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Conserved domains on  [gi|47174755|ref|NP_998803|]
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uncharacterized protein LOC337226 [Danio rerio]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 1000080)

EF-hand (EFh) domain-containing protein may be involved in binding intracellular calcium and in calcium signal transduction

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00184 super family cl33172
calmodulin; Provisional
 5-150 7.38e-40

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 131.42  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755    5 SEDQILEFKEAFLLFDRTGDGKITYNQCGDVMRALGQNPVNAEVLKVLGNPKAEemNHKLLDFEQFLPMLQAiaKNKDQG 84
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47174755   85 TFEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGHE-DANGCINYEELVRMVMS 150
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 5-150 7.38e-40

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 131.42  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755    5 SEDQILEFKEAFLLFDRTGDGKITYNQCGDVMRALGQNPVNAEVLKVLGNPKAEemNHKLLDFEQFLPMLQAiaKNKDQG 84
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47174755   85 TFEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGHE-DANGCINYEELVRMVMS 150
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 88-149 1.11e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 51.39  E-value: 1.11e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47174755  88 DFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGH-EDANGCINYEELVRMVM 149
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 11-39 1.46e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.97  E-value: 1.46e-04
                           10        20
                   ....*....|....*....|....*....
gi 47174755     11 EFKEAFLLFDRTGDGKITYNQCGDVMRAL 39
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
12-150 7.71e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 7.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  12 FKEAFLLFDRTGDGKITYNQCGDVMRALGQNpvNAEVLKVLGNPKaeemnhklLDFEQFLPMLQAIAKNKDQGTFEDFve 91
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWAT--LFSEADTDGDGR--------ISREEFVAGMESLFEATVEPFARAA-- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  92 gLRVFDKEGNGTVMGAELRHVLTTLGekMTEEEVETLLAGHE-DANGCINYEELVRMVMS 150
Cdd:COG5126  75 -FDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDtDGDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
11-40 8.13e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 8.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 47174755    11 EFKEAFLLFDRTGDGKITYNQCGDVMRALG 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
 
Name Accession Description Interval E-value
PTZ00184 PTZ00184
calmodulin; Provisional
 5-150 7.38e-40

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 131.42  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755    5 SEDQILEFKEAFLLFDRTGDGKITYNQCGDVMRALGQNPVNAEVLKVLGNPKAEemNHKLLDFEQFLPMLQAiaKNKDQG 84
Cdd:PTZ00184   6 TEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDAD--GNGTIDFPEFLTLMAR--KMKDTD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47174755   85 TFEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGHE-DANGCINYEELVRMVMS 150
Cdd:PTZ00184  82 SEEEIKEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADvDGDGQINYEEFVKMMMS 148
PTZ00183 PTZ00183
centrin; Provisional
 3-147 4.77e-16

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 70.49  E-value: 4.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755    3 DFSEDQILEFKEAFLLFDRTGDGKITYNQCGDVMRALGQNPVNAEVLKVLGNPKAEemNHKLLDFEQFLPMLQAIAKNKD 82
Cdd:PTZ00183  10 GLTEDQKKEIREAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEIKQMIADVDKD--GSGKIDFEEFLDIMTKKLGERD 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47174755   83 qgTFEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEV-ETLLAGHEDANGCINYEELVRM 147
Cdd:PTZ00183  88 --PREEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELqEMIDEADRNGDGEISEEEFYRI 151
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 88-149 1.11e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 51.39  E-value: 1.11e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47174755  88 DFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGH-EDANGCINYEELVRMVM 149
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVdKDGDGKIDFEEFLELMA 63
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
 12-71 1.04e-05

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 41.18  E-value: 1.04e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  12 FKEAFLLFDRTGDGKITYNQCGDVMRALGQnPVNAEVLKVLgnpkAEEMNHKllDFEQFL 71
Cdd:cd22949   5 FREAFILFDRDGDGELTMYEAVLAMRSCGI-PLTNDEKDAL----PASMNWD--QFENWA 57
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 11-39 1.46e-04

EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in pairs. Links between disease states and genes encoding EF-hands, particularly the S100 subclass, are emerging. Each motif consists of a 12 residue loop flanked on either side by a 12 residue alpha-helix. EF-hands undergo a conformational change unpon binding calcium ions.


Pssm-ID: 197492 [Multi-domain]  Cd Length: 29  Bit Score: 36.97  E-value: 1.46e-04
                           10        20
                   ....*....|....*....|....*....
gi 47174755     11 EFKEAFLLFDRTGDGKITYNQCGDVMRAL 39
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
12-150 7.71e-04

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 37.46  E-value: 7.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  12 FKEAFLLFDRTGDGKITYNQCGDVMRALGQNpvNAEVLKVLGNPKaeemnhklLDFEQFLPMLQAIAKNKDQGTFEDFve 91
Cdd:COG5126   7 LDRRFDLLDADGDGVLERDDFEALFRRLWAT--LFSEADTDGDGR--------ISREEFVAGMESLFEATVEPFARAA-- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  92 gLRVFDKEGNGTVMGAELRHVLTTLGekMTEEEVETLLAGHE-DANGCINYEELVRMVMS 150
Cdd:COG5126  75 -FDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFARLDtDGDGKISFEEFVAAVRD 131
EF-hand_6 pfam13405
EF-hand domain;
11-40 8.13e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 35.23  E-value: 8.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 47174755    11 EFKEAFLLFDRTGDGKITYNQCGDVMRALG 40
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EF-hand_7 pfam13499
EF-hand domain pair;
94-149 9.87e-04

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 35.69  E-value: 9.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 47174755    94 RVFDKEGNGTVMGAELRHVLTTL--GEKMTEEEVETLLAGH-EDANGCINYEELVRMVM 149
Cdd:pfam13499   9 KLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFKEFdLDKDGRISFEEFLELYS 67
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 11-52 1.39e-03

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 35.22  E-value: 1.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 47174755  11 EFKEAFLLFDRTGDGKITYNQCGDVMRALGQNPVNAEVLKVL 52
Cdd:cd00051   1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMI 42
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
 62-148 1.72e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 35.97  E-value: 1.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  62 HKLLDFEQFLPMLqaiakNKDQGTFEDFVEGLRVFDKEGNGTVMGAELRHVLTTL---GEKMTEEEVETLL-AGHEDANG 137
Cdd:cd16251  14 HGSFNYKKFFEHV-----GLKQKSEDQIKKVFQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLaAGDTDGDG 88

                        90
                ....*....|.
gi 47174755 138 CINYEELVRMV 148
Cdd:cd16251  89 KIGVEEFATLV 99
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 11-39 2.04e-03

EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering/transport proteins. The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and do not undergo calcium dependent conformational changes.


Pssm-ID: 425435 [Multi-domain]  Cd Length: 29  Bit Score: 33.91  E-value: 2.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 47174755    11 EFKEAFLLFDRTGDGKITYNQCGDVMRAL 39
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 59-148 2.76e-03

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 35.58  E-value: 2.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755  59 EMNHK-LLDFEQFLPMLQAIAKNKDQGtfEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKM-----TEEEVETLL-AG 131
Cdd:cd16252  10 EMRHHgSFNYSKFFEYMQKFQTSEQQE--EAIRKAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIqAA 87

                        90
                ....*....|....*..
gi 47174755 132 HEDANGCINYEELVRMV 148
Cdd:cd16252  88 DTDGDGRIDFQEFSDMV 104
EFh_HEF cd15902
EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand ...
 5-145 6.16e-03

EF-hand, calcium binding motif, found in the hexa-EF hand proteins family; The hexa-EF hand proteins family, also named the calbindin sub-family, contains a group of six EF-hand Ca2+-binding proteins, including calretinin (CR, also termed 29 kDa calbindin), calbindin D28K (CB, also termed vitamin D-dependent calcium-binding protein, avian-type), and secretagogin (SCGN). CR is a cytosolic hexa-EF-hand calcium-binding protein predominantly expressed in a variety of normal and tumorigenic t-specific neurons of the central and peripheral nervous system. It is a multifunctional protein implicated in many biological processes, including cell proliferation, differentiation, and cell death. CB is highly expressed in brain tissue. It is a strong calcium-binding and buffering protein responsible for preventing a neuronal death as well as maintaining and controlling calcium homeostasis. SCGN is a six EF-hand calcium-binding protein expressed in neuroendocrine, pancreatic endocrine and retinal cells. It plays a crucial role in cell apoptosis, receptor signaling and differentiation. It is also involved in vesicle secretion through binding to various proteins, including interacts with SNAP25, SNAP23, DOC2alpha, ARFGAP2, rootletin, KIF5B, beta-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2. SCGN functions as a Ca2+ sensor/coincidence detector modulating vesicular exocytosis of neurotransmitters, neuropeptides or hormones. Although the family members share a significant amount of secondary sequence homology, they display altered structural and biochemical characteristics, and operate in distinct fashions. CB contains six EF-hand motifs in a single globular domain, where EF-hands 1, 3, 4, 5 bind four calcium ions. CR contains six EF-hand motifs within two independent domains, CR I-II and CR III-VI. They harbor two and four EF-hand motifs, respectively. The first 5 EF-hand motifs are capable of binding calcium ions, while the EF-hand 6 is inactive. SCGN consists of the three globular domains each of which contains a pair of EF-hand motifs. Human SCGN simultaneously binds four calcium ions through its EF-hands 3, 4, 5 and 6 in one high affinity and three low affinity calcium-binding sites. In contrast, SCGNs in other lower eukaryotes, such as D. rerio, X. laevis, M. domestica, G. gallus, O. anatinus, are fully competent in terms of six calcium-binding.


Pssm-ID: 320075 [Multi-domain]  Cd Length: 254  Bit Score: 35.79  E-value: 6.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47174755   5 SEDQILEFKEAFL-LFDRTGDGKITYNqcgDVMRALgqnPVNAEVLKVLGNPKAEEMnhklldfeqflpmlqaiaknkdq 83
Cdd:cd15902 128 SPPKLDEYTKLILkEFDANKDGKLELD---EMAKLL---PVQENFLLKFQILGAMDL----------------------- 178

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47174755  84 gTFEDFVEGLRVFDKEGNGTVMGAELRHVLTTLGEKMTEEEVETLLAGHEDA---------NGCINYEELV 145
Cdd:cd15902 179 -TKEDFEKVFEHYDKDNNGVIEGNELDALLKDLLEKNKADIDKPDLENFRDAilracdknkDGKIQKTELA 248
 
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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