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Conserved domains on  [gi|82503244|ref|YP_401688|]
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tegument serine/threonine protein kinase [Human gammaherpesvirus 4]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
 84-241 4.27e-06

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14066:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 272  Bit Score: 48.04  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  84 LGRGSYGAVY-AHADNAT---VKLYD------SVTELYHELMVCDMIQ---IGK--ATAEDGQDKALV-DYlsactscha 147
Cdd:cd14066   1 IGSGGFGTVYkGVLENGTvvaVKRLNemncaaSKKEFLTELEMLGRLRhpnLVRllGYCLESDEKLLVyEY--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244 148 lfMPQfrCSLQDYGHWHDGSiEPL-----VRGFQGLKDAVYFLNRHCG--LFHSDISPSNILVDFTDTMwgmgrlVLTDY 220
Cdd:cd14066  72 --MPN--GSLEDRLHCHKGS-PPLpwpqrLKIAKGIARGLEYLHEECPppIIHGDIKSSNILLDEDFEP------KLTDF 140

                       170       180
                ....*....|....*....|...
gi 82503244 221 GTASL--HDRNKMLDVRLKSSKG 241
Cdd:cd14066 141 GLARLipPSESVSKTSAVKGTIG 163
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 84-241 4.27e-06

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 48.04  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  84 LGRGSYGAVY-AHADNAT---VKLYD------SVTELYHELMVCDMIQ---IGK--ATAEDGQDKALV-DYlsactscha 147
Cdd:cd14066   1 IGSGGFGTVYkGVLENGTvvaVKRLNemncaaSKKEFLTELEMLGRLRhpnLVRllGYCLESDEKLLVyEY--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244 148 lfMPQfrCSLQDYGHWHDGSiEPL-----VRGFQGLKDAVYFLNRHCG--LFHSDISPSNILVDFTDTMwgmgrlVLTDY 220
Cdd:cd14066  72 --MPN--GSLEDRLHCHKGS-PPLpwpqrLKIAKGIARGLEYLHEECPppIIHGDIKSSNILLDEDFEP------KLTDF 140

                       170       180
                ....*....|....*....|...
gi 82503244 221 GTASL--HDRNKMLDVRLKSSKG 241
Cdd:cd14066 141 GLARLipPSESVSKTSAVKGTIG 163
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
190-231 2.17e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 43.46  E-value: 2.17e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 82503244 190 GLFHSDISPSNILVDFTdtmwgmGRLVLTDYGTASLHDRNKM 231
Cdd:COG0515 127 GIVHRDIKPANILLTPD------GRVKLIDFGIARALGGATL 162
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
 84-241 4.27e-06

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 48.04  E-value: 4.27e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  84 LGRGSYGAVY-AHADNAT---VKLYD------SVTELYHELMVCDMIQ---IGK--ATAEDGQDKALV-DYlsactscha 147
Cdd:cd14066   1 IGSGGFGTVYkGVLENGTvvaVKRLNemncaaSKKEFLTELEMLGRLRhpnLVRllGYCLESDEKLLVyEY--------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244 148 lfMPQfrCSLQDYGHWHDGSiEPL-----VRGFQGLKDAVYFLNRHCG--LFHSDISPSNILVDFTDTMwgmgrlVLTDY 220
Cdd:cd14066  72 --MPN--GSLEDRLHCHKGS-PPLpwpqrLKIAKGIARGLEYLHEECPppIIHGDIKSSNILLDEDFEP------KLTDF 140

                       170       180
                ....*....|....*....|...
gi 82503244 221 GTASL--HDRNKMLDVRLKSSKG 241
Cdd:cd14066 141 GLARLipPSESVSKTSAVKGTIG 163
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
 84-262 1.14e-05

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 46.11  E-value: 1.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  84 LGRGSYGAVYAHADNATVKLY-----------DSVTELYHELMVcdMIQIgkataedgQDKALVDYLSACTS--CHALFM 150
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKKVavkvipkeklkKLLEELLREIEI--LKKL--------NHPNIVKLYDVFETenFLYLVM 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244 151 PQF-RCSLQDYGHWHDGSIEP--LVRGFQGLKDAVYFLNRHcGLFHSDISPSNILVDftdtmwGMGRLVLTDYGTASLHD 227
Cdd:cd00180  71 EYCeGGSLKDLLKENKGPLSEeeALSILRQLLSALEYLHSN-GIIHRDLKPENILLD------SDGTVKLADFGLAKDLD 143

                       170       180       190
                ....*....|....*....|....*....|....*
gi 82503244 228 RNKmldvRLKSSKGRQLYRLYCQREPFSIAKDTYK 262
Cdd:cd00180 144 SDD----SLLKTTGGTTPPYYAPPELLGGRYYGPK 174
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
 180-231 1.10e-04

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 43.73  E-value: 1.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 82503244 180 DAVYFLNRHcGLFHSDISPSNILVDFTdtmwgmGRLVLTDYGTASLHDRNKM 231
Cdd:cd14014 111 DALAAAHRA-GIVHRDIKPANILLTED------GRVKLTDFGIARALGDSGL 155
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
 83-225 1.39e-04

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 43.23  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  83 LLGRGSYGAVYAHADNATVKLY-----------DSVTELYHELMVCDMIQigkataeDGQDKALVDYlsactschalfmp 151
Cdd:cd06917   8 LVGRGSYGAVYRGYHVKTGRVValkvlnldtddDDVSDIQKEVALLSQLK-------LGQPKNIIKY------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244 152 qFRCSLQDYGHW------HDGSIEPLVRGfQGLKD------------AVYFLNrHCGLFHSDISPSNILVDFTdtmwgmG 213
Cdd:cd06917  68 -YGSYLKGPSLWiimdycEGGSIRTLMRA-GPIAEryiavimrevlvALKFIH-KDGIIHRDIKAANILVTNT------G 138

                       170
                ....*....|..
gi 82503244 214 RLVLTDYGTASL 225
Cdd:cd06917 139 NVKLCDFGVAAS 150
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
190-231 2.17e-04

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 43.46  E-value: 2.17e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 82503244 190 GLFHSDISPSNILVDFTdtmwgmGRLVLTDYGTASLHDRNKM 231
Cdd:COG0515 127 GIVHRDIKPANILLTPD------GRVKLIDFGIARALGGATL 162
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
 175-230 1.27e-03

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 40.47  E-value: 1.27e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 82503244 175 FQGLKDAVYFLNRHcGLFHSDISPSNILVDftdtmwGMGRLVLTDYGTASLHDRNK 230
Cdd:cd14663 106 FQQLIDAVDYCHSR-GVFHRDLKPENLLLD------EDGNLKISDFGLSALSEQFR 154
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
 83-221 1.34e-03

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 40.21  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 82503244  83 LLGRGSYGAVYAHADNATVKLY----------DSVTELYHELMVcDMIQIGKATAEDGQDKALVDYLSACTSCHAL---- 148
Cdd:cd06628   7 LIGSGSFGSVYLGMNASSGELMavkqvelpsvSAENKDRKKSML-DALQREIALLRELQHENIVQYLGSSSDANHLnifl 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 82503244 149 -FMP--QFRCSLQDYGHWHdgsiEPLVRGF--QGLKDAVYFLNRhcGLFHSDISPSNILVDftdtmwGMGRLVLTDYG 221
Cdd:cd06628  86 eYVPggSVATLLNNYGAFE----ESLVRNFvrQILKGLNYLHNR--GIIHRDIKGANILVD------NKGGIKISDFG 151
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
 148-223 3.23e-03

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 39.40  E-value: 3.23e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 82503244 148 LFMPQFRCSLQDYGHWHDGSIEPLVRGFQGLKDAVYFLNRHcGLFHSDISPSNILVDFTDTmwGMGRLVLTDYGTA 223
Cdd:cd14018 117 LVMKNYPCTLRQYLWVNTPSYRLARVMILQLLEGVDHLVRH-GIAHRDLKSDNILLELDFD--GCPWLVIADFGCC 189
 
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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