTSGNKLAQVLHQIG 1546 Clonorchis si...
NP_500901     591 DLPEFVHQNVLKGI----GADWPRLGRALevPHRDIQHIRQNYPG---QECKNTLKIWIHLKke-dANQDNLDQALRQIG 662  nematode
CAZ29219       71 AKSELDLRQVAYHL----KSDWRILAQCLglSDEDQYNITSLPNRpeeEYAYTSLLLWQERNgnelTSGTQLAEALQAIG 146  Schistosoma m...
2YQF_A         90 RgEIVNMLE 98   human
4D8O_A        570 RmDIVHLME 578  human
CAF93693     2878 RmDIVHLIE 2886 Tetraodon nigroviridis
XP_002112080  588 ReDVIEHFE 596  Trichoplax adhaerens
CAF93751     2051 RaDIVAALE 2059 Tetraodon nigroviridis
AAC98956      206 RdDVVREMN 214  Onchocerca ochengi
EKC24774     1787 ReDVVQKCM 1795 Pacific oyster
GAA49432     1547 RaDVVQACM 1555 Clonorchis sinensis
NP_500901     663 RdDIVRSIA 671  nematode
CAZ29219      147 RkDILEYCM 155  Schistosoma mansoni
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