NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1477052693|ref|NP_001352879|]
View 

caspase recruitment domain-containing protein 8 isoform k [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
79-330 5.05e-141

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


:

Pssm-ID: 463919  Cd Length: 252  Bit Score: 402.80  E-value: 5.05e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693  79 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQ-GEVDV 157
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQaGHVDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 158 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 237
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 238 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 316
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238
                         250
                  ....*....|....
gi 1477052693 317 HGTLVWDTEVKPVD 330
Cdd:pfam13553 239 SETLVWEALVRPGD 252
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
347-429 1.03e-21

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


:

Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 88.77  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 347 FVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSYL 426
Cdd:pfam00619   3 LLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLASDL 82

                  ...
gi 1477052693 427 RQQ 429
Cdd:pfam00619  83 EGL 85
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
79-330 5.05e-141

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 402.80  E-value: 5.05e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693  79 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQ-GEVDV 157
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQaGHVDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 158 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 237
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 238 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 316
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238
                         250
                  ....*....|....
gi 1477052693 317 HGTLVWDTEVKPVD 330
Cdd:pfam13553 239 SETLVWEALVRPGD 252
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
347-429 1.03e-21

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 88.77  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 347 FVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSYL 426
Cdd:pfam00619   3 LLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLASDL 82

                  ...
gi 1477052693 427 RQQ 429
Cdd:pfam00619  83 EGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
349-426 5.90e-14

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 66.77  E-value: 5.90e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1477052693 349 KENHRQLQARMgDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERD-PYLVSYL 426
Cdd:cd01671     2 RKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
349-427 1.42e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 48.87  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693  349 KENHRQLQARMGD---LKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSY 425
Cdd:smart00114   6 KRLLRRNRVRLGEelgVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETDQKLADF 85

                   ..
gi 1477052693  426 LR 427
Cdd:smart00114  86 LE 87
 
Name Accession Description Interval E-value
FIIND pfam13553
Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 ...
79-330 5.05e-141

Function to find; The function to find (FIIND) was initially discovered in two proteins, NLRP1 (aka NALP1, CARD7, NAC, DEFCAP) and CARD8 (aka TUCAN, Cardinal). NLRP1 is a member of the Nod-like receptor (NLR) protein superfamily and is involved in apoptosis and inflammation. To date, it is the only NLR protein known to have a FIIND domain. The FIIND domain is also present in the CARD8 protein where, like in NLRP1, it is followed by a C-terminal CARD domain. Both proteins are described to form an "inflammasome", a macro-molecular complex able to process caspase 1 and activate pro-IL1beta. The FIIND domain is present in only a very small subset of the kingdom of life, comprising primates, rodents (mouse, rat), carnivores (dog) and a few more, such as horse. The function of this domain is yet to be determined. Publications describing the newly discovered NLRP1 protein failed to identify it as a separate domain; for example, it was taken as part of the adjacent leucine rich repeat domain (LRR). Upon discovery of CARD8 it was noted that the N-terminal region shared significant sequence identity with an undescribed region in NLRP1. Before getting its final name, FIIND, this domain was termed NALP1-associated domain (NAD).


Pssm-ID: 463919  Cd Length: 252  Bit Score: 402.80  E-value: 5.05e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693  79 FPTAGWYLWSATGLGFLVRDEVTVTIAFGSWSQHLalDLQHHEQWLVGGPLFDVTAEPEeAVAEIHLPHFISLQ-GEVDV 157
Cdd:pfam13553   3 LPGAGSYQCSVTGLVFVVRRAVTIEYEFLSWSQFL--DLLPPQHWMVAGPLFDIKAEPG-AVTAIHLPHFICLQaGHVDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 158 SWFLVAHFKNEGMVLEHPARVEPFYAVLESPSFSLMGILLRIaSGTRLSIPITSNTLIYYHPHPEDIKFHLYLVPSDALL 237
Cdd:pfam13553  80 SLFQVAHFKDEGMLLEPPARVEPSHVVLEVPSFSPVGVLLRI-HATSPPIPIHGVVLLYYHLHPEDVTFHLYLIPNDCSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 238 TKAIDDEEDR-FHGVRLQTSPPMEPLNFGSSYIVSNSANLKVMPKELKLSYRSPGEIQHFSKFYAGQMKEPIQLEITEKR 316
Cdd:pfam13553 159 IKAIDDEEKKsFQFVRIDKPPPCQSLYFGSRYRLSSSPELEITPKELEFCYRSPGEIQLFSEVYFGQMGEGIKLSLTDKK 238
                         250
                  ....*....|....
gi 1477052693 317 HGTLVWDTEVKPVD 330
Cdd:pfam13553 239 SETLVWEALVRPGD 252
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
347-429 1.03e-21

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 88.77  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 347 FVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSYL 426
Cdd:pfam00619   3 LLKKNRVALVERLGTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLASDL 82

                  ...
gi 1477052693 427 RQQ 429
Cdd:pfam00619  83 EGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
349-426 5.90e-14

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 66.77  E-value: 5.90e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1477052693 349 KENHRQLQARMgDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERD-PYLVSYL 426
Cdd:cd01671     2 RKNRVELVEDL-DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGqPHLAELL 79
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
349-427 1.42e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 48.87  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693  349 KENHRQLQARMGD---LKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLVSY 425
Cdd:smart00114   6 KRLLRRNRVRLGEelgVDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETDQKLADF 85

                   ..
gi 1477052693  426 LR 427
Cdd:smart00114  86 LE 87
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
362-422 2.64e-06

Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260036  Cd Length: 83  Bit Score: 45.28  E-value: 2.64e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1477052693 362 LKGVLDDLQDNEVLTENEKELVEQEK-TRQSKNEALLSMVEKKGDLALDVLFRSISERDPYL 422
Cdd:cd08325    18 INGLLDDLLEKNVLNEEEMEKIKEENnTIVDKARVLIDSVTEKGQMAGQIFIQHLCNRDKQL 79
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
347-423 5.40e-05

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260039  Cd Length: 81  Bit Score: 41.43  E-value: 5.40e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1477052693 347 FVKENHRQLQARMGDLKGVLDDLQDNeVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLV 423
Cdd:cd08330     2 FVDRHREALIQRVTNVDPILDELRGK-VLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLV 77
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
344-429 8.61e-05

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 41.28  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1477052693 344 GAAFVKENHRQLQARMGDLKGVLDDLQDNEVLTENEKELVEQEKTRQSKNEALLSMVEKKGDLALDVLFRSISERDPYLV 423
Cdd:cd08329     7 DLSLIRKNRMALFQHLTCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLY 86

                  ....*.
gi 1477052693 424 SYLRQQ 429
Cdd:cd08329    87 RDLFVQ 92
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH