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Conserved domains on  [gi|113931150|ref|NP_081639|]
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calcineurin B homologous protein 2 [Mus musculus]

Protein Classification

EF-hand domain-containing protein( domain architecture ID 11473824)

EF-hand (EFh) domain-containing protein similar to Homo sapiens guanylyl cyclase-activating proteins (GCAP1 and GCAP2), myosin regulatory light chain proteins, (MYL2, MYL5, MYL9, MYL10, and MYL12), and Kv channel-interacting proteins (KChIP1, KChIP2 and KChIP4)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-184 1.28e-14

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


:

Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.51  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113931150  30 RLYHRFQALDRDEKGFLSRLDLQQIGALAVnplgDRIIDSFFPNGSQRLYFAGFARVLAYFRPIDEEdatlrdpkqpepl 109
Cdd:COG5126    6 KLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEFVAGMESLFEATVE------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 110 nsrmNKLRFAFQLYDLDRDGKISRNEMlqvLRLMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSLEKM 184
Cdd:COG5126   69 ----PFARAAFDLLDTDGDGKISADEF---RRLLTALGVSEEEADEL----FARLDTDGDGKISFEEFVAAVRDY 132
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-184 1.28e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.51  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113931150  30 RLYHRFQALDRDEKGFLSRLDLQQIGALAVnplgDRIIDSFFPNGSQRLYFAGFARVLAYFRPIDEEdatlrdpkqpepl 109
Cdd:COG5126    6 KLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEFVAGMESLFEATVE------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 110 nsrmNKLRFAFQLYDLDRDGKISRNEMlqvLRLMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSLEKM 184
Cdd:COG5126   69 ----PFARAAFDLLDTDGDGKISADEF---RRLLTALGVSEEEADEL----FARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-179 3.86e-12

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: 58.71  E-value: 3.86e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 115 KLRFAFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTK 179
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEM----IREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
113-179 4.70e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.70e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113931150  113 MNKLRFAFQLYDLDRDGKISRNEMLQVLR-LMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTK 179
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRkLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLE 64
PTZ00184 PTZ00184
calmodulin; Provisional
 115-181 8.16e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.98  E-value: 8.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113931150 115 KLRFAFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSL 181
Cdd:PTZ00184  85 EIKEAFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEEVDEM----IREADVDGDGQINYEEFVKMM 146
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 115-143 4.24e-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: 36.20  E-value: 4.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 113931150   115 KLRFAFQLYDLDRDGKISRNEMLQVLRLM 143
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
 
Name Accession Description Interval E-value
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
30-184 1.28e-14

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 67.51  E-value: 1.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113931150  30 RLYHRFQALDRDEKGFLSRLDLQQIGALAVnplgDRIIDSFFPNGSQRLYFAGFARVLAYFRPIDEEdatlrdpkqpepl 109
Cdd:COG5126    6 KLDRRFDLLDADGDGVLERDDFEALFRRLW----ATLFSEADTDGDGRISREEFVAGMESLFEATVE------------- 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 110 nsrmNKLRFAFQLYDLDRDGKISRNEMlqvLRLMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSLEKM 184
Cdd:COG5126   69 ----PFARAAFDLLDTDGDGKISADEF---RRLLTALGVSEEEADEL----FARLDTDGDGKISFEEFVAAVRDY 132
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
 115-179 3.86e-12

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: 58.71  E-value: 3.86e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 115 KLRFAFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTK 179
Cdd:cd00051    1 ELREAFRLFDKDGDGTISADELKAALKSL-GEGLSEEEIDEM----IREVDKDGDGKIDFEEFLE 60
EF-hand_7 pfam13499
EF-hand domain pair;
113-179 4.70e-11

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 56.11  E-value: 4.70e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113931150  113 MNKLRFAFQLYDLDRDGKISRNEMLQVLR-LMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTK 179
Cdd:pfam13499   1 EEKLKEAFKLLDSDGDGYLDVEELKKLLRkLEEGEPLSDEEVEEL----FKEFDLDKDGRISFEEFLE 64
PTZ00184 PTZ00184
calmodulin; Provisional
 115-181 8.16e-06

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 43.98  E-value: 8.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113931150 115 KLRFAFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSL 181
Cdd:PTZ00184  85 EIKEAFKVFDRDGNGFISAAELRHVMTNL-GEKLTDEEVDEM----IREADVDGDGQINYEEFVKMM 146
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
 116-183 1.15e-05

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: 42.52  E-value: 1.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113931150 116 LRFAFQLYDLDRDGKISRNEMLQVLRL----MVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSLEK 183
Cdd:cd16252   39 IRKAFQMLDKDKSGFIEWNEIKYILSTvpssMPVAPLSDEEAEAM----IQAADTDGDGRIDFQEFSDMVKK 106
PTZ00183 PTZ00183
centrin; Provisional
 119-186 2.41e-05

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 42.75  E-value: 2.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113931150 119 AFQLYDLDRDGKISRNEMLQVLRlMVGVQVTDEQLESITDrtvqEADEDGDGAVSFLEFTKSLEKMNI 186
Cdd:PTZ00183  95 AFRLFDDDKTGKISLKNLKRVAK-ELGETITDEELQEMID----EADRNGDGEISEEEFYRIMKKTNL 157
EFh_PI-PLC cd15898
EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4. ...
 115-179 3.29e-05

EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes; PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.


Pssm-ID: 320029 [Multi-domain]  Cd Length: 137  Bit Score: 41.88  E-value: 3.29e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113931150 115 KLRFAFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTK 179
Cdd:cd15898    1 WLRRQWIKADKDGDGKLSLKEIKKLLKRL-NIRVSEKELKKL----FKEVDTNGDGTLTFDEFEE 60
EF-hand_6 pfam13405
EF-hand domain;
115-143 2.12e-04

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.16  E-value: 2.12e-04
                          10        20
                  ....*....|....*....|....*....
gi 113931150  115 KLRFAFQLYDLDRDGKISRNEMLQVLRLM 143
Cdd:pfam13405   1 ELREAFKLFDKDGDGKISLEELRKALRSL 29
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
112-184 2.59e-04

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


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 39.39  E-value: 2.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 113931150 112 RMNKLRFAFQLYDLDRDGKISRNEMLQVLRLMVgvqvtdeqlesitDRTVQEADEDGDGAVSFLEFTKSLEKM 184
Cdd:COG5126    3 QRRKLDRRFDLLDADGDGVLERDDFEALFRRLW-------------ATLFSEADTDGDGRISREEFVAGMESL 62
EF-hand_1 pfam00036
EF hand; The EF-hands can be divided into two classes: signalling proteins and buffering ...
 115-143 3.03e-04

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: 36.61  E-value: 3.03e-04
                          10        20
                  ....*....|....*....|....*....
gi 113931150  115 KLRFAFQLYDLDRDGKISRNEMLQVLRLM 143
Cdd:pfam00036   1 ELKEIFRLFDKDGDGKIDFEEFKELLKKL 29
EFh smart00054
EF-hand, calcium binding motif; EF-hands are calcium-binding motifs that occur at least in ...
 115-143 4.24e-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: 36.20  E-value: 4.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 113931150   115 KLRFAFQLYDLDRDGKISRNEMLQVLRLM 143
Cdd:smart00054   1 ELKEAFRLFDKDGDGKIDFEEFKDLLKAL 29
EF-hand_8 pfam13833
EF-hand domain pair;
128-183 6.72e-04

EF-hand domain pair;


Pssm-ID: 404678 [Multi-domain]  Cd Length: 54  Bit Score: 36.52  E-value: 6.72e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 113931150  128 DGKISRNEMLQVLRLMVGVQVTDEQLESItdrtVQEADEDGDGAVSFLEFTKSLEK 183
Cdd:pfam13833   2 KGVITREELKRALALLGLKDLSEDEVDIL----FREFDTDGDGYISFDEFCVLLER 53
PPP2R3 cd21339
serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine ...
 8-136 2.47e-03

serine/threonine protein phosphatase 2A regulatory subunit B"; Heterotrimeric serine/threonine protein phosphatase 2A (PP2A) consists of scaffolding (A), catalytic (C), and variable (B, B', and B") subunits. The variable subunits dictate subcellular localization and substrate specificity of the PP2A holoenzyme. This family includes PP2A regulatory B'' subunits alpha, beta and gamma, encoded by PPP2R3A, PPP2R3B and PPP2R3C, respectively. It also includes subunit delta encoded by PPP2R3D in mouse. These B-family regulatory subunits play various roles including regulation of cytoskeletal assembly, neuronal differentiation, mitogen-activated protein kinase signaling, and apoptosis. Subunits alpha and beta contain two-domain elongated structure with two calcium EF-hands which mediate Ca2+-dependent changes in phosphatase activity.


Pssm-ID: 410336  Cd Length: 259  Bit Score: 37.56  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113931150   8 IALIPDVEHIRRETG-FSQASLLRLYHRFQALDRDEKGFLSRLDLQQIGALAvnpLGDRIIDSFFPNGSQRLYFAGFARV 86
Cdd:cd21339   83 LALLEEEEDINQETNwFSYEHFYVIYCKFWELDTDHDLMISKEDLSRYNDAA---MSNVFIDRIFSGAVTRGKTIQKEGE 159

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 113931150  87 LAYFRPIDEEDAtLRDPKQPeplnsrmNKLRFAFQLYDLDRDGKISRNEM 136
Cdd:cd21339  160 MSYADFVWFLIS-EEDKKEP-------TSIEYWFRCLDIDGDGYLSVFEL 201
PTZ00184 PTZ00184
calmodulin; Provisional
 119-177 3.34e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 36.66  E-value: 3.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 113931150 119 AFQLYDLDRDGKISRNEMLQVLRLMvGVQVTDEQLESItdrtVQEADEDGDGAVSFLEF 177
Cdd:PTZ00184  16 AFSLFDKDGDGTITTKELGTVMRSL-GQNPTEAELQDM----INEVDADGNGTIDFPEF 69
EFh_CREC cd15899
EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin ...
 85-179 4.40e-03

EF-hand, calcium binding motif, found in CREC-EF hand family; The CREC (Cab45/reticulocalbin/ERC45/calumenin)-EF hand family contains a group of six EF-hand, low-affinity Ca2+-binding proteins, including reticulocalbin (RCN-1), ER Ca2+-binding protein of 55 kDa (ERC-55, also known as TCBP-49 or E6BP), reticulocalbin-3 (RCN-3), Ca2+-binding protein of 45 kDa (Cab45 and its splice variant Cab45b), and calumenin ( also known as crocalbin or CBP-50). The proteins are not only localized in various parts of the secretory pathway, but also found in the cytosolic compartment and at the cell surface. They interact with different ligands or proteins and have been implicated in the secretory process, chaperone activity, signal transduction as well as in a large variety of disease processes.


Pssm-ID: 320021 [Multi-domain]  Cd Length: 267  Bit Score: 37.04  E-value: 4.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113931150  85 RVLAYFRPIDEEDATLRDPKQPEPLNSRMNKLRFAFQLYDLDRDGKISRNEMLQVLRlmvgVQVTDEQLESITDRTVQEA 164
Cdd:cd15899   94 KNDTYGSVGDDEENVADNIKEDEEYKKLLLKDKKRFEAADQDGDLILTLEEFLAFLH----PEESPYMLDFVIKETLEDL 169

                         90
                 ....*....|....*
gi 113931150 165 DEDGDGAVSFLEFTK 179
Cdd:cd15899  170 DKNGDGFISLEEFIS 184
 
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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